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Database: PDB
Entry: 2BVN
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Original site: 2BVN 
HEADER    ELONGATION FACTOR                       30-JUN-05   2BVN              
TITLE     E. COLI EF-TU:GDPNP IN COMPLEX WITH THE ANTIBIOTIC                    
TITLE    2 ENACYLOXIN IIA                                                       
COMPND    MOL_ID: 1;                                                            
COMPND   2 MOLECULE: ELONGATION FACTOR TU;                                      
COMPND   3 CHAIN: A, B;                                                         
COMPND   4 SYNONYM: EF-TU, P-43;                                                
COMPND   5 EC: 3.6.1.48                                                         
SOURCE    MOL_ID: 1;                                                            
SOURCE   2 ORGANISM_SCIENTIFIC: ESCHERICHIA COLI;                               
SOURCE   3 ORGANISM_TAXID: 511693;                                              
SOURCE   4 STRAIN: BL21                                                         
KEYWDS    TRANSLATION, ELONGATION FACTOR, GTPASE, ANTIBIOTIC, GTP-              
KEYWDS   2 BINDING, PHOSPHORYLATION                                             
EXPDTA    X-RAY DIFFRACTION                                                     
AUTHOR    A.PARMEGGIANI,I.M.KRAB,T.WATANABE,R.C.NIELSEN,C.DAHLBERG,             
AUTHOR   2 J.NYBORG,P.NISSEN                                                    
REVDAT   3   24-FEB-09 2BVN    1       VERSN                                    
REVDAT   2   01-FEB-06 2BVN    1       JRNL                                     
REVDAT   1   01-SEP-05 2BVN    0                                                
JRNL        AUTH   A.PARMEGGIANI,I.M.KRAB,T.WATANABE,R.C.NIELSEN,               
JRNL        AUTH 2 C.DAHLBERG,J.NYBORG,P.NISSEN                                 
JRNL        TITL   ENACYLOXIN IIA PINPOINTS A BINDING POCKET OF                 
JRNL        TITL 2 ELONGATION FACTOR TU FOR DEVELOPMENT OF NOVEL                
JRNL        TITL 3 ANTIBIOTICS.                                                 
JRNL        REF    J.BIOL.CHEM.                  V. 281  2893 2006              
JRNL        REFN                   ISSN 0021-9258                               
JRNL        PMID   16257965                                                     
JRNL        DOI    10.1074/JBC.M505951200                                       
REMARK   2                                                                      
REMARK   2 RESOLUTION.    2.3  ANGSTROMS.                                       
REMARK   3                                                                      
REMARK   3 REFINEMENT.                                                          
REMARK   3   PROGRAM     : CNS 1.1                                              
REMARK   3   AUTHORS     : BRUNGER,ADAMS,CLORE,DELANO,GROS,GROSSE-              
REMARK   3               : KUNSTLEVE,JIANG,KUSZEWSKI,NILGES, PANNU,             
REMARK   3               : READ,RICE,SIMONSON,WARREN                            
REMARK   3                                                                      
REMARK   3  REFINEMENT TARGET : MAXIMUM LIKELIHOOD                              
REMARK   3                                                                      
REMARK   3  DATA USED IN REFINEMENT.                                            
REMARK   3   RESOLUTION RANGE HIGH (ANGSTROMS) : 2.30                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 29.06                          
REMARK   3   DATA CUTOFF            (SIGMA(F)) : 0.0                            
REMARK   3   DATA CUTOFF HIGH         (ABS(F)) : 3463299.91                     
REMARK   3   DATA CUTOFF LOW          (ABS(F)) : NULL                           
REMARK   3   COMPLETENESS (WORKING+TEST)   (%) : 99.8                           
REMARK   3   NUMBER OF REFLECTIONS             : 37612                          
REMARK   3                                                                      
REMARK   3  FIT TO DATA USED IN REFINEMENT.                                     
REMARK   3   CROSS-VALIDATION METHOD          : THROUGHOUT                      
REMARK   3   FREE R VALUE TEST SET SELECTION  : RANDOM                          
REMARK   3   R VALUE            (WORKING SET) : 0.230                           
REMARK   3   FREE R VALUE                     : 0.271                           
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 4.0                             
REMARK   3   FREE R VALUE TEST SET COUNT      : 1510                            
REMARK   3   ESTIMATED ERROR OF FREE R VALUE  : 0.007                           
REMARK   3                                                                      
REMARK   3  FIT IN THE HIGHEST RESOLUTION BIN.                                  
REMARK   3   TOTAL NUMBER OF BINS USED           : 15                           
REMARK   3   BIN RESOLUTION RANGE HIGH       (A) : 2.30                         
REMARK   3   BIN RESOLUTION RANGE LOW        (A) : 2.35                         
REMARK   3   BIN COMPLETENESS (WORKING+TEST) (%) : 100.0                        
REMARK   3   REFLECTIONS IN BIN    (WORKING SET) : 1133                         
REMARK   3   BIN R VALUE           (WORKING SET) : 0.367                        
REMARK   3   BIN FREE R VALUE                    : 0.430                        
REMARK   3   BIN FREE R VALUE TEST SET SIZE  (%) : 4.5                          
REMARK   3   BIN FREE R VALUE TEST SET COUNT     : 53                           
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            : 5737                                    
REMARK   3   NUCLEIC ACID ATOMS       : 0                                       
REMARK   3   HETEROGEN ATOMS          : 160                                     
REMARK   3   SOLVENT ATOMS            : 181                                     
REMARK   3                                                                      
REMARK   3  B VALUES.                                                           
REMARK   3   FROM WILSON PLOT           (A**2) : 40.4                           
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : 49.81                          
REMARK   3   OVERALL ANISOTROPIC B VALUE.                                       
REMARK   3    B11 (A**2) : 6.04                                                 
REMARK   3    B22 (A**2) : 6.04                                                 
REMARK   3    B33 (A**2) : -12.07                                               
REMARK   3    B12 (A**2) : 0.00                                                 
REMARK   3    B13 (A**2) : 0.00                                                 
REMARK   3    B23 (A**2) : 0.00                                                 
REMARK   3                                                                      
REMARK   3  ESTIMATED COORDINATE ERROR.                                         
REMARK   3   ESD FROM LUZZATI PLOT        (A) : 0.33                            
REMARK   3   ESD FROM SIGMAA              (A) : 0.33                            
REMARK   3   LOW RESOLUTION CUTOFF        (A) : 5.00                            
REMARK   3                                                                      
REMARK   3  CROSS-VALIDATED ESTIMATED COORDINATE ERROR.                         
REMARK   3   ESD FROM C-V LUZZATI PLOT    (A) : 0.39                            
REMARK   3   ESD FROM C-V SIGMAA          (A) : 0.36                            
REMARK   3                                                                      
REMARK   3  RMS DEVIATIONS FROM IDEAL VALUES.                                   
REMARK   3   BOND LENGTHS                 (A) : 0.007                           
REMARK   3   BOND ANGLES            (DEGREES) : 1.41                            
REMARK   3   DIHEDRAL ANGLES        (DEGREES) : NULL                            
REMARK   3   IMPROPER ANGLES        (DEGREES) : NULL                            
REMARK   3                                                                      
REMARK   3  ISOTROPIC THERMAL MODEL : RESTRAINED                                
REMARK   3                                                                      
REMARK   3  ISOTROPIC THERMAL FACTOR RESTRAINTS.    RMS    SIGMA                
REMARK   3   MAIN-CHAIN BOND              (A**2) : 3.37  ; 1.50                 
REMARK   3   MAIN-CHAIN ANGLE             (A**2) : 4.85  ; 2.00                 
REMARK   3   SIDE-CHAIN BOND              (A**2) : 5.28  ; 2.00                 
REMARK   3   SIDE-CHAIN ANGLE             (A**2) : 7.13  ; 2.50                 
REMARK   3                                                                      
REMARK   3  BULK SOLVENT MODELING.                                              
REMARK   3   METHOD USED : CNS BULK SOLVENT MODEL USED                          
REMARK   3   KSOL        : 0.313266                                             
REMARK   3   BSOL        : 33.7032                                              
REMARK   3                                                                      
REMARK   3  NCS MODEL : RESTRAINTS                                              
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  PARAMETER FILE  2  : NULL                                           
REMARK   3  TOPOLOGY FILE  1   : NULL                                           
REMARK   3  TOPOLOGY FILE  2   : NULL                                           
REMARK   3                                                                      
REMARK   3  OTHER REFINEMENT REMARKS: NULL                                      
REMARK   4                                                                      
REMARK   4 2BVN COMPLIES WITH FORMAT V. 3.15, 01-DEC-08                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBE ON  01-JUL-05.                 
REMARK 100 THE PDBE ID CODE IS EBI-24676.                                       
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : 25-MAY-03                          
REMARK 200  TEMPERATURE           (KELVIN) : 100.0                              
REMARK 200  PH                             : 6.80                               
REMARK 200  NUMBER OF CRYSTALS USED        : 1                                  
REMARK 200                                                                      
REMARK 200  SYNCHROTRON              (Y/N) : Y                                  
REMARK 200  RADIATION SOURCE               : MAX II                             
REMARK 200  BEAMLINE                       : I711                               
REMARK 200  X-RAY GENERATOR MODEL          : NULL                               
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M                                  
REMARK 200  WAVELENGTH OR RANGE        (A) : 0.9792                             
REMARK 200  MONOCHROMATOR                  : NULL                               
REMARK 200  OPTICS                         : NULL                               
REMARK 200                                                                      
REMARK 200  DETECTOR TYPE                  : CCD                                
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   : 37737                              
REMARK 200  RESOLUTION RANGE HIGH      (A) : 2.300                              
REMARK 200  RESOLUTION RANGE LOW       (A) : 30.000                             
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : -3.000                             
REMARK 200                                                                      
REMARK 200 OVERALL.                                                             
REMARK 200  COMPLETENESS FOR RANGE     (%) : 92.5                               
REMARK 200  DATA REDUNDANCY                : 10.000                             
REMARK 200  R MERGE                    (I) : 0.10000                            
REMARK 200  R SYM                      (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR THE DATA SET  : 24.1000                            
REMARK 200                                                                      
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.                                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.30                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 2.35                     
REMARK 200  COMPLETENESS FOR SHELL     (%) : 53.8                               
REMARK 200  DATA REDUNDANCY IN SHELL       : 7.70                               
REMARK 200  R MERGE FOR SHELL          (I) : 0.54000                            
REMARK 200  R SYM FOR SHELL            (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR SHELL         : 2.100                              
REMARK 200                                                                      
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH                              
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT        
REMARK 200 SOFTWARE USED: AMORE                                                 
REMARK 200 STARTING MODEL: PDB ENTRY 1OB2                                       
REMARK 200                                                                      
REMARK 200 REMARK: NULL                                                         
REMARK 280                                                                      
REMARK 280 CRYSTAL                                                              
REMARK 280 SOLVENT CONTENT, VS   (%): 47                                        
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.4                      
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: 2 MICROL PROTEIN SOLUTION MIXED          
REMARK 280  WITH 1 MICROL RESERVOIR SOLUTION (450 MM NACL. 22% PEG6000,         
REMARK 280  6% GLYCEROL, 7 MM MGCL2, 100 MM TRIS-HCL PH 7.5), SITTING           
REMARK 280  DROP 19 DEG. C                                                      
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY                                            
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 43 21 2                        
REMARK 290                                                                      
REMARK 290      SYMOP   SYMMETRY                                                
REMARK 290     NNNMMM   OPERATOR                                                
REMARK 290       1555   X,Y,Z                                                   
REMARK 290       2555   -X,-Y,Z+1/2                                             
REMARK 290       3555   -Y+1/2,X+1/2,Z+3/4                                      
REMARK 290       4555   Y+1/2,-X+1/2,Z+1/4                                      
REMARK 290       5555   -X+1/2,Y+1/2,-Z+3/4                                     
REMARK 290       6555   X+1/2,-Y+1/2,-Z+1/4                                     
REMARK 290       7555   Y,X,-Z                                                  
REMARK 290       8555   -Y,-X,-Z+1/2                                            
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      167.86500            
REMARK 290   SMTRY1   3  0.000000 -1.000000  0.000000       36.03500            
REMARK 290   SMTRY2   3  1.000000  0.000000  0.000000       36.03500            
REMARK 290   SMTRY3   3  0.000000  0.000000  1.000000      251.79750            
REMARK 290   SMTRY1   4  0.000000  1.000000  0.000000       36.03500            
REMARK 290   SMTRY2   4 -1.000000  0.000000  0.000000       36.03500            
REMARK 290   SMTRY3   4  0.000000  0.000000  1.000000       83.93250            
REMARK 290   SMTRY1   5 -1.000000  0.000000  0.000000       36.03500            
REMARK 290   SMTRY2   5  0.000000  1.000000  0.000000       36.03500            
REMARK 290   SMTRY3   5  0.000000  0.000000 -1.000000      251.79750            
REMARK 290   SMTRY1   6  1.000000  0.000000  0.000000       36.03500            
REMARK 290   SMTRY2   6  0.000000 -1.000000  0.000000       36.03500            
REMARK 290   SMTRY3   6  0.000000  0.000000 -1.000000       83.93250            
REMARK 290   SMTRY1   7  0.000000  1.000000  0.000000        0.00000            
REMARK 290   SMTRY2   7  1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY3   7  0.000000  0.000000 -1.000000        0.00000            
REMARK 290   SMTRY1   8  0.000000 -1.000000  0.000000        0.00000            
REMARK 290   SMTRY2   8 -1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY3   8  0.000000  0.000000 -1.000000      167.86500            
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 GENERATING THE BIOMOLECULE                                           
REMARK 350 COORDINATES FOR A COMPLETE MULTIMER REPRESENTING THE KNOWN           
REMARK 350 BIOLOGICALLY SIGNIFICANT OLIGOMERIZATION STATE OF THE                
REMARK 350 MOLECULE CAN BE GENERATED BY APPLYING BIOMT TRANSFORMATIONS          
REMARK 350 GIVEN BELOW.  BOTH NON-CRYSTALLOGRAPHIC AND                          
REMARK 350 CRYSTALLOGRAPHIC OPERATIONS ARE GIVEN.                               
REMARK 350                                                                      
REMARK 350 BIOMOLECULE:  1                                                      
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: MONOMERIC                         
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: MONOMERIC                  
REMARK 350 SOFTWARE USED: PQS                                                   
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A                                     
REMARK 350   BIOMT1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 350   BIOMT2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 350   BIOMT3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 350 BIOMOLECULE:  2                                                      
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: MONOMERIC                         
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: MONOMERIC                  
REMARK 350 SOFTWARE USED: PQS                                                   
REMARK 350 APPLY THE FOLLOWING TO CHAINS: 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     THR A     8                                                      
REMARK 465     ALA A    42                                                      
REMARK 465     ALA A    43                                                      
REMARK 465     ARG A    44                                                      
REMARK 465     ALA A    45                                                      
REMARK 465     PHE A    46                                                      
REMARK 465     ASP A    47                                                      
REMARK 465     GLN A    48                                                      
REMARK 465     ILE A    49                                                      
REMARK 465     ASP A    50                                                      
REMARK 465     ASN A    51                                                      
REMARK 465     ALA A    52                                                      
REMARK 465     PRO A    53                                                      
REMARK 465     GLU A    54                                                      
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     GLY B    41                                                      
REMARK 465     ALA B    42                                                      
REMARK 465     ALA B    43                                                      
REMARK 465     ARG B    44                                                      
REMARK 465     ALA B    45                                                      
REMARK 465     PHE B    46                                                      
REMARK 465     ASP B    47                                                      
REMARK 465     GLN B    48                                                      
REMARK 465     ILE B    49                                                      
REMARK 465     ASP B    50                                                      
REMARK 465     ASN B    51                                                      
REMARK 465     ALA B    52                                                      
REMARK 465     PRO B    53                                                      
REMARK 465     GLU B    54                                                      
REMARK 465     GLU B    55                                                      
REMARK 465     LYS B    56                                                      
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: TORSION ANGLES                                             
REMARK 500                                                                      
REMARK 500 TORSION ANGLES OUTSIDE THE EXPECTED RAMACHANDRAN REGIONS:            
REMARK 500 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;               
REMARK 500 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).                             
REMARK 500 STANDARD TABLE:                                                      
REMARK 500 FORMAT:(10X,I3,1X,A3,1X,A1,I4,A1,4X,F7.2,3X,F7.2)                    
REMARK 500                                                                      
REMARK 500 EXPECTED VALUES: GJ KLEYWEGT AND TA JONES (1996). PHI/PSI-           
REMARK 500 CHOLOGY: RAMACHANDRAN REVISITED. STRUCTURE 4, 1395 - 1400            
REMARK 500                                                                      
REMARK 500  M RES CSSEQI        PSI       PHI                                   
REMARK 500    GLU A 215      -70.93   -104.81                                   
REMARK 500    ILE A 247      -69.02     66.96                                   
REMARK 500    LYS A 263      150.05    176.29                                   
REMARK 500    ARG A 333     -112.80     55.11                                   
REMARK 500    LEU A 392      -72.09   -122.67                                   
REMARK 500    ILE B  60      -28.48     85.01                                   
REMARK 500    ASP B 161       33.11     70.18                                   
REMARK 500    GLU B 215      -74.11   -106.17                                   
REMARK 500    ILE B 247      -69.37     66.20                                   
REMARK 500    ARG B 333     -115.03     54.91                                   
REMARK 500    LEU B 392      -73.52   -122.09                                   
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 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 A1395  MG                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 HOH A2004   O                                                      
REMARK 620 2 THR A  25   OG1  84.1                                              
REMARK 620 3 HOH A2003   O    85.0  70.1                                        
REMARK 620 4 GNP A1394   O1G  93.0 165.8  95.8                                  
REMARK 620 5 GNP A1394   O2B 166.5  84.3  84.5  96.5                            
REMARK 620 N                    1     2     3     4                             
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              MG B1395  MG                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 HOH B2007   O                                                      
REMARK 620 2 THR B  25   OG1  78.7                                              
REMARK 620 3 GNP B1394   O1G  91.4 170.1                                        
REMARK 620 4 HOH B2005   O   163.4  84.7 105.2                                  
REMARK 620 5 HOH B2006   O    86.3  85.0  94.9  91.6                            
REMARK 620 6 GNP B1394   O2B  91.3  89.5  90.4  89.2 174.3                      
REMARK 620 N                    1     2     3     4     5                       
REMARK 700                                                                      
REMARK 700 SHEET                                                                
REMARK 700 DETERMINATION METHOD: DSSP                                           
REMARK 700 THE SHEETS PRESENTED AS "AD" IN EACH CHAIN ON SHEET RECORDS          
REMARK 700 BELOW IS ACTUALLY AN  6-STRANDED BARREL THIS IS REPRESENTED BY       
REMARK 700 A  7-STRANDED SHEET IN WHICH THE FIRST AND LAST STRANDS              
REMARK 700 ARE IDENTICAL.                                                       
REMARK 700                                                                      
REMARK 700 THE SHEETS PRESENTED AS "BD" IN EACH CHAIN ON SHEET RECORDS          
REMARK 700 BELOW IS ACTUALLY AN  6-STRANDED BARREL THIS IS REPRESENTED BY       
REMARK 700 A  7-STRANDED SHEET IN WHICH THE FIRST AND LAST STRANDS              
REMARK 700 ARE IDENTICAL.                                                       
REMARK 700                                                                      
REMARK 700 THE SHEET STRUCTURE OF THIS MOLECULE IS BIFURCATED. IN               
REMARK 700 ORDER TO REPRESENT THIS FEATURE IN THE SHEET RECORDS BELOW,          
REMARK 700 TWO SHEETS ARE DEFINED.                                              
REMARK 800                                                                      
REMARK 800 SITE                                                                 
REMARK 800 SITE_IDENTIFIER: AC1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE  MG A1395                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE  MG B1395                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE GNP A1394                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC4                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ENX A1396                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC5                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE GNP B1394                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC6                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ENX B1396                 
DBREF  2BVN A    1   393  UNP    P0A6N1   EFTU_ECOLI       1    393             
DBREF  2BVN B    1   393  UNP    P0A6N1   EFTU_ECOLI       1    393             
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  A1395       1                                                       
HET     MG  B1395       1                                                       
HET    GNP  A1394      32                                                       
HET    ENX  A1396      47                                                       
HET    GNP  B1394      32                                                       
HET    ENX  B1396      47                                                       
HETNAM      MG MAGNESIUM ION                                                    
HETNAM     GNP PHOSPHOAMINOPHOSPHONIC ACID-GUANYLATE ESTER                      
HETNAM     ENX ENACYLOXIN IIA                                                   
FORMUL   3   MG    2(MG 2+)                                                     
FORMUL   5  GNP    2(C10 H17 N6 O13 P3)                                         
FORMUL   6  ENX    2(C33 H45 CL2 N O11)                                         
FORMUL   9  HOH   *181(H2 O1)                                                   
HELIX    1   1 GLY A   23  GLY A   40  1                                  18    
HELIX    2   2 GLY A   59  ASN A   63  5                                   5    
HELIX    3   3 HIS A   84  ASP A   86  5                                   3    
HELIX    4   4 TYR A   87  ALA A   96  1                                  10    
HELIX    5   5 MET A  112  GLY A  126  1                                  15    
HELIX    6   6 LYS A  136  VAL A  140  5                                   5    
HELIX    7   7 ASP A  142  TYR A  160  1                                  19    
HELIX    8   8 SER A  173  GLU A  179  1                                   7    
HELIX    9   9 ASP A  181  ILE A  199  1                                  19    
HELIX   10  10 LYS A  282  ILE A  286  5                                   5    
HELIX   11  11 SER A  312  GLY A  316  5                                   5    
HELIX   12  12 GLY B   23  GLY B   40  1                                  18    
HELIX   13  13 HIS B   84  ASP B   86  5                                   3    
HELIX   14  14 TYR B   87  ALA B   96  1                                  10    
HELIX   15  15 MET B  112  GLY B  126  1                                  15    
HELIX   16  16 LYS B  136  VAL B  140  5                                   5    
HELIX   17  17 ASP B  142  TYR B  160  1                                  19    
HELIX   18  18 SER B  173  GLU B  179  1                                   7    
HELIX   19  19 ASP B  181  ILE B  199  1                                  19    
HELIX   20  20 LYS B  282  ILE B  286  5                                   5    
HELIX   21  21 SER B  312  GLY B  316  5                                   5    
SHEET    1  AA 6 HIS A  66  ASP A  70  0                                        
SHEET    2  AA 6 HIS A  75  ASP A  80 -1  O  TYR A  76   N  TYR A  69           
SHEET    3  AA 6 HIS A  11  ILE A  17  1  O  VAL A  12   N  ALA A  77           
SHEET    4  AA 6 ALA A 101  ALA A 106  1  O  ILE A 102   N  ILE A  17           
SHEET    5  AA 6 ILE A 130  ASN A 135  1  O  ILE A 131   N  LEU A 103           
SHEET    6  AA 6 ILE A 169  ARG A 171  1  O  VAL A 170   N  LEU A 134           
SHEET    1  AB 7 LEU A 211  PRO A 213  0                                        
SHEET    2  AB 7 VAL A 291  ALA A 293 -1  O  LEU A 292   N  LEU A 212           
SHEET    3  AB 7 GLU A 241  VAL A 245 -1  O  GLU A 243   N  ALA A 293           
SHEET    4  AB 7 GLN A 251  MET A 260 -1  O  GLN A 251   N  ILE A 244           
SHEET    5  AB 7 ASN A 273  ARG A 279 -1  O  GLY A 275   N  GLU A 259           
SHEET    6  AB 7 GLY A 224  ARG A 230 -1  O  THR A 225   N  LEU A 278           
SHEET    7  AB 7 VAL A 217  ILE A 220 -1  O  PHE A 218   N  VAL A 226           
SHEET    1  AC 5 LEU A 211  PRO A 213  0                                        
SHEET    2  AC 5 VAL A 291  ALA A 293 -1  O  LEU A 292   N  LEU A 212           
SHEET    3  AC 5 GLU A 241  VAL A 245 -1  O  GLU A 243   N  ALA A 293           
SHEET    4  AC 5 GLN A 251  MET A 260 -1  O  GLN A 251   N  ILE A 244           
SHEET    5  AC 5 LYS A 263  LEU A 265 -1  O  LYS A 263   N  MET A 260           
SHEET    1  AD 2 ILE A 235  LYS A 237  0                                        
SHEET    2  AD 2 GLU A 267  ARG A 269 -1  O  GLY A 268   N  ILE A 236           
SHEET    1  AE 7 LYS A 299  ILE A 310  0                                        
SHEET    2  AE 7 ASN A 355  MET A 368 -1  O  ILE A 356   N  VAL A 308           
SHEET    3  AE 7 THR A 335  GLU A 342 -1  O  THR A 338   N  ILE A 363           
SHEET    4  AE 7 GLN A 329  PHE A 332 -1  O  PHE A 330   N  VAL A 337           
SHEET    5  AE 7 ARG A 373  GLU A 378 -1  O  ALA A 375   N  TYR A 331           
SHEET    6  AE 7 ARG A 381  VAL A 391 -1  O  ARG A 381   N  GLU A 378           
SHEET    7  AE 7 LYS A 299  ILE A 310 -1  O  GLU A 305   N  ALA A 389           
SHEET    1  AF 2 PHE A 322  PHE A 323  0                                        
SHEET    2  AF 2 MET A 349  VAL A 350 -1  O  VAL A 350   N  PHE A 322           
SHEET    1  BA 6 HIS B  66  ASP B  70  0                                        
SHEET    2  BA 6 HIS B  75  ASP B  80 -1  O  TYR B  76   N  TYR B  69           
SHEET    3  BA 6 HIS B  11  ILE B  17  1  O  VAL B  12   N  ALA B  77           
SHEET    4  BA 6 ALA B 101  ALA B 106  1  O  ILE B 102   N  ILE B  17           
SHEET    5  BA 6 ILE B 130  ASN B 135  1  O  ILE B 131   N  LEU B 103           
SHEET    6  BA 6 ILE B 169  ARG B 171  1  O  VAL B 170   N  LEU B 134           
SHEET    1  BB10 LEU B 211  PRO B 213  0                                        
SHEET    2  BB10 VAL B 291  ALA B 293 -1  O  LEU B 292   N  LEU B 212           
SHEET    3  BB10 GLU B 241  VAL B 245 -1  O  GLU B 243   N  ALA B 293           
SHEET    4  BB10 GLN B 251  MET B 260 -1  O  GLN B 251   N  ILE B 244           
SHEET    5  BB10 VAL B 217  ILE B 220                                           
SHEET    6  BB10 GLY B 224  ARG B 230 -1  O  GLY B 224   N  ILE B 220           
SHEET    7  BB10 ASN B 273  ARG B 279 -1  O  VAL B 274   N  GLY B 229           
SHEET    8  BB10 GLN B 251  MET B 260 -1  O  THR B 254   N  ARG B 279           
SHEET    9  BB10 LYS B 263  LEU B 265 -1  O  LYS B 263   N  MET B 260           
SHEET   10  BB10 GLN B 251  MET B 260 -1  O  VAL B 258   N  LEU B 265           
SHEET    1  BC 2 ILE B 235  LYS B 237  0                                        
SHEET    2  BC 2 GLU B 267  ARG B 269 -1  O  GLY B 268   N  ILE B 236           
SHEET    1  BD 7 LYS B 299  ILE B 310  0                                        
SHEET    2  BD 7 ASN B 355  MET B 368 -1  O  ILE B 356   N  VAL B 308           
SHEET    3  BD 7 THR B 335  GLU B 342 -1  O  THR B 338   N  ILE B 363           
SHEET    4  BD 7 GLN B 329  PHE B 332 -1  O  PHE B 330   N  VAL B 337           
SHEET    5  BD 7 ARG B 373  GLU B 378 -1  O  ALA B 375   N  TYR B 331           
SHEET    6  BD 7 ARG B 381  VAL B 391 -1  O  ARG B 381   N  GLU B 378           
SHEET    7  BD 7 LYS B 299  ILE B 310 -1  O  GLU B 305   N  ALA B 389           
SHEET    1  BE 2 PHE B 322  PHE B 323  0                                        
SHEET    2  BE 2 MET B 349  VAL B 350 -1  O  VAL B 350   N  PHE B 322           
LINK         O1G GNP A1394                MG    MG A1395     1555   1555  1.94  
LINK         O2B GNP A1394                MG    MG A1395     1555   1555  2.00  
LINK        MG    MG A1395                 O   HOH A2003     1555   1555  2.11  
LINK        MG    MG A1395                 OG1 THR A  25     1555   1555  2.18  
LINK        MG    MG A1395                 O   HOH A2004     1555   1555  2.05  
LINK         O2B GNP B1394                MG    MG B1395     1555   1555  2.04  
LINK        MG    MG B1395                 O   HOH B2006     1555   1555  2.22  
LINK        MG    MG B1395                 O   HOH B2005     1555   1555  1.96  
LINK        MG    MG B1395                 O1G GNP B1394     1555   1555  2.10  
LINK        MG    MG B1395                 OG1 THR B  25     1555   1555  2.05  
LINK        MG    MG B1395                 O   HOH B2007     1555   1555  2.11  
SITE     1 AC1  4 THR A  25  GNP A1394  HOH A2003  HOH A2004                    
SITE     1 AC2  5 THR B  25  GNP B1394  HOH B2005  HOH B2006                    
SITE     2 AC2  5 HOH B2007                                                     
SITE     1 AC3 20 VAL A  20  ASP A  21  HIS A  22  GLY A  23                    
SITE     2 AC3 20 LYS A  24  THR A  25  THR A  26  PRO A  82                    
SITE     3 AC3 20 GLY A  83  ASN A 135  LYS A 136  ASP A 138                    
SITE     4 AC3 20 MET A 139  SER A 173  ALA A 174  LEU A 175                    
SITE     5 AC3 20  MG A1395  HOH A2003  HOH A2004  HOH A2082                    
SITE     1 AC4 18 ALA A  96  LEU A 120  ARG A 123  GLN A 124                    
SITE     2 AC4 18 VAL A 125  GLN A 159  TYR A 160  LEU A 311                    
SITE     3 AC4 18 LYS A 313  ASP A 314  GLU A 315  TYR A 331                    
SITE     4 AC4 18 ARG A 333  ARG A 373  PHE A 374  ALA A 375                    
SITE     5 AC4 18 HOH A2081  HOH A2083                                          
SITE     1 AC5 20 VAL B  20  ASP B  21  HIS B  22  GLY B  23                    
SITE     2 AC5 20 LYS B  24  THR B  25  THR B  26  PRO B  82                    
SITE     3 AC5 20 GLY B  83  ASN B 135  LYS B 136  ASP B 138                    
SITE     4 AC5 20 MET B 139  SER B 173  ALA B 174  LEU B 175                    
SITE     5 AC5 20  MG B1395  HOH B2005  HOH B2007  HOH B2095                    
SITE     1 AC6 16 ALA B  96  LEU B 120  ARG B 123  GLN B 124                    
SITE     2 AC6 16 VAL B 125  GLN B 159  TYR B 160  LEU B 311                    
SITE     3 AC6 16 LYS B 313  ASP B 314  GLU B 315  ARG B 333                    
SITE     4 AC6 16 ARG B 373  PHE B 374  ALA B 375  HOH B2097                    
CRYST1   72.070   72.070  335.730  90.00  90.00  90.00 P 43 21 2    16          
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      0.013875  0.000000  0.000000        0.00000                         
SCALE2      0.000000  0.013875  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.002979        0.00000                         
MTRIX1   1 -0.500380 -0.865800  0.002900       -0.22612    1                    
MTRIX2   1  0.865800 -0.500380  0.000420       -0.61432    1                    
MTRIX3   1  0.001090  0.002720  1.000000       -0.07002    1                    
(ATOM LINES ARE NOT SHOWN.)
END                                                                             
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