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Database: PDB
Entry: 1OB2
LinkDB: 1OB2
Original site: 1OB2 
HEADER    HYDROLASE/NUCLEAR PROTEIN               24-JAN-03   1OB2              
TITLE     E. COLI ELONGATION FACTOR EF-TU COMPLEXED WITH THE                    
TITLE    2 ANTIBIOTIC KIRROMYCIN, A GTP ANALOG, AND PHE-TRNA                    
COMPND    MOL_ID: 1;                                                            
COMPND   2 MOLECULE: ELONGATION FACTOR TU;                                      
COMPND   3 CHAIN: A;                                                            
COMPND   4 SYNONYM: EF-TU, P-43;                                                
COMPND   5 EC: 3.6.1.48;                                                        
COMPND   6 MOL_ID: 2;                                                           
COMPND   7 MOLECULE: TRANSFER-RNA, PHE;                                         
COMPND   8 CHAIN: B;                                                            
COMPND   9 OTHER_DETAILS: AMINO-ACYLATED (PHE) AT THE 3' END                    
SOURCE    MOL_ID: 1;                                                            
SOURCE   2 ORGANISM_SCIENTIFIC: ESCHERICHIA COLI;                               
SOURCE   3 ORGANISM_TAXID: 511693;                                              
SOURCE   4 STRAIN: BL21;                                                        
SOURCE   5 MOL_ID: 2;                                                           
SOURCE   6 ORGANISM_SCIENTIFIC: SACCHAROMYCES CEREVISIAE;                       
SOURCE   7 ORGANISM_COMMON: BAKER'S YEAST;                                      
SOURCE   8 ORGANISM_TAXID: 4932;                                                
SOURCE   9 OTHER_DETAILS: SIGMA-ALDRICH COMPOUND                                
KEYWDS    HYDROLASE/NUCLEAR PROTEIN, HYDROLASE, GTPASE, TRANSLATION             
KEYWDS   2 ELONGATION FACTOR, TRANSFER RNA                                      
EXPDTA    X-RAY DIFFRACTION                                                     
AUTHOR    O.KRISTENSEN,P.NISSEN,J.NYBORG                                        
REVDAT   5   14-NOV-12 1OB2    1       COMPND REMARK VERSN  DBREF               
REVDAT   5 2                           SEQADV MODRES HETSYN FORMUL              
REVDAT   4   24-FEB-09 1OB2    1       VERSN                                    
REVDAT   3   14-JUN-06 1OB2    1       ATOM                                     
REVDAT   2   31-AUG-04 1OB2    1       JRNL                                     
REVDAT   1   27-MAY-04 1OB2    0                                                
JRNL        AUTH   R.C.NIELSEN,O.KRISTENSEN,M.KJELDGAARD,S.THIRUP,              
JRNL        AUTH 2 P.NISSEN                                                     
JRNL        TITL   KIRROMYCIN DEFINES A SPECIFIC DOMAIN ARRANGEMENT             
JRNL        TITL 2 OF ELONGATION FACTOR EF-TU                                   
JRNL        REF    TO BE PUBLISHED                                              
JRNL        REFN                                                                
REMARK   2                                                                      
REMARK   2 RESOLUTION.    3.35 ANGSTROMS.                                       
REMARK   3                                                                      
REMARK   3 REFINEMENT.                                                          
REMARK   3   PROGRAM     : CNS 1.1                                              
REMARK   3   AUTHORS     : BRUNGER,ADAMS,CLORE,DELANO,GROS,GROSSE-              
REMARK   3               : KUNSTLEVE,JIANG,KUSZEWSKI,NILGES,PANNU,              
REMARK   3               : READ,RICE,SIMONSON,WARREN                            
REMARK   3                                                                      
REMARK   3  REFINEMENT TARGET : NULL                                            
REMARK   3                                                                      
REMARK   3  DATA USED IN REFINEMENT.                                            
REMARK   3   RESOLUTION RANGE HIGH (ANGSTROMS) : 3.35                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 47.64                          
REMARK   3   DATA CUTOFF            (SIGMA(F)) : 0.0                            
REMARK   3   DATA CUTOFF HIGH         (ABS(F)) : 6224852.51                     
REMARK   3   DATA CUTOFF LOW          (ABS(F)) : NULL                           
REMARK   3   COMPLETENESS (WORKING+TEST)   (%) : 97.8                           
REMARK   3   NUMBER OF REFLECTIONS             : 18794                          
REMARK   3                                                                      
REMARK   3  FIT TO DATA USED IN REFINEMENT.                                     
REMARK   3   CROSS-VALIDATION METHOD          : THROUGHOUT                      
REMARK   3   FREE R VALUE TEST SET SELECTION  : RANDOM                          
REMARK   3   R VALUE            (WORKING SET) : 0.220                           
REMARK   3   FREE R VALUE                     : 0.265                           
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 5.1                             
REMARK   3   FREE R VALUE TEST SET COUNT      : 963                             
REMARK   3   ESTIMATED ERROR OF FREE R VALUE  : 0.009                           
REMARK   3                                                                      
REMARK   3  FIT IN THE HIGHEST RESOLUTION BIN.                                  
REMARK   3   TOTAL NUMBER OF BINS USED           : 6                            
REMARK   3   BIN RESOLUTION RANGE HIGH       (A) : 3.35                         
REMARK   3   BIN RESOLUTION RANGE LOW        (A) : 3.56                         
REMARK   3   BIN COMPLETENESS (WORKING+TEST) (%) : 99.2                         
REMARK   3   REFLECTIONS IN BIN    (WORKING SET) : 2928                         
REMARK   3   BIN R VALUE           (WORKING SET) : 0.249                        
REMARK   3   BIN FREE R VALUE                    : 0.285                        
REMARK   3   BIN FREE R VALUE TEST SET SIZE  (%) : 5.2                          
REMARK   3   BIN FREE R VALUE TEST SET COUNT     : 162                          
REMARK   3   ESTIMATED ERROR OF BIN FREE R VALUE : 0.022                        
REMARK   3                                                                      
REMARK   3  NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.                    
REMARK   3   PROTEIN ATOMS            : 3035                                    
REMARK   3   NUCLEIC ACID ATOMS       : 1349                                    
REMARK   3   HETEROGEN ATOMS          : 426                                     
REMARK   3   SOLVENT ATOMS            : 0                                       
REMARK   3                                                                      
REMARK   3  B VALUES.                                                           
REMARK   3   FROM WILSON PLOT           (A**2) : 43.0                           
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : 41.6                           
REMARK   3   OVERALL ANISOTROPIC B VALUE.                                       
REMARK   3    B11 (A**2) : 0.61                                                 
REMARK   3    B22 (A**2) : -0.30                                                
REMARK   3    B33 (A**2) : -0.30                                                
REMARK   3    B12 (A**2) : 0.00                                                 
REMARK   3    B13 (A**2) : 0.00                                                 
REMARK   3    B23 (A**2) : 0.00                                                 
REMARK   3                                                                      
REMARK   3  ESTIMATED COORDINATE ERROR.                                         
REMARK   3   ESD FROM LUZZATI PLOT        (A) : 0.37                            
REMARK   3   ESD FROM SIGMAA              (A) : 0.37                            
REMARK   3   LOW RESOLUTION CUTOFF        (A) : 5.00                            
REMARK   3                                                                      
REMARK   3  CROSS-VALIDATED ESTIMATED COORDINATE ERROR.                         
REMARK   3   ESD FROM C-V LUZZATI PLOT    (A) : 0.44                            
REMARK   3   ESD FROM C-V SIGMAA          (A) : 0.40                            
REMARK   3                                                                      
REMARK   3  RMS DEVIATIONS FROM IDEAL VALUES.                                   
REMARK   3   BOND LENGTHS                 (A) : 0.009                           
REMARK   3   BOND ANGLES            (DEGREES) : 1.5                             
REMARK   3   DIHEDRAL ANGLES        (DEGREES) : 27.5                            
REMARK   3   IMPROPER ANGLES        (DEGREES) : 1.35                            
REMARK   3                                                                      
REMARK   3  ISOTROPIC THERMAL MODEL : RESTRAINED                                
REMARK   3                                                                      
REMARK   3  ISOTROPIC THERMAL FACTOR RESTRAINTS.    RMS    SIGMA                
REMARK   3   MAIN-CHAIN BOND              (A**2) : 4.17  ; 1.50                 
REMARK   3   MAIN-CHAIN ANGLE             (A**2) : 6.78  ; 2.00                 
REMARK   3   SIDE-CHAIN BOND              (A**2) : 4.99  ; 2.00                 
REMARK   3   SIDE-CHAIN ANGLE             (A**2) : 7.47  ; 2.50                 
REMARK   3                                                                      
REMARK   3  BULK SOLVENT MODELING.                                              
REMARK   3   METHOD USED : FLAT MODEL                                           
REMARK   3   KSOL        : 0.303178                                             
REMARK   3   BSOL        : 62.1852                                              
REMARK   3                                                                      
REMARK   3  NCS MODEL : NULL                                                    
REMARK   3                                                                      
REMARK   3  NCS RESTRAINTS.                         RMS   SIGMA/WEIGHT          
REMARK   3   GROUP  1  POSITIONAL            (A) : NULL  ; NULL                 
REMARK   3   GROUP  1  B-FACTOR           (A**2) : NULL  ; NULL                 
REMARK   3                                                                      
REMARK   3  PARAMETER FILE  1  : PROTEIN_REP.PARAM                              
REMARK   3  PARAMETER FILE  2  : TRNAPHE-MULTI.PARAM                            
REMARK   3  PARAMETER FILE  3  : LIGANDS_HICUP.PAR                              
REMARK   3  PARAMETER FILE  4  : MG.PAR                                         
REMARK   3  PARAMETER FILE  5  : NULL                                           
REMARK   3  TOPOLOGY FILE  1   : PROTEIN.TOP                                    
REMARK   3  TOPOLOGY FILE  2   : TRNAPHE-MULTI.TOP                              
REMARK   3  TOPOLOGY FILE  3   : LIGANDS_HICUP.TOP                              
REMARK   3  TOPOLOGY FILE  4   : MG.TOP                                         
REMARK   3  TOPOLOGY FILE  5   : NULL                                           
REMARK   3                                                                      
REMARK   3  OTHER REFINEMENT REMARKS: REFINEMENT WAS INITIATED WITH X-PLOR      
REMARK   3  AND COMPLETED WITH CNS. ANTICODON LOOP OF TRNA IS DISORDERED        
REMARK   3  AND ONLY THE CHAIN TRACE IN THIS REGION IS VISIBLE IN THE           
REMARK   3  ELECTRON DENSITY MAPS.                                              
REMARK   4                                                                      
REMARK   4 1OB2 COMPLIES WITH FORMAT V. 3.30, 13-JUL-11                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBE ON 27-JAN-03.                  
REMARK 100 THE PDBE ID CODE IS EBI-12010.                                       
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : 11-JUN-96                          
REMARK 200  TEMPERATURE           (KELVIN) : 100                                
REMARK 200  PH                             : 6.4                                
REMARK 200  NUMBER OF CRYSTALS USED        : 1                                  
REMARK 200                                                                      
REMARK 200  SYNCHROTRON              (Y/N) : Y                                  
REMARK 200  RADIATION SOURCE               : SRS                                
REMARK 200  BEAMLINE                       : PX9.6                              
REMARK 200  X-RAY GENERATOR MODEL          : NULL                               
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M                                  
REMARK 200  WAVELENGTH OR RANGE        (A) : 0.87                               
REMARK 200  MONOCHROMATOR                  : NULL                               
REMARK 200  OPTICS                         : NULL                               
REMARK 200                                                                      
REMARK 200  DETECTOR TYPE                  : IMAGE PLATE                        
REMARK 200  DETECTOR MANUFACTURER          : MARRESEARCH                        
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : DENZO                              
REMARK 200  DATA SCALING SOFTWARE          : AGROVATA                           
REMARK 200                                                                      
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 18794                              
REMARK 200  RESOLUTION RANGE HIGH      (A) : 3.35                               
REMARK 200  RESOLUTION RANGE LOW       (A) : 48.0                               
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : -3.0                               
REMARK 200                                                                      
REMARK 200 OVERALL.                                                             
REMARK 200  COMPLETENESS FOR RANGE     (%) : 98.5                               
REMARK 200  DATA REDUNDANCY                : 5.0                                
REMARK 200  R MERGE                    (I) : 0.154                              
REMARK 200  R SYM                      (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR THE DATA SET  : 10.1                               
REMARK 200                                                                      
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.                                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 3.35                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 3.53                     
REMARK 200  COMPLETENESS FOR SHELL     (%) : 99.5                               
REMARK 200  DATA REDUNDANCY IN SHELL       : 5.1                                
REMARK 200  R MERGE FOR SHELL          (I) : 0.429                              
REMARK 200  R SYM FOR SHELL            (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR SHELL         : 3.0                                
REMARK 200                                                                      
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH                              
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT        
REMARK 200 SOFTWARE USED: AMORE                                                 
REMARK 200 STARTING MODEL: PDB ENTRY 1TTT                                       
REMARK 200                                                                      
REMARK 200 REMARK: NULL                                                         
REMARK 280                                                                      
REMARK 280 CRYSTAL                                                              
REMARK 280 SOLVENT CONTENT, VS  (%): 70                                         
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 4.51                     
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: 1.8M AMMONIUM SULPHATE,                  
REMARK 280  10 MM MAGNESIUM CHLORIDE, 20 MM TRIS-MES, PH 6.4                    
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY                                            
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 41 3 2                         
REMARK 290                                                                      
REMARK 290      SYMOP   SYMMETRY                                                
REMARK 290     NNNMMM   OPERATOR                                                
REMARK 290       1555   X,Y,Z                                                   
REMARK 290       2555   -X+1/2,-Y,Z+1/2                                         
REMARK 290       3555   -X,Y+1/2,-Z+1/2                                         
REMARK 290       4555   X+1/2,-Y+1/2,-Z                                         
REMARK 290       5555   Z,X,Y                                                   
REMARK 290       6555   Z+1/2,-X+1/2,-Y                                         
REMARK 290       7555   -Z+1/2,-X,Y+1/2                                         
REMARK 290       8555   -Z,X+1/2,-Y+1/2                                         
REMARK 290       9555   Y,Z,X                                                   
REMARK 290      10555   -Y,Z+1/2,-X+1/2                                         
REMARK 290      11555   Y+1/2,-Z+1/2,-X                                         
REMARK 290      12555   -Y+1/2,-Z,X+1/2                                         
REMARK 290      13555   Y+3/4,X+1/4,-Z+1/4                                      
REMARK 290      14555   -Y+3/4,-X+3/4,-Z+3/4                                    
REMARK 290      15555   Y+1/4,-X+1/4,Z+3/4                                      
REMARK 290      16555   -Y+1/4,X+3/4,Z+1/4                                      
REMARK 290      17555   X+3/4,Z+1/4,-Y+1/4                                      
REMARK 290      18555   -X+1/4,Z+3/4,Y+1/4                                      
REMARK 290      19555   -X+3/4,-Z+3/4,-Y+3/4                                    
REMARK 290      20555   X+1/4,-Z+1/4,Y+3/4                                      
REMARK 290      21555   Z+3/4,Y+1/4,-X+1/4                                      
REMARK 290      22555   Z+1/4,-Y+1/4,X+3/4                                      
REMARK 290      23555   -Z+1/4,Y+3/4,X+1/4                                      
REMARK 290      24555   -Z+3/4,-Y+3/4,-X+3/4                                    
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       98.20500            
REMARK 290   SMTRY2   2  0.000000 -1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   2  0.000000  0.000000  1.000000       98.20500            
REMARK 290   SMTRY1   3 -1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   3  0.000000  1.000000  0.000000       98.20500            
REMARK 290   SMTRY3   3  0.000000  0.000000 -1.000000       98.20500            
REMARK 290   SMTRY1   4  1.000000  0.000000  0.000000       98.20500            
REMARK 290   SMTRY2   4  0.000000 -1.000000  0.000000       98.20500            
REMARK 290   SMTRY3   4  0.000000  0.000000 -1.000000        0.00000            
REMARK 290   SMTRY1   5  0.000000  0.000000  1.000000        0.00000            
REMARK 290   SMTRY2   5  1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY3   5  0.000000  1.000000  0.000000        0.00000            
REMARK 290   SMTRY1   6  0.000000  0.000000  1.000000       98.20500            
REMARK 290   SMTRY2   6 -1.000000  0.000000  0.000000       98.20500            
REMARK 290   SMTRY3   6  0.000000 -1.000000  0.000000        0.00000            
REMARK 290   SMTRY1   7  0.000000  0.000000 -1.000000       98.20500            
REMARK 290   SMTRY2   7 -1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY3   7  0.000000  1.000000  0.000000       98.20500            
REMARK 290   SMTRY1   8  0.000000  0.000000 -1.000000        0.00000            
REMARK 290   SMTRY2   8  1.000000  0.000000  0.000000       98.20500            
REMARK 290   SMTRY3   8  0.000000 -1.000000  0.000000       98.20500            
REMARK 290   SMTRY1   9  0.000000  1.000000  0.000000        0.00000            
REMARK 290   SMTRY2   9  0.000000  0.000000  1.000000        0.00000            
REMARK 290   SMTRY3   9  1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY1  10  0.000000 -1.000000  0.000000        0.00000            
REMARK 290   SMTRY2  10  0.000000  0.000000  1.000000       98.20500            
REMARK 290   SMTRY3  10 -1.000000  0.000000  0.000000       98.20500            
REMARK 290   SMTRY1  11  0.000000  1.000000  0.000000       98.20500            
REMARK 290   SMTRY2  11  0.000000  0.000000 -1.000000       98.20500            
REMARK 290   SMTRY3  11 -1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY1  12  0.000000 -1.000000  0.000000       98.20500            
REMARK 290   SMTRY2  12  0.000000  0.000000 -1.000000        0.00000            
REMARK 290   SMTRY3  12  1.000000  0.000000  0.000000       98.20500            
REMARK 290   SMTRY1  13  0.000000  1.000000  0.000000      147.30750            
REMARK 290   SMTRY2  13  1.000000  0.000000  0.000000       49.10250            
REMARK 290   SMTRY3  13  0.000000  0.000000 -1.000000       49.10250            
REMARK 290   SMTRY1  14  0.000000 -1.000000  0.000000      147.30750            
REMARK 290   SMTRY2  14 -1.000000  0.000000  0.000000      147.30750            
REMARK 290   SMTRY3  14  0.000000  0.000000 -1.000000      147.30750            
REMARK 290   SMTRY1  15  0.000000  1.000000  0.000000       49.10250            
REMARK 290   SMTRY2  15 -1.000000  0.000000  0.000000       49.10250            
REMARK 290   SMTRY3  15  0.000000  0.000000  1.000000      147.30750            
REMARK 290   SMTRY1  16  0.000000 -1.000000  0.000000       49.10250            
REMARK 290   SMTRY2  16  1.000000  0.000000  0.000000      147.30750            
REMARK 290   SMTRY3  16  0.000000  0.000000  1.000000       49.10250            
REMARK 290   SMTRY1  17  1.000000  0.000000  0.000000      147.30750            
REMARK 290   SMTRY2  17  0.000000  0.000000  1.000000       49.10250            
REMARK 290   SMTRY3  17  0.000000 -1.000000  0.000000       49.10250            
REMARK 290   SMTRY1  18 -1.000000  0.000000  0.000000       49.10250            
REMARK 290   SMTRY2  18  0.000000  0.000000  1.000000      147.30750            
REMARK 290   SMTRY3  18  0.000000  1.000000  0.000000       49.10250            
REMARK 290   SMTRY1  19 -1.000000  0.000000  0.000000      147.30750            
REMARK 290   SMTRY2  19  0.000000  0.000000 -1.000000      147.30750            
REMARK 290   SMTRY3  19  0.000000 -1.000000  0.000000      147.30750            
REMARK 290   SMTRY1  20  1.000000  0.000000  0.000000       49.10250            
REMARK 290   SMTRY2  20  0.000000  0.000000 -1.000000       49.10250            
REMARK 290   SMTRY3  20  0.000000  1.000000  0.000000      147.30750            
REMARK 290   SMTRY1  21  0.000000  0.000000  1.000000      147.30750            
REMARK 290   SMTRY2  21  0.000000  1.000000  0.000000       49.10250            
REMARK 290   SMTRY3  21 -1.000000  0.000000  0.000000       49.10250            
REMARK 290   SMTRY1  22  0.000000  0.000000  1.000000       49.10250            
REMARK 290   SMTRY2  22  0.000000 -1.000000  0.000000       49.10250            
REMARK 290   SMTRY3  22  1.000000  0.000000  0.000000      147.30750            
REMARK 290   SMTRY1  23  0.000000  0.000000 -1.000000       49.10250            
REMARK 290   SMTRY2  23  0.000000  1.000000  0.000000      147.30750            
REMARK 290   SMTRY3  23  1.000000  0.000000  0.000000       49.10250            
REMARK 290   SMTRY1  24  0.000000  0.000000 -1.000000      147.30750            
REMARK 290   SMTRY2  24  0.000000 -1.000000  0.000000      147.30750            
REMARK 290   SMTRY3  24 -1.000000  0.000000  0.000000      147.30750            
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: 11980 ANGSTROM**2                         
REMARK 350 SURFACE AREA OF THE COMPLEX: 27380 ANGSTROM**2                       
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -37.6 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 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      G B   1   OP3     G B   1   P      -0.084                       
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    GLU A   3     -129.69    -68.66                                   
REMARK 500    LYS A   4      -45.74   -160.53                                   
REMARK 500    PHE A   5       98.38     57.34                                   
REMARK 500    THR A   8      135.08    175.64                                   
REMARK 500    LYS A   9      155.67     65.24                                   
REMARK 500    ASP A  21        3.93     34.07                                   
REMARK 500    LYS A  24      -91.78      4.37                                   
REMARK 500    ALA A  30      -74.38    -40.92                                   
REMARK 500    VAL A  34      -72.26    -59.12                                   
REMARK 500    ALA A  36       23.45    -71.65                                   
REMARK 500    LYS A  37      -56.53   -155.20                                   
REMARK 500    THR A  38        7.33    -63.02                                   
REMARK 500    TYR A  39        7.63   -170.83                                   
REMARK 500    ALA A  42      106.94    177.33                                   
REMARK 500    ASP A  47      -33.26    -35.12                                   
REMARK 500    ASP A  50       54.97    -93.78                                   
REMARK 500    ILE A  60        0.14   -153.56                                   
REMARK 500    THR A  61      109.05     61.55                                   
REMARK 500    THR A  71     -167.93   -105.01                                   
REMARK 500    VAL A 127      113.76     15.67                                   
REMARK 500    ASP A 142       69.29   -174.18                                   
REMARK 500    GLU A 143      -16.21    -32.93                                   
REMARK 500    GLU A 155      -35.66    -38.02                                   
REMARK 500    LEU A 156      -71.67    -65.94                                   
REMARK 500    LEU A 157      -71.17    -33.78                                   
REMARK 500    SER A 158       -1.27    -51.31                                   
REMARK 500    ASP A 161       60.41     87.33                                   
REMARK 500    ASP A 166       -9.08    -56.43                                   
REMARK 500    ALA A 177      -74.66    -47.56                                   
REMARK 500    LEU A 178      -36.43    -31.68                                   
REMARK 500    ASP A 181      103.39    -40.41                                   
REMARK 500    ALA A 192       -7.80    -54.29                                   
REMARK 500    ILE A 199      -92.62     -7.10                                   
REMARK 500    GLU A 201      124.89     23.62                                   
REMARK 500    ALA A 205      -75.86    -53.38                                   
REMARK 500    ILE A 206      -40.80     52.85                                   
REMARK 500    ASP A 207       25.36    -75.22                                   
REMARK 500    LEU A 211      128.35   -174.50                                   
REMARK 500    ASP A 216      144.08   -172.93                                   
REMARK 500    ARG A 223      -93.40    -89.87                                   
REMARK 500    ILE A 247      -60.61     68.75                                   
REMARK 500    THR A 256       18.46   -149.91                                   
REMARK 500    PHE A 261       73.58     65.43                                   
REMARK 500    ARG A 262       13.41     47.34                                   
REMARK 500    LEU A 264      150.50    -35.85                                   
REMARK 500    ALA A 270      137.42    -33.52                                   
REMARK 500    LEU A 278      100.47     39.70                                   
REMARK 500    GLU A 285       -3.52   -152.03                                   
REMARK 500    ASP A 314       -1.09    -55.55                                   
REMARK 500    ARG A 333     -112.55     58.52                                   
REMARK 500                                                                      
REMARK 500 THIS ENTRY HAS      51 RAMACHANDRAN OUTLIERS.                        
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: PLANAR GROUPS                                              
REMARK 500                                                                      
REMARK 500 PLANAR GROUPS IN THE FOLLOWING RESIDUES HAVE A TOTAL                 
REMARK 500 RMS DISTANCE OF ALL ATOMS FROM THE BEST-FIT PLANE                    
REMARK 500 BY MORE THAN AN EXPECTED VALUE OF 6*RMSD, WITH AN                    
REMARK 500 RMSD 0.02 ANGSTROMS, OR AT LEAST ONE ATOM HAS                        
REMARK 500 AN RMSD GREATER THAN THIS VALUE                                      
REMARK 500 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;               
REMARK 500 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).                             
REMARK 500                                                                      
REMARK 500  M RES CSSEQI        RMS     TYPE                                    
REMARK 500      U B   8         0.07    SIDE CHAIN                              
REMARK 500      G B  22         0.06    SIDE CHAIN                              
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    HIS A  22        24.9      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 A1398  MG                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 THR A  25   OG1                                                    
REMARK 620 2 GNP A1397   O1G 107.7                                              
REMARK 620 3 GNP A1397   O2B  77.3  79.1                                        
REMARK 620 4 THR A  61   OG1  74.8 100.1 150.3                                  
REMARK 620 5 GNP A1397   O3G 164.9  57.4 100.6 103.8                            
REMARK 620 6 GNP A1397   O2A  98.5 132.4  68.6 125.3  94.5                      
REMARK 620 N                    1     2     3     4     5                       
REMARK 700                                                                      
REMARK 700 SHEET                                                                
REMARK 700 DETERMINATION METHOD: DSSP                                           
REMARK 700 THE SHEETS PRESENTED AS "AD" IN EACH CHAIN ON SHEET RECORDS          
REMARK 700 BELOW IS ACTUALLY AN  6-STRANDED BARREL THIS IS REPRESENTED BY       
REMARK 700 A  7-STRANDED SHEET IN WHICH THE FIRST AND LAST STRANDS              
REMARK 700 ARE IDENTICAL.                                                       
REMARK 800                                                                      
REMARK 800 SITE                                                                 
REMARK 800 SITE_IDENTIFIER: AC1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE KIR A1394                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SUC A1396                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE GNP A1397                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC4                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE  MG A1398                 
REMARK 900                                                                      
REMARK 900 RELATED ENTRIES                                                      
REMARK 900 RELATED ID: 1D8T   RELATED DB: PDB                                   
REMARK 900  CRYSTAL STRUCTURE OF ELONGATION FACTOR, TU (                        
REMARK 900  EF-TU-MGGDP) COMPLEXED WITH GE2270A, A                              
REMARK 900  THIAZOLYL PEPTIDE ANTIBIOTIC                                        
REMARK 900 RELATED ID: 1DG1   RELATED DB: PDB                                   
REMARK 900  WHOLE, UNMODIFIED, EF-TU(ELONGATION FACTOR                          
REMARK 900  TU).                                                                
REMARK 900 RELATED ID: 1EFC   RELATED DB: PDB                                   
REMARK 900  INTACT ELONGATION FACTOR FROM E.COLI                                
REMARK 900 RELATED ID: 1EFM   RELATED DB: PDB                                   
REMARK 900  TRYPSIN-MODIFIED ELONGATION FACTOR TU (EF-TU                        
REMARK 900  -GDP)                                                               
REMARK 900 RELATED ID: 1EFU   RELATED DB: PDB                                   
REMARK 900  ELONGATION FACTOR COMPLEX EF-TU/EF-TS FROM                          
REMARK 900   ESCHERICHIA COLI                                                   
REMARK 900 RELATED ID: 1ETU   RELATED DB: PDB                                   
REMARK 900  ELONGATION FACTOR TU (DOMAIN I) - GUANOSINE                         
REMARK 900  DIPHOSPHATE COMPLEX                                                 
REMARK 900 RELATED ID: 1LS2   RELATED DB: PDB                                   
REMARK 900  FITTING OF EF-TU AND TRNA IN THE LOW                                
REMARK 900  RESOLUTION CRYO-EM MAPOF AN EF-TU TERNARY                           
REMARK 900   COMPLEX (GDP AND KIRROMYCIN) BOUND TOE.                            
REMARK 900  COLI 70S RIBOSOME                                                   
REMARK 900 RELATED ID: 1QZD   RELATED DB: PDB                                   
REMARK 900  EF-TU.KIRROMYCIN COORDINATES FITTED INTO THE                        
REMARK 900   CRYO-EM MAP OFEF-TU TERNARY COMPLEX (GDP                           
REMARK 900  .KIRROMYCIN) BOUND 70S RIBOSOME                                     
DBREF  1OB2 A    1   393  UNP    P0CE48   EFTU2_ECOLI      2     394            
DBREF  1OB2 B    1    77  PDB    1OB2     1OB2             1     77             
SEQADV 1OB2 ALA A    1  UNP  P0CE48    SER     2 CONFLICT                       
SEQRES   1 A  393  ALA LYS GLU LYS PHE GLU ARG THR LYS PRO HIS VAL ASN          
SEQRES   2 A  393  VAL GLY THR ILE GLY HIS VAL ASP HIS GLY LYS THR THR          
SEQRES   3 A  393  LEU THR ALA ALA ILE THR THR VAL LEU ALA LYS THR TYR          
SEQRES   4 A  393  GLY GLY ALA ALA ARG ALA PHE ASP GLN ILE ASP ASN ALA          
SEQRES   5 A  393  PRO GLU GLU LYS ALA ARG GLY ILE THR ILE ASN THR SER          
SEQRES   6 A  393  HIS VAL GLU TYR ASP THR PRO THR ARG HIS TYR ALA HIS          
SEQRES   7 A  393  VAL ASP CYS PRO GLY HIS ALA ASP TYR VAL LYS ASN MET          
SEQRES   8 A  393  ILE THR GLY ALA ALA GLN MET ASP GLY ALA ILE LEU VAL          
SEQRES   9 A  393  VAL ALA ALA THR ASP GLY PRO MET PRO GLN THR ARG GLU          
SEQRES  10 A  393  HIS ILE LEU LEU GLY ARG GLN VAL GLY VAL PRO TYR ILE          
SEQRES  11 A  393  ILE VAL PHE LEU ASN LYS CYS ASP MET VAL ASP ASP GLU          
SEQRES  12 A  393  GLU LEU LEU GLU LEU VAL GLU MET GLU VAL ARG GLU LEU          
SEQRES  13 A  393  LEU SER GLN TYR ASP PHE PRO GLY ASP ASP THR PRO ILE          
SEQRES  14 A  393  VAL ARG GLY SER ALA LEU LYS ALA LEU GLU GLY ASP ALA          
SEQRES  15 A  393  GLU TRP GLU ALA LYS ILE LEU GLU LEU ALA GLY PHE LEU          
SEQRES  16 A  393  ASP SER TYR ILE PRO GLU PRO GLU ARG ALA ILE ASP LYS          
SEQRES  17 A  393  PRO PHE LEU LEU PRO ILE GLU ASP VAL PHE SER ILE SER          
SEQRES  18 A  393  GLY ARG GLY THR VAL VAL THR GLY ARG VAL GLU ARG GLY          
SEQRES  19 A  393  ILE ILE LYS VAL GLY GLU GLU VAL GLU ILE VAL GLY ILE          
SEQRES  20 A  393  LYS GLU THR GLN LYS SER THR CYS THR GLY VAL GLU MET          
SEQRES  21 A  393  PHE ARG LYS LEU LEU ASP GLU GLY ARG ALA GLY GLU ASN          
SEQRES  22 A  393  VAL GLY VAL LEU LEU ARG GLY ILE LYS ARG GLU GLU ILE          
SEQRES  23 A  393  GLU ARG GLY GLN VAL LEU ALA LYS PRO GLY THR ILE LYS          
SEQRES  24 A  393  PRO HIS THR LYS PHE GLU SER GLU VAL TYR ILE LEU SER          
SEQRES  25 A  393  LYS ASP GLU GLY GLY ARG HIS THR PRO PHE PHE LYS GLY          
SEQRES  26 A  393  TYR ARG PRO GLN PHE TYR PHE ARG THR THR ASP VAL THR          
SEQRES  27 A  393  GLY THR ILE GLU LEU PRO GLU GLY VAL GLU MET VAL MET          
SEQRES  28 A  393  PRO GLY ASP ASN ILE LYS MET VAL VAL THR LEU ILE HIS          
SEQRES  29 A  393  PRO ILE ALA MET ASP ASP GLY LEU ARG PHE ALA ILE ARG          
SEQRES  30 A  393  GLU GLY GLY ARG THR VAL GLY ALA GLY VAL VAL ALA LYS          
SEQRES  31 A  393  VAL LEU SER                                                  
SEQRES   1 B   77    G   C   G   G   A   U   U   U   A 2MG   C   U   C          
SEQRES   2 B   77    A   G H2U H2U   G   G   G   A   G   A   G   C M2G          
SEQRES   3 B   77    C   C   A   G   A OMC   U OMG   A   A  YG   A PSU          
SEQRES   4 B   77  5MC   U   G   G   A   G 7MG   U   C 5MC   U   G   U          
SEQRES   5 B   77    G   U PSU   C   G MAD   U   C   C   A   C   A   G          
SEQRES   6 B   77    A   A   U   U   C   G   C   A   C   C   A PHA              
MODRES 1OB2 2MG B   10    G  2N-METHYLGUANOSINE-5'-MONOPHOSPHATE                
MODRES 1OB2 H2U B   16    U  5,6-DIHYDROURIDINE-5'-MONOPHOSPHATE                
MODRES 1OB2 H2U B   17    U  5,6-DIHYDROURIDINE-5'-MONOPHOSPHATE                
MODRES 1OB2 M2G B   26    G  N2-DIMETHYLGUANOSINE-5'-MONOPHOSPHATE              
MODRES 1OB2 OMC B   32    C  O2'-METHYLYCYTIDINE-5'-MONOPHOSPHATE               
MODRES 1OB2 OMG B   34    G  O2'-METHYLGUANOSINE-5'-MONOPHOSPHATE               
MODRES 1OB2  YG B   37    G  WYBUTOSINE                                         
MODRES 1OB2 PSU B   39    U  PSEUDOURIDINE-5'-MONOPHOSPHATE                     
MODRES 1OB2 5MC B   40    C  5-METHYLCYTIDINE-5'-MONOPHOSPHATE                  
MODRES 1OB2 7MG B   46    G  7N-METHYL-8-HYDROGUANOSINE-5'-MONOPHOSPHATE        
MODRES 1OB2 5MC B   49    C  5-METHYLCYTIDINE-5'-MONOPHOSPHATE                  
MODRES 1OB2 PSU B   55    U  PSEUDOURIDINE-5'-MONOPHOSPHATE                     
MODRES 1OB2 MAD B   58    A  6-HYDRO-1-METHYLADENOSINE-5'-MONOPHOSPHATE         
MODRES 1OB2 PHA B   77  PHE  PHENYLALANINAL                                     
HET    KIR  A1394      57                                                       
HET    2MG  B  10      24                                                       
HET    H2U  B  16      20                                                       
HET    H2U  B  17      20                                                       
HET    M2G  B  26      25                                                       
HET    OMC  B  32      21                                                       
HET    OMG  B  34      24                                                       
HET     YG  B  37      39                                                       
HET    PSU  B  39      20                                                       
HET    5MC  B  40      21                                                       
HET    7MG  B  46      24                                                       
HET    5MC  B  49      21                                                       
HET    PSU  B  55      20                                                       
HET    MAD  B  58      23                                                       
HET    PHA  B  77      11                                                       
HET    SUC  A1396      23                                                       
HET    GNP  A1397      32                                                       
HET     MG  A1398       1                                                       
HETNAM     KIR KIRROMYCIN                                                       
HETNAM     2MG 2N-METHYLGUANOSINE-5'-MONOPHOSPHATE                              
HETNAM     H2U 5,6-DIHYDROURIDINE-5'-MONOPHOSPHATE                              
HETNAM     M2G N2-DIMETHYLGUANOSINE-5'-MONOPHOSPHATE                            
HETNAM     OMC O2'-METHYLYCYTIDINE-5'-MONOPHOSPHATE                             
HETNAM     OMG O2'-METHYLGUANOSINE-5'-MONOPHOSPHATE                             
HETNAM      YG WYBUTOSINE                                                       
HETNAM     PSU PSEUDOURIDINE-5'-MONOPHOSPHATE                                   
HETNAM     5MC 5-METHYLCYTIDINE-5'-MONOPHOSPHATE                                
HETNAM     7MG 7N-METHYL-8-HYDROGUANOSINE-5'-MONOPHOSPHATE                      
HETNAM     PHA PHENYLALANINAL                                                   
HETNAM     SUC SUCROSE                                                          
HETNAM     GNP PHOSPHOAMINOPHOSPHONIC ACID-GUANYLATE ESTER                      
HETNAM      MG MAGNESIUM ION                                                    
HETNAM     MAD 6-HYDRO-1-METHYLADENOSINE-5'-MONOPHOSPHATE                       
HETSYN      YG Y-BASE; 1H-IMIDAZO(1,2-ALPHA)PURINE-7-BUTANOIC ACID,4,           
HETSYN   2  YG  9-DIHYDRO-ALPHA-((METHOXYCARBONYL)AMINO)-4,6-DIMETHYL-          
HETSYN   3  YG  9-OXO-METHYL ESTER                                              
HETSYN     KIR MOCIMYCIN; DELVOMYCIN; MYC-8003                                  
FORMUL   3  KIR    C43 H60 N2 O12                                               
FORMUL   4  2MG    C11 H16 N5 O8 P                                              
FORMUL   5  H2U    2(C9 H15 N2 O9 P)                                            
FORMUL   6  M2G    C12 H18 N5 O8 P                                              
FORMUL   7  OMC    C10 H16 N3 O8 P                                              
FORMUL   8  OMG    C11 H16 N5 O8 P                                              
FORMUL   9   YG    C21 H29 N6 O12 P                                             
FORMUL  10  PSU    2(C9 H13 N2 O9 P)                                            
FORMUL  11  5MC    2(C10 H16 N3 O8 P)                                           
FORMUL  12  7MG    C11 H18 N5 O8 P                                              
FORMUL  13  PHA    C9 H11 N O                                                   
FORMUL  14  SUC    C12 H22 O11                                                  
FORMUL  15  GNP    C10 H17 N6 O13 P3                                            
FORMUL  16   MG    MG 2+                                                        
FORMUL  17  MAD    C11 H16 N5 O7 P                                              
HELIX    1   1 GLY A   23  TYR A   39  1                                  17    
HELIX    2   2 ALA A   45  ASP A   50  1                                   6    
HELIX    3   3 ALA A   52  GLY A   59  1                                   8    
HELIX    4   4 HIS A   84  ASP A   86  5                                   3    
HELIX    5   5 TYR A   87  GLN A   97  1                                  11    
HELIX    6   6 MET A  112  VAL A  125  1                                  14    
HELIX    7   7 LYS A  136  VAL A  140  5                                   5    
HELIX    8   8 ASP A  142  ASP A  161  1                                  20    
HELIX    9   9 SER A  173  GLY A  180  1                                   8    
HELIX   10  10 ASP A  181  GLY A  193  1                                  13    
HELIX   11  11 GLY A  193  TYR A  198  1                                   6    
HELIX   12  12 LYS A  282  ILE A  286  5                                   5    
HELIX   13  13 SER A  312  GLY A  316  5                                   5    
SHEET    1  AA 6 SER A  65  ASP A  70  0                                        
SHEET    2  AA 6 HIS A  75  ASP A  80 -1  O  TYR A  76   N  TYR A  69           
SHEET    3  AA 6 HIS A  11  ILE A  17  1  O  VAL A  12   N  ALA A  77           
SHEET    4  AA 6 ALA A 101  ALA A 106  1  O  ILE A 102   N  ILE A  17           
SHEET    5  AA 6 ILE A 130  ASN A 135  1  O  ILE A 131   N  LEU A 103           
SHEET    6  AA 6 ILE A 169  ARG A 171  1  O  VAL A 170   N  LEU A 134           
SHEET    1  AB 4 LEU A 211  PRO A 213  0                                        
SHEET    2  AB 4 VAL A 291  ALA A 293 -1  O  LEU A 292   N  LEU A 212           
SHEET    3  AB 4 GLU A 241  VAL A 245 -1  O  GLU A 243   N  ALA A 293           
SHEET    4  AB 4 GLN A 251  THR A 254 -1  O  GLN A 251   N  ILE A 244           
SHEET    1  AC 3 ASP A 216  SER A 219  0                                        
SHEET    2  AC 3 THR A 225  ARG A 230 -1  O  VAL A 226   N  PHE A 218           
SHEET    3  AC 3 ASN A 273  VAL A 276 -1  O  VAL A 274   N  GLY A 229           
SHEET    1  AD 7 PRO A 300  TYR A 309  0                                        
SHEET    2  AD 7 ASN A 355  ALA A 367 -1  O  ILE A 356   N  VAL A 308           
SHEET    3  AD 7 THR A 335  THR A 340 -1  O  THR A 338   N  ILE A 363           
SHEET    4  AD 7 GLN A 329  PHE A 332 -1  O  PHE A 330   N  VAL A 337           
SHEET    5  AD 7 ARG A 373  GLU A 378 -1  O  ALA A 375   N  TYR A 331           
SHEET    6  AD 7 ARG A 381  VAL A 391 -1  O  ARG A 381   N  GLU A 378           
SHEET    7  AD 7 PRO A 300  TYR A 309 -1  O  GLU A 305   N  LYS A 390           
LINK        MG    MG A1398                 OG1 THR A  25     1555   1555  2.03  
LINK        MG    MG A1398                 O1G GNP A1397     1555   1555  1.86  
LINK        MG    MG A1398                 O2B GNP A1397     1555   1555  2.34  
LINK        MG    MG A1398                 O2A GNP A1397     1555   1555  2.84  
LINK        MG    MG A1398                 O3G GNP A1397     1555   1555  2.83  
LINK        MG    MG A1398                 OG1 THR A  61     1555   1555  2.53  
LINK         O3'   A B   9                 P   2MG B  10     1555   1555  1.60  
LINK         O3' 2MG B  10                 P     C B  11     1555   1555  1.61  
LINK         O3'   G B  15                 P   H2U B  16     1555   1555  1.61  
LINK         O3' H2U B  16                 P   H2U B  17     1555   1555  1.61  
LINK         O3' H2U B  17                 P     G B  18     1555   1555  1.61  
LINK         O3'   C B  25                 P   M2G B  26     1555   1555  1.61  
LINK         O3' M2G B  26                 P     C B  27     1555   1555  1.61  
LINK         O3'   A B  31                 P   OMC B  32     1555   1555  1.61  
LINK         O3' OMC B  32                 P     U B  33     1555   1555  1.61  
LINK         O3'   U B  33                 P   OMG B  34     1555   1555  1.61  
LINK         O3' OMG B  34                 P     A B  35     1555   1555  1.61  
LINK         O3'   A B  36                 P    YG B  37     1555   1555  1.61  
LINK         O3'  YG B  37                 P     A B  38     1555   1555  1.61  
LINK         O3'   A B  38                 P   PSU B  39     1555   1555  1.61  
LINK         O3' PSU B  39                 P   5MC B  40     1555   1555  1.61  
LINK         O3' 5MC B  40                 P     U B  41     1555   1555  1.61  
LINK         O3'   G B  45                 P   7MG B  46     1555   1555  1.61  
LINK         O3' 7MG B  46                 P     U B  47     1555   1555  1.61  
LINK         O3'   C B  48                 P   5MC B  49     1555   1555  1.60  
LINK         O3' 5MC B  49                 P     U B  50     1555   1555  1.61  
LINK         O3'   U B  54                 P   PSU B  55     1555   1555  1.60  
LINK         O3' PSU B  55                 P     C B  56     1555   1555  1.61  
LINK         O3'   G B  57                 P   MAD B  58     1555   1555  1.60  
LINK         O3' MAD B  58                 P     U B  59     1555   1555  1.60  
LINK         O3'   A B  76                 C   PHA B  77     1555   1555  1.31  
CISPEP   1 ILE A  199    PRO A  200          0         0.25                     
SITE     1 AC1 14 LEU A 120  ARG A 123  GLN A 124  VAL A 125                    
SITE     2 AC1 14 TYR A 160  ASP A 161  LYS A 313  ASP A 314                    
SITE     3 AC1 14 GLU A 315  ARG A 333  ARG A 373  PHE A 374                    
SITE     4 AC1 14 ALA A 375  ALA A 385                                          
SITE     1 AC2 11 GLU A   3  PHE A   5  GLU A   6  THR A   8                    
SITE     2 AC2 11 LYS A   9  TYR A  39  GLY A  40  GLU A  68                    
SITE     3 AC2 11 ASP A  70  HIS A  75  LYS A 263                               
SITE     1 AC3 20 VAL A  20  ASP A  21  HIS A  22  GLY A  23                    
SITE     2 AC3 20 LYS A  24  THR A  25  THR A  26  PHE A  46                    
SITE     3 AC3 20 ILE A  60  THR A  61  GLY A  83  HIS A  84                    
SITE     4 AC3 20 ASN A 135  LYS A 136  ASP A 138  MET A 139                    
SITE     5 AC3 20 SER A 173  ALA A 174  LEU A 175   MG A1398                    
SITE     1 AC4  3 THR A  25  THR A  61  GNP A1397                               
CRYST1  196.410  196.410  196.410  90.00  90.00  90.00 P 41 3 2     24          
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      0.005091  0.000000  0.000000        0.00000                         
SCALE2      0.000000  0.005091  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.005091        0.00000                         
(ATOM LINES ARE NOT SHOWN.)
END                                                                             
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