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Database: PDB
Entry: 5JBQ
LinkDB: 5JBQ
Original site: 5JBQ 
HEADER    RNA BINDING PROTEIN/ANTIMICROBIAL       13-APR-16   5JBQ              
TITLE     EF-TU (ESCHERICHIA COLI) IN COMPLEX WITH THIOMURACIN ANALOG           
CAVEAT     5JBQ    SER B 1 HAS WRONG CHIRALITY AT ATOM CA                       
COMPND    MOL_ID: 1;                                                            
COMPND   2 MOLECULE: ELONGATION FACTOR TU 1;                                    
COMPND   3 CHAIN: A;                                                            
COMPND   4 SYNONYM: EF-TU 1,BACTERIOPHAGE Q BETA RNA-DIRECTED RNA POLYMERASE    
COMPND   5 SUBUNIT III,P-43;                                                    
COMPND   6 ENGINEERED: YES;                                                     
COMPND   7 MOL_ID: 2;                                                           
COMPND   8 MOLECULE: THIOMURACIN ANALOG;                                        
COMPND   9 CHAIN: B;                                                            
COMPND  10 ENGINEERED: YES                                                      
SOURCE    MOL_ID: 1;                                                            
SOURCE   2 ORGANISM_SCIENTIFIC: ESCHERICHIA COLI (STRAIN K12);                  
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;                                                      
SOURCE  10 ORGANISM_SCIENTIFIC: SYNTHETIC CONSTRUCT;                            
SOURCE  11 ORGANISM_TAXID: 32630                                                
KEYWDS    NATURAL PRODUCT INHIBITOR, ELONGATION FACTOR, RNA BINDING PROTEIN-    
KEYWDS   2 ANTIMICROBIAL COMPLEX                                                
EXPDTA    X-RAY DIFFRACTION                                                     
AUTHOR    D.PALESTRANT,T.STAMS                                                  
REVDAT   2   10-AUG-16 5JBQ    1       JRNL                                     
REVDAT   1   13-JUL-16 5JBQ    0                                                
JRNL        AUTH   M.J.LAMARCHE,J.A.LEEDS,J.BREWER,K.DEAN,J.DING,J.DZINK-FOX,   
JRNL        AUTH 2 G.GAMBER,A.JAIN,R.KERRIGAN,P.KRASTEL,K.LEE,F.LOMBARDO,       
JRNL        AUTH 3 D.MCKENNEY,G.NECKERMANN,C.OSBORNE,D.PALESTRANT,M.A.PATANE,   
JRNL        AUTH 4 E.M.RANN,Z.ROBINSON,E.SCHMITT,T.STAMS,S.TIAMFOOK,D.YU,       
JRNL        AUTH 5 L.WHITEHEAD                                                  
JRNL        TITL   ANTIBACTERIAL AND SOLUBILITY OPTIMIZATION OF THIOMURACIN A.  
JRNL        REF    J.MED.CHEM.                   V.  59  6920 2016              
JRNL        REFN                   ISSN 0022-2623                               
JRNL        PMID   27355833                                                     
JRNL        DOI    10.1021/ACS.JMEDCHEM.6B00726                                 
REMARK   2                                                                      
REMARK   2 RESOLUTION.    2.01 ANGSTROMS.                                       
REMARK   3                                                                      
REMARK   3 REFINEMENT.                                                          
REMARK   3   PROGRAM     : BUSTER 2.11.6                                        
REMARK   3   AUTHORS     : BRICOGNE,BLANC,BRANDL,FLENSBURG,KELLER,              
REMARK   3               : PACIOREK,ROVERSI,SHARFF,SMART,VONRHEIN,              
REMARK   3               : WOMACK,MATTHEWS,TEN EYCK,TRONRUD                     
REMARK   3                                                                      
REMARK   3  DATA USED IN REFINEMENT.                                            
REMARK   3   RESOLUTION RANGE HIGH (ANGSTROMS) : 2.01                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 42.69                          
REMARK   3   DATA CUTOFF            (SIGMA(F)) : 0.000                          
REMARK   3   COMPLETENESS FOR RANGE        (%) : 98.6                           
REMARK   3   NUMBER OF REFLECTIONS             : 30901                          
REMARK   3                                                                      
REMARK   3  FIT TO DATA USED IN REFINEMENT.                                     
REMARK   3   CROSS-VALIDATION METHOD           : THROUGHOUT                     
REMARK   3   FREE R VALUE TEST SET SELECTION   : RANDOM                         
REMARK   3   R VALUE     (WORKING + TEST SET)  : 0.207                          
REMARK   3   R VALUE            (WORKING SET)  : 0.205                          
REMARK   3   FREE R VALUE                      : 0.253                          
REMARK   3   FREE R VALUE TEST SET SIZE   (%)  : 4.880                          
REMARK   3   FREE R VALUE TEST SET COUNT       : 1507                           
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               : 16                       
REMARK   3   BIN RESOLUTION RANGE HIGH   (ANGSTROMS) : 2.01                     
REMARK   3   BIN RESOLUTION RANGE LOW    (ANGSTROMS) : 2.08                     
REMARK   3   BIN COMPLETENESS (WORKING+TEST)     (%) : 88.99                    
REMARK   3   REFLECTIONS IN BIN (WORKING + TEST SET) : 2515                     
REMARK   3   BIN R VALUE        (WORKING + TEST SET) : 0.2242                   
REMARK   3   REFLECTIONS IN BIN        (WORKING SET) : 2376                     
REMARK   3   BIN R VALUE               (WORKING SET) : 0.2235                   
REMARK   3   BIN FREE R VALUE                        : 0.2352                   
REMARK   3   BIN FREE R VALUE TEST SET SIZE      (%) : 5.53                     
REMARK   3   BIN FREE R VALUE TEST SET COUNT         : 139                      
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            : 3117                                    
REMARK   3   NUCLEIC ACID ATOMS       : 0                                       
REMARK   3   HETEROGEN ATOMS          : 35                                      
REMARK   3   SOLVENT ATOMS            : 224                                     
REMARK   3                                                                      
REMARK   3  B VALUES.                                                           
REMARK   3   FROM WILSON PLOT           (A**2) : 25.55                          
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : 27.36                          
REMARK   3   OVERALL ANISOTROPIC B VALUE.                                       
REMARK   3    B11 (A**2) : 5.39800                                              
REMARK   3    B22 (A**2) : -2.56400                                             
REMARK   3    B33 (A**2) : -2.83400                                             
REMARK   3    B12 (A**2) : 0.00000                                              
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) : 0.268               
REMARK   3   DPI (BLOW EQ-10) BASED ON R VALUE        (A) : 0.192               
REMARK   3   DPI (BLOW EQ-9) BASED ON FREE R VALUE    (A) : 0.172               
REMARK   3   DPI (CRUICKSHANK) BASED ON R VALUE       (A) : 0.181               
REMARK   3   DPI (CRUICKSHANK) BASED ON FREE R VALUE  (A) : 0.168               
REMARK   3                                                                      
REMARK   3   REFERENCES: BLOW, D. (2002) ACTA CRYST D58, 792-797                
REMARK   3               CRUICKSHANK, D.W.J. (1999) ACTA CRYST D55, 583-601     
REMARK   3                                                                      
REMARK   3 CORRELATION COEFFICIENTS.                                            
REMARK   3   CORRELATION COEFFICIENT FO-FC      : 0.927                         
REMARK   3   CORRELATION COEFFICIENT FO-FC FREE : 0.895                         
REMARK   3                                                                      
REMARK   3   NUMBER OF GEOMETRIC FUNCTION TERMS DEFINED : 15                    
REMARK   3   TERM                          COUNT    WEIGHT   FUNCTION.          
REMARK   3    BOND LENGTHS              : 3218   ; 2.000  ; HARMONIC            
REMARK   3    BOND ANGLES               : 4373   ; 2.000  ; HARMONIC            
REMARK   3    TORSION ANGLES            : 1136   ; 2.000  ; SINUSOIDAL          
REMARK   3    TRIGONAL CARBON PLANES    : 76     ; 2.000  ; HARMONIC            
REMARK   3    GENERAL PLANES            : 483    ; 5.000  ; HARMONIC            
REMARK   3    ISOTROPIC THERMAL FACTORS : 3218   ; 20.000 ; HARMONIC            
REMARK   3    BAD NON-BONDED CONTACTS   : 0      ; 5.000  ; SEMIHARMONIC        
REMARK   3    IMPROPER TORSIONS         : NULL   ; NULL   ; NULL                
REMARK   3    PSEUDOROTATION ANGLES     : NULL   ; NULL   ; NULL                
REMARK   3    CHIRAL IMPROPER TORSION   : 421    ; 5.000  ; SEMIHARMONIC        
REMARK   3    SUM OF OCCUPANCIES        : NULL   ; NULL   ; NULL                
REMARK   3    UTILITY DISTANCES         : NULL   ; NULL   ; NULL                
REMARK   3    UTILITY ANGLES            : NULL   ; NULL   ; NULL                
REMARK   3    UTILITY TORSION           : NULL   ; NULL   ; NULL                
REMARK   3    IDEAL-DIST CONTACT TERM   : 3744   ; 4.000  ; SEMIHARMONIC        
REMARK   3                                                                      
REMARK   3   RMS DEVIATIONS FROM IDEAL VALUES.                                  
REMARK   3    BOND LENGTHS                       (A) : 0.010                    
REMARK   3    BOND ANGLES                  (DEGREES) : 1.16                     
REMARK   3    PEPTIDE OMEGA TORSION ANGLES (DEGREES) : 3.58                     
REMARK   3    OTHER TORSION ANGLES         (DEGREES) : 18.96                    
REMARK   3                                                                      
REMARK   3  TLS DETAILS                                                         
REMARK   3   NUMBER OF TLS GROUPS  : NULL                                       
REMARK   3                                                                      
REMARK   3  OTHER REFINEMENT REMARKS: NULL                                      
REMARK   4                                                                      
REMARK   4 5JBQ COMPLIES WITH FORMAT V. 3.30, 13-JUL-11                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 03-JUN-16.                  
REMARK 100 THE DEPOSITION ID IS D_1000220314.                                   
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : 30-APR-07                          
REMARK 200  TEMPERATURE           (KELVIN) : 100.0                              
REMARK 200  PH                             : 8.2                                
REMARK 200  NUMBER OF CRYSTALS USED        : 1                                  
REMARK 200                                                                      
REMARK 200  SYNCHROTRON              (Y/N) : N                                  
REMARK 200  RADIATION SOURCE               : ROTATING ANODE                     
REMARK 200  BEAMLINE                       : NULL                               
REMARK 200  X-RAY GENERATOR MODEL          : RIGAKU FR-E SUPERBRIGHT            
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M                                  
REMARK 200  WAVELENGTH OR RANGE        (A) : 1.5418                             
REMARK 200  MONOCHROMATOR                  : NULL                               
REMARK 200  OPTICS                         : NULL                               
REMARK 200                                                                      
REMARK 200  DETECTOR TYPE                  : CCD                                
REMARK 200  DETECTOR MANUFACTURER          : RIGAKU SATURN 92                   
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : XDS                                
REMARK 200  DATA SCALING SOFTWARE          : SCALA                              
REMARK 200                                                                      
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 31079                              
REMARK 200  RESOLUTION RANGE HIGH      (A) : 2.006                              
REMARK 200  RESOLUTION RANGE LOW       (A) : 42.690                             
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : NULL                               
REMARK 200                                                                      
REMARK 200 OVERALL.                                                             
REMARK 200  COMPLETENESS FOR RANGE     (%) : 98.5                               
REMARK 200  DATA REDUNDANCY                : 4.700                              
REMARK 200  R MERGE                    (I) : 0.06500                            
REMARK 200  R SYM                      (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR THE DATA SET  : 15.7000                            
REMARK 200                                                                      
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.                                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.01                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 2.01                     
REMARK 200  COMPLETENESS FOR SHELL     (%) : 66.2                               
REMARK 200  DATA REDUNDANCY IN SHELL       : 2.60                               
REMARK 200  R MERGE FOR SHELL          (I) : 0.25000                            
REMARK 200  R SYM FOR SHELL            (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR SHELL         : 4.200                              
REMARK 200                                                                      
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH                              
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: FOURIER SYNTHESIS            
REMARK 200 SOFTWARE USED: BUSTER                                                
REMARK 200 STARTING MODEL: NULL                                                 
REMARK 200                                                                      
REMARK 200 REMARK: NULL                                                         
REMARK 280                                                                      
REMARK 280 CRYSTAL                                                              
REMARK 280 SOLVENT CONTENT, VS   (%): 53.36                                     
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.64                     
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: 0.2M MGSO4, 18% PEG3350, 100MM TRIS      
REMARK 280  CRYO 20% ETHYLENE GLYCOL, PH 8.2, VAPOR DIFFUSION, SITTING DROP,    
REMARK 280  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       40.17500            
REMARK 290   SMTRY2   3  0.000000  1.000000  0.000000       62.67000            
REMARK 290   SMTRY3   3  0.000000  0.000000 -1.000000        0.00000            
REMARK 290   SMTRY1   4  1.000000  0.000000  0.000000       40.17500            
REMARK 290   SMTRY2   4  0.000000 -1.000000  0.000000       62.67000            
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: 2320 ANGSTROM**2                          
REMARK 350 SURFACE AREA OF THE COMPLEX: 18150 ANGSTROM**2                       
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -40.0 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 MG    MG A 402  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     SER A     1                                                      
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: COVALENT BOND LENGTHS                                      
REMARK 500                                                                      
REMARK 500 THE STEREOCHEMICAL PARAMETERS OF THE FOLLOWING RESIDUES              
REMARK 500 HAVE VALUES WHICH DEVIATE FROM EXPECTED VALUES BY MORE               
REMARK 500 THAN 6*RMSD (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN               
REMARK 500 IDENTIFIER; SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).                 
REMARK 500                                                                      
REMARK 500 STANDARD TABLE:                                                      
REMARK 500 FORMAT: (10X,I3,1X,2(A3,1X,A1,I4,A1,1X,A4,3X),1X,F6.3)               
REMARK 500                                                                      
REMARK 500 EXPECTED VALUES PROTEIN: ENGH AND HUBER, 1999                        
REMARK 500 EXPECTED VALUES NUCLEIC ACID: CLOWNEY ET AL 1996                     
REMARK 500                                                                      
REMARK 500  M RES CSSEQI ATM1   RES CSSEQI ATM2   DEVIATION                     
REMARK 500    SER B   1   CA    SER B   1   CB     -0.118                       
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    ALA A  57      -82.39    -84.68                                   
REMARK 500    GLU A 143      -31.51   -132.42                                   
REMARK 500    GLU A 215      -79.06   -110.94                                   
REMARK 500    ILE A 247      -56.00     69.56                                   
REMARK 500    ARG A 333      -87.44     61.33                                   
REMARK 500    ASN B   3     -159.10   -107.21                                   
REMARK 500    H14 B   5      -30.93   -157.99                                   
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 403  MG                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 THR A  25   OG1                                                    
REMARK 620 2 GDP A 401   O2B  86.7                                              
REMARK 620 N                    1                                               
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              MG A 402  MG                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 HOH A 510   O                                                      
REMARK 620 2 HOH A 636   O    97.0                                              
REMARK 620 3 HOH A 554   O    97.6 165.4                                        
REMARK 620 4 HOH A 636   O    72.3  92.2  92.3                                  
REMARK 620 5 HOH A 510   O   164.9  72.3  93.4  97.0                            
REMARK 620 6 HOH A 554   O    93.4  92.3  86.7 165.4  97.6                      
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 401                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MG A 402                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MG A 403                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC4                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 A 404                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC5                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR CHAIN B OF THIOMURACIN ANALOG     
DBREF  5JBQ A    0   393  UNP    P0CE47   EFTU1_ECOLI      1    394             
DBREF  5JBQ B    1    13  PDB    5JBQ     5JBQ             1     13             
SEQRES   1 A  394  MET SER 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   13  SER BB9 ASN BB6 H14 BB9 TYR 05N BB9 BB9 MH6 BB9 6RK          
HET    BB9  B   2       6                                                       
HET    BB6  B   4       7                                                       
HET    H14  B   5      11                                                       
HET    BB9  B   6       6                                                       
HET    05N  B   8       8                                                       
HET    BB9  B   9       5                                                       
HET    BB9  B  10       5                                                       
HET    MH6  B  11       4                                                       
HET    BB9  B  12       6                                                       
HET    6RK  B  13      10                                                       
HET    GDP  A 401      28                                                       
HET     MG  A 402       1                                                       
HET     MG  A 403       1                                                       
HET    SO4  A 404       5                                                       
HETNAM     BB9 (2Z)-2-AMINO-3-SULFANYLPROP-2-ENOIC ACID                         
HETNAM     BB6 (2Z)-2-AMINO-3-SULFANYLBUT-2-ENOIC ACID                          
HETNAM     H14 (2S,3R)-BETA-HYDROXY-PHENYLALANINE                               
HETNAM     05N (3R,4R)-4-HYDROXY-3-METHYL-L-PROLINE                             
HETNAM     MH6 3-HYDROXY-2-IMINOPROPANOIC ACID                                  
HETNAM     6RK 4-AZANYLCYCLOHEXANE-1-CARBOXYLIC ACID                            
HETNAM     GDP GUANOSINE-5'-DIPHOSPHATE                                         
HETNAM      MG MAGNESIUM ION                                                    
HETNAM     SO4 SULFATE ION                                                      
HETSYN     H14 BETA-HYDROXY-PHENYLALANINE, THREO-BETA-HYDROXY-L-                
HETSYN   2 H14  PHENYLALANINE, (BETAS)-BETA-HYDROXY-L-PHENYLALANINE,            
HETSYN   3 H14  L-THREO-3-PHENYLSERINE, L-THREO-BETA-PHENYLSERINE, 3-           
HETSYN   4 H14  HYDROXY-L-PHENYLALANINE                                         
FORMUL   2  BB9    5(C3 H5 N O2 S)                                              
FORMUL   2  BB6    C4 H7 N O2 S                                                 
FORMUL   2  H14    C9 H11 N O3                                                  
FORMUL   2  05N    C6 H11 N O3                                                  
FORMUL   2  MH6    C3 H5 N O3                                                   
FORMUL   2  6RK    C7 H13 N O2                                                  
FORMUL   3  GDP    C10 H15 N5 O11 P2                                            
FORMUL   4   MG    2(MG 2+)                                                     
FORMUL   6  SO4    O4 S 2-                                                      
FORMUL   7  HOH   *224(H2 O)                                                    
HELIX    1 AA1 LYS A    2  ARG A    7  5                                   6    
HELIX    2 AA2 GLY A   23  GLY A   40  1                                  18    
HELIX    3 AA3 ALA A   45  ASN A   51  1                                   7    
HELIX    4 AA4 GLY A   83  GLY A   94  1                                  12    
HELIX    5 AA5 MET A  112  GLY A  126  1                                  15    
HELIX    6 AA6 LYS A  136  VAL A  140  5                                   5    
HELIX    7 AA7 GLU A  143  TYR A  160  1                                  18    
HELIX    8 AA8 PRO A  163  THR A  167  5                                   5    
HELIX    9 AA9 SER A  173  GLU A  179  1                                   7    
HELIX   10 AB1 ASP A  181  ILE A  199  1                                  19    
HELIX   11 AB2 ARG A  204  LYS A  208  5                                   5    
HELIX   12 AB3 LYS A  282  ILE A  286  5                                   5    
SHEET    1 AA1 6 SER A  65  ASP A  70  0                                        
SHEET    2 AA1 6 HIS A  75  ASP A  80 -1  O  HIS A  78   N  VAL A  67           
SHEET    3 AA1 6 HIS A  11  ILE A  17  1  N  VAL A  14   O  ALA A  77           
SHEET    4 AA1 6 ALA A 101  ALA A 106  1  O  ILE A 102   N  GLY A  15           
SHEET    5 AA1 6 ILE A 130  ASN A 135  1  O  ILE A 131   N  LEU A 103           
SHEET    6 AA1 6 ILE A 169  ARG A 171  1  O  VAL A 170   N  LEU A 134           
SHEET    1 AA2 2 GLU A  54  LYS A  56  0                                        
SHEET    2 AA2 2 THR A  61  ASN A  63 -1  O  ILE A  62   N  GLU A  55           
SHEET    1 AA3 7 LEU A 211  PRO A 213  0                                        
SHEET    2 AA3 7 VAL A 291  ALA A 293 -1  O  LEU A 292   N  LEU A 212           
SHEET    3 AA3 7 GLU A 241  VAL A 245 -1  N  GLU A 243   O  ALA A 293           
SHEET    4 AA3 7 GLN A 251  MET A 260 -1  O  SER A 253   N  VAL A 242           
SHEET    5 AA3 7 ASN A 273  LEU A 278 -1  O  LEU A 277   N  THR A 256           
SHEET    6 AA3 7 GLY A 224  ARG A 230 -1  N  VAL A 227   O  VAL A 276           
SHEET    7 AA3 7 VAL A 217  ILE A 220 -1  N  PHE A 218   O  VAL A 226           
SHEET    1 AA4 5 LEU A 211  PRO A 213  0                                        
SHEET    2 AA4 5 VAL A 291  ALA A 293 -1  O  LEU A 292   N  LEU A 212           
SHEET    3 AA4 5 GLU A 241  VAL A 245 -1  N  GLU A 243   O  ALA A 293           
SHEET    4 AA4 5 GLN A 251  MET A 260 -1  O  SER A 253   N  VAL A 242           
SHEET    5 AA4 5 LYS A 263  LEU A 265 -1  O  LEU A 265   N  VAL A 258           
SHEET    1 AA5 2 ILE A 235  LYS A 237  0                                        
SHEET    2 AA5 2 GLU A 267  ARG A 269 -1  O  GLY A 268   N  ILE A 236           
SHEET    1 AA6 7 LYS A 299  ILE A 310  0                                        
SHEET    2 AA6 7 ASN A 355  MET A 368 -1  O  LEU A 362   N  THR A 302           
SHEET    3 AA6 7 THR A 335  GLU A 342 -1  N  THR A 340   O  THR A 361           
SHEET    4 AA6 7 GLN A 329  PHE A 332 -1  N  PHE A 330   O  VAL A 337           
SHEET    5 AA6 7 ARG A 373  GLU A 378 -1  O  ALA A 375   N  TYR A 331           
SHEET    6 AA6 7 ARG A 381  GLY A 393 -1  O  GLY A 386   N  PHE A 374           
SHEET    7 AA6 7 LYS A 299  ILE A 310 -1  N  TYR A 309   O  ALA A 385           
SHEET    1 AA7 2 PHE A 322  PHE A 323  0                                        
SHEET    2 AA7 2 MET A 349  VAL A 350 -1  O  VAL A 350   N  PHE A 322           
LINK         OG1 THR A  25                MG    MG A 403     1555   1555  2.07  
LINK         CA  SER B   1                 C   BB9 B  10     1555   1555  1.43  
LINK         C   SER B   1                 SG  BB9 B   2     1555   1555  1.75  
LINK         C   SER B   1                 N   BB9 B   2     1555   1555  1.34  
LINK         CB  SER B   1                 CB  MH6 B  11     1555   1555  1.40  
LINK         C   BB9 B   2                 N   ASN B   3     1555   1555  1.33  
LINK         C   ASN B   3                 SG  BB6 B   4     1555   1555  1.74  
LINK         C   ASN B   3                 N   BB6 B   4     1555   1555  1.33  
LINK         C   BB6 B   4                 N   H14 B   5     1555   1555  1.34  
LINK         C   H14 B   5                 SG  BB9 B   6     1555   1555  1.75  
LINK         C   H14 B   5                 N   BB9 B   6     1555   1555  1.34  
LINK         C   BB9 B   6                 N   TYR B   7     1555   1555  1.33  
LINK         C   TYR B   7                 N3  05N B   8     1555   1555  1.36  
LINK         C22 05N B   8                 N   BB9 B   9     1555   1555  1.33  
LINK         C22 05N B   8                 SG  BB9 B   9     1555   1555  1.76  
LINK         C   BB9 B   9                 SG  BB9 B  10     1555   1555  1.74  
LINK         C   BB9 B   9                 N   BB9 B  10     1555   1555  1.32  
LINK         C   BB9 B  10                 N   MH6 B  11     1555   1555  1.35  
LINK         C   MH6 B  11                 N   BB9 B  12     1555   1555  1.33  
LINK         C   MH6 B  11                 SG  BB9 B  12     1555   1555  1.76  
LINK         C   BB9 B  12                 N4  6RK B  13     1555   1555  1.34  
LINK         O2B GDP A 401                MG    MG A 403     1555   1555  2.20  
LINK        MG    MG A 402                 O   HOH A 510     1555   1555  2.41  
LINK        MG    MG A 402                 O   HOH A 636     1555   1555  2.22  
LINK        MG    MG A 402                 O   HOH A 554     1555   1555  2.12  
LINK        MG    MG A 402                 O   HOH A 636     1555   2555  2.22  
LINK        MG    MG A 402                 O   HOH A 510     1555   2555  2.41  
LINK        MG    MG A 402                 O   HOH A 554     1555   2555  2.12  
CISPEP   1 GLY A  379    GLY A  380          0        -2.50                     
SITE     1 AC1 20 ASP A  21  HIS A  22  GLY A  23  LYS A  24                    
SITE     2 AC1 20 THR A  25  THR A  26  PHE A  46  ASN A 135                    
SITE     3 AC1 20 LYS A 136  ASP A 138  MET A 139  SER A 173                    
SITE     4 AC1 20 ALA A 174  LEU A 175   MG A 403  HOH A 576                    
SITE     5 AC1 20 HOH A 578  HOH A 603  HOH A 627  HOH A 654                    
SITE     1 AC2  3 HOH A 510  HOH A 554  HOH A 636                               
SITE     1 AC3  2 THR A  25  GDP A 401                                          
SITE     1 AC4  5 ARG A 262  ARG A 318  HIS A 319  THR A 320                    
SITE     2 AC4  5 ARG A 381                                                     
SITE     1 AC5 27 THR A  73  ALA A 182  GLU A 215  ILE A 220                    
SITE     2 AC5 27 ARG A 223  THR A 228  GLY A 257  GLU A 259                    
SITE     3 AC5 27 PHE A 261  ARG A 262  LEU A 264  ASN A 273                    
SITE     4 AC5 27 VAL A 274  GLY A 275  LEU A 277  THR A 320                    
SITE     5 AC5 27 PRO A 321  PHE A 323  LYS A 324  GLY A 325                    
SITE     6 AC5 27 HOH A 527  HOH B 101  HOH B 102  HOH B 103                    
SITE     7 AC5 27 HOH B 104  HOH B 105  HOH B 106                               
CRYST1   80.350  125.340   45.400  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      0.012446  0.000000  0.000000        0.00000                         
SCALE2      0.000000  0.007978  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.022026        0.00000                         
(ATOM LINES ARE NOT SHOWN.)
END                                                                             
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