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Database: PDB
Entry: 2FX3
LinkDB: 2FX3
Original site: 2FX3 
HEADER    TRANSLATION                             03-FEB-06   2FX3              
TITLE     CRYSTAL STRUCTURE DETERMINATION OF E. COLI ELONGATION                 
TITLE    2 FACTOR, TU USING A TWINNED DATA SET                                  
COMPND    MOL_ID: 1;                                                            
COMPND   2 MOLECULE: ELONGATION FACTOR TU;                                      
COMPND   3 CHAIN: A;                                                            
COMPND   4 SYNONYM: EF-TU                                                       
SOURCE    MOL_ID: 1;                                                            
SOURCE   2 ORGANISM_SCIENTIFIC: ESCHERICHIA COLI;                               
SOURCE   3 ORGANISM_TAXID: 562;                                                 
SOURCE   4 OTHER_DETAILS: GENE: TUFA                                            
KEYWDS    EF-TU, MEROHEDRAL TWINNING, TRANSLATION                               
EXPDTA    X-RAY DIFFRACTION                                                     
AUTHOR    S.E.HEFFRON,R.MOELLER,F.JURNAK                                        
REVDAT   2   24-FEB-09 2FX3    1       VERSN                                    
REVDAT   1   28-MAR-06 2FX3    0                                                
JRNL        AUTH   S.E.HEFFRON,R.MOELLER,F.JURNAK                               
JRNL        TITL   SOLVING THE STRUCTURE OF ESCHERICHIA COLI                    
JRNL        TITL 2 ELONGATION FACTOR TU USING A TWINNED DATA SET.               
JRNL        REF    ACTA CRYSTALLOGR.,SECT.D      V.  62   433 2006              
JRNL        REFN                   ISSN 0907-4449                               
JRNL        PMID   16552145                                                     
JRNL        DOI    10.1107/S0907444906004021                                    
REMARK   1                                                                      
REMARK   2                                                                      
REMARK   2 RESOLUTION.    3.40 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 : ENGH & HUBER                                    
REMARK   3                                                                      
REMARK   3  DATA USED IN REFINEMENT.                                            
REMARK   3   RESOLUTION RANGE HIGH (ANGSTROMS) : 3.40                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 60.23                          
REMARK   3   DATA CUTOFF            (SIGMA(F)) : 0.000                          
REMARK   3   DATA CUTOFF HIGH         (ABS(F)) : NULL                           
REMARK   3   DATA CUTOFF LOW          (ABS(F)) : NULL                           
REMARK   3   COMPLETENESS (WORKING+TEST)   (%) : 87.1                           
REMARK   3   NUMBER OF REFLECTIONS             : 6083                           
REMARK   3                                                                      
REMARK   3  FIT TO DATA USED IN REFINEMENT.                                     
REMARK   3   CROSS-VALIDATION METHOD          : THROUGHOUT                      
REMARK   3   FREE R VALUE TEST SET SELECTION  : USED CNS TASK FILE MAKE_        
REMARK   3                                      CV_TWIN.INP TO SELECT CROSS     
REMARK   3                                      -VALIDATION SET SUCH THAT       
REMARK   3                                      PAIRS OF TWIN-RELATED           
REMARK   3                                      REFLECTIONS WERE DESIGNATED     
REMARK   3                                      TO BE IN THE SAME SET,          
REMARK   3                                      EITHER THE WORKING SET OR       
REMARK   3                                      THE TEST SET.                   
REMARK   3   R VALUE            (WORKING SET) : 0.197                           
REMARK   3   FREE R VALUE                     : 0.262                           
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 8.400                           
REMARK   3   FREE R VALUE TEST SET COUNT      : 586                             
REMARK   3   ESTIMATED ERROR OF FREE R VALUE  : NULL                            
REMARK   3                                                                      
REMARK   3  FIT IN THE HIGHEST RESOLUTION BIN.                                  
REMARK   3   TOTAL NUMBER OF BINS USED           : NULL                         
REMARK   3   BIN RESOLUTION RANGE HIGH       (A) : NULL                         
REMARK   3   BIN RESOLUTION RANGE LOW        (A) : NULL                         
REMARK   3   BIN COMPLETENESS (WORKING+TEST) (%) : NULL                         
REMARK   3   REFLECTIONS IN BIN    (WORKING SET) : NULL                         
REMARK   3   BIN R VALUE           (WORKING SET) : NULL                         
REMARK   3   BIN FREE R VALUE                    : NULL                         
REMARK   3   BIN FREE R VALUE TEST SET SIZE  (%) : NULL                         
REMARK   3   BIN FREE R VALUE TEST SET COUNT     : NULL                         
REMARK   3   ESTIMATED ERROR OF BIN FREE R VALUE : NULL                         
REMARK   3                                                                      
REMARK   3  NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.                    
REMARK   3   PROTEIN ATOMS            : 2981                                    
REMARK   3   NUCLEIC ACID ATOMS       : 0                                       
REMARK   3   HETEROGEN ATOMS          : 29                                      
REMARK   3   SOLVENT ATOMS            : 4                                       
REMARK   3                                                                      
REMARK   3  B VALUES.                                                           
REMARK   3   FROM WILSON PLOT           (A**2) : NULL                           
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : 75.70                          
REMARK   3   OVERALL ANISOTROPIC B VALUE.                                       
REMARK   3    B11 (A**2) : 8.81900                                              
REMARK   3    B22 (A**2) : 8.81900                                              
REMARK   3    B33 (A**2) : -17.63900                                            
REMARK   3    B12 (A**2) : 2.01100                                              
REMARK   3    B13 (A**2) : 0.00000                                              
REMARK   3    B23 (A**2) : 0.00000                                              
REMARK   3                                                                      
REMARK   3  ESTIMATED COORDINATE ERROR.                                         
REMARK   3   ESD FROM LUZZATI PLOT        (A) : NULL                            
REMARK   3   ESD FROM SIGMAA              (A) : NULL                            
REMARK   3   LOW RESOLUTION CUTOFF        (A) : NULL                            
REMARK   3                                                                      
REMARK   3  CROSS-VALIDATED ESTIMATED COORDINATE ERROR.                         
REMARK   3   ESD FROM C-V LUZZATI PLOT    (A) : NULL                            
REMARK   3   ESD FROM C-V SIGMAA          (A) : NULL                            
REMARK   3                                                                      
REMARK   3  RMS DEVIATIONS FROM IDEAL VALUES.                                   
REMARK   3   BOND LENGTHS                 (A) : 0.011                           
REMARK   3   BOND ANGLES            (DEGREES) : 1.73                            
REMARK   3   DIHEDRAL ANGLES        (DEGREES) : 24.69                           
REMARK   3   IMPROPER ANGLES        (DEGREES) : 1.18                            
REMARK   3                                                                      
REMARK   3  ISOTROPIC THERMAL MODEL : ISOTROPIC                                 
REMARK   3                                                                      
REMARK   3  ISOTROPIC THERMAL FACTOR RESTRAINTS.    RMS    SIGMA                
REMARK   3   MAIN-CHAIN BOND              (A**2) : NULL  ; NULL                 
REMARK   3   MAIN-CHAIN ANGLE             (A**2) : NULL  ; NULL                 
REMARK   3   SIDE-CHAIN BOND              (A**2) : NULL  ; NULL                 
REMARK   3   SIDE-CHAIN ANGLE             (A**2) : NULL  ; NULL                 
REMARK   3                                                                      
REMARK   3  BULK SOLVENT MODELING.                                              
REMARK   3   METHOD USED : NULL                                                 
REMARK   3   KSOL        : NULL                                                 
REMARK   3   BSOL        : 73.77                                                
REMARK   3                                                                      
REMARK   3  NCS MODEL : NULL                                                    
REMARK   3                                                                      
REMARK   3  NCS RESTRAINTS.                         RMS   SIGMA/WEIGHT          
REMARK   3   GROUP  1  POSITIONAL            (A) : NULL  ; NULL                 
REMARK   3   GROUP  1  B-FACTOR           (A**2) : NULL  ; NULL                 
REMARK   3                                                                      
REMARK   3  PARAMETER FILE  1  : CNS_TOPPAR:PROTEIN_REP.PARAM                   
REMARK   3  PARAMETER FILE  2  : MYTOPPAR:GDP_CNS4.PARAM                        
REMARK   3  PARAMETER FILE  3  : CNS_TOPPAR:ION.PARAM                           
REMARK   3  PARAMETER FILE  4  : CNS_TOPPAR:WATER_REP.PARAM                     
REMARK   3  PARAMETER FILE  5  : NULL                                           
REMARK   3  TOPOLOGY FILE  1   : NULL                                           
REMARK   3  TOPOLOGY FILE  2   : NULL                                           
REMARK   3  TOPOLOGY FILE  3   : NULL                                           
REMARK   3  TOPOLOGY FILE  4   : NULL                                           
REMARK   3  TOPOLOGY FILE  5   : NULL                                           
REMARK   3                                                                      
REMARK   3  OTHER REFINEMENT REMARKS: USED CNS SPECIALIZED TASK FILES FOR       
REMARK   3  REFINEMENT WITH HEMIHEDRALLY TWINNED DATA. TWIN OPERATOR WAS        
REMARK   3  (-H,-K,L), AND TWIN FRACTION WAS 0.294. R-FACTORS REPORTED ARE      
REMARK   3  THE TWINNED R-FACTORS FROM CNS. (R-FACTORS AFTER DETWINNING: R      
REMARK   3  -WORK=0.2867, R-FREE=0.3267)                                        
REMARK   4                                                                      
REMARK   4 2FX3 COMPLIES WITH FORMAT V. 3.15, 01-DEC-08                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 20-FEB-06.                  
REMARK 100 THE RCSB ID CODE IS RCSB036414.                                      
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : 24-AUG-04                          
REMARK 200  TEMPERATURE           (KELVIN) : 95                                 
REMARK 200  PH                             : 7.8                                
REMARK 200  NUMBER OF CRYSTALS USED        : 1                                  
REMARK 200                                                                      
REMARK 200  SYNCHROTRON              (Y/N) : Y                                  
REMARK 200  RADIATION SOURCE               : ALS                                
REMARK 200  BEAMLINE                       : 5.0.2                              
REMARK 200  X-RAY GENERATOR MODEL          : NULL                               
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M                                  
REMARK 200  WAVELENGTH OR RANGE        (A) : 1.033                              
REMARK 200  MONOCHROMATOR                  : NULL                               
REMARK 200  OPTICS                         : NULL                               
REMARK 200                                                                      
REMARK 200  DETECTOR TYPE                  : CCD                                
REMARK 200  DETECTOR MANUFACTURER          : ADSC QUANTUM 4                     
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : MOSFLM                             
REMARK 200  DATA SCALING SOFTWARE          : CCP4 (SCALA)                       
REMARK 200                                                                      
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 6312                               
REMARK 200  RESOLUTION RANGE HIGH      (A) : 3.400                              
REMARK 200  RESOLUTION RANGE LOW       (A) : 60.232                             
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : NULL                               
REMARK 200                                                                      
REMARK 200 OVERALL.                                                             
REMARK 200  COMPLETENESS FOR RANGE     (%) : 90.2                               
REMARK 200  DATA REDUNDANCY                : 6.600                              
REMARK 200  R MERGE                    (I) : 0.17400                            
REMARK 200  R SYM                      (I) : 0.17400                            
REMARK 200  <I/SIGMA(I)> FOR THE DATA SET  : 3.2000                             
REMARK 200                                                                      
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.                                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 3.40                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 3.58                     
REMARK 200  COMPLETENESS FOR SHELL     (%) : 84.9                               
REMARK 200  DATA REDUNDANCY IN SHELL       : 6.90                               
REMARK 200  R MERGE FOR SHELL          (I) : 0.48000                            
REMARK 200  R SYM FOR SHELL            (I) : 0.48000                            
REMARK 200  <I/SIGMA(I)> FOR SHELL         : 1.500                              
REMARK 200                                                                      
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH                              
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT        
REMARK 200 SOFTWARE USED: PHASER                                                
REMARK 200 STARTING MODEL: PDB ENTRY 1D8T, CHAIN A                              
REMARK 200                                                                      
REMARK 200 REMARK: NULL                                                         
REMARK 280                                                                      
REMARK 280 CRYSTAL                                                              
REMARK 280 SOLVENT CONTENT, VS   (%): 55.05                                     
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.74                     
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: 0.45 MM EF-TU IN 50 MM TRIS, PH          
REMARK 280  7.8, 10 MM GDP, 10 MM MAGNESIUM CHLORIDE, 0.5% PEG 3350, 5.5        
REMARK 280  MM AMMONIUM ACETATE, 2.7 MM AMMONIUM CITRATE, 1.34 MM CHEMDIV       
REMARK 280  COMPOUND 1013-0135, VAPOR DIFFUSION, SITTING DROP, TEMPERATURE      
REMARK 280  293K                                                                
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY                                            
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 31 2 1                         
REMARK 290                                                                      
REMARK 290      SYMOP   SYMMETRY                                                
REMARK 290     NNNMMM   OPERATOR                                                
REMARK 290       1555   X,Y,Z                                                   
REMARK 290       2555   -Y,X-Y,Z+1/3                                            
REMARK 290       3555   -X+Y,-X,Z+2/3                                           
REMARK 290       4555   Y,X,-Z                                                  
REMARK 290       5555   X-Y,-Y,-Z+2/3                                           
REMARK 290       6555   -X,-X+Y,-Z+1/3                                          
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 -0.500000 -0.866025  0.000000        0.00000            
REMARK 290   SMTRY2   2  0.866025 -0.500000  0.000000        0.00000            
REMARK 290   SMTRY3   2  0.000000  0.000000  1.000000       56.48000            
REMARK 290   SMTRY1   3 -0.500000  0.866025  0.000000        0.00000            
REMARK 290   SMTRY2   3 -0.866025 -0.500000  0.000000        0.00000            
REMARK 290   SMTRY3   3  0.000000  0.000000  1.000000      112.96000            
REMARK 290   SMTRY1   4 -0.500000  0.866025  0.000000        0.00000            
REMARK 290   SMTRY2   4  0.866025  0.500000  0.000000        0.00000            
REMARK 290   SMTRY3   4  0.000000  0.000000 -1.000000        0.00000            
REMARK 290   SMTRY1   5  1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   5  0.000000 -1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   5  0.000000  0.000000 -1.000000      112.96000            
REMARK 290   SMTRY1   6 -0.500000 -0.866025  0.000000        0.00000            
REMARK 290   SMTRY2   6 -0.866025  0.500000  0.000000        0.00000            
REMARK 290   SMTRY3   6  0.000000  0.000000 -1.000000       56.48000            
REMARK 290                                                                      
REMARK 290 REMARK: NULL                                                         
REMARK 300                                                                      
REMARK 300 BIOMOLECULE: 1                                                       
REMARK 300 SEE REMARK 350 FOR THE AUTHOR PROVIDED AND/OR PROGRAM                
REMARK 300 GENERATED ASSEMBLY INFORMATION FOR THE STRUCTURE IN                  
REMARK 300 THIS ENTRY. THE REMARK MAY ALSO PROVIDE INFORMATION ON               
REMARK 300 BURIED SURFACE AREA.                                                 
REMARK 350                                                                      
REMARK 350 COORDINATES FOR A COMPLETE MULTIMER REPRESENTING THE KNOWN           
REMARK 350 BIOLOGICALLY SIGNIFICANT OLIGOMERIZATION STATE OF THE                
REMARK 350 MOLECULE CAN BE GENERATED BY APPLYING BIOMT TRANSFORMATIONS          
REMARK 350 GIVEN BELOW.  BOTH NON-CRYSTALLOGRAPHIC AND                          
REMARK 350 CRYSTALLOGRAPHIC OPERATIONS ARE GIVEN.                               
REMARK 350                                                                      
REMARK 350 BIOMOLECULE: 1                                                       
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: MONOMERIC                         
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A                                     
REMARK 350   BIOMT1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 350   BIOMT2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 350   BIOMT3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 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 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   OG1  THR A   320     O    THR A    38     3454     2.16            
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    THR A   8      -33.67    114.19                                   
REMARK 500    LYS A   9      107.79    -59.50                                   
REMARK 500    PRO A  10      136.67    -39.43                                   
REMARK 500    VAL A  14     -165.89   -129.37                                   
REMARK 500    ALA A  29      -75.00    -45.77                                   
REMARK 500    ALA A  30      -35.05    -33.66                                   
REMARK 500    THR A  33      -74.77    -53.11                                   
REMARK 500    GLN A  48      -19.86    -46.24                                   
REMARK 500    GLU A  54     -159.10    -89.14                                   
REMARK 500    ARG A  58       -0.74     56.05                                   
REMARK 500    THR A  71     -167.71   -102.03                                   
REMARK 500    PRO A  72      -74.39    -68.25                                   
REMARK 500    ALA A  95      -33.34    -38.44                                   
REMARK 500    PRO A 113      -74.87    -44.22                                   
REMARK 500    LYS A 136       17.92     54.38                                   
REMARK 500    GLU A 143      -74.44    -37.12                                   
REMARK 500    VAL A 153      -82.66    -74.12                                   
REMARK 500    ARG A 154      -27.93    -33.73                                   
REMARK 500    PRO A 163       68.92    -65.77                                   
REMARK 500    ALA A 182      -39.02    -37.85                                   
REMARK 500    PRO A 202      173.63    -57.73                                   
REMARK 500    LYS A 208      164.26    -45.57                                   
REMARK 500    LEU A 212      114.11   -162.52                                   
REMARK 500    SER A 221      -90.16     30.98                                   
REMARK 500    ARG A 223       61.07   -161.58                                   
REMARK 500    ILE A 247      -88.65     75.59                                   
REMARK 500    SER A 253     -167.97   -164.09                                   
REMARK 500    CYS A 255       98.94    -67.31                                   
REMARK 500    PHE A 261       66.55     66.86                                   
REMARK 500    ARG A 262       -1.79     49.69                                   
REMARK 500    GLU A 267      139.48   -177.04                                   
REMARK 500    ARG A 288      158.33    -48.85                                   
REMARK 500    PRO A 295      101.83    -52.31                                   
REMARK 500    ILE A 298      143.33   -171.85                                   
REMARK 500    THR A 302      -24.81   -141.17                                   
REMARK 500    LEU A 311     -177.91    -62.13                                   
REMARK 500    ARG A 318      152.13    -43.90                                   
REMARK 500    LYS A 324      173.63    -46.83                                   
REMARK 500    ARG A 333      -57.91     60.32                                   
REMARK 500    PRO A 344      154.56    -46.64                                   
REMARK 500    LEU A 392      -77.53   -114.89                                   
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 998  MG                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 THR A  25   OG1                                                    
REMARK 620 2 GDP A 999   O2B  75.6                                              
REMARK 620 N                    1                                               
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 998                  
REMARK 800 SITE_IDENTIFIER: AC2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE GDP A 999                 
DBREF  2FX3 A    1   393  UNP    Q83JC4   EFTU_SHIFL       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 GLY                                                  
HET     MG  A 998       1                                                       
HET    GDP  A 999      28                                                       
HETNAM      MG MAGNESIUM ION                                                    
HETNAM     GDP GUANOSINE-5'-DIPHOSPHATE                                         
FORMUL   2   MG    MG 2+                                                        
FORMUL   3  GDP    C10 H15 N5 O11 P2                                            
FORMUL   4  HOH   *4(H2 O)                                                      
HELIX    1   1 GLY A   23  GLY A   40  1                                  18    
HELIX    2   2 ALA A   45  ASN A   51  1                                   7    
HELIX    3   3 GLY A   83  GLY A   94  1                                  12    
HELIX    4   4 MET A  112  GLY A  126  1                                  15    
HELIX    5   5 LYS A  136  VAL A  140  5                                   5    
HELIX    6   6 ASP A  142  TYR A  160  1                                  19    
HELIX    7   7 PRO A  163  THR A  167  5                                   5    
HELIX    8   8 SER A  173  GLY A  180  1                                   8    
HELIX    9   9 ASP A  181  ILE A  199  1                                  19    
HELIX   10  10 LYS A  282  ILE A  286  5                                   5    
SHEET    1   A 6 SER A  65  ASP A  70  0                                        
SHEET    2   A 6 HIS A  75  ASP A  80 -1  O  HIS A  78   N  VAL A  67           
SHEET    3   A 6 HIS A  11  GLY A  18  1  N  VAL A  12   O  ALA A  77           
SHEET    4   A 6 ALA A 101  ALA A 106  1  O  ILE A 102   N  GLY A  15           
SHEET    5   A 6 ILE A 130  ASN A 135  1  O  ASN A 135   N  VAL A 105           
SHEET    6   A 6 ILE A 169  ARG A 171  1  O  VAL A 170   N  VAL A 132           
SHEET    1   B 2 LYS A  56  ALA A  57  0                                        
SHEET    2   B 2 ILE A  60  THR A  61 -1  O  ILE A  60   N  ALA A  57           
SHEET    1   C 7 LEU A 211  PRO A 213  0                                        
SHEET    2   C 7 VAL A 291  ALA A 293 -1  O  LEU A 292   N  LEU A 212           
SHEET    3   C 7 GLU A 241  VAL A 245 -1  N  GLU A 243   O  ALA A 293           
SHEET    4   C 7 GLN A 251  MET A 260 -1  O  GLN A 251   N  ILE A 244           
SHEET    5   C 7 ASN A 273  LEU A 278 -1  O  LEU A 277   N  THR A 256           
SHEET    6   C 7 THR A 225  ARG A 230 -1  N  VAL A 227   O  VAL A 276           
SHEET    7   C 7 ASP A 216  PHE A 218 -1  N  PHE A 218   O  VAL A 226           
SHEET    1   D 5 LEU A 211  PRO A 213  0                                        
SHEET    2   D 5 VAL A 291  ALA A 293 -1  O  LEU A 292   N  LEU A 212           
SHEET    3   D 5 GLU A 241  VAL A 245 -1  N  GLU A 243   O  ALA A 293           
SHEET    4   D 5 GLN A 251  MET A 260 -1  O  GLN A 251   N  ILE A 244           
SHEET    5   D 5 LYS A 263  LEU A 265 -1  O  LEU A 265   N  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  O  GLY A 268   N  ILE A 236           
SHEET    1   F 6 GLN A 329  TYR A 331  0                                        
SHEET    2   F 6 ARG A 373  GLU A 378 -1  O  ARG A 377   N  GLN A 329           
SHEET    3   F 6 ARG A 381  VAL A 391 -1  O  VAL A 383   N  ILE A 376           
SHEET    4   F 6 LYS A 299  ILE A 310 -1  N  GLU A 305   O  LYS A 390           
SHEET    5   F 6 ASN A 355  MET A 368 -1  O  MET A 358   N  SER A 306           
SHEET    6   F 6 GLY A 339  GLU A 342 -1  N  THR A 340   O  THR A 361           
SHEET    1   G 2 PHE A 322  PHE A 323  0                                        
SHEET    2   G 2 MET A 349  VAL A 350 -1  O  VAL A 350   N  PHE A 322           
LINK        MG    MG A 998                 OG1 THR A  25     1555   1555  2.14  
LINK        MG    MG A 998                 O2B GDP A 999     1555   1555  2.46  
SITE     1 AC1  4 THR A  25  ASP A  50  CYS A  81  GDP A 999                    
SITE     1 AC2 17 HIS A  19  VAL A  20  ASP A  21  HIS A  22                    
SITE     2 AC2 17 GLY A  23  LYS A  24  THR A  25  THR A  26                    
SITE     3 AC2 17 PHE A  46  ASN A 135  LYS A 136  ASP A 138                    
SITE     4 AC2 17 MET A 139  SER A 173  ALA A 174  LEU A 175                    
SITE     5 AC2 17  MG A 998                                                     
CRYST1   69.550   69.550  169.440  90.00  90.00 120.00 P 31 2 1      6          
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      0.014378  0.008301  0.000000        0.00000                         
SCALE2      0.000000  0.016602  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.005902        0.00000                         
(ATOM LINES ARE NOT SHOWN.)
END                                                                             
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