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Database: PDB
Entry: 3U2Q
LinkDB: 3U2Q
Original site: 3U2Q 
HEADER    TRANSLATION FACTOR/ANTIBIOTIC           04-OCT-11   3U2Q              
TITLE     EF-TU (ESCHERICHIA COLI) IN COMPLEX WITH NVP-LFF571                   
COMPND    MOL_ID: 1;                                                            
COMPND   2 MOLECULE: ELONGATION FACTOR TU 1;                                    
COMPND   3 CHAIN: A;                                                            
COMPND   4 SYNONYM: EF-TU 1, P-43;                                              
COMPND   5 ENGINEERED: YES;                                                     
COMPND   6 MOL_ID: 2;                                                           
COMPND   7 MOLECULE: NVP-LFF571;                                                
COMPND   8 CHAIN: B;                                                            
COMPND   9 ENGINEERED: YES                                                      
SOURCE    MOL_ID: 1;                                                            
SOURCE   2 ORGANISM_SCIENTIFIC: ESCHERICHIA COLI;                               
SOURCE   3 ORGANISM_TAXID: 83333;                                               
SOURCE   4 STRAIN: K12;                                                         
SOURCE   5 GENE: TUFA, B3339, JW3301;                                           
SOURCE   6 EXPRESSION_SYSTEM: ESCHERICHIA COLI;                                 
SOURCE   7 EXPRESSION_SYSTEM_TAXID: 562;                                        
SOURCE   8 MOL_ID: 2;                                                           
SOURCE   9 SYNTHETIC: YES                                                       
KEYWDS    TRANSLATION FACTOR-ANTIBIOTIC COMPLEX                                 
EXPDTA    X-RAY DIFFRACTION                                                     
AUTHOR    D.J.PALESTRANT                                                        
REVDAT   1   02-MAY-12 3U2Q    0                                                
JRNL        AUTH   M.J.LAMARCHE,J.A.LEEDS,A.AMARAL,J.T.BREWER,S.M.BUSHELL,      
JRNL        AUTH 2 G.DENG,J.M.DEWHURST,J.DING,J.DZINK-FOX,G.GAMBER,A.JAIN,      
JRNL        AUTH 3 K.LEE,L.LEE,T.LISTER,D.MCKENNEY,S.MULLIN,C.OSBORNE,          
JRNL        AUTH 4 D.PALESTRANT,M.A.PATANE,E.M.RANN,M.SACHDEVA,J.SHAO,          
JRNL        AUTH 5 S.TIAMFOOK,A.TRZASKO,L.WHITEHEAD,A.YIFRU,D.YU,W.YAN,Q.ZHU    
JRNL        TITL   DISCOVERY OF LFF571: AN INVESTIGATIONAL AGENT FOR            
JRNL        TITL 2 CLOSTRIDIUM DIFFICILE INFECTION.                             
JRNL        REF    J.MED.CHEM.                   V.  55  2376 2012              
JRNL        REFN                   ISSN 0022-2623                               
JRNL        PMID   22315981                                                     
JRNL        DOI    10.1021/JM201685H                                            
REMARK   2                                                                      
REMARK   2 RESOLUTION.    2.70 ANGSTROMS.                                       
REMARK   3                                                                      
REMARK   3 REFINEMENT.                                                          
REMARK   3   PROGRAM     : CNX 2002                                             
REMARK   3   AUTHORS     : BRUNGER,ADAMS,CLORE,DELANO,GROS,GROSSE-              
REMARK   3               : KUNSTLEVE,JIANG,KUSZEWSKI,NILGES,PANNU,              
REMARK   3               : READ,RICE,SIMONSON,WARREN,ACCELRYS                   
REMARK   3               : SOFTWARE INC.(BADGER,BERARD,KUMAR,SZALMA,            
REMARK   3               : YIP,DZAKULA)                                         
REMARK   3                                                                      
REMARK   3  DATA USED IN REFINEMENT.                                            
REMARK   3   RESOLUTION RANGE HIGH (ANGSTROMS) : 2.70                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 39.02                          
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)   (%) : NULL                           
REMARK   3   NUMBER OF REFLECTIONS             : 11365                          
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) : NULL                            
REMARK   3   R VALUE            (WORKING SET) : 0.233                           
REMARK   3   FREE R VALUE                     : 0.315                           
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : NULL                            
REMARK   3   FREE R VALUE TEST SET COUNT      : 582                             
REMARK   3   ESTIMATED ERROR OF FREE R VALUE  : NULL                            
REMARK   3                                                                      
REMARK   3  FIT/AGREEMENT OF MODEL WITH ALL DATA.                               
REMARK   3   R VALUE     (WORKING + TEST SET, NO CUTOFF) : NULL                 
REMARK   3   R VALUE            (WORKING SET, NO CUTOFF) : NULL                 
REMARK   3   FREE R VALUE                    (NO CUTOFF) : NULL                 
REMARK   3   FREE R VALUE TEST SET SIZE   (%, NO CUTOFF) : NULL                 
REMARK   3   FREE R VALUE TEST SET COUNT     (NO CUTOFF) : NULL                 
REMARK   3   ESTIMATED ERROR OF FREE R VALUE (NO CUTOFF) : NULL                 
REMARK   3   TOTAL NUMBER OF REFLECTIONS     (NO CUTOFF) : 11365                
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            : 3058                                    
REMARK   3   NUCLEIC ACID ATOMS       : 0                                       
REMARK   3   HETEROGEN ATOMS          : 29                                      
REMARK   3   SOLVENT ATOMS            : 89                                      
REMARK   3                                                                      
REMARK   3  B VALUES.                                                           
REMARK   3   FROM WILSON PLOT           (A**2) : NULL                           
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : NULL                           
REMARK   3   OVERALL ANISOTROPIC B VALUE.                                       
REMARK   3    B11 (A**2) : NULL                                                 
REMARK   3    B22 (A**2) : NULL                                                 
REMARK   3    B33 (A**2) : NULL                                                 
REMARK   3    B12 (A**2) : NULL                                                 
REMARK   3    B13 (A**2) : NULL                                                 
REMARK   3    B23 (A**2) : NULL                                                 
REMARK   3                                                                      
REMARK   3  ESTIMATED COORDINATE ERROR.                                         
REMARK   3   ESD FROM LUZZATI PLOT        (A) : NULL                            
REMARK   3   ESD FROM SIGMAA              (A) : NULL                            
REMARK   3   LOW RESOLUTION CUTOFF        (A) : NULL                            
REMARK   3                                                                      
REMARK   3  CROSS-VALIDATED ESTIMATED COORDINATE ERROR.                         
REMARK   3   ESD FROM C-V LUZZATI PLOT    (A) : NULL                            
REMARK   3   ESD FROM C-V SIGMAA          (A) : NULL                            
REMARK   3                                                                      
REMARK   3  RMS DEVIATIONS FROM IDEAL VALUES.                                   
REMARK   3   BOND LENGTHS                 (A) : 0.007                           
REMARK   3   BOND ANGLES            (DEGREES) : 1.40                            
REMARK   3   DIHEDRAL ANGLES        (DEGREES) : NULL                            
REMARK   3   IMPROPER ANGLES        (DEGREES) : NULL                            
REMARK   3                                                                      
REMARK   3  ISOTROPIC THERMAL MODEL : OVERALL                                   
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        : NULL                                                 
REMARK   3                                                                      
REMARK   3  NCS MODEL : NULL                                                    
REMARK   3                                                                      
REMARK   3                                                                      
REMARK   3  OTHER REFINEMENT REMARKS: NULL                                      
REMARK   4                                                                      
REMARK   4 3U2Q COMPLIES WITH FORMAT V. 3.30, 13-JUL-11                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 04-JAN-12.                  
REMARK 100 THE RCSB ID CODE IS RCSB068231.                                      
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : 21-MAR-08                          
REMARK 200  TEMPERATURE           (KELVIN) : 100.0                              
REMARK 200  PH                             : 8.23                               
REMARK 200  NUMBER OF CRYSTALS USED        : 1                                  
REMARK 200                                                                      
REMARK 200  SYNCHROTRON              (Y/N) : Y                                  
REMARK 200  RADIATION SOURCE               : APS                                
REMARK 200  BEAMLINE                       : 17-ID                              
REMARK 200  X-RAY GENERATOR MODEL          : NULL                               
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M                                  
REMARK 200  WAVELENGTH OR RANGE        (A) : 1.00000                            
REMARK 200  MONOCHROMATOR                  : SI 111                             
REMARK 200  OPTICS                         : NULL                               
REMARK 200                                                                      
REMARK 200  DETECTOR TYPE                  : CCD                                
REMARK 200  DETECTOR MANUFACTURER          : ADSC QUANTUM 210                   
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : HKL-2000                           
REMARK 200  DATA SCALING SOFTWARE          : HKL-2000                           
REMARK 200                                                                      
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 11365                              
REMARK 200  RESOLUTION RANGE HIGH      (A) : 2.700                              
REMARK 200  RESOLUTION RANGE LOW       (A) : 50.000                             
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : 2.000                              
REMARK 200                                                                      
REMARK 200 OVERALL.                                                             
REMARK 200  COMPLETENESS FOR RANGE     (%) : 93.5                               
REMARK 200  DATA REDUNDANCY                : 6.200                              
REMARK 200  R MERGE                    (I) : 0.09900                            
REMARK 200  R SYM                      (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR THE DATA SET  : 9.7000                             
REMARK 200                                                                      
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.                                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.70                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 2.80                     
REMARK 200  COMPLETENESS FOR SHELL     (%) : 77.2                               
REMARK 200  DATA REDUNDANCY IN SHELL       : 4.00                               
REMARK 200  R MERGE FOR SHELL          (I) : 0.41600                            
REMARK 200  R SYM FOR SHELL            (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR SHELL         : 2.790                              
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                                       
REMARK 200                                                                      
REMARK 200 REMARK: NULL                                                         
REMARK 280                                                                      
REMARK 280 CRYSTAL                                                              
REMARK 280 SOLVENT CONTENT, VS   (%): 46.56                                     
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.30                     
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: 50MM TRIS PH8, 50MM NACL , PH 8.23,      
REMARK 280  VAPOR DIFFUSION, SITTING DROP, TEMPERATURE 293K                     
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       41.65150            
REMARK 290   SMTRY2   3  0.000000  1.000000  0.000000       66.23650            
REMARK 290   SMTRY3   3  0.000000  0.000000 -1.000000        0.00000            
REMARK 290   SMTRY1   4  1.000000  0.000000  0.000000       41.65150            
REMARK 290   SMTRY2   4  0.000000 -1.000000  0.000000       66.23650            
REMARK 290   SMTRY3   4  0.000000  0.000000 -1.000000        0.00000            
REMARK 290                                                                      
REMARK 290 REMARK: NULL                                                         
REMARK 300                                                                      
REMARK 300 BIOMOLECULE: 1                                                       
REMARK 300 SEE REMARK 350 FOR THE AUTHOR PROVIDED AND/OR PROGRAM                
REMARK 300 GENERATED ASSEMBLY INFORMATION FOR THE STRUCTURE IN                  
REMARK 300 THIS ENTRY. THE REMARK MAY ALSO PROVIDE INFORMATION ON               
REMARK 300 BURIED SURFACE AREA.                                                 
REMARK 350                                                                      
REMARK 350 COORDINATES FOR A COMPLETE MULTIMER REPRESENTING THE KNOWN           
REMARK 350 BIOLOGICALLY SIGNIFICANT OLIGOMERIZATION STATE OF THE                
REMARK 350 MOLECULE CAN BE GENERATED BY APPLYING BIOMT TRANSFORMATIONS          
REMARK 350 GIVEN BELOW.  BOTH NON-CRYSTALLOGRAPHIC AND                          
REMARK 350 CRYSTALLOGRAPHIC OPERATIONS ARE GIVEN.                               
REMARK 350                                                                      
REMARK 350 BIOMOLECULE: 1                                                       
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: DIMERIC                           
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: DIMERIC                    
REMARK 350 SOFTWARE USED: PISA                                                  
REMARK 350 TOTAL BURIED SURFACE AREA: 2310 ANGSTROM**2                          
REMARK 350 SURFACE AREA OF THE COMPLEX: 17620 ANGSTROM**2                       
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -22.0 KCAL/MOL                        
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, 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 375                                                                      
REMARK 375 SPECIAL POSITION                                                     
REMARK 375 THE FOLLOWING ATOMS ARE FOUND TO BE WITHIN 0.15 ANGSTROMS            
REMARK 375 OF A SYMMETRY RELATED ATOM AND ARE ASSUMED TO BE ON SPECIAL          
REMARK 375 POSITIONS.                                                           
REMARK 375                                                                      
REMARK 375 ATOM RES CSSEQI                                                      
REMARK 375      HOH A 443  LIES ON A SPECIAL POSITION.                          
REMARK 465                                                                      
REMARK 465 MISSING RESIDUES                                                     
REMARK 465 THE FOLLOWING RESIDUES WERE NOT LOCATED IN THE                       
REMARK 465 EXPERIMENT. (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN               
REMARK 465 IDENTIFIER; SSSEQ=SEQUENCE NUMBER; I=INSERTION CODE.)                
REMARK 465                                                                      
REMARK 465   M RES C SSSEQI                                                     
REMARK 465     MET A     0                                                      
REMARK 465     ALA A     1                                                      
REMARK 465     LYS A     2                                                      
REMARK 465     GLU A     3                                                      
REMARK 465     LYS A     4                                                      
REMARK 465     PHE A     5                                                      
REMARK 465     ARG A    58                                                      
REMARK 465     GLY A    59                                                      
REMARK 465     ILE A    60                                                      
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   7      -78.77    115.10                                   
REMARK 500    PRO A  10      128.08    -36.88                                   
REMARK 500    ASP A  21       39.67     35.36                                   
REMARK 500    THR A  33      -81.43    -62.45                                   
REMARK 500    LYS A  37      -79.03    -59.15                                   
REMARK 500    PHE A  46      -74.47    -36.37                                   
REMARK 500    ALA A  52       74.13   -117.30                                   
REMARK 500    PRO A  53     -135.67    -72.14                                   
REMARK 500    GLU A  54     -161.23    -20.21                                   
REMARK 500    GLU A  55     -171.49    164.03                                   
REMARK 500    LYS A  56     -103.24    177.77                                   
REMARK 500    PRO A 111      109.96    -52.02                                   
REMARK 500    VAL A 127      109.15    -46.93                                   
REMARK 500    LEU A 134       99.13    -62.91                                   
REMARK 500    CYS A 137        2.45    -68.50                                   
REMARK 500    LEU A 146        3.73    -63.31                                   
REMARK 500    PRO A 163       68.69    -59.03                                   
REMARK 500    SER A 173       99.12   -160.58                                   
REMARK 500    ALA A 174        1.22    -58.10                                   
REMARK 500    LEU A 175      -62.22   -103.14                                   
REMARK 500    ASP A 181       76.57    -63.16                                   
REMARK 500    ALA A 182      -37.81    -35.62                                   
REMARK 500    ALA A 205      -48.01    -21.44                                   
REMARK 500    GLU A 215      -68.01   -106.64                                   
REMARK 500    SER A 221      -62.95    -16.47                                   
REMARK 500    ILE A 247      -58.03     58.78                                   
REMARK 500    SER A 253      150.30    175.14                                   
REMARK 500    ARG A 262       -7.42     86.64                                   
REMARK 500    ALA A 270      130.86    -35.77                                   
REMARK 500    PRO A 328     -166.88   -100.81                                   
REMARK 500    ARG A 333      -71.33     51.53                                   
REMARK 500    LYS A 390      116.53   -168.14                                   
REMARK 500    MEN B   3     -167.62   -118.89                                   
REMARK 500    VAL B   5      -50.94   -145.51                                   
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 503  MG                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 HOH A 433   O                                                      
REMARK 620 2 THR A  25   OG1 144.9                                              
REMARK 620 3 GDP A 501   O2B 111.9  85.9                                        
REMARK 620 4 HOH A 405   O    86.8  58.7 124.7                                  
REMARK 620 5 GDP A 501   O2A 114.9  95.8  85.6 134.3                            
REMARK 620 6 GDP A 501   O1B  58.9 142.6  57.5 135.0  89.0                      
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 GDP A 501                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MG A 503                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR CHAIN B OF NVP-LFF571             
REMARK 900                                                                      
REMARK 900 RELATED ENTRIES                                                      
REMARK 900 RELATED ID: 3U6K   RELATED DB: PDB                                   
REMARK 900 EF-TU (ESCHERICHIA COLI) IN COMPLEX WITH NVP-LDK733                  
REMARK 900 RELATED ID: 3U6B   RELATED DB: PDB                                   
REMARK 900 EF-TU (ESCHERICHIA COLI) IN COMPLEX WITH NVP-LDI028                  
REMARK 999                                                                      
REMARK 999 SEQUENCE                                                             
REMARK 999 THE GE2270A-LIKE ANTIBIOTIC COMPOUND IS REPRESENTED AS POLYMER. THE  
REMARK 999 FIRST 11 RESIDUES OF THE ANTIBIOTIC ARE IDENTICAL TO THE             
REMARK 999 CORRESPONDING RESIDUES IN GE2270A, WITH ONLY THE LAST RESIDUE        
REMARK 999 MODIFIED.                                                            
DBREF  3U2Q A    2   393  UNP    P0CE47   EFTU1_ECOLI      3    394             
DBREF  3U2Q B    1    12  UNP    Q7M0J8   THCL_PLARO       1     12             
SEQADV 3U2Q MET A    0  UNP  P0CE47              EXPRESSION TAG                 
SEQADV 3U2Q ALA A    1  UNP  P0CE47              EXPRESSION TAG                 
SEQADV 3U2Q 7BB B   12  UNP  Q7M0J8    CYS    12 SEE REMARK 999                 
SEQRES   1 A  394  MET ALA LYS GLU LYS PHE GLU ARG THR LYS PRO HIS VAL          
SEQRES   2 A  394  ASN VAL GLY THR ILE GLY HIS VAL ASP HIS GLY LYS THR          
SEQRES   3 A  394  THR LEU THR ALA ALA ILE THR THR VAL LEU ALA LYS THR          
SEQRES   4 A  394  TYR GLY GLY ALA ALA ARG ALA PHE ASP GLN ILE ASP ASN          
SEQRES   5 A  394  ALA PRO GLU GLU LYS ALA ARG GLY ILE THR ILE ASN THR          
SEQRES   6 A  394  SER HIS VAL GLU TYR ASP THR PRO THR ARG HIS TYR ALA          
SEQRES   7 A  394  HIS VAL ASP CYS PRO GLY HIS ALA ASP TYR VAL LYS ASN          
SEQRES   8 A  394  MET ILE THR GLY ALA ALA GLN MET ASP GLY ALA ILE LEU          
SEQRES   9 A  394  VAL VAL ALA ALA THR ASP GLY PRO MET PRO GLN THR ARG          
SEQRES  10 A  394  GLU HIS ILE LEU LEU GLY ARG GLN VAL GLY VAL PRO TYR          
SEQRES  11 A  394  ILE ILE VAL PHE LEU ASN LYS CYS ASP MET VAL ASP ASP          
SEQRES  12 A  394  GLU GLU LEU LEU GLU LEU VAL GLU MET GLU VAL ARG GLU          
SEQRES  13 A  394  LEU LEU SER GLN TYR ASP PHE PRO GLY ASP ASP THR PRO          
SEQRES  14 A  394  ILE VAL ARG GLY SER ALA LEU LYS ALA LEU GLU GLY ASP          
SEQRES  15 A  394  ALA GLU TRP GLU ALA LYS ILE LEU GLU LEU ALA GLY PHE          
SEQRES  16 A  394  LEU ASP SER TYR ILE PRO GLU PRO GLU ARG ALA ILE ASP          
SEQRES  17 A  394  LYS PRO PHE LEU LEU PRO ILE GLU ASP VAL PHE SER ILE          
SEQRES  18 A  394  SER GLY ARG GLY THR VAL VAL THR GLY ARG VAL GLU ARG          
SEQRES  19 A  394  GLY ILE ILE LYS VAL GLY GLU GLU VAL GLU ILE VAL GLY          
SEQRES  20 A  394  ILE LYS GLU THR GLN LYS SER THR CYS THR GLY VAL GLU          
SEQRES  21 A  394  MET PHE ARG LYS LEU LEU ASP GLU GLY ARG ALA GLY GLU          
SEQRES  22 A  394  ASN VAL GLY VAL LEU LEU ARG GLY ILE LYS ARG GLU GLU          
SEQRES  23 A  394  ILE GLU ARG GLY GLN VAL LEU ALA LYS PRO GLY THR ILE          
SEQRES  24 A  394  LYS PRO HIS THR LYS PHE GLU SER GLU VAL TYR ILE LEU          
SEQRES  25 A  394  SER LYS ASP GLU GLY GLY ARG HIS THR PRO PHE PHE LYS          
SEQRES  26 A  394  GLY TYR ARG PRO GLN PHE TYR PHE ARG THR THR ASP VAL          
SEQRES  27 A  394  THR GLY THR ILE GLU LEU PRO GLU GLY VAL GLU MET VAL          
SEQRES  28 A  394  MET PRO GLY ASP ASN ILE LYS MET VAL VAL THR LEU ILE          
SEQRES  29 A  394  HIS PRO ILE ALA MET ASP ASP GLY LEU ARG PHE ALA ILE          
SEQRES  30 A  394  ARG GLU GLY GLY ARG THR VAL GLY ALA GLY VAL VAL ALA          
SEQRES  31 A  394  LYS VAL LEU GLY                                              
SEQRES   1 B   12  SER BB9 MEN BB6 VAL BB7 GLY BB8 BB9 BB9 MH6 7BB              
MODRES 3U2Q BB9 B    2  CYS                                                     
MODRES 3U2Q MEN B    3  ASN  N-METHYL ASPARAGINE                                
MODRES 3U2Q BB6 B    4  CYS  (2Z)-2-AMINO-3-SULFANYLBUT-2-ENOIC ACID            
MODRES 3U2Q BB7 B    6  CYS                                                     
MODRES 3U2Q BB8 B    8  PHE  (2S,3S)-BETA-HYDROXY-PHENYLALANINE                 
MODRES 3U2Q BB9 B    9  CYS                                                     
MODRES 3U2Q BB9 B   10  CYS                                                     
MODRES 3U2Q MH6 B   11  SER  3-HYDROXY-2-IMINOPROPANOIC ACID                    
HET    BB9  B   2       6                                                       
HET    MEN  B   3       8                                                       
HET    BB6  B   4       7                                                       
HET    BB7  B   6       9                                                       
HET    BB8  B   8      11                                                       
HET    BB9  B   9       5                                                       
HET    BB9  B  10       5                                                       
HET    MH6  B  11       4                                                       
HET    7BB  B  12      24                                                       
HET    GDP  A 501      28                                                       
HET     MG  A 503       1                                                       
HETNAM     BB9 (2Z)-2-AMINO-3-SULFANYLPROP-2-ENOIC ACID                         
HETNAM     MEN N-METHYL ASPARAGINE                                              
HETNAM     BB6 (2Z)-2-AMINO-3-SULFANYLBUT-2-ENOIC ACID                          
HETNAM     BB7 (2Z)-2-AMINO-4-METHOXY-3-SULFANYLBUT-2-ENOIC ACID                
HETNAM     BB8 (2S,3S)-BETA-HYDROXY-PHENYLALANINE                               
HETNAM     MH6 3-HYDROXY-2-IMINOPROPANOIC ACID                                  
HETNAM     7BB TRANS-4-({[(E)-1-AMINO-2-SULFANYLETHENYL](4-                     
HETNAM   2 7BB  CARBOXYBUTYL)CARBAMOYL}OXY)CYCLOHEXANECARBOXYLIC ACID           
HETNAM     GDP GUANOSINE-5'-DIPHOSPHATE                                         
HETNAM      MG MAGNESIUM ION                                                    
HETSYN     BB8 BETA-HYDROXY-PHENYLALANINE, THREO-BETA-HYDROXY-L-                
HETSYN   2 BB8  PHENYLALANINE, (BETAS)-BETA-HYDROXY-L-PHENYLALANINE,            
HETSYN   3 BB8  L-THREO-3-PHENYLSERINE, L-THREO-BETA-PHENYLSERINE, 3-           
HETSYN   4 BB8  HYDROXY-L-PHENYLALANINE                                         
FORMUL   2  BB9    3(C3 H5 N O2 S)                                              
FORMUL   2  MEN    C5 H10 N2 O3                                                 
FORMUL   2  BB6    C4 H7 N O2 S                                                 
FORMUL   2  BB7    C5 H9 N O3 S                                                 
FORMUL   2  BB8    C9 H11 N O3                                                  
FORMUL   2  MH6    C3 H5 N O3                                                   
FORMUL   2  7BB    C15 H24 N2 O6 S                                              
FORMUL   3  GDP    C10 H15 N5 O11 P2                                            
FORMUL   4   MG    MG 2+                                                        
FORMUL   5  HOH   *89(H2 O)                                                     
HELIX    1   1 GLY A   23  GLY A   40  1                                  18    
HELIX    2   2 ALA A   45  ILE A   49  5                                   5    
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 GLU A  147  TYR A  160  1                                  14    
HELIX    6   6 LEU A  175  GLY A  180  1                                   6    
HELIX    7   7 ASP A  181  ILE A  199  1                                  19    
HELIX    8   8 ARG A  204  LYS A  208  5                                   5    
HELIX    9   9 LYS A  282  ILE A  286  5                                   5    
HELIX   10  10 SER A  312  GLY A  316  5                                   5    
SHEET    1   A 6 SER A  65  THR A  71  0                                        
SHEET    2   A 6 ARG A  74  ASP A  80 -1  O  TYR A  76   N  TYR A  69           
SHEET    3   A 6 HIS A  11  ILE A  17  1  N  VAL A  14   O  ALA A  77           
SHEET    4   A 6 ALA A 101  ALA A 106  1  O  VAL A 104   N  ILE A  17           
SHEET    5   A 6 ILE A 130  ASN A 135  1  O  ILE A 131   N  ALA A 101           
SHEET    6   A 6 ILE A 169  ARG A 171  1  O  VAL A 170   N  VAL A 132           
SHEET    1   B 7 LEU A 211  PRO A 213  0                                        
SHEET    2   B 7 VAL A 291  ALA A 293 -1  O  LEU A 292   N  LEU A 212           
SHEET    3   B 7 GLU A 241  VAL A 245 -1  N  GLU A 243   O  ALA A 293           
SHEET    4   B 7 GLN A 251  MET A 260 -1  O  SER A 253   N  VAL A 242           
SHEET    5   B 7 ASN A 273  ARG A 279 -1  O  LEU A 277   N  THR A 256           
SHEET    6   B 7 GLY A 224  ARG A 230 -1  N  THR A 225   O  LEU A 278           
SHEET    7   B 7 VAL A 217  ILE A 220 -1  N  ILE A 220   O  GLY A 224           
SHEET    1   C 5 LEU A 211  PRO A 213  0                                        
SHEET    2   C 5 VAL A 291  ALA A 293 -1  O  LEU A 292   N  LEU A 212           
SHEET    3   C 5 GLU A 241  VAL A 245 -1  N  GLU A 243   O  ALA A 293           
SHEET    4   C 5 GLN A 251  MET A 260 -1  O  SER A 253   N  VAL A 242           
SHEET    5   C 5 LYS A 263  LEU A 265 -1  O  LEU A 265   N  VAL A 258           
SHEET    1   D 2 ILE A 235  LYS A 237  0                                        
SHEET    2   D 2 GLU A 267  ARG A 269 -1  O  GLY A 268   N  ILE A 236           
SHEET    1   E 7 LYS A 299  ILE A 310  0                                        
SHEET    2   E 7 ASN A 355  MET A 368 -1  O  MET A 358   N  SER A 306           
SHEET    3   E 7 THR A 335  GLU A 342 -1  N  THR A 338   O  ILE A 363           
SHEET    4   E 7 GLN A 329  PHE A 332 -1  N  PHE A 330   O  VAL A 337           
SHEET    5   E 7 ARG A 373  GLU A 378 -1  O  ALA A 375   N  TYR A 331           
SHEET    6   E 7 ARG A 381  VAL A 391 -1  O  GLY A 384   N  ILE A 376           
SHEET    7   E 7 LYS A 299  ILE A 310 -1  N  TYR A 309   O  ALA A 385           
SHEET    1   F 2 PHE A 322  PHE A 323  0                                        
SHEET    2   F 2 MET A 349  VAL A 350 -1  O  VAL A 350   N  PHE A 322           
LINK         C   SER B   1                 N   BB9 B   2     1555   1555  1.33  
LINK         C   BB9 B   2                 N   MEN B   3     1555   1555  1.32  
LINK         C   BB6 B   4                 N   VAL B   5     1555   1555  1.38  
LINK         C   BB7 B   6                 N   GLY B   7     1555   1555  1.34  
LINK         C   BB8 B   8                 N   BB9 B   9     1555   1555  1.31  
LINK         C   BB9 B   9                 N   BB9 B  10     1555   1555  1.32  
LINK         C   BB9 B  10                 N   MH6 B  11     1555   1555  1.33  
LINK        MG    MG A 503                 O   HOH A 433     1555   1555  2.43  
LINK         OG1 THR A  25                MG    MG A 503     1555   1555  2.49  
LINK         O2B GDP A 501                MG    MG A 503     1555   1555  2.51  
LINK        MG    MG A 503                 O   HOH A 405     1555   1555  2.57  
LINK         O2A GDP A 501                MG    MG A 503     1555   1555  2.71  
LINK         O1B GDP A 501                MG    MG A 503     1555   1555  2.72  
LINK         CB  SER B   1                 CB  MH6 B  11     1555   1555  1.43  
LINK         CA  SER B   1                 C   BB9 B  10     1555   1555  1.44  
LINK         C   SER B   1                 SG  BB9 B   2     1555   1555  1.72  
LINK         C   BB9 B   9                 SG  BB9 B  10     1555   1555  1.74  
LINK         C   MEN B   3                 SG  BB6 B   4     1555   1555  1.74  
LINK         C   MH6 B  11                 SG  7BB B  12     1555   1555  1.76  
LINK         C   BB8 B   8                 SG  BB9 B   9     1555   1555  1.78  
LINK         C   VAL B   5                 SG  BB7 B   6     1555   1555  1.79  
LINK         C   MH6 B  11                 N   7BB B  12     1555   1555  1.31  
SITE     1 AC1 18 HIS A  19  VAL A  20  ASP A  21  HIS A  22                    
SITE     2 AC1 18 GLY A  23  LYS A  24  THR A  25  THR A  26                    
SITE     3 AC1 18 PHE A  46  ASP A  50  ASN A 135  LYS A 136                    
SITE     4 AC1 18 ASP A 138  MET A 139  SER A 173  LEU A 175                    
SITE     5 AC1 18 HOH A 433   MG A 503                                          
SITE     1 AC2  5 THR A  25  ASP A  50  HOH A 405  HOH A 433                    
SITE     2 AC2  5 GDP A 501                                                     
SITE     1 AC3 25 THR A  38  TYR A  39  PRO A  72  GLU A 215                    
SITE     2 AC3 25 ASP A 216  PHE A 218  THR A 228  THR A 256                    
SITE     3 AC3 25 GLY A 257  GLU A 259  PHE A 261  ARG A 262                    
SITE     4 AC3 25 ASN A 273  VAL A 274  GLY A 275  LEU A 277                    
SITE     5 AC3 25 LYS A 303  HIS A 319  THR A 320  PRO A 321                    
SITE     6 AC3 25 PHE A 323  HOH A 407  HOH B  13  HOH B  18                    
SITE     7 AC3 25 HOH B  87                                                     
CRYST1   83.303  132.473   37.433  90.00  90.00  90.00 P 21 21 2     4          
ORIGX1      1.000000  0.000000  0.000000        0.00000                         
ORIGX2      0.000000  1.000000  0.000000        0.00000                         
ORIGX3      0.000000  0.000000  1.000000        0.00000                         
SCALE1      0.012004  0.000000  0.000000        0.00000                         
SCALE2      0.000000  0.007549  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.026714        0.00000                         
(ATOM LINES ARE NOT SHOWN.)
END                                                                             
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