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Database: PDB
Entry: 3U6B
LinkDB: 3U6B
Original site: 3U6B 
HEADER    TRANSLATION FACTOR/ANTIBIOTIC           12-OCT-11   3U6B              
TITLE     EF-TU (ESCHERICHIA COLI) IN COMPLEX WITH NVP-LDI028                   
COMPND    MOL_ID: 1;                                                            
COMPND   2 MOLECULE: ELONGATION FACTOR TU 1;                                    
COMPND   3 CHAIN: A, B;                                                         
COMPND   4 SYNONYM: EF-TU 1, P-43;                                              
COMPND   5 ENGINEERED: YES;                                                     
COMPND   6 MOL_ID: 2;                                                           
COMPND   7 MOLECULE: THIOCILLIN GE2270 ANALOGUE NVP-LDI028;                     
COMPND   8 CHAIN: C, D;                                                         
COMPND   9 SYNONYM: EF-TU 1, P-43 ,EF-TU;                                       
COMPND  10 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 EXPRESSION_SYSTEM_STRAIN: BL21 (STAR);                               
SOURCE   9 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;                              
SOURCE  10 EXPRESSION_SYSTEM_PLASMID: PET15B;                                   
SOURCE  11 MOL_ID: 2;                                                           
SOURCE  12 SYNTHETIC: YES                                                       
KEYWDS    TRANSLATION FACTOR-ANTIBIOTIC COMPLEX                                 
EXPDTA    X-RAY DIFFRACTION                                                     
AUTHOR    D.J.PALESTRANT                                                        
REVDAT   2   18-APR-12 3U6B    1       COMPND                                   
REVDAT   1   08-FEB-12 3U6B    0                                                
JRNL        AUTH   M.J.LAMARCHE,J.A.LEEDS,K.AMARAL,J.T.BREWER,S.M.BUSHELL,      
JRNL        AUTH 2 J.M.DEWHURST,J.DZINK-FOX,E.GANGL,J.GOLDOVITZ,A.JAIN,         
JRNL        AUTH 3 S.MULLIN,G.NECKERMANN,C.OSBORNE,D.PALESTRANT,M.A.PATANE,     
JRNL        AUTH 4 E.M.RANN,M.SACHDEVA,J.SHAO,S.TIAMFOOK,L.WHITEHEAD,D.YU       
JRNL        TITL   ANTIBACTERIAL OPTIMIZATION OF 4-AMINOTHIAZOLYL ANALOGUES OF  
JRNL        TITL 2 THE NATURAL PRODUCT GE2270 A: IDENTIFICATION OF THE          
JRNL        TITL 3 CYCLOALKYLCARBOXYLIC ACIDS.                                  
JRNL        REF    J.MED.CHEM.                   V.  54  8099 2011              
JRNL        REFN                   ISSN 0022-2623                               
JRNL        PMID   21999529                                                     
JRNL        DOI    10.1021/JM200938F                                            
REMARK   2                                                                      
REMARK   2 RESOLUTION.    2.12 ANGSTROMS.                                       
REMARK   3                                                                      
REMARK   3 REFINEMENT.                                                          
REMARK   3   PROGRAM     : BUSTER 2.11.2                                        
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) : 2.12                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 8.00                           
REMARK   3   DATA CUTOFF            (SIGMA(F)) : 0.000                          
REMARK   3   COMPLETENESS FOR RANGE        (%) : 85.8                           
REMARK   3   NUMBER OF REFLECTIONS             : 37531                          
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)  : 0.199                          
REMARK   3   R VALUE            (WORKING SET)  : 0.196                          
REMARK   3   FREE R VALUE                      : 0.257                          
REMARK   3   FREE R VALUE TEST SET SIZE   (%)  : 4.960                          
REMARK   3   FREE R VALUE TEST SET COUNT       : 1861                           
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               : 19                       
REMARK   3   BIN RESOLUTION RANGE HIGH   (ANGSTROMS) : 2.12                     
REMARK   3   BIN RESOLUTION RANGE LOW    (ANGSTROMS) : 2.18                     
REMARK   3   BIN COMPLETENESS (WORKING+TEST)     (%) : 85.85                    
REMARK   3   REFLECTIONS IN BIN (WORKING + TEST SET) : 2543                     
REMARK   3   BIN R VALUE        (WORKING + TEST SET) : 0.2379                   
REMARK   3   REFLECTIONS IN BIN        (WORKING SET) : 2458                     
REMARK   3   BIN R VALUE               (WORKING SET) : 0.2356                   
REMARK   3   BIN FREE R VALUE                        : 0.3036                   
REMARK   3   BIN FREE R VALUE TEST SET SIZE      (%) : 3.34                     
REMARK   3   BIN FREE R VALUE TEST SET COUNT         : 85                       
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            : 5875                                    
REMARK   3   NUCLEIC ACID ATOMS       : 0                                       
REMARK   3   HETEROGEN ATOMS          : 58                                      
REMARK   3   SOLVENT ATOMS            : 111                                     
REMARK   3                                                                      
REMARK   3  B VALUES.                                                           
REMARK   3   FROM WILSON PLOT           (A**2) : 34.08                          
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : 37.97                          
REMARK   3   OVERALL ANISOTROPIC B VALUE.                                       
REMARK   3    B11 (A**2) : -1.44850                                             
REMARK   3    B22 (A**2) : -1.55720                                             
REMARK   3    B33 (A**2) : 3.00570                                              
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) : 0.29                
REMARK   3   DPI (BLOW EQ-10) BASED ON R VALUE        (A) : NULL                
REMARK   3   DPI (BLOW EQ-9) BASED ON FREE R VALUE    (A) : NULL                
REMARK   3   DPI (CRUICKSHANK) BASED ON R VALUE       (A) : NULL                
REMARK   3   DPI (CRUICKSHANK) BASED ON FREE R VALUE  (A) : NULL                
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      : 0.942                         
REMARK   3   CORRELATION COEFFICIENT FO-FC FREE : 0.896                         
REMARK   3                                                                      
REMARK   3   NUMBER OF GEOMETRIC FUNCTION TERMS DEFINED : 15                    
REMARK   3   TERM                          COUNT    WEIGHT   FUNCTION.          
REMARK   3    BOND LENGTHS              : 6056   ; 2.000  ; HARMONIC            
REMARK   3    BOND ANGLES               : 8231   ; 2.000  ; HARMONIC            
REMARK   3    TORSION ANGLES            : 2046   ; 2.000  ; SINUSOIDAL          
REMARK   3    TRIGONAL CARBON PLANES    : 137    ; 2.000  ; HARMONIC            
REMARK   3    GENERAL PLANES            : 915    ; 5.000  ; HARMONIC            
REMARK   3    ISOTROPIC THERMAL FACTORS : 6056   ; 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   : NULL   ; NULL   ; NULL                
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   : NULL   ; NULL   ; NULL                
REMARK   3                                                                      
REMARK   3   RMS DEVIATIONS FROM IDEAL VALUES.                                  
REMARK   3    BOND LENGTHS                       (A) : 0.010                    
REMARK   3    BOND ANGLES                  (DEGREES) : 1.25                     
REMARK   3    PEPTIDE OMEGA TORSION ANGLES (DEGREES) : NULL                     
REMARK   3    OTHER TORSION ANGLES         (DEGREES) : NULL                     
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 3U6B 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 RCSB068360.                                      
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : 15-OCT-06                          
REMARK 200  TEMPERATURE           (KELVIN) : 100.0                              
REMARK 200  PH                             : 6.5                                
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                  : NULL                               
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   : 39701                              
REMARK 200  RESOLUTION RANGE HIGH      (A) : 2.120                              
REMARK 200  RESOLUTION RANGE LOW       (A) : 50.000                             
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : 1.000                              
REMARK 200                                                                      
REMARK 200 OVERALL.                                                             
REMARK 200  COMPLETENESS FOR RANGE     (%) : 91.0                               
REMARK 200  DATA REDUNDANCY                : 5.900                              
REMARK 200  R MERGE                    (I) : 0.09800                            
REMARK 200  R SYM                      (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR THE DATA SET  : 23.7000                            
REMARK 200                                                                      
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.                                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.14                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 2.28                     
REMARK 200  COMPLETENESS FOR SHELL     (%) : 80.0                               
REMARK 200  DATA REDUNDANCY IN SHELL       : 5.60                               
REMARK 200  R MERGE FOR SHELL          (I) : 0.32200                            
REMARK 200  R SYM FOR SHELL            (I) : 0.25700                            
REMARK 200  <I/SIGMA(I)> FOR SHELL         : 8.030                              
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: NULL                                                 
REMARK 200                                                                      
REMARK 200 REMARK: NULL                                                         
REMARK 280                                                                      
REMARK 280 CRYSTAL                                                              
REMARK 280 SOLVENT CONTENT, VS   (%): 42.34                                     
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.13                     
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: 0.2M AMMONIUM ACETATE, 22% PEG 3350,     
REMARK 280  0.1M BIS-TRIS PH6.5 , VAPOR DIFFUSION, SITTING DROP, TEMPERATURE    
REMARK 280  293K                                                                
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY                                            
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: C 2 2 21                         
REMARK 290                                                                      
REMARK 290      SYMOP   SYMMETRY                                                
REMARK 290     NNNMMM   OPERATOR                                                
REMARK 290       1555   X,Y,Z                                                   
REMARK 290       2555   -X,-Y,Z+1/2                                             
REMARK 290       3555   -X,Y,-Z+1/2                                             
REMARK 290       4555   X,-Y,-Z                                                 
REMARK 290       5555   X+1/2,Y+1/2,Z                                           
REMARK 290       6555   -X+1/2,-Y+1/2,Z+1/2                                     
REMARK 290       7555   -X+1/2,Y+1/2,-Z+1/2                                     
REMARK 290       8555   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       78.24150            
REMARK 290   SMTRY1   3 -1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   3  0.000000  1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   3  0.000000  0.000000 -1.000000       78.24150            
REMARK 290   SMTRY1   4  1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   4  0.000000 -1.000000  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       48.62300            
REMARK 290   SMTRY2   5  0.000000  1.000000  0.000000       50.18800            
REMARK 290   SMTRY3   5  0.000000  0.000000  1.000000        0.00000            
REMARK 290   SMTRY1   6 -1.000000  0.000000  0.000000       48.62300            
REMARK 290   SMTRY2   6  0.000000 -1.000000  0.000000       50.18800            
REMARK 290   SMTRY3   6  0.000000  0.000000  1.000000       78.24150            
REMARK 290   SMTRY1   7 -1.000000  0.000000  0.000000       48.62300            
REMARK 290   SMTRY2   7  0.000000  1.000000  0.000000       50.18800            
REMARK 290   SMTRY3   7  0.000000  0.000000 -1.000000       78.24150            
REMARK 290   SMTRY1   8  1.000000  0.000000  0.000000       48.62300            
REMARK 290   SMTRY2   8  0.000000 -1.000000  0.000000       50.18800            
REMARK 290   SMTRY3   8  0.000000  0.000000 -1.000000        0.00000            
REMARK 290                                                                      
REMARK 290 REMARK: NULL                                                         
REMARK 300                                                                      
REMARK 300 BIOMOLECULE: 1, 2                                                    
REMARK 300 SEE REMARK 350 FOR THE AUTHOR PROVIDED AND/OR PROGRAM                
REMARK 300 GENERATED ASSEMBLY INFORMATION FOR THE STRUCTURE IN                  
REMARK 300 THIS ENTRY. THE REMARK MAY ALSO PROVIDE INFORMATION ON               
REMARK 300 BURIED SURFACE AREA.                                                 
REMARK 350                                                                      
REMARK 350 COORDINATES FOR A COMPLETE MULTIMER REPRESENTING THE KNOWN           
REMARK 350 BIOLOGICALLY SIGNIFICANT OLIGOMERIZATION STATE OF THE                
REMARK 350 MOLECULE CAN BE GENERATED BY APPLYING BIOMT TRANSFORMATIONS          
REMARK 350 GIVEN BELOW.  BOTH NON-CRYSTALLOGRAPHIC AND                          
REMARK 350 CRYSTALLOGRAPHIC OPERATIONS ARE GIVEN.                               
REMARK 350                                                                      
REMARK 350 BIOMOLECULE: 1                                                       
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: DIMERIC                           
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: DIMERIC                    
REMARK 350 SOFTWARE USED: PISA                                                  
REMARK 350 TOTAL BURIED SURFACE AREA: 2090 ANGSTROM**2                          
REMARK 350 SURFACE AREA OF THE COMPLEX: 16700 ANGSTROM**2                       
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -21.0 KCAL/MOL                        
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, C                                  
REMARK 350   BIOMT1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 350   BIOMT2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 350   BIOMT3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 350                                                                      
REMARK 350 BIOMOLECULE: 2                                                       
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: DIMERIC                           
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: DIMERIC                    
REMARK 350 SOFTWARE USED: PISA                                                  
REMARK 350 TOTAL BURIED SURFACE AREA: 2080 ANGSTROM**2                          
REMARK 350 SURFACE AREA OF THE COMPLEX: 17370 ANGSTROM**2                       
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -21.0 KCAL/MOL                        
REMARK 350 APPLY THE FOLLOWING TO CHAINS: B, D                                  
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 B 524  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     ALA A    42                                                      
REMARK 465     ALA A    43                                                      
REMARK 465     ARG A    44                                                      
REMARK 465     ALA A    45                                                      
REMARK 465     PHE A    46                                                      
REMARK 465     ASP A    47                                                      
REMARK 465     GLN A    48                                                      
REMARK 465     ILE A    49                                                      
REMARK 465     ASP A    50                                                      
REMARK 465     ASN A    51                                                      
REMARK 465     ALA A    52                                                      
REMARK 465     PRO A    53                                                      
REMARK 465     GLU A    54                                                      
REMARK 465     GLU A    55                                                      
REMARK 465     LYS A    56                                                      
REMARK 465     ALA A    57                                                      
REMARK 465     SER A   221                                                      
REMARK 465     GLY A   222                                                      
REMARK 465     ARG A   223                                                      
REMARK 465     GLY A   224                                                      
REMARK 465     MET B     0                                                      
REMARK 465     ALA B     1                                                      
REMARK 465     ARG B    44                                                      
REMARK 465     ALA B    45                                                      
REMARK 465     PHE B    46                                                      
REMARK 465     ASP B    47                                                      
REMARK 465     GLN B    48                                                      
REMARK 465     ILE B    49                                                      
REMARK 465     ASP B    50                                                      
REMARK 465     ASN B    51                                                      
REMARK 465     ALA B    52                                                      
REMARK 465     PRO B    53                                                      
REMARK 465     GLU B    54                                                      
REMARK 465     GLU B    55                                                      
REMARK 465     SER B   221                                                      
REMARK 465     GLY B   222                                                      
REMARK 465     ARG B   223                                                      
REMARK 465     GLY B   224                                                      
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 C   1   CA    SER C   1   CB     -0.118                       
REMARK 500    SER D   1   CA    SER D   1   CB     -0.134                       
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  96       74.83   -100.39                                   
REMARK 500    ASP A 141       38.03    -96.04                                   
REMARK 500    ILE A 247      -67.95     55.44                                   
REMARK 500    ARG A 262      -11.67     73.79                                   
REMARK 500    ARG A 283      -39.11    -38.41                                   
REMARK 500    ARG A 327       73.48   -116.67                                   
REMARK 500    ARG A 333      -70.81     58.71                                   
REMARK 500    ARG B   7       77.05    -64.56                                   
REMARK 500    THR B   8       13.97   -156.76                                   
REMARK 500    ASP B  21       -0.21     71.06                                   
REMARK 500    ARG B  58      -33.53     84.66                                   
REMARK 500    ASP B 141       69.36   -114.41                                   
REMARK 500    ASP B 161       -1.92     78.16                                   
REMARK 500    GLU B 215      -68.89    -96.13                                   
REMARK 500    ILE B 247      -65.19     57.86                                   
REMARK 500    ARG B 262       -5.49     82.95                                   
REMARK 500    ALA B 270      130.55    -38.54                                   
REMARK 500    PHE B 323     -165.09   -114.42                                   
REMARK 500    ARG B 333      -65.34     63.66                                   
REMARK 500    MEN D   3     -167.14   -100.31                                   
REMARK 500    VAL D   5      -24.11   -171.60                                   
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: CHIRAL CENTERS                                             
REMARK 500                                                                      
REMARK 500 UNEXPECTED CONFIGURATION OF THE FOLLOWING CHIRAL                     
REMARK 500 CENTER(S) USING IMPROPER CA--C--CB--N CHIRALITY                      
REMARK 500 FOR AMINO ACIDS AND C1'--O4'--N1(N9)--C2' FOR                        
REMARK 500 NUCLEIC ACIDS OR EQUIVALENT ANGLE                                    
REMARK 500 M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN                            
REMARK 500 IDENTIFIER; SSEQ=SEQUENCE NUMBER; I=INSERTION CODE                   
REMARK 500                                                                      
REMARK 500 STANDARD TABLE:                                                      
REMARK 500 FORMAT: (10X,I3,1X,A3,1X,A1,I4,A1,6X,F5.1,6X,A1,10X,A1,3X,A16)       
REMARK 500                                                                      
REMARK 500  M RES CSSEQI    IMPROPER   EXPECTED   FOUND DETAILS                 
REMARK 500    ARG A 377        24.2      L          L   OUTSIDE RANGE           
REMARK 500    ARG B  58        23.0      L          L   OUTSIDE RANGE           
REMARK 500    MET B 358        24.6      L          L   OUTSIDE RANGE           
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 401  MG                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 GDP A 402   O2B                                                    
REMARK 620 2 HOH A 514   O    91.2                                              
REMARK 620 3 HOH A 503   O   102.8 165.7                                        
REMARK 620 4 THR A  25   OG1  95.4  80.8  94.5                                  
REMARK 620 5 HOH A 517   O    95.3  89.4  92.5 165.6                            
REMARK 620 6 HOH A 531   O   167.7  78.0  87.8  77.3  90.5                      
REMARK 620 N                    1     2     3     4     5                       
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              MG B 402  MG                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 THR B  25   OG1                                                    
REMARK 620 2 HOH B 512   O    87.8                                              
REMARK 620 3 HOH B 505   O    91.8 172.4                                        
REMARK 620 4 GDP B 401   O2B  93.1  93.9  93.6                                  
REMARK 620 5 HOH B 516   O    90.0  77.5  95.0 170.8                            
REMARK 620 6 HOH B 514   O   177.0  91.7  88.4  89.9  87.0                      
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 MG A 401                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE GDP A 402                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE GDP B 401                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC4                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MG B 402                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC5                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR CHAIN C OF NVP-LDI028             
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC6                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR CHAIN D OF NVP-LDI028             
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: 3U2Q   RELATED DB: PDB                                   
REMARK 900 EF-TU (ESCHERICHIA COLI) IN COMPLEX WITH NVP-LFF571                  
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  3U6B A    2   393  UNP    P0CE47   EFTU1_ECOLI      3    394             
DBREF  3U6B B    2   393  UNP    P0CE47   EFTU1_ECOLI      3    394             
DBREF  3U6B C    1    12  UNP    Q7M0J8   THCL_PLARO       1     12             
DBREF  3U6B D    1    12  UNP    Q7M0J8   THCL_PLARO       1     12             
SEQADV 3U6B MET A    0  UNP  P0CE47              EXPRESSION TAG                 
SEQADV 3U6B ALA A    1  UNP  P0CE47              EXPRESSION TAG                 
SEQADV 3U6B MET B    0  UNP  P0CE47              EXPRESSION TAG                 
SEQADV 3U6B ALA B    1  UNP  P0CE47              EXPRESSION TAG                 
SEQADV 3U6B 8BB C   12  UNP  Q7M0J8    CYS    12 SEE REMARK 999                 
SEQADV 3U6B 8BB D   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  394  MET ALA LYS GLU LYS PHE GLU ARG THR LYS PRO HIS VAL          
SEQRES   2 B  394  ASN VAL GLY THR ILE GLY HIS VAL ASP HIS GLY LYS THR          
SEQRES   3 B  394  THR LEU THR ALA ALA ILE THR THR VAL LEU ALA LYS THR          
SEQRES   4 B  394  TYR GLY GLY ALA ALA ARG ALA PHE ASP GLN ILE ASP ASN          
SEQRES   5 B  394  ALA PRO GLU GLU LYS ALA ARG GLY ILE THR ILE ASN THR          
SEQRES   6 B  394  SER HIS VAL GLU TYR ASP THR PRO THR ARG HIS TYR ALA          
SEQRES   7 B  394  HIS VAL ASP CYS PRO GLY HIS ALA ASP TYR VAL LYS ASN          
SEQRES   8 B  394  MET ILE THR GLY ALA ALA GLN MET ASP GLY ALA ILE LEU          
SEQRES   9 B  394  VAL VAL ALA ALA THR ASP GLY PRO MET PRO GLN THR ARG          
SEQRES  10 B  394  GLU HIS ILE LEU LEU GLY ARG GLN VAL GLY VAL PRO TYR          
SEQRES  11 B  394  ILE ILE VAL PHE LEU ASN LYS CYS ASP MET VAL ASP ASP          
SEQRES  12 B  394  GLU GLU LEU LEU GLU LEU VAL GLU MET GLU VAL ARG GLU          
SEQRES  13 B  394  LEU LEU SER GLN TYR ASP PHE PRO GLY ASP ASP THR PRO          
SEQRES  14 B  394  ILE VAL ARG GLY SER ALA LEU LYS ALA LEU GLU GLY ASP          
SEQRES  15 B  394  ALA GLU TRP GLU ALA LYS ILE LEU GLU LEU ALA GLY PHE          
SEQRES  16 B  394  LEU ASP SER TYR ILE PRO GLU PRO GLU ARG ALA ILE ASP          
SEQRES  17 B  394  LYS PRO PHE LEU LEU PRO ILE GLU ASP VAL PHE SER ILE          
SEQRES  18 B  394  SER GLY ARG GLY THR VAL VAL THR GLY ARG VAL GLU ARG          
SEQRES  19 B  394  GLY ILE ILE LYS VAL GLY GLU GLU VAL GLU ILE VAL GLY          
SEQRES  20 B  394  ILE LYS GLU THR GLN LYS SER THR CYS THR GLY VAL GLU          
SEQRES  21 B  394  MET PHE ARG LYS LEU LEU ASP GLU GLY ARG ALA GLY GLU          
SEQRES  22 B  394  ASN VAL GLY VAL LEU LEU ARG GLY ILE LYS ARG GLU GLU          
SEQRES  23 B  394  ILE GLU ARG GLY GLN VAL LEU ALA LYS PRO GLY THR ILE          
SEQRES  24 B  394  LYS PRO HIS THR LYS PHE GLU SER GLU VAL TYR ILE LEU          
SEQRES  25 B  394  SER LYS ASP GLU GLY GLY ARG HIS THR PRO PHE PHE LYS          
SEQRES  26 B  394  GLY TYR ARG PRO GLN PHE TYR PHE ARG THR THR ASP VAL          
SEQRES  27 B  394  THR GLY THR ILE GLU LEU PRO GLU GLY VAL GLU MET VAL          
SEQRES  28 B  394  MET PRO GLY ASP ASN ILE LYS MET VAL VAL THR LEU ILE          
SEQRES  29 B  394  HIS PRO ILE ALA MET ASP ASP GLY LEU ARG PHE ALA ILE          
SEQRES  30 B  394  ARG GLU GLY GLY ARG THR VAL GLY ALA GLY VAL VAL ALA          
SEQRES  31 B  394  LYS VAL LEU GLY                                              
SEQRES   1 C   12  SER BB9 MEN BB6 VAL BB7 GLY BB8 BB9 BB9 MH6 8BB              
SEQRES   1 D   12  SER BB9 MEN BB6 VAL BB7 GLY BB8 BB9 BB9 MH6 8BB              
MODRES 3U6B BB9 C    2  CYS                                                     
MODRES 3U6B MEN C    3  ASN  N-METHYL ASPARAGINE                                
MODRES 3U6B BB6 C    4  CYS  (2Z)-2-AMINO-3-SULFANYLBUT-2-ENOIC ACID            
MODRES 3U6B BB7 C    6  CYS                                                     
MODRES 3U6B BB8 C    8  PHE  (2S,3S)-BETA-HYDROXY-PHENYLALANINE                 
MODRES 3U6B BB9 C    9  CYS                                                     
MODRES 3U6B BB9 C   10  CYS                                                     
MODRES 3U6B MH6 C   11  SER  3-HYDROXY-2-IMINOPROPANOIC ACID                    
MODRES 3U6B BB9 D    2  CYS                                                     
MODRES 3U6B MEN D    3  ASN  N-METHYL ASPARAGINE                                
MODRES 3U6B BB6 D    4  CYS  (2Z)-2-AMINO-3-SULFANYLBUT-2-ENOIC ACID            
MODRES 3U6B BB7 D    6  CYS                                                     
MODRES 3U6B BB8 D    8  PHE  (2S,3S)-BETA-HYDROXY-PHENYLALANINE                 
MODRES 3U6B BB9 D    9  CYS                                                     
MODRES 3U6B BB9 D   10  CYS                                                     
MODRES 3U6B MH6 D   11  SER  3-HYDROXY-2-IMINOPROPANOIC ACID                    
HET    BB9  C   2       6                                                       
HET    MEN  C   3       8                                                       
HET    BB6  C   4       7                                                       
HET    BB7  C   6       9                                                       
HET    BB8  C   8      11                                                       
HET    BB9  C   9       5                                                       
HET    BB9  C  10       5                                                       
HET    MH6  C  11       4                                                       
HET    8BB  C  12      16                                                       
HET    BB9  D   2       6                                                       
HET    MEN  D   3       8                                                       
HET    BB6  D   4       7                                                       
HET    BB7  D   6       9                                                       
HET    BB8  D   8      11                                                       
HET    BB9  D   9       5                                                       
HET    BB9  D  10       5                                                       
HET    MH6  D  11       4                                                       
HET    8BB  D  12      16                                                       
HET     MG  A 401       1                                                       
HET    GDP  A 402      28                                                       
HET    GDP  B 401      28                                                       
HET     MG  B 402       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     8BB TRANS-4-{[(E)-1-AMINO-2-                                         
HETNAM   2 8BB  SULFANYLETHENYL]CARBAMOYL}CYCLOHEXANECARBOXYLIC ACID            
HETNAM      MG MAGNESIUM ION                                                    
HETNAM     GDP GUANOSINE-5'-DIPHOSPHATE                                         
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   3  BB9    6(C3 H5 N O2 S)                                              
FORMUL   3  MEN    2(C5 H10 N2 O3)                                              
FORMUL   3  BB6    2(C4 H7 N O2 S)                                              
FORMUL   3  BB7    2(C5 H9 N O3 S)                                              
FORMUL   3  BB8    2(C9 H11 N O3)                                               
FORMUL   3  MH6    2(C3 H5 N O3)                                                
FORMUL   3  8BB    2(C10 H16 N2 O3 S)                                           
FORMUL   5   MG    2(MG 2+)                                                     
FORMUL   6  GDP    2(C10 H15 N5 O11 P2)                                         
FORMUL   9  HOH   *111(H2 O)                                                    
HELIX    1   1 GLY A   23  TYR A   39  1                                  17    
HELIX    2   2 GLY A   83  GLY A   94  1                                  12    
HELIX    3   3 MET A  112  GLY A  126  1                                  15    
HELIX    4   4 ASP A  142  TYR A  160  1                                  19    
HELIX    5   5 PRO A  163  THR A  167  5                                   5    
HELIX    6   6 SER A  173  GLU A  179  1                                   7    
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    
HELIX   11  11 GLU B    3  ARG B    7  1                                   5    
HELIX   12  12 GLY B   23  GLY B   40  1                                  18    
HELIX   13  13 GLY B   83  GLY B   94  1                                  12    
HELIX   14  14 MET B  112  VAL B  125  1                                  14    
HELIX   15  15 ASP B  142  TYR B  160  1                                  19    
HELIX   16  16 PRO B  163  THR B  167  5                                   5    
HELIX   17  17 SER B  173  GLU B  179  1                                   7    
HELIX   18  18 ASP B  181  ILE B  199  1                                  19    
HELIX   19  19 ARG B  204  LYS B  208  5                                   5    
HELIX   20  20 LYS B  282  ILE B  286  5                                   5    
HELIX   21  21 SER B  312  GLY B  316  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  ILE A  17  1  N  VAL A  14   O  ALA A  77           
SHEET    4   A 6 GLY A 100  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  LEU A 134           
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  LEU A 278 -1  O  LEU A 277   N  THR A 256           
SHEET    6   B 7 VAL A 226  ARG A 230 -1  N  VAL A 227   O  VAL A 276           
SHEET    7   B 7 VAL A 217  PHE A 218 -1  N  PHE A 218   O  VAL A 226           
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  LEU A 362   N  THR A 302           
SHEET    3   E 7 THR A 335  GLU A 342 -1  N  THR A 340   O  THR A 361           
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  ARG A 377   N  GLN A 329           
SHEET    6   E 7 ARG A 381  GLY A 393 -1  O  GLY A 384   N  ILE A 376           
SHEET    7   E 7 LYS A 299  ILE A 310 -1  N  GLU A 305   O  LYS A 390           
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           
SHEET    1   G 6 SER B  65  ASP B  70  0                                        
SHEET    2   G 6 HIS B  75  ASP B  80 -1  O  HIS B  78   N  VAL B  67           
SHEET    3   G 6 HIS B  11  ILE B  17  1  N  VAL B  14   O  ALA B  77           
SHEET    4   G 6 GLY B 100  ALA B 106  1  O  VAL B 104   N  ILE B  17           
SHEET    5   G 6 ILE B 130  ASN B 135  1  O  ILE B 131   N  LEU B 103           
SHEET    6   G 6 ILE B 169  ARG B 171  1  O  VAL B 170   N  LEU B 134           
SHEET    1   H 7 LEU B 211  PRO B 213  0                                        
SHEET    2   H 7 VAL B 291  ALA B 293 -1  O  LEU B 292   N  LEU B 212           
SHEET    3   H 7 GLU B 241  VAL B 245 -1  N  GLU B 243   O  ALA B 293           
SHEET    4   H 7 GLN B 251  MET B 260 -1  O  SER B 253   N  VAL B 242           
SHEET    5   H 7 ASN B 273  ARG B 279 -1  O  LEU B 277   N  THR B 256           
SHEET    6   H 7 VAL B 226  ARG B 230 -1  N  GLY B 229   O  VAL B 274           
SHEET    7   H 7 VAL B 217  PHE B 218 -1  N  PHE B 218   O  VAL B 226           
SHEET    1   I 5 LEU B 211  PRO B 213  0                                        
SHEET    2   I 5 VAL B 291  ALA B 293 -1  O  LEU B 292   N  LEU B 212           
SHEET    3   I 5 GLU B 241  VAL B 245 -1  N  GLU B 243   O  ALA B 293           
SHEET    4   I 5 GLN B 251  MET B 260 -1  O  SER B 253   N  VAL B 242           
SHEET    5   I 5 LYS B 263  LEU B 265 -1  O  LEU B 265   N  VAL B 258           
SHEET    1   J 2 ILE B 235  LYS B 237  0                                        
SHEET    2   J 2 GLU B 267  ARG B 269 -1  O  GLY B 268   N  ILE B 236           
SHEET    1   K 7 LYS B 299  ILE B 310  0                                        
SHEET    2   K 7 ASN B 355  MET B 368 -1  O  ILE B 356   N  VAL B 308           
SHEET    3   K 7 THR B 335  GLU B 342 -1  N  THR B 340   O  THR B 361           
SHEET    4   K 7 GLN B 329  PHE B 332 -1  N  PHE B 330   O  VAL B 337           
SHEET    5   K 7 ARG B 373  GLU B 378 -1  O  ALA B 375   N  TYR B 331           
SHEET    6   K 7 ARG B 381  VAL B 391 -1  O  GLY B 384   N  ILE B 376           
SHEET    7   K 7 LYS B 299  ILE B 310 -1  N  GLU B 305   O  LYS B 390           
LINK         C   SER C   1                 N   BB9 C   2     1555   1555  1.36  
LINK         C   BB9 C   2                 N   MEN C   3     1555   1555  1.35  
LINK         C   BB6 C   4                 N   VAL C   5     1555   1555  1.35  
LINK         C   BB7 C   6                 N   GLY C   7     1555   1555  1.35  
LINK         C   BB8 C   8                 N   BB9 C   9     1555   1555  1.31  
LINK         C   BB9 C   9                 N   BB9 C  10     1555   1555  1.33  
LINK         C   BB9 C  10                 N   MH6 C  11     1555   1555  1.35  
LINK         C   MH6 C  11                 N   8BB C  12     1555   1555  1.34  
LINK         C   MH6 C  11                 SG  8BB C  12     1555   1555  1.76  
LINK         C   SER D   1                 N   BB9 D   2     1555   1555  1.34  
LINK         C   BB9 D   2                 N   MEN D   3     1555   1555  1.33  
LINK         C   BB6 D   4                 N   VAL D   5     1555   1555  1.35  
LINK         C   BB7 D   6                 N   GLY D   7     1555   1555  1.35  
LINK         C   BB8 D   8                 N   BB9 D   9     1555   1555  1.31  
LINK         C   BB9 D   9                 N   BB9 D  10     1555   1555  1.34  
LINK         C   BB9 D  10                 N   MH6 D  11     1555   1555  1.35  
LINK         C   MH6 D  11                 N   8BB D  12     1555   1555  1.34  
LINK         C   MH6 D  11                 SG  8BB D  12     1555   1555  1.77  
LINK        MG    MG A 401                 O2B GDP A 402     1555   1555  1.97  
LINK        MG    MG A 401                 O   HOH A 514     1555   1555  1.97  
LINK         OG1 THR B  25                MG    MG B 402     1555   1555  1.97  
LINK        MG    MG B 402                 O   HOH B 512     1555   1555  2.00  
LINK        MG    MG A 401                 O   HOH A 503     1555   1555  2.01  
LINK        MG    MG B 402                 O   HOH B 505     1555   1555  2.03  
LINK         OG1 THR A  25                MG    MG A 401     1555   1555  2.09  
LINK         O2B GDP B 401                MG    MG B 402     1555   1555  2.10  
LINK        MG    MG B 402                 O   HOH B 516     1555   1555  2.14  
LINK        MG    MG A 401                 O   HOH A 517     1555   1555  2.16  
LINK        MG    MG B 402                 O   HOH B 514     1555   1555  2.20  
LINK        MG    MG A 401                 O   HOH A 531     1555   1555  2.24  
LINK         CB  SER D   1                 CB  MH6 D  11     1555   1555  1.39  
LINK         CB  SER C   1                 CB  MH6 C  11     1555   1555  1.40  
LINK         CA  SER C   1                 C   BB9 C  10     1555   1555  1.42  
LINK         CA  SER D   1                 C   BB9 D  10     1555   1555  1.42  
LINK         C   MEN D   3                 SG  BB6 D   4     1555   1555  1.74  
LINK         C   MEN C   3                 SG  BB6 C   4     1555   1555  1.75  
LINK         C   VAL C   5                 SG  BB7 C   6     1555   1555  1.75  
LINK         C   BB9 D   9                 SG  BB9 D  10     1555   1555  1.75  
LINK         C   VAL D   5                 SG  BB7 D   6     1555   1555  1.76  
LINK         C   SER D   1                 SG  BB9 D   2     1555   1555  1.76  
LINK         C   BB8 C   8                 SG  BB9 C   9     1555   1555  1.76  
LINK         C   BB8 D   8                 SG  BB9 D   9     1555   1555  1.77  
LINK         C   SER C   1                 SG  BB9 C   2     1555   1555  1.77  
LINK         C   BB9 C   9                 SG  BB9 C  10     1555   1555  1.77  
CISPEP   1 ALA B   95    ALA B   96          0         3.72                     
SITE     1 AC1  6 THR A  25  GDP A 402  HOH A 503  HOH A 514                    
SITE     2 AC1  6 HOH A 517  HOH A 531                                          
SITE     1 AC2 18 ASP A  21  HIS A  22  GLY A  23  LYS A  24                    
SITE     2 AC2 18 THR A  25  THR A  26  ASN A 135  LYS A 136                    
SITE     3 AC2 18 ASP A 138  MET A 139  SER A 173  ALA A 174                    
SITE     4 AC2 18 LEU A 175   MG A 401  HOH A 514  HOH A 517                    
SITE     5 AC2 18 HOH A 554  HOH A 562                                          
SITE     1 AC3 20 HIS B  19  ASP B  21  HIS B  22  GLY B  23                    
SITE     2 AC3 20 LYS B  24  THR B  25  THR B  26  ASN B 135                    
SITE     3 AC3 20 LYS B 136  ASP B 138  MET B 139  SER B 173                    
SITE     4 AC3 20 ALA B 174  LEU B 175   MG B 402  HOH B 505                    
SITE     5 AC3 20 HOH B 509  HOH B 512  HOH B 514  HOH B 515                    
SITE     1 AC4  6 THR B  25  GDP B 401  HOH B 505  HOH B 512                    
SITE     2 AC4  6 HOH B 514  HOH B 516                                          
SITE     1 AC5 17 GLU B 143  GLU B 215  ASP B 216  PHE B 218                    
SITE     2 AC5 17 VAL B 226  THR B 228  THR B 256  GLY B 257                    
SITE     3 AC5 17 GLU B 259  PHE B 261  ARG B 262  ARG B 269                    
SITE     4 AC5 17 ASN B 273  VAL B 274  GLY B 275  LEU B 277                    
SITE     5 AC5 17 HOH C 101                                                     
SITE     1 AC6 17 GLU A 143  ILE A 206  GLU A 215  ASP A 216                    
SITE     2 AC6 17 PHE A 218  THR A 228  THR A 256  GLY A 257                    
SITE     3 AC6 17 GLU A 259  MET A 260  PHE A 261  ARG A 262                    
SITE     4 AC6 17 ARG A 269  ASN A 273  VAL A 274  GLY A 275                    
SITE     5 AC6 17 LEU A 277                                                     
CRYST1   97.246  100.376  156.483  90.00  90.00  90.00 C 2 2 21     16          
ORIGX1      1.000000  0.000000  0.000000        0.00000                         
ORIGX2      0.000000  1.000000  0.000000        0.00000                         
ORIGX3      0.000000  0.000000  1.000000        0.00000                         
SCALE1      0.010283  0.000000  0.000000        0.00000                         
SCALE2      0.000000  0.009963  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.006390        0.00000                         
(ATOM LINES ARE NOT SHOWN.)
END                                                                             
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