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Database: PDB
Entry: 1EFU
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Original site: 1EFU 
HEADER    COMPLEX (TWO ELONGATION FACTORS)        09-JUL-96   1EFU              
TITLE     ELONGATION FACTOR COMPLEX EF-TU/EF-TS FROM ESCHERICHIA COLI           
COMPND    MOL_ID: 1;                                                            
COMPND   2 MOLECULE: ELONGATION FACTOR TU;                                      
COMPND   3 CHAIN: A, C;                                                         
COMPND   4 SYNONYM: ELONGATION FACTOR FOR TRANSFER, HEAT UNSTABLE, EF-          
COMPND   5 TU;                                                                  
COMPND   6 ENGINEERED: YES;                                                     
COMPND   7 MOL_ID: 2;                                                           
COMPND   8 MOLECULE: ELONGATION FACTOR TS;                                      
COMPND   9 CHAIN: B, D;                                                         
COMPND  10 SYNONYM: ELONGATION FACTOR FOR TRANSFER, HEAT STABLE, EF-            
COMPND  11 TS;                                                                  
COMPND  12 ENGINEERED: YES                                                      
SOURCE    MOL_ID: 1;                                                            
SOURCE   2 ORGANISM_SCIENTIFIC: ESCHERICHIA COLI;                               
SOURCE   3 ORGANISM_TAXID: 562;                                                 
SOURCE   4 STRAIN: N4830-1;                                                     
SOURCE   5 EXPRESSION_SYSTEM: ESCHERICHIA COLI;                                 
SOURCE   6 EXPRESSION_SYSTEM_TAXID: 562;                                        
SOURCE   7 EXPRESSION_SYSTEM_PLASMID: CPC40;                                    
SOURCE   8 EXPRESSION_SYSTEM_GENE: TSF;                                         
SOURCE   9 MOL_ID: 2;                                                           
SOURCE  10 ORGANISM_SCIENTIFIC: ESCHERICHIA COLI;                               
SOURCE  11 ORGANISM_TAXID: 562;                                                 
SOURCE  12 STRAIN: N4830-1;                                                     
SOURCE  13 EXPRESSION_SYSTEM: ESCHERICHIA COLI;                                 
SOURCE  14 EXPRESSION_SYSTEM_TAXID: 562;                                        
SOURCE  15 EXPRESSION_SYSTEM_PLASMID: CPC40;                                    
SOURCE  16 EXPRESSION_SYSTEM_GENE: TSF;                                         
SOURCE  17 OTHER_DETAILS: THE CPC40 WITH THE TSF GENE INSERTED WAS              
SOURCE  18 USED TO TRANSFORM N4830-1. THIS LEAD TO THE COPURIFICATION           
SOURCE  19 OF EF-TU AND EF-TS.                                                  
KEYWDS    ELONGATION FACTOR, COMPLEX (TWO ELONGATION FACTORS)                   
EXPDTA    X-RAY DIFFRACTION                                                     
AUTHOR    T.KAWASHIMA,C.BERTHET-COLOMINAS,M.WULFF,S.CUSACK,R.LEBERMAN           
REVDAT   2   24-FEB-09 1EFU    1       VERSN                                    
REVDAT   1   11-JAN-97 1EFU    0                                                
JRNL        AUTH   T.KAWASHIMA,C.BERTHET-COLOMINAS,M.WULFF,S.CUSACK,            
JRNL        AUTH 2 R.LEBERMAN                                                   
JRNL        TITL   THE STRUCTURE OF THE ESCHERICHIA COLI EF-TU.EF-TS            
JRNL        TITL 2 COMPLEX AT 2.5 A RESOLUTION.                                 
JRNL        REF    NATURE                        V. 379   511 1996              
JRNL        REFN                   ISSN 0028-0836                               
JRNL        PMID   8596629                                                      
JRNL        DOI    10.1038/379511A0                                             
REMARK   1                                                                      
REMARK   1 REFERENCE 1                                                          
REMARK   1  AUTH   T.KAWASHIMA,C.BERTHET-COLOMINAS,S.CUSACK,R.LEBERMAN          
REMARK   1  TITL   INTERCONVERSION OF CRYSTALS OF THE ESCHERICHIA               
REMARK   1  TITL 2 COLI EF-TU.EF-TS COMPLEX BETWEEN HIGH-AND                    
REMARK   1  TITL 3 LOW-DIFFRACTION FORMS                                        
REMARK   1  REF    ACTA CRYSTALLOGR.,SECT.D      V.  50   799 1996              
REMARK   1  REFN                   ISSN 0907-4449                               
REMARK   2                                                                      
REMARK   2 RESOLUTION.    2.50 ANGSTROMS.                                       
REMARK   3                                                                      
REMARK   3 REFINEMENT.                                                          
REMARK   3   PROGRAM     : X-PLOR                                               
REMARK   3   AUTHORS     : BRUNGER                                              
REMARK   3                                                                      
REMARK   3  DATA USED IN REFINEMENT.                                            
REMARK   3   RESOLUTION RANGE HIGH (ANGSTROMS) : 2.50                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 8.00                           
REMARK   3   DATA CUTOFF            (SIGMA(F)) : 0.000                          
REMARK   3   DATA CUTOFF HIGH         (ABS(F)) : NULL                           
REMARK   3   DATA CUTOFF LOW          (ABS(F)) : NULL                           
REMARK   3   COMPLETENESS (WORKING+TEST)   (%) : NULL                           
REMARK   3   NUMBER OF REFLECTIONS             : 52652                          
REMARK   3                                                                      
REMARK   3  FIT TO DATA USED IN REFINEMENT.                                     
REMARK   3   CROSS-VALIDATION METHOD          : NULL                            
REMARK   3   FREE R VALUE TEST SET SELECTION  : NULL                            
REMARK   3   R VALUE            (WORKING SET) : 0.175                           
REMARK   3   FREE R VALUE                     : 0.283                           
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 5.000                           
REMARK   3   FREE R VALUE TEST SET COUNT      : NULL                            
REMARK   3   ESTIMATED ERROR OF FREE R VALUE  : NULL                            
REMARK   3                                                                      
REMARK   3  FIT IN THE HIGHEST RESOLUTION BIN.                                  
REMARK   3   TOTAL NUMBER OF BINS USED           : NULL                         
REMARK   3   BIN RESOLUTION RANGE HIGH       (A) : 2.50                         
REMARK   3   BIN RESOLUTION RANGE LOW        (A) : 2.61                         
REMARK   3   BIN COMPLETENESS (WORKING+TEST) (%) : 99.20                        
REMARK   3   REFLECTIONS IN BIN    (WORKING SET) : 6155                         
REMARK   3   BIN R VALUE           (WORKING SET) : 0.2762                       
REMARK   3   BIN FREE R VALUE                    : 0.3506                       
REMARK   3   BIN FREE R VALUE TEST SET SIZE  (%) : NULL                         
REMARK   3   BIN FREE R VALUE TEST SET COUNT     : NULL                         
REMARK   3   ESTIMATED ERROR OF BIN FREE R VALUE : NULL                         
REMARK   3                                                                      
REMARK   3  NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.                    
REMARK   3   PROTEIN ATOMS            : 9840                                    
REMARK   3   NUCLEIC ACID ATOMS       : 0                                       
REMARK   3   HETEROGEN ATOMS          : 0                                       
REMARK   3   SOLVENT ATOMS            : 1183                                    
REMARK   3                                                                      
REMARK   3  B VALUES.                                                           
REMARK   3   FROM WILSON PLOT           (A**2) : 47.66                          
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : 37.30                          
REMARK   3   OVERALL ANISOTROPIC B VALUE.                                       
REMARK   3    B11 (A**2) : NULL                                                 
REMARK   3    B22 (A**2) : NULL                                                 
REMARK   3    B33 (A**2) : NULL                                                 
REMARK   3    B12 (A**2) : NULL                                                 
REMARK   3    B13 (A**2) : NULL                                                 
REMARK   3    B23 (A**2) : NULL                                                 
REMARK   3                                                                      
REMARK   3  ESTIMATED COORDINATE ERROR.                                         
REMARK   3   ESD FROM LUZZATI PLOT        (A) : NULL                            
REMARK   3   ESD FROM SIGMAA              (A) : 0.01                            
REMARK   3   LOW RESOLUTION CUTOFF        (A) : NULL                            
REMARK   3                                                                      
REMARK   3  CROSS-VALIDATED ESTIMATED COORDINATE ERROR.                         
REMARK   3   ESD FROM C-V LUZZATI PLOT    (A) : NULL                            
REMARK   3   ESD FROM C-V SIGMAA          (A) : NULL                            
REMARK   3                                                                      
REMARK   3  RMS DEVIATIONS FROM IDEAL VALUES.                                   
REMARK   3   BOND LENGTHS                 (A) : 0.007                           
REMARK   3   BOND ANGLES            (DEGREES) : 1.42                            
REMARK   3   DIHEDRAL ANGLES        (DEGREES) : 23.90                           
REMARK   3   IMPROPER ANGLES        (DEGREES) : 1.25                            
REMARK   3                                                                      
REMARK   3  ISOTROPIC THERMAL MODEL : NULL                                      
REMARK   3                                                                      
REMARK   3  ISOTROPIC THERMAL FACTOR RESTRAINTS.    RMS    SIGMA                
REMARK   3   MAIN-CHAIN BOND              (A**2) : NULL  ; 1.500                
REMARK   3   MAIN-CHAIN ANGLE             (A**2) : NULL  ; 2.000                
REMARK   3   SIDE-CHAIN BOND              (A**2) : NULL  ; 2.000                
REMARK   3   SIDE-CHAIN ANGLE             (A**2) : NULL  ; 2.500                
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  : NULL                                           
REMARK   3  TOPOLOGY FILE  1   : NULL                                           
REMARK   3                                                                      
REMARK   3  OTHER REFINEMENT REMARKS: NULL                                      
REMARK   4                                                                      
REMARK   4 1EFU COMPLIES WITH FORMAT V. 3.15, 01-DEC-08                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY BNL.                                
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : 13-MAR-95                          
REMARK 200  TEMPERATURE           (KELVIN) : 110                                
REMARK 200  PH                             : 7.7                                
REMARK 200  NUMBER OF CRYSTALS USED        : 1                                  
REMARK 200                                                                      
REMARK 200  SYNCHROTRON              (Y/N) : Y                                  
REMARK 200  RADIATION SOURCE               : ESRF                               
REMARK 200  BEAMLINE                       : ID09                               
REMARK 200  X-RAY GENERATOR MODEL          : NULL                               
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M                                  
REMARK 200  WAVELENGTH OR RANGE        (A) : 0.883                              
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 : MOSFLM V. 5.3                      
REMARK 200  DATA SCALING SOFTWARE          : CCP4                               
REMARK 200                                                                      
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 51804                              
REMARK 200  RESOLUTION RANGE HIGH      (A) : 2.480                              
REMARK 200  RESOLUTION RANGE LOW       (A) : 44.280                             
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : 4.000                              
REMARK 200                                                                      
REMARK 200 OVERALL.                                                             
REMARK 200  COMPLETENESS FOR RANGE     (%) : 98.2                               
REMARK 200  DATA REDUNDANCY                : 3.800                              
REMARK 200  R MERGE                    (I) : NULL                               
REMARK 200  R SYM                      (I) : 0.04300                            
REMARK 200  <I/SIGMA(I)> FOR THE DATA SET  : 13.8000                            
REMARK 200                                                                      
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.                                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.48                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 2.55                     
REMARK 200  COMPLETENESS FOR SHELL     (%) : 80.3                               
REMARK 200  DATA REDUNDANCY IN SHELL       : 3.20                               
REMARK 200  R MERGE FOR SHELL          (I) : NULL                               
REMARK 200  R SYM FOR SHELL            (I) : 0.15100                            
REMARK 200  <I/SIGMA(I)> FOR SHELL         : 4.900                              
REMARK 200                                                                      
REMARK 200 DIFFRACTION PROTOCOL: NULL                                           
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MULTIPLE ISOMORPHOUS         
REMARK 200  REPLACEMENT                                                         
REMARK 200 SOFTWARE USED: X-PLOR                                                
REMARK 200 STARTING MODEL: NULL                                                 
REMARK 200                                                                      
REMARK 200 REMARK: NULL                                                         
REMARK 280                                                                      
REMARK 280 CRYSTAL                                                              
REMARK 280 SOLVENT CONTENT, VS   (%): 43.00                                     
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.67                     
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: PH 7.7                                   
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY                                            
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 21 21 21                       
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                                                                      
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       36.76650            
REMARK 290   SMTRY2   2  0.000000 -1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   2  0.000000  0.000000  1.000000       97.27500            
REMARK 290   SMTRY1   3 -1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   3  0.000000  1.000000  0.000000       54.26850            
REMARK 290   SMTRY3   3  0.000000  0.000000 -1.000000       97.27500            
REMARK 290   SMTRY1   4  1.000000  0.000000  0.000000       36.76650            
REMARK 290   SMTRY2   4  0.000000 -1.000000  0.000000       54.26850            
REMARK 290   SMTRY3   4  0.000000  0.000000 -1.000000        0.00000            
REMARK 290                                                                      
REMARK 290 REMARK: NULL                                                         
REMARK 300                                                                      
REMARK 300 BIOMOLECULE: 1                                                       
REMARK 300 SEE REMARK 350 FOR THE AUTHOR PROVIDED AND/OR PROGRAM                
REMARK 300 GENERATED ASSEMBLY INFORMATION FOR THE STRUCTURE IN                  
REMARK 300 THIS ENTRY. THE REMARK MAY ALSO PROVIDE INFORMATION ON               
REMARK 300 BURIED SURFACE AREA.                                                 
REMARK 350                                                                      
REMARK 350 COORDINATES FOR A COMPLETE MULTIMER REPRESENTING THE KNOWN           
REMARK 350 BIOLOGICALLY SIGNIFICANT OLIGOMERIZATION STATE OF THE                
REMARK 350 MOLECULE CAN BE GENERATED BY APPLYING BIOMT TRANSFORMATIONS          
REMARK 350 GIVEN BELOW.  BOTH NON-CRYSTALLOGRAPHIC AND                          
REMARK 350 CRYSTALLOGRAPHIC OPERATIONS ARE GIVEN.                               
REMARK 350                                                                      
REMARK 350 BIOMOLECULE: 1                                                       
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: TETRAMERIC                        
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: TETRAMERIC                 
REMARK 350 SOFTWARE USED: PISA                                                  
REMARK 350 TOTAL BURIED SURFACE AREA: 10850 ANGSTROM**2                         
REMARK 350 SURFACE AREA OF THE COMPLEX: 53920 ANGSTROM**2                       
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -61.0 KCAL/MOL                        
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, B, C, 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 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     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     ARG A    58                                                      
REMARK 465     GLY A    59                                                      
REMARK 465     ILE A    60                                                      
REMARK 465     THR A    61                                                      
REMARK 465     ILE A    62                                                      
REMARK 465     ASN A    63                                                      
REMARK 465     ALA C    43                                                      
REMARK 465     ARG C    44                                                      
REMARK 465     ALA C    45                                                      
REMARK 465     PHE C    46                                                      
REMARK 465     ASP C    47                                                      
REMARK 465     GLN C    48                                                      
REMARK 465     ILE C    49                                                      
REMARK 465     ASP C    50                                                      
REMARK 465     ASN C    51                                                      
REMARK 465     ALA C    52                                                      
REMARK 465     PRO C    53                                                      
REMARK 465     GLU C    54                                                      
REMARK 465     GLU C    55                                                      
REMARK 465     LYS C    56                                                      
REMARK 465     ALA C    57                                                      
REMARK 465     ARG C    58                                                      
REMARK 465     GLY C    59                                                      
REMARK 465     ILE C    60                                                      
REMARK 465     THR C    61                                                      
REMARK 465     ILE C    62                                                      
REMARK 465     ASN C    63                                                      
REMARK 470                                                                      
REMARK 470 MISSING ATOM                                                         
REMARK 470 THE FOLLOWING RESIDUES HAVE MISSING ATOMS(M=MODEL NUMBER;            
REMARK 470 RES=RESIDUE NAME; C=CHAIN IDENTIFIER; SSEQ=SEQUENCE NUMBER;          
REMARK 470 I=INSERTION CODE):                                                   
REMARK 470   M RES CSSEQI  ATOMS                                                
REMARK 470     ALA A  42    CA   C    O    CB                                   
REMARK 470     ALA C  42    CA   C    O    CB                                   
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    SER A  65       93.83    -59.62                                   
REMARK 500    ALA A  96      123.89    173.24                                   
REMARK 500    PRO A 163       73.19    -65.79                                   
REMARK 500    SER A 173       99.80   -160.65                                   
REMARK 500    ASP A 181       96.51    -67.52                                   
REMARK 500    PHE A 210      137.89    -39.41                                   
REMARK 500    GLU A 215      -61.74   -109.24                                   
REMARK 500    ILE A 220      -52.22   -140.43                                   
REMARK 500    SER A 221      120.85     75.54                                   
REMARK 500    ARG A 223      -68.59   -145.00                                   
REMARK 500    ILE A 247      -60.17     61.69                                   
REMARK 500    ARG A 262       13.23     54.78                                   
REMARK 500    PHE A 323     -163.76   -120.13                                   
REMARK 500    ARG A 333      -70.95     58.47                                   
REMARK 500    LYS B 208      -60.85    -28.67                                   
REMARK 500    GLU B 236       81.73   -160.91                                   
REMARK 500    GLU B 247        1.09    -69.47                                   
REMARK 500    GLU B 265      -54.03    -29.94                                   
REMARK 500    GLU B 268      125.70     81.67                                   
REMARK 500    LYS B 280      -87.88    -85.38                                   
REMARK 500    GLN B 281     -114.23    -87.57                                   
REMARK 500    CYS C  81       76.29   -112.47                                   
REMARK 500    ALA C  95       64.12   -115.37                                   
REMARK 500    ALA C  96      -83.19   -168.92                                   
REMARK 500    GLN C  97       64.17     36.96                                   
REMARK 500    ASP C 141       45.00    -74.56                                   
REMARK 500    ASP C 142      122.46    176.05                                   
REMARK 500    PRO C 163       70.15    -68.90                                   
REMARK 500    ASP C 181       90.64    -66.59                                   
REMARK 500    GLU C 215      -78.39   -106.02                                   
REMARK 500    SER C 221      -52.51     83.27                                   
REMARK 500    ARG C 223      -50.61   -146.81                                   
REMARK 500    ILE C 247      -49.29     71.22                                   
REMARK 500    CYS C 255       94.56    -69.84                                   
REMARK 500    THR C 256       53.80    -92.94                                   
REMARK 500    LYS C 263      122.87   -172.62                                   
REMARK 500    VAL C 274     -167.69   -124.01                                   
REMARK 500    GLU C 284        3.15    -69.43                                   
REMARK 500    PHE C 323     -165.38   -118.73                                   
REMARK 500    ARG C 333      -69.93     60.00                                   
REMARK 500    LYS D 176       54.75     37.70                                   
REMARK 500    GLU D 183        3.94    -67.52                                   
REMARK 500    GLU D 236       83.21   -170.28                                   
REMARK 500    PRO D 237       -9.24    -54.14                                   
REMARK 500    SER D 279        3.18    -65.95                                   
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 525                                                                      
REMARK 525 SOLVENT                                                              
REMARK 525                                                                      
REMARK 525 THE SOLVENT MOLECULES HAVE CHAIN IDENTIFIERS THAT                    
REMARK 525 INDICATE THE POLYMER CHAIN WITH WHICH THEY ARE MOST                  
REMARK 525 CLOSELY ASSOCIATED. THE REMARK LISTS ALL THE SOLVENT                 
REMARK 525 MOLECULES WHICH ARE MORE THAN 5A AWAY FROM THE                       
REMARK 525 NEAREST POLYMER CHAIN (M = MODEL NUMBER;                             
REMARK 525 RES=RESIDUE NAME; C=CHAIN IDENTIFIER; SSEQ=SEQUENCE                  
REMARK 525 NUMBER; I=INSERTION CODE):                                           
REMARK 525                                                                      
REMARK 525  M RES CSSEQI                                                        
REMARK 525    HOH B 378        DISTANCE =  7.15 ANGSTROMS                       
REMARK 525    HOH B 379        DISTANCE =  9.00 ANGSTROMS                       
REMARK 525    HOH C 454        DISTANCE =  5.13 ANGSTROMS                       
REMARK 525    HOH B 424        DISTANCE =  8.23 ANGSTROMS                       
REMARK 525    HOH D 374        DISTANCE =  6.31 ANGSTROMS                       
REMARK 525    HOH D 375        DISTANCE =  6.80 ANGSTROMS                       
REMARK 525    HOH B 448        DISTANCE =  5.37 ANGSTROMS                       
REMARK 525    HOH D 483        DISTANCE =  5.32 ANGSTROMS                       
REMARK 525    HOH B 649        DISTANCE =  5.93 ANGSTROMS                       
REMARK 525    HOH D 531        DISTANCE =  5.34 ANGSTROMS                       
REMARK 525    HOH D 574        DISTANCE =  8.74 ANGSTROMS                       
REMARK 525    HOH B1183        DISTANCE =  5.53 ANGSTROMS                       
DBREF  1EFU A    9   393  UNP    P0A6N1   EFTU_ECOLI       9    393             
DBREF  1EFU B    1   282  UNP    P0A6P1   EFTS_ECOLI       1    282             
DBREF  1EFU C    9   393  UNP    P0A6N1   EFTU_ECOLI       9    393             
DBREF  1EFU D    1   282  UNP    P0A6P1   EFTS_ECOLI       1    282             
SEQRES   1 A  385  LYS PRO HIS VAL ASN VAL GLY THR ILE GLY HIS VAL ASP          
SEQRES   2 A  385  HIS GLY LYS THR THR LEU THR ALA ALA ILE THR THR VAL          
SEQRES   3 A  385  LEU ALA LYS THR TYR GLY GLY ALA ALA ARG ALA PHE ASP          
SEQRES   4 A  385  GLN ILE ASP ASN ALA PRO GLU GLU LYS ALA ARG GLY ILE          
SEQRES   5 A  385  THR ILE ASN THR SER HIS VAL GLU TYR ASP THR PRO THR          
SEQRES   6 A  385  ARG HIS TYR ALA HIS VAL ASP CYS PRO GLY HIS ALA ASP          
SEQRES   7 A  385  TYR VAL LYS ASN MET ILE THR GLY ALA ALA GLN MET ASP          
SEQRES   8 A  385  GLY ALA ILE LEU VAL VAL ALA ALA THR ASP GLY PRO MET          
SEQRES   9 A  385  PRO GLN THR ARG GLU HIS ILE LEU LEU GLY ARG GLN VAL          
SEQRES  10 A  385  GLY VAL PRO TYR ILE ILE VAL PHE LEU ASN LYS CYS ASP          
SEQRES  11 A  385  MET VAL ASP ASP GLU GLU LEU LEU GLU LEU VAL GLU MET          
SEQRES  12 A  385  GLU VAL ARG GLU LEU LEU SER GLN TYR ASP PHE PRO GLY          
SEQRES  13 A  385  ASP ASP THR PRO ILE VAL ARG GLY SER ALA LEU LYS ALA          
SEQRES  14 A  385  LEU GLU GLY ASP ALA GLU TRP GLU ALA LYS ILE LEU GLU          
SEQRES  15 A  385  LEU ALA GLY PHE LEU ASP SER TYR ILE PRO GLU PRO GLU          
SEQRES  16 A  385  ARG ALA ILE ASP LYS PRO PHE LEU LEU PRO ILE GLU ASP          
SEQRES  17 A  385  VAL PHE SER ILE SER GLY ARG GLY THR VAL VAL THR GLY          
SEQRES  18 A  385  ARG VAL GLU ARG GLY ILE ILE LYS VAL GLY GLU GLU VAL          
SEQRES  19 A  385  GLU ILE VAL GLY ILE LYS GLU THR GLN LYS SER THR CYS          
SEQRES  20 A  385  THR GLY VAL GLU MET PHE ARG LYS LEU LEU ASP GLU GLY          
SEQRES  21 A  385  ARG ALA GLY GLU ASN VAL GLY VAL LEU LEU ARG GLY ILE          
SEQRES  22 A  385  LYS ARG GLU GLU ILE GLU ARG GLY GLN VAL LEU ALA LYS          
SEQRES  23 A  385  PRO GLY THR ILE LYS PRO HIS THR LYS PHE GLU SER GLU          
SEQRES  24 A  385  VAL TYR ILE LEU SER LYS ASP GLU GLY GLY ARG HIS THR          
SEQRES  25 A  385  PRO PHE PHE LYS GLY TYR ARG PRO GLN PHE TYR PHE ARG          
SEQRES  26 A  385  THR THR ASP VAL THR GLY THR ILE GLU LEU PRO GLU GLY          
SEQRES  27 A  385  VAL GLU MET VAL MET PRO GLY ASP ASN ILE LYS MET VAL          
SEQRES  28 A  385  VAL THR LEU ILE HIS PRO ILE ALA MET ASP ASP GLY LEU          
SEQRES  29 A  385  ARG PHE ALA ILE ARG GLU GLY GLY ARG THR VAL GLY ALA          
SEQRES  30 A  385  GLY VAL VAL ALA LYS VAL LEU SER                              
SEQRES   1 B  282  ALA GLU ILE THR ALA SER LEU VAL LYS GLU LEU ARG GLU          
SEQRES   2 B  282  ARG THR GLY ALA GLY MET MET ASP CYS LYS LYS ALA LEU          
SEQRES   3 B  282  THR GLU ALA ASN GLY ASP ILE GLU LEU ALA ILE GLU ASN          
SEQRES   4 B  282  MET ARG LYS SER GLY ALA ILE LYS ALA ALA LYS LYS ALA          
SEQRES   5 B  282  GLY ASN VAL ALA ALA ASP GLY VAL ILE LYS THR LYS ILE          
SEQRES   6 B  282  ASP GLY ASN TYR GLY ILE ILE LEU GLU VAL ASN CYS GLN          
SEQRES   7 B  282  THR ASP PHE VAL ALA LYS ASP ALA GLY PHE GLN ALA PHE          
SEQRES   8 B  282  ALA ASP LYS VAL LEU ASP ALA ALA VAL ALA GLY LYS ILE          
SEQRES   9 B  282  THR ASP VAL GLU VAL LEU LYS ALA GLN PHE GLU GLU GLU          
SEQRES  10 B  282  ARG VAL ALA LEU VAL ALA LYS ILE GLY GLU ASN ILE ASN          
SEQRES  11 B  282  ILE ARG ARG VAL ALA ALA LEU GLU GLY ASP VAL LEU GLY          
SEQRES  12 B  282  SER TYR GLN HIS GLY ALA ARG ILE GLY VAL LEU VAL ALA          
SEQRES  13 B  282  ALA LYS GLY ALA ASP GLU GLU LEU VAL LYS HIS ILE ALA          
SEQRES  14 B  282  MET HIS VAL ALA ALA SER LYS PRO GLU PHE ILE LYS PRO          
SEQRES  15 B  282  GLU ASP VAL SER ALA GLU VAL VAL GLU LYS GLU TYR GLN          
SEQRES  16 B  282  VAL GLN LEU ASP ILE ALA MET GLN SER GLY LYS PRO LYS          
SEQRES  17 B  282  GLU ILE ALA GLU LYS MET VAL GLU GLY ARG MET LYS LYS          
SEQRES  18 B  282  PHE THR GLY GLU VAL SER LEU THR GLY GLN PRO PHE VAL          
SEQRES  19 B  282  MET GLU PRO SER LYS THR VAL GLY GLN LEU LEU LYS GLU          
SEQRES  20 B  282  HIS ASN ALA GLU VAL THR GLY PHE ILE ARG PHE GLU VAL          
SEQRES  21 B  282  GLY GLU GLY ILE GLU LYS VAL GLU THR ASP PHE ALA ALA          
SEQRES  22 B  282  GLU VAL ALA ALA MET SER LYS GLN SER                          
SEQRES   1 C  385  LYS PRO HIS VAL ASN VAL GLY THR ILE GLY HIS VAL ASP          
SEQRES   2 C  385  HIS GLY LYS THR THR LEU THR ALA ALA ILE THR THR VAL          
SEQRES   3 C  385  LEU ALA LYS THR TYR GLY GLY ALA ALA ARG ALA PHE ASP          
SEQRES   4 C  385  GLN ILE ASP ASN ALA PRO GLU GLU LYS ALA ARG GLY ILE          
SEQRES   5 C  385  THR ILE ASN THR SER HIS VAL GLU TYR ASP THR PRO THR          
SEQRES   6 C  385  ARG HIS TYR ALA HIS VAL ASP CYS PRO GLY HIS ALA ASP          
SEQRES   7 C  385  TYR VAL LYS ASN MET ILE THR GLY ALA ALA GLN MET ASP          
SEQRES   8 C  385  GLY ALA ILE LEU VAL VAL ALA ALA THR ASP GLY PRO MET          
SEQRES   9 C  385  PRO GLN THR ARG GLU HIS ILE LEU LEU GLY ARG GLN VAL          
SEQRES  10 C  385  GLY VAL PRO TYR ILE ILE VAL PHE LEU ASN LYS CYS ASP          
SEQRES  11 C  385  MET VAL ASP ASP GLU GLU LEU LEU GLU LEU VAL GLU MET          
SEQRES  12 C  385  GLU VAL ARG GLU LEU LEU SER GLN TYR ASP PHE PRO GLY          
SEQRES  13 C  385  ASP ASP THR PRO ILE VAL ARG GLY SER ALA LEU LYS ALA          
SEQRES  14 C  385  LEU GLU GLY ASP ALA GLU TRP GLU ALA LYS ILE LEU GLU          
SEQRES  15 C  385  LEU ALA GLY PHE LEU ASP SER TYR ILE PRO GLU PRO GLU          
SEQRES  16 C  385  ARG ALA ILE ASP LYS PRO PHE LEU LEU PRO ILE GLU ASP          
SEQRES  17 C  385  VAL PHE SER ILE SER GLY ARG GLY THR VAL VAL THR GLY          
SEQRES  18 C  385  ARG VAL GLU ARG GLY ILE ILE LYS VAL GLY GLU GLU VAL          
SEQRES  19 C  385  GLU ILE VAL GLY ILE LYS GLU THR GLN LYS SER THR CYS          
SEQRES  20 C  385  THR GLY VAL GLU MET PHE ARG LYS LEU LEU ASP GLU GLY          
SEQRES  21 C  385  ARG ALA GLY GLU ASN VAL GLY VAL LEU LEU ARG GLY ILE          
SEQRES  22 C  385  LYS ARG GLU GLU ILE GLU ARG GLY GLN VAL LEU ALA LYS          
SEQRES  23 C  385  PRO GLY THR ILE LYS PRO HIS THR LYS PHE GLU SER GLU          
SEQRES  24 C  385  VAL TYR ILE LEU SER LYS ASP GLU GLY GLY ARG HIS THR          
SEQRES  25 C  385  PRO PHE PHE LYS GLY TYR ARG PRO GLN PHE TYR PHE ARG          
SEQRES  26 C  385  THR THR ASP VAL THR GLY THR ILE GLU LEU PRO GLU GLY          
SEQRES  27 C  385  VAL GLU MET VAL MET PRO GLY ASP ASN ILE LYS MET VAL          
SEQRES  28 C  385  VAL THR LEU ILE HIS PRO ILE ALA MET ASP ASP GLY LEU          
SEQRES  29 C  385  ARG PHE ALA ILE ARG GLU GLY GLY ARG THR VAL GLY ALA          
SEQRES  30 C  385  GLY VAL VAL ALA LYS VAL LEU SER                              
SEQRES   1 D  282  ALA GLU ILE THR ALA SER LEU VAL LYS GLU LEU ARG GLU          
SEQRES   2 D  282  ARG THR GLY ALA GLY MET MET ASP CYS LYS LYS ALA LEU          
SEQRES   3 D  282  THR GLU ALA ASN GLY ASP ILE GLU LEU ALA ILE GLU ASN          
SEQRES   4 D  282  MET ARG LYS SER GLY ALA ILE LYS ALA ALA LYS LYS ALA          
SEQRES   5 D  282  GLY ASN VAL ALA ALA ASP GLY VAL ILE LYS THR LYS ILE          
SEQRES   6 D  282  ASP GLY ASN TYR GLY ILE ILE LEU GLU VAL ASN CYS GLN          
SEQRES   7 D  282  THR ASP PHE VAL ALA LYS ASP ALA GLY PHE GLN ALA PHE          
SEQRES   8 D  282  ALA ASP LYS VAL LEU ASP ALA ALA VAL ALA GLY LYS ILE          
SEQRES   9 D  282  THR ASP VAL GLU VAL LEU LYS ALA GLN PHE GLU GLU GLU          
SEQRES  10 D  282  ARG VAL ALA LEU VAL ALA LYS ILE GLY GLU ASN ILE ASN          
SEQRES  11 D  282  ILE ARG ARG VAL ALA ALA LEU GLU GLY ASP VAL LEU GLY          
SEQRES  12 D  282  SER TYR GLN HIS GLY ALA ARG ILE GLY VAL LEU VAL ALA          
SEQRES  13 D  282  ALA LYS GLY ALA ASP GLU GLU LEU VAL LYS HIS ILE ALA          
SEQRES  14 D  282  MET HIS VAL ALA ALA SER LYS PRO GLU PHE ILE LYS PRO          
SEQRES  15 D  282  GLU ASP VAL SER ALA GLU VAL VAL GLU LYS GLU TYR GLN          
SEQRES  16 D  282  VAL GLN LEU ASP ILE ALA MET GLN SER GLY LYS PRO LYS          
SEQRES  17 D  282  GLU ILE ALA GLU LYS MET VAL GLU GLY ARG MET LYS LYS          
SEQRES  18 D  282  PHE THR GLY GLU VAL SER LEU THR GLY GLN PRO PHE VAL          
SEQRES  19 D  282  MET GLU PRO SER LYS THR VAL GLY GLN LEU LEU LYS GLU          
SEQRES  20 D  282  HIS ASN ALA GLU VAL THR GLY PHE ILE ARG PHE GLU VAL          
SEQRES  21 D  282  GLY GLU GLY ILE GLU LYS VAL GLU THR ASP PHE ALA ALA          
SEQRES  22 D  282  GLU VAL ALA ALA MET SER LYS GLN SER                          
FORMUL   5  HOH   *1183(H2 O)                                                   
HELIX    1   1 LYS A   24  TYR A   39  1                                  16    
HELIX    2   2 HIS A   84  ILE A   92  1                                   9    
HELIX    3   3 PRO A  113  GLN A  124  5                                  12    
HELIX    4   4 CYS A  137  MET A  139  5                                   3    
HELIX    5   5 GLU A  143  TYR A  160  1                                  18    
HELIX    6   6 ALA A  174  LEU A  178  1                                   5    
HELIX    7   7 ALA A  182  TYR A  198  1                                  17    
HELIX    8   8 ALA A  205  ASP A  207  5                                   3    
HELIX    9   9 ARG A  283  GLU A  285  5                                   3    
HELIX   10  10 LYS A  313  GLU A  315  5                                   3    
HELIX   11  11 ALA B    5  THR B   15  1                                  11    
HELIX   12  12 MET B   19  GLU B   28  1                                  10    
HELIX   13  13 ILE B   33  GLY B   53  1                                  21    
HELIX   14  14 ASP B   80  ALA B   83  1                                   4    
HELIX   15  15 ALA B   86  ALA B  101  1                                  16    
HELIX   16  16 VAL B  107  ILE B  125  1                                  19    
HELIX   17  17 GLU B  162  SER B  175  1                                  14    
HELIX   18  18 PRO B  182  ASP B  184  5                                   3    
HELIX   19  19 ALA B  187  GLN B  203  1                                  17    
HELIX   20  20 LYS B  208  VAL B  226  1                                  19    
HELIX   21  21 VAL B  241  HIS B  248  1                                   8    
HELIX   22  22 PHE B  271  MET B  278  1                                   8    
HELIX   23  23 LYS C   24  TYR C   39  1                                  16    
HELIX   24  24 HIS C   84  ILE C   92  1                                   9    
HELIX   25  25 PRO C  113  GLN C  124  5                                  12    
HELIX   26  26 CYS C  137  MET C  139  5                                   3    
HELIX   27  27 GLU C  143  TYR C  160  1                                  18    
HELIX   28  28 GLY C  164  ASP C  166  5                                   3    
HELIX   29  29 ALA C  174  LEU C  178  1                                   5    
HELIX   30  30 ALA C  182  SER C  197  1                                  16    
HELIX   31  31 ARG C  283  GLU C  285  5                                   3    
HELIX   32  32 ALA D    5  THR D   15  1                                  11    
HELIX   33  33 MET D   19  ALA D   29  1                                  11    
HELIX   34  34 ILE D   33  GLY D   53  1                                  21    
HELIX   35  35 ASP D   80  LYS D   84  1                                   5    
HELIX   36  36 ALA D   86  ALA D  101  1                                  16    
HELIX   37  37 VAL D  107  ILE D  125  1                                  19    
HELIX   38  38 GLU D  162  SER D  175  1                                  14    
HELIX   39  39 PRO D  182  ASP D  184  5                                   3    
HELIX   40  40 ALA D  187  SER D  204  1                                  18    
HELIX   41  41 LYS D  208  VAL D  226  1                                  19    
HELIX   42  42 VAL D  241  HIS D  248  1                                   8    
HELIX   43  43 PHE D  271  LYS D  280  1                                  10    
SHEET    1   A 6 ILE A 169  ARG A 171  0                                        
SHEET    2   A 6 ILE A 130  ASN A 135  1  N  VAL A 132   O  VAL A 170           
SHEET    3   A 6 GLY A 100  ALA A 106  1  N  ALA A 101   O  ILE A 131           
SHEET    4   A 6 PRO A  10  GLY A  18  1  N  GLY A  15   O  GLY A 100           
SHEET    5   A 6 ARG A  74  ASP A  80  1  N  HIS A  75   O  PRO A  10           
SHEET    6   A 6 VAL A  67  ASP A  70 -1  N  TYR A  69   O  TYR A  76           
SHEET    1   B 4 LEU A 211  PRO A 213  0                                        
SHEET    2   B 4 VAL A 291  LYS A 294 -1  N  LEU A 292   O  LEU A 212           
SHEET    3   B 4 GLU A 241  VAL A 245 -1  N  VAL A 245   O  VAL A 291           
SHEET    4   B 4 GLN A 251  THR A 254 -1  N  SER A 253   O  VAL A 242           
SHEET    1   C 5 ASP A 216  PHE A 218  0                                        
SHEET    2   C 5 THR A 225  ARG A 230 -1  N  THR A 228   O  ASP A 216           
SHEET    3   C 5 ASN A 273  LEU A 278 -1  N  LEU A 278   O  THR A 225           
SHEET    4   C 5 CYS A 255  MET A 260 -1  N  GLU A 259   O  GLY A 275           
SHEET    5   C 5 LYS A 263  LEU A 265 -1  N  LEU A 265   O  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  N  GLY A 268   O  ILE A 236           
SHEET    1   E 7 GLY A 339  LEU A 343  0                                        
SHEET    2   E 7 ASN A 355  LEU A 362 -1  N  THR A 361   O  THR A 340           
SHEET    3   E 7 LYS A 303  ILE A 310 -1  N  VAL A 308   O  ILE A 356           
SHEET    4   E 7 ARG A 381  VAL A 391 -1  N  LYS A 390   O  GLU A 305           
SHEET    5   E 7 ARG A 373  GLU A 378 -1  N  GLU A 378   O  ARG A 381           
SHEET    6   E 7 GLN A 329  PHE A 332 -1  N  TYR A 331   O  ALA A 375           
SHEET    7   E 7 THR A 335  THR A 338 -1  N  VAL A 337   O  PHE A 330           
SHEET    1   F 3 ASP B  58  ASP B  66  0                                        
SHEET    2   F 3 TYR B  69  CYS B  77 -1  N  CYS B  77   O  ASP B  58           
SHEET    3   F 3 ASN B 130  GLU B 138 -1  N  LEU B 137   O  GLY B  70           
SHEET    1   G 3 VAL B 141  HIS B 147  0                                        
SHEET    2   G 3 ILE B 151  LYS B 158 -1  N  ALA B 157   O  VAL B 141           
SHEET    3   G 3 GLU B 251  GLU B 259 -1  N  PHE B 258   O  GLY B 152           
SHEET    1   H 6 ILE C 169  ARG C 171  0                                        
SHEET    2   H 6 ILE C 130  ASN C 135  1  N  VAL C 132   O  VAL C 170           
SHEET    3   H 6 GLY C 100  ALA C 106  1  N  ALA C 101   O  ILE C 131           
SHEET    4   H 6 PRO C  10  GLY C  18  1  N  GLY C  15   O  GLY C 100           
SHEET    5   H 6 ARG C  74  ASP C  80  1  N  HIS C  75   O  PRO C  10           
SHEET    6   H 6 VAL C  67  ASP C  70 -1  N  TYR C  69   O  TYR C  76           
SHEET    1   I 4 LEU C 211  PRO C 213  0                                        
SHEET    2   I 4 VAL C 291  ALA C 293 -1  N  LEU C 292   O  LEU C 212           
SHEET    3   I 4 GLU C 241  VAL C 245 -1  N  VAL C 245   O  VAL C 291           
SHEET    4   I 4 GLN C 251  THR C 254 -1  N  SER C 253   O  VAL C 242           
SHEET    1   J 5 VAL C 217  SER C 219  0                                        
SHEET    2   J 5 THR C 225  ARG C 230 -1  N  VAL C 226   O  PHE C 218           
SHEET    3   J 5 ASN C 273  LEU C 277 -1  N  VAL C 276   O  VAL C 227           
SHEET    4   J 5 VAL C 258  MET C 260 -1  N  GLU C 259   O  GLY C 275           
SHEET    5   J 5 LYS C 263  LEU C 265 -1  N  LEU C 265   O  VAL C 258           
SHEET    1   K 2 ILE C 235  LYS C 237  0                                        
SHEET    2   K 2 GLU C 267  ARG C 269 -1  N  GLY C 268   O  ILE C 236           
SHEET    1   L 7 GLY C 339  LEU C 343  0                                        
SHEET    2   L 7 ASN C 355  LEU C 362 -1  N  THR C 361   O  THR C 340           
SHEET    3   L 7 LYS C 303  ILE C 310 -1  N  VAL C 308   O  ILE C 356           
SHEET    4   L 7 ARG C 381  VAL C 391 -1  N  LYS C 390   O  GLU C 305           
SHEET    5   L 7 ARG C 373  GLU C 378 -1  N  GLU C 378   O  ARG C 381           
SHEET    6   L 7 GLN C 329  PHE C 332 -1  N  TYR C 331   O  ALA C 375           
SHEET    7   L 7 THR C 335  THR C 338 -1  N  VAL C 337   O  PHE C 330           
SHEET    1   M 3 ASP D  58  ASP D  66  0                                        
SHEET    2   M 3 TYR D  69  CYS D  77 -1  N  CYS D  77   O  ASP D  58           
SHEET    3   M 3 ASN D 130  GLU D 138 -1  N  LEU D 137   O  GLY D  70           
SHEET    1   N 3 VAL D 141  HIS D 147  0                                        
SHEET    2   N 3 ILE D 151  LYS D 158 -1  N  ALA D 157   O  VAL D 141           
SHEET    3   N 3 GLU D 251  GLU D 259 -1  N  PHE D 258   O  GLY D 152           
CRYST1   73.533  108.537  194.550  90.00  90.00  90.00 P 21 21 21    8          
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      0.013599  0.000000  0.000000        0.00000                         
SCALE2      0.000000  0.009213  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.005140        0.00000                         
(ATOM LINES ARE NOT SHOWN.)
END                                                                             
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