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Database: PDB
Entry: 1ETU
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HEADER    TRANSPORT AND PROTECTION PROTEIN        15-JAN-88   1ETU              
TITLE     STRUCTURAL DETAILS OF THE BINDING OF GUANOSINE DIPHOSPHATE            
TITLE    2 TO ELONGATION FACTOR TU FROM E. COLI AS STUDIED BY X-RAY             
TITLE    3 CRYSTALLOGRAPHY                                                      
COMPND    MOL_ID: 1;                                                            
COMPND   2 MOLECULE: ELONGATION FACTOR TU;                                      
COMPND   3 CHAIN: A;                                                            
COMPND   4 ENGINEERED: YES                                                      
SOURCE    MOL_ID: 1;                                                            
SOURCE   2 ORGANISM_SCIENTIFIC: ESCHERICHIA COLI;                               
SOURCE   3 ORGANISM_TAXID: 83333;                                               
SOURCE   4 STRAIN: K12                                                          
KEYWDS    TRANSPORT AND PROTECTION PROTEIN                                      
EXPDTA    X-RAY DIFFRACTION                                                     
AUTHOR    B.F.C.CLARK,T.F.M.LACOUR,M.KJELDGAARD,K.MORIKAWA,J.NYBORG,            
AUTHOR   2 R.RUBIN,S.THIRUP                                                     
REVDAT   8   25-AUG-09 1ETU    1       SOURCE                                   
REVDAT   7   24-FEB-09 1ETU    1       VERSN                                    
REVDAT   6   01-APR-03 1ETU    1       JRNL                                     
REVDAT   5   15-OCT-91 1ETU    1       REMARK                                   
REVDAT   4   15-JUL-90 1ETU    1       HET    FORMUL                            
REVDAT   3   12-JUL-89 1ETU    1       HET                                      
REVDAT   2   09-JAN-89 1ETU    1       SEQRES                                   
REVDAT   1   16-JUL-88 1ETU    0                                                
JRNL        AUTH   T.F.LA COUR,J.NYBORG,S.THIRUP,B.F.CLARK                      
JRNL        TITL   STRUCTURAL DETAILS OF THE BINDING OF GUANOSINE               
JRNL        TITL 2 DIPHOSPHATE TO ELONGATION FACTOR TU FROM E. COLI AS          
JRNL        TITL 3 STUDIED BY X-RAY CRYSTALLOGRAPHY.                            
JRNL        REF    EMBO J.                       V.   4  2385 1985              
JRNL        REFN                   ISSN 0261-4189                               
JRNL        PMID   3908095                                                      
REMARK   1                                                                      
REMARK   1 REFERENCE 1                                                          
REMARK   1  AUTH   F.MCCORMICK,B.F.C.CLARK,T.F.M.LACOUR,M.KJELDGAARD,           
REMARK   1  AUTH 2 L.NORSKOV-LAURITSEN,J.NYBORG                                 
REMARK   1  TITL   A MODEL FOR THE TERTIARY STRUCTURE OF P21, THE               
REMARK   1  TITL 2 PRODUCT OF THE RAS ONCOGENE                                  
REMARK   1  REF    SCIENCE                       V. 230    78 1985              
REMARK   1  REFN                   ISSN 0036-8075                               
REMARK   1 REFERENCE 2                                                          
REMARK   1  AUTH   B.F.C.CLARK,T.F.M.LACOUR,K.M.NIELSEN,J.NYBORG,               
REMARK   1  AUTH 2 H.U.PETERSEN,G.E.SIBOSKA,F.P.WIKMAN                          
REMARK   1  TITL   STRUCTURE OF BACTERIAL ELONGATION FACTOR EF-TU AND           
REMARK   1  TITL 2 ITS INTERACTION WITH AMINOACYL-TRNA                          
REMARK   1  EDIT   B.F.C.CLARK, H.U.PETERSEN                                    
REMARK   1  REF    GENE EXPRESSION. THE                   127 1984              
REMARK   1  REF  2 TRANSLATIONAL STEP AND ITS                                   
REMARK   1  REF  3 CONTROL                                                      
REMARK   1  PUBL   MUNKSGARD, COPENHAGEN, DENMARK                               
REMARK   1  REFN                                                                
REMARK   1 REFERENCE 3                                                          
REMARK   1  AUTH   J.R.RUBIN,K.MORIKAWA,J.NYBORG,T.F.M.LACOUR,                  
REMARK   1  AUTH 2 B.F.C.CLARK,D.L.MILLER                                       
REMARK   1  TITL   STRUCTURAL FEATURES OF THE GDP BINDING SITE OF               
REMARK   1  TITL 2 ELONGATION FACTOR TU FROM ESCHERICHIA COLI AS                
REMARK   1  TITL 3 DETERMINED BY X-RAY DIFFRACTION                              
REMARK   1  REF    FEBS LETT.                    V. 129   177 1981              
REMARK   1  REFN                   ISSN 0014-5793                               
REMARK   1 REFERENCE 4                                                          
REMARK   1  AUTH   K.MORIKAWA,T.F.M.LACOUR,J.NYBORG,K.M.RASMUSSEN,              
REMARK   1  AUTH 2 D.L.MILLER,B.F.C.CLARK                                       
REMARK   1  TITL   HIGH RESOLUTION X-RAY CRYSTALLOGRAPHIC ANALYSIS OF           
REMARK   1  TITL 2 A MODIFIED FORM OF THE ELONGATION FACTOR TU(COLON)           
REMARK   1  TITL 3 GUANOSINE DIPHOSPHATE COMPLEX                                
REMARK   1  REF    J.MOL.BIOL.                   V. 125   325 1978              
REMARK   1  REFN                   ISSN 0022-2836                               
REMARK   2                                                                      
REMARK   2 RESOLUTION.    2.90 ANGSTROMS.                                       
REMARK   3                                                                      
REMARK   3 REFINEMENT.                                                          
REMARK   3   PROGRAM     : NULL                                                 
REMARK   3   AUTHORS     : NULL                                                 
REMARK   3                                                                      
REMARK   3  DATA USED IN REFINEMENT.                                            
REMARK   3   RESOLUTION RANGE HIGH (ANGSTROMS) : 2.90                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : NULL                           
REMARK   3   DATA CUTOFF            (SIGMA(F)) : NULL                           
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             : NULL                           
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) : NULL                            
REMARK   3   FREE R VALUE                     : NULL                            
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : NULL                            
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) : NULL                         
REMARK   3   BIN RESOLUTION RANGE LOW        (A) : NULL                         
REMARK   3   BIN COMPLETENESS (WORKING+TEST) (%) : NULL                         
REMARK   3   REFLECTIONS IN BIN    (WORKING SET) : NULL                         
REMARK   3   BIN R VALUE           (WORKING SET) : NULL                         
REMARK   3   BIN FREE R VALUE                    : NULL                         
REMARK   3   BIN FREE R VALUE TEST SET SIZE  (%) : NULL                         
REMARK   3   BIN FREE R VALUE TEST SET COUNT     : NULL                         
REMARK   3   ESTIMATED ERROR OF BIN FREE R VALUE : NULL                         
REMARK   3                                                                      
REMARK   3  NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.                    
REMARK   3   PROTEIN ATOMS            : 1366                                    
REMARK   3   NUCLEIC ACID ATOMS       : 0                                       
REMARK   3   HETEROGEN ATOMS          : 29                                      
REMARK   3   SOLVENT ATOMS            : 0                                       
REMARK   3                                                                      
REMARK   3  B VALUES.                                                           
REMARK   3   FROM WILSON PLOT           (A**2) : NULL                           
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : NULL                           
REMARK   3   OVERALL ANISOTROPIC B VALUE.                                       
REMARK   3    B11 (A**2) : NULL                                                 
REMARK   3    B22 (A**2) : NULL                                                 
REMARK   3    B33 (A**2) : NULL                                                 
REMARK   3    B12 (A**2) : NULL                                                 
REMARK   3    B13 (A**2) : NULL                                                 
REMARK   3    B23 (A**2) : NULL                                                 
REMARK   3                                                                      
REMARK   3  ESTIMATED COORDINATE ERROR.                                         
REMARK   3   ESD FROM LUZZATI PLOT        (A) : NULL                            
REMARK   3   ESD FROM SIGMAA              (A) : NULL                            
REMARK   3   LOW RESOLUTION CUTOFF        (A) : NULL                            
REMARK   3                                                                      
REMARK   3  CROSS-VALIDATED ESTIMATED COORDINATE ERROR.                         
REMARK   3   ESD FROM C-V LUZZATI PLOT    (A) : NULL                            
REMARK   3   ESD FROM C-V SIGMAA          (A) : NULL                            
REMARK   3                                                                      
REMARK   3  RMS DEVIATIONS FROM IDEAL VALUES.                                   
REMARK   3   BOND LENGTHS                 (A) : NULL                            
REMARK   3   BOND ANGLES            (DEGREES) : NULL                            
REMARK   3   DIHEDRAL ANGLES        (DEGREES) : NULL                            
REMARK   3   IMPROPER ANGLES        (DEGREES) : NULL                            
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  ; NULL                 
REMARK   3   MAIN-CHAIN ANGLE             (A**2) : NULL  ; NULL                 
REMARK   3   SIDE-CHAIN BOND              (A**2) : NULL  ; NULL                 
REMARK   3   SIDE-CHAIN ANGLE             (A**2) : NULL  ; NULL                 
REMARK   3                                                                      
REMARK   3  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:                                           
REMARK   3  ATOMS WITH AN OCCUPANCY OF 0.0 ARE POORLY DEFINED IN THE            
REMARK   3  DENSITY.                                                            
REMARK   4                                                                      
REMARK   4 1ETU 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        : NULL                               
REMARK 200  TEMPERATURE           (KELVIN) : NULL                               
REMARK 200  PH                             : NULL                               
REMARK 200  NUMBER OF CRYSTALS USED        : NULL                               
REMARK 200                                                                      
REMARK 200  SYNCHROTRON              (Y/N) : NULL                               
REMARK 200  RADIATION SOURCE               : NULL                               
REMARK 200  BEAMLINE                       : NULL                               
REMARK 200  X-RAY GENERATOR MODEL          : NULL                               
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : NULL                               
REMARK 200  WAVELENGTH OR RANGE        (A) : NULL                               
REMARK 200  MONOCHROMATOR                  : NULL                               
REMARK 200  OPTICS                         : NULL                               
REMARK 200                                                                      
REMARK 200  DETECTOR TYPE                  : NULL                               
REMARK 200  DETECTOR MANUFACTURER          : NULL                               
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : NULL                               
REMARK 200  DATA SCALING SOFTWARE          : NULL                               
REMARK 200                                                                      
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : NULL                               
REMARK 200  RESOLUTION RANGE HIGH      (A) : NULL                               
REMARK 200  RESOLUTION RANGE LOW       (A) : NULL                               
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : NULL                               
REMARK 200                                                                      
REMARK 200 OVERALL.                                                             
REMARK 200  COMPLETENESS FOR RANGE     (%) : NULL                               
REMARK 200  DATA REDUNDANCY                : NULL                               
REMARK 200  R MERGE                    (I) : NULL                               
REMARK 200  R SYM                      (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR THE DATA SET  : NULL                               
REMARK 200                                                                      
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.                                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : NULL                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : NULL                     
REMARK 200  COMPLETENESS FOR SHELL     (%) : NULL                               
REMARK 200  DATA REDUNDANCY IN SHELL       : NULL                               
REMARK 200  R MERGE FOR SHELL          (I) : NULL                               
REMARK 200  R SYM FOR SHELL            (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR SHELL         : NULL                               
REMARK 200                                                                      
REMARK 200 DIFFRACTION PROTOCOL: NULL                                           
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: NULL                         
REMARK 200 SOFTWARE USED: NULL                                                  
REMARK 200 STARTING MODEL: NULL                                                 
REMARK 200                                                                      
REMARK 200 REMARK: NULL                                                         
REMARK 280                                                                      
REMARK 280 CRYSTAL                                                              
REMARK 280 SOLVENT CONTENT, VS   (%): 73.26                                     
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 4.60                     
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: NULL                                     
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY                                            
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: C 2 2 21                         
REMARK 290                                                                      
REMARK 290      SYMOP   SYMMETRY                                                
REMARK 290     NNNMMM   OPERATOR                                                
REMARK 290       1555   X,Y,Z                                                   
REMARK 290       2555   -X,-Y,Z+1/2                                             
REMARK 290       3555   -X,Y,-Z+1/2                                             
REMARK 290       4555   X,-Y,-Z                                                 
REMARK 290       5555   X+1/2,Y+1/2,Z                                           
REMARK 290       6555   -X+1/2,-Y+1/2,Z+1/2                                     
REMARK 290       7555   -X+1/2,Y+1/2,-Z+1/2                                     
REMARK 290       8555   X+1/2,-Y+1/2,-Z                                         
REMARK 290                                                                      
REMARK 290     WHERE NNN -> OPERATOR NUMBER                                     
REMARK 290           MMM -> TRANSLATION VECTOR                                  
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY TRANSFORMATIONS                            
REMARK 290 THE FOLLOWING TRANSFORMATIONS OPERATE ON THE ATOM/HETATM             
REMARK 290 RECORDS IN THIS ENTRY TO PRODUCE CRYSTALLOGRAPHICALLY                
REMARK 290 RELATED MOLECULES.                                                   
REMARK 290   SMTRY1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 290   SMTRY1   2 -1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   2  0.000000 -1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   2  0.000000  0.000000  1.000000       80.40000            
REMARK 290   SMTRY1   3 -1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   3  0.000000  1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   3  0.000000  0.000000 -1.000000       80.40000            
REMARK 290   SMTRY1   4  1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   4  0.000000 -1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   4  0.000000  0.000000 -1.000000        0.00000            
REMARK 290   SMTRY1   5  1.000000  0.000000  0.000000       49.10000            
REMARK 290   SMTRY2   5  0.000000  1.000000  0.000000       50.40000            
REMARK 290   SMTRY3   5  0.000000  0.000000  1.000000        0.00000            
REMARK 290   SMTRY1   6 -1.000000  0.000000  0.000000       49.10000            
REMARK 290   SMTRY2   6  0.000000 -1.000000  0.000000       50.40000            
REMARK 290   SMTRY3   6  0.000000  0.000000  1.000000       80.40000            
REMARK 290   SMTRY1   7 -1.000000  0.000000  0.000000       49.10000            
REMARK 290   SMTRY2   7  0.000000  1.000000  0.000000       50.40000            
REMARK 290   SMTRY3   7  0.000000  0.000000 -1.000000       80.40000            
REMARK 290   SMTRY1   8  1.000000  0.000000  0.000000       49.10000            
REMARK 290   SMTRY2   8  0.000000 -1.000000  0.000000       50.40000            
REMARK 290   SMTRY3   8  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: MONOMERIC                         
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A                                     
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     SER A     1                                                      
REMARK 465     LYS A     2                                                      
REMARK 465     GLU A     3                                                      
REMARK 465     LYS A     4                                                      
REMARK 465     GLY A    41                                                      
REMARK 465     ALA A    42                                                      
REMARK 465     ALA A    43                                                      
REMARK 465     ARG A    44                                                      
REMARK 465     ALA A    45                                                      
REMARK 465     PHE A    46                                                      
REMARK 465     ASP A    47                                                      
REMARK 465     GLN A    48                                                      
REMARK 465     ILE A    49                                                      
REMARK 465     ASP A    50                                                      
REMARK 465     ASN A    51                                                      
REMARK 465     ALA A    52                                                      
REMARK 465     PRO A    53                                                      
REMARK 465     GLU A    54                                                      
REMARK 465     GLU A    55                                                      
REMARK 465     LYS A    56                                                      
REMARK 465     ALA A    57                                                      
REMARK 465     ARG A    58                                                      
REMARK 465     GLY A    59                                                      
REMARK 465     GLU A   201                                                      
REMARK 465     PRO A   202                                                      
REMARK 465     GLU A   203                                                      
REMARK 465     ARG A   204                                                      
REMARK 465     ALA A   205                                                      
REMARK 465     ILE A   206                                                      
REMARK 465     ASP A   207                                                      
REMARK 465     LYS A   208                                                      
REMARK 465     PRO A   209                                                      
REMARK 465     PHE A   210                                                      
REMARK 465     LEU A   211                                                      
REMARK 465     LEU A   212                                                      
REMARK 465     PRO A   213                                                      
REMARK 465     ILE A   214                                                      
REMARK 465     GLU A   215                                                      
REMARK 465     ASP A   216                                                      
REMARK 465     VAL A   217                                                      
REMARK 465     PHE A   218                                                      
REMARK 465     SER A   219                                                      
REMARK 465     ILE A   220                                                      
REMARK 465     SER A   221                                                      
REMARK 465     GLY A   222                                                      
REMARK 465     ARG A   223                                                      
REMARK 465     GLY A   224                                                      
REMARK 465     THR A   225                                                      
REMARK 465     VAL A   226                                                      
REMARK 465     VAL A   227                                                      
REMARK 465     THR A   228                                                      
REMARK 465     GLY A   229                                                      
REMARK 465     ARG A   230                                                      
REMARK 465     VAL A   231                                                      
REMARK 465     GLU A   232                                                      
REMARK 465     ARG A   233                                                      
REMARK 465     GLY A   234                                                      
REMARK 465     ILE A   235                                                      
REMARK 465     ILE A   236                                                      
REMARK 465     LYS A   237                                                      
REMARK 465     VAL A   238                                                      
REMARK 465     GLY A   239                                                      
REMARK 465     GLU A   240                                                      
REMARK 465     GLU A   241                                                      
REMARK 465     VAL A   242                                                      
REMARK 465     GLU A   243                                                      
REMARK 465     ILE A   244                                                      
REMARK 465     VAL A   245                                                      
REMARK 465     GLY A   246                                                      
REMARK 465     ILE A   247                                                      
REMARK 465     LYS A   248                                                      
REMARK 465     GLU A   249                                                      
REMARK 465     THR A   250                                                      
REMARK 465     GLN A   251                                                      
REMARK 465     LYS A   252                                                      
REMARK 465     SER A   253                                                      
REMARK 465     THR A   254                                                      
REMARK 465     CYS A   255                                                      
REMARK 465     THR A   256                                                      
REMARK 465     GLY A   257                                                      
REMARK 465     VAL A   258                                                      
REMARK 465     GLU A   259                                                      
REMARK 465     MET A   260                                                      
REMARK 465     PHE A   261                                                      
REMARK 465     ARG A   262                                                      
REMARK 465     LYS A   263                                                      
REMARK 465     LEU A   264                                                      
REMARK 465     LEU A   265                                                      
REMARK 465     ASP A   266                                                      
REMARK 465     GLU A   267                                                      
REMARK 465     GLY A   268                                                      
REMARK 465     ARG A   269                                                      
REMARK 465     ALA A   270                                                      
REMARK 465     GLY A   271                                                      
REMARK 465     GLU A   272                                                      
REMARK 465     ASN A   273                                                      
REMARK 465     VAL A   274                                                      
REMARK 465     GLY A   275                                                      
REMARK 465     VAL A   276                                                      
REMARK 465     LEU A   277                                                      
REMARK 465     LEU A   278                                                      
REMARK 465     ARG A   279                                                      
REMARK 465     GLY A   280                                                      
REMARK 465     ILE A   281                                                      
REMARK 465     LYS A   282                                                      
REMARK 465     ARG A   283                                                      
REMARK 465     GLU A   284                                                      
REMARK 465     GLU A   285                                                      
REMARK 465     ILE A   286                                                      
REMARK 465     GLU A   287                                                      
REMARK 465     ARG A   288                                                      
REMARK 465     GLY A   289                                                      
REMARK 465     GLN A   290                                                      
REMARK 465     VAL A   291                                                      
REMARK 465     LEU A   292                                                      
REMARK 465     ALA A   293                                                      
REMARK 465     LYS A   294                                                      
REMARK 465     PRO A   295                                                      
REMARK 465     GLY A   296                                                      
REMARK 465     THR A   297                                                      
REMARK 465     ILE A   298                                                      
REMARK 465     LYS A   299                                                      
REMARK 465     PRO A   300                                                      
REMARK 465     HIS A   301                                                      
REMARK 465     THR A   302                                                      
REMARK 465     LYS A   303                                                      
REMARK 465     PHE A   304                                                      
REMARK 465     GLU A   305                                                      
REMARK 465     SER A   306                                                      
REMARK 465     GLU A   307                                                      
REMARK 465     VAL A   308                                                      
REMARK 465     TYR A   309                                                      
REMARK 465     ILE A   310                                                      
REMARK 465     LEU A   311                                                      
REMARK 465     SER A   312                                                      
REMARK 465     LYS A   313                                                      
REMARK 465     ASP A   314                                                      
REMARK 465     GLU A   315                                                      
REMARK 465     GLY A   316                                                      
REMARK 465     GLY A   317                                                      
REMARK 465     ARG A   318                                                      
REMARK 465     HIS A   319                                                      
REMARK 465     THR A   320                                                      
REMARK 465     PRO A   321                                                      
REMARK 465     PHE A   322                                                      
REMARK 465     PHE A   323                                                      
REMARK 465     LYS A   324                                                      
REMARK 465     GLY A   325                                                      
REMARK 465     TYR A   326                                                      
REMARK 465     ARG A   327                                                      
REMARK 465     PRO A   328                                                      
REMARK 465     GLN A   329                                                      
REMARK 465     PHE A   330                                                      
REMARK 465     TYR A   331                                                      
REMARK 465     PHE A   332                                                      
REMARK 465     ARG A   333                                                      
REMARK 465     THR A   334                                                      
REMARK 465     THR A   335                                                      
REMARK 465     ASP A   336                                                      
REMARK 465     VAL A   337                                                      
REMARK 465     THR A   338                                                      
REMARK 465     GLY A   339                                                      
REMARK 465     THR A   340                                                      
REMARK 465     ILE A   341                                                      
REMARK 465     GLU A   342                                                      
REMARK 465     LEU A   343                                                      
REMARK 465     PRO A   344                                                      
REMARK 465     GLU A   345                                                      
REMARK 465     GLY A   346                                                      
REMARK 465     VAL A   347                                                      
REMARK 465     GLU A   348                                                      
REMARK 465     MET A   349                                                      
REMARK 465     VAL A   350                                                      
REMARK 465     MET A   351                                                      
REMARK 465     PRO A   352                                                      
REMARK 465     GLY A   353                                                      
REMARK 465     ASP A   354                                                      
REMARK 465     ASN A   355                                                      
REMARK 465     ILE A   356                                                      
REMARK 465     LYS A   357                                                      
REMARK 465     MET A   358                                                      
REMARK 465     VAL A   359                                                      
REMARK 465     VAL A   360                                                      
REMARK 465     THR A   361                                                      
REMARK 465     LEU A   362                                                      
REMARK 465     ILE A   363                                                      
REMARK 465     HIS A   364                                                      
REMARK 465     PRO A   365                                                      
REMARK 465     ILE A   366                                                      
REMARK 465     ALA A   367                                                      
REMARK 465     MET A   368                                                      
REMARK 465     ASP A   369                                                      
REMARK 465     ASP A   370                                                      
REMARK 465     GLY A   371                                                      
REMARK 465     LEU A   372                                                      
REMARK 465     ARG A   373                                                      
REMARK 465     PHE A   374                                                      
REMARK 465     ALA A   375                                                      
REMARK 465     ILE A   376                                                      
REMARK 465     ARG A   377                                                      
REMARK 465     GLU A   378                                                      
REMARK 465     GLY A   379                                                      
REMARK 465     GLY A   380                                                      
REMARK 465     ARG A   381                                                      
REMARK 465     THR A   382                                                      
REMARK 465     VAL A   383                                                      
REMARK 465     GLY A   384                                                      
REMARK 465     ALA A   385                                                      
REMARK 465     GLY A   386                                                      
REMARK 465     VAL A   387                                                      
REMARK 465     VAL A   388                                                      
REMARK 465     ALA A   389                                                      
REMARK 465     LYS A   390                                                      
REMARK 465     VAL A   391                                                      
REMARK 465     LEU A   392                                                      
REMARK 465     GLY A   393                                                      
REMARK 475                                                                      
REMARK 475 ZERO OCCUPANCY RESIDUES                                              
REMARK 475 THE FOLLOWING RESIDUES WERE MODELED WITH ZERO OCCUPANCY.             
REMARK 475 THE LOCATION AND PROPERTIES OF THESE RESIDUES MAY NOT                
REMARK 475 BE RELIABLE. (M=MODEL NUMBER; RES=RESIDUE NAME;                      
REMARK 475 C=CHAIN IDENTIFIER; SSEQ=SEQUENCE NUMBER; I=INSERTION CODE)          
REMARK 475   M RES C SSEQI                                                      
REMARK 475     PHE A    5                                                       
REMARK 475     GLU A    6                                                       
REMARK 475     ARG A    7                                                       
REMARK 475     THR A    8                                                       
REMARK 475     ILE A   17                                                       
REMARK 475     GLY A   18                                                       
REMARK 475     ALA A   30                                                       
REMARK 475     GLY A   40                                                       
REMARK 475     VAL A   79                                                       
REMARK 475     ALA A  101                                                       
REMARK 475     ALA A  107                                                       
REMARK 475     LEU A  121                                                       
REMARK 475     GLY A  164                                                       
REMARK 475     ASP A  165                                                       
REMARK 475     ASP A  166                                                       
REMARK 475     ASP A  181                                                       
REMARK 475     LEU A  191                                                       
REMARK 480                                                                      
REMARK 480 ZERO OCCUPANCY ATOM                                                  
REMARK 480 THE FOLLOWING RESIDUES HAVE ATOMS MODELED WITH ZERO                  
REMARK 480 OCCUPANCY. THE LOCATION AND PROPERTIES OF THESE ATOMS                
REMARK 480 MAY NOT BE RELIABLE. (M=MODEL NUMBER; RES=RESIDUE NAME;              
REMARK 480 C=CHAIN IDENTIFIER; SSEQ=SEQUENCE NUMBER; I=INSERTION CODE):         
REMARK 480   M RES C SSEQI ATOMS                                                
REMARK 480     LYS A    9   CG    CD    CE    NZ                                
REMARK 480     THR A   16   CA    C     O     CB    OG1                         
REMARK 480     ASP A   21   CB    CG    OD1   OD2                               
REMARK 480     HIS A   22   O                                                   
REMARK 480     LEU A   27   CB    CG    CD1   CD2                               
REMARK 480     ALA A   29   CB                                                  
REMARK 480     THR A   32   CB    CG2                                           
REMARK 480     VAL A   34   O                                                   
REMARK 480     LEU A   35   CD1                                                 
REMARK 480     THR A   38   CB    CG2                                           
REMARK 480     TYR A   39   CD1   CD2   CE1   CE2   CZ    OH                    
REMARK 480     THR A   61   CB    OG1   CG2                                     
REMARK 480     ILE A   62   CG2                                                 
REMARK 480     THR A   64   CB    OG1   CG2                                     
REMARK 480     VAL A   67   N     CA    C     O     CG1   CG2                   
REMARK 480     GLU A   68   CG    CD    OE1   OE2                               
REMARK 480     TYR A   69   CE2   OH                                            
REMARK 480     ASP A   70   N     CA                                            
REMARK 480     TYR A   76   CD2                                                 
REMARK 480     ALA A   77   CB                                                  
REMARK 480     ASP A   80   N     CA                                            
REMARK 480     VAL A   88   CG1   CG2                                           
REMARK 480     LYS A   89   CE    NZ                                            
REMARK 480     MET A   91   CB    CG    SD    CE                                
REMARK 480     ILE A   92   CD1                                                 
REMARK 480     ALA A   95   N     CB                                            
REMARK 480     ALA A   96   C     O                                             
REMARK 480     GLN A   97   CD    OE1   NE2                                     
REMARK 480     ILE A  102   N                                                   
REMARK 480     LEU A  103   N     CA    C     O                                 
REMARK 480     MET A  112   CE                                                  
REMARK 480     PRO A  113   N     CA    CB    CG    CD                          
REMARK 480     ARG A  116   O                                                   
REMARK 480     GLU A  117   N     CB    CG    CD    OE1   OE2                   
REMARK 480     HIS A  118   O                                                   
REMARK 480     ILE A  119   CB    CG1   CG2   CD1                               
REMARK 480     LEU A  120   O     CG    CD1   CD2                               
REMARK 480     ARG A  123   NE    CZ    NH1   NH2                               
REMARK 480     GLN A  124   O     CB    CG    CD    OE1   NE2                   
REMARK 480     ILE A  130   N     CB    CG1   CG2   CD1                         
REMARK 480     ILE A  131   CG2                                                 
REMARK 480     VAL A  132   CG2                                                 
REMARK 480     LYS A  136   CB    CG    CD    CE    NZ                          
REMARK 480     ASP A  138   O     CB    CG    OD1   OD2                         
REMARK 480     VAL A  140   CG2                                                 
REMARK 480     ASP A  142   O     CB    CG    OD1   OD2                         
REMARK 480     GLU A  143   CB    CG    CD    OE1   OE2                         
REMARK 480     GLU A  144   CB    CG    CD    OE1   OE2                         
REMARK 480     GLU A  147   CG    CD    OE1   OE2                               
REMARK 480     LEU A  148   O     CG    CD1   CD2                               
REMARK 480     VAL A  149   CG1   CG2                                           
REMARK 480     GLU A  150   CG    CD    OE1   OE2                               
REMARK 480     MET A  151   CB    CG                                            
REMARK 480     GLU A  152   O     CD    OE1   OE2                               
REMARK 480     LEU A  156   O     CG    CD1   CD2                               
REMARK 480     GLN A  159   CG    CD    OE1   NE2                               
REMARK 480     TYR A  160   CB    CG    CD1   CD2   CE1   CE2   CZ              
REMARK 480     TYR A  160   OH                                                  
REMARK 480     ASP A  161   CB    CG    OD1   OD2                               
REMARK 480     PHE A  162   CG    CD1   CD2   CE1   CE2   CZ                    
REMARK 480     THR A  167   N     CA    CB    OG1   CG2                         
REMARK 480     ILE A  169   CG1   CG2   CD1                                     
REMARK 480     ARG A  171   CB    CG    CD    NE    CZ    NH1   NH2             
REMARK 480     LEU A  175   CB    CG    CD1   CD2                               
REMARK 480     LYS A  176   O     CE    NZ                                      
REMARK 480     ALA A  177   O                                                   
REMARK 480     GLY A  180   O                                                   
REMARK 480     GLU A  183   CG    CD    OE1   OE2                               
REMARK 480     TRP A  184   CE3   CZ3   CH2                                     
REMARK 480     LYS A  187   CB    CG    CD    CE    NZ                          
REMARK 480     LEU A  189   N     CA    CB    CG    CD1   CD2                   
REMARK 480     GLU A  190   N     CB    CG    CD    OE1   OE2                   
REMARK 480     ALA A  192   CB                                                  
REMARK 480     PHE A  194   CA    CD2   CE2                                     
REMARK 480     LEU A  195   CG    CD1   CD2                                     
REMARK 480     SER A  197   OG                                                  
REMARK 480     ILE A  199   CG1   CG2   CD1                                     
REMARK 480     PRO A  200   C     O                                             
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: CLOSE CONTACTS IN SAME ASYMMETRIC UNIT                     
REMARK 500                                                                      
REMARK 500 THE FOLLOWING ATOMS ARE IN CLOSE CONTACT.                            
REMARK 500                                                                      
REMARK 500  ATM1  RES C  SSEQI   ATM2  RES C  SSEQI           DISTANCE          
REMARK 500   OG1  THR A     8     CD2  HIS A    11              0.68            
REMARK 500   CB   THR A     8     NE2  HIS A    11              0.80            
REMARK 500   CB   THR A     8     CD2  HIS A    11              1.26            
REMARK 500   OG1  THR A     8     NE2  HIS A    11              1.41            
REMARK 500   O    ILE A    31     CD1  LEU A    35              1.44            
REMARK 500   OG1  THR A     8     CG   HIS A    11              1.48            
REMARK 500   CA   THR A     8     NE2  HIS A    11              1.56            
REMARK 500   O    GLU A   144     CD1  LEU A   148              1.78            
REMARK 500   OG1  THR A    16     CE1  HIS A    78              1.80            
REMARK 500   CB   LEU A   146     NH2  ARG A   171              1.87            
REMARK 500   O    ASP A    86     OD1  ASN A    90              1.94            
REMARK 500   CG2  THR A     8     CD2  HIS A    11              2.07            
REMARK 500   ND2  ASN A    13     CB   ALA A    77              2.10            
REMARK 500   O    GLU A   147     N    MET A   151              2.10            
REMARK 500   CB   THR A     8     CE1  HIS A    11              2.10            
REMARK 500   C    LEU A   146     NH2  ARG A   171              2.11            
REMARK 500   O    GLY A    23     N    LEU A    27              2.11            
REMARK 500   OG1  THR A     8     CE1  HIS A    11              2.15            
REMARK 500   OD1  ASP A    70     ND1  HIS A    75              2.16            
REMARK 500   CA   LEU A   146     NH2  ARG A   171              2.18            
REMARK 500   OG1  THR A     8     ND1  HIS A    11              2.19            
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: CLOSE CONTACTS                                             
REMARK 500                                                                      
REMARK 500 THE FOLLOWING ATOMS THAT ARE RELATED BY CRYSTALLOGRAPHIC             
REMARK 500 SYMMETRY ARE IN CLOSE CONTACT.  AN ATOM LOCATED WITHIN 0.15          
REMARK 500 ANGSTROMS OF A SYMMETRY RELATED ATOM IS ASSUMED TO BE ON A           
REMARK 500 SPECIAL POSITION AND IS, THEREFORE, LISTED IN REMARK 375             
REMARK 500 INSTEAD OF REMARK 500.  ATOMS WITH NON-BLANK ALTERNATE               
REMARK 500 LOCATION INDICATORS ARE NOT INCLUDED IN THE CALCULATIONS.            
REMARK 500                                                                      
REMARK 500 DISTANCE CUTOFF:                                                     
REMARK 500 2.2 ANGSTROMS FOR CONTACTS NOT INVOLVING HYDROGEN ATOMS              
REMARK 500 1.6 ANGSTROMS FOR CONTACTS INVOLVING HYDROGEN ATOMS                  
REMARK 500                                                                      
REMARK 500  ATM1  RES C  SSEQI   ATM2  RES C  SSEQI  SSYMOP   DISTANCE          
REMARK 500   ND2  ASN A    63     OG   SER A    65     3755     1.38            
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
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    ARG A   7   N     ARG A   7   CA      0.153                       
REMARK 500    LYS A   9   N     LYS A   9   CA     -0.139                       
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: COVALENT BOND ANGLES                                       
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,A3,1X,A1,I4,A1,3(1X,A4,2X),12X,F5.1)              
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   ATM2   ATM3                                     
REMARK 500    ARG A   7   NE  -  CZ  -  NH2 ANGL. DEV. =   3.3 DEGREES          
REMARK 500    GLU A   6   O   -  C   -  N   ANGL. DEV. = -11.9 DEGREES          
REMARK 500    LYS A   9   CB  -  CA  -  C   ANGL. DEV. =  12.1 DEGREES          
REMARK 500    LYS A   9   N   -  CA  -  C   ANGL. DEV. = -19.2 DEGREES          
REMARK 500    HIS A  11   O   -  C   -  N   ANGL. DEV. =   9.7 DEGREES          
REMARK 500    ASN A  13   O   -  C   -  N   ANGL. DEV. =  11.8 DEGREES          
REMARK 500    LYS A  37   CB  -  CA  -  C   ANGL. DEV. = -13.0 DEGREES          
REMARK 500    ILE A  60   CB  -  CA  -  C   ANGL. DEV. =  29.1 DEGREES          
REMARK 500    ILE A  60   CA  -  C   -  N   ANGL. DEV. = -21.8 DEGREES          
REMARK 500    ILE A  60   O   -  C   -  N   ANGL. DEV. =  18.6 DEGREES          
REMARK 500    ASN A  63   CA  -  C   -  N   ANGL. DEV. = -15.0 DEGREES          
REMARK 500    ASN A  63   O   -  C   -  N   ANGL. DEV. =  14.5 DEGREES          
REMARK 500    HIS A  66   O   -  C   -  N   ANGL. DEV. =   9.8 DEGREES          
REMARK 500    TYR A  69   CB  -  CG  -  CD2 ANGL. DEV. =  -5.0 DEGREES          
REMARK 500    GLU A  68   O   -  C   -  N   ANGL. DEV. =  11.6 DEGREES          
REMARK 500    THR A  71   O   -  C   -  N   ANGL. DEV. = -13.0 DEGREES          
REMARK 500    ARG A  74   NE  -  CZ  -  NH2 ANGL. DEV. =   3.7 DEGREES          
REMARK 500    TYR A  76   CB  -  CG  -  CD1 ANGL. DEV. =  -5.2 DEGREES          
REMARK 500    CYS A  81   CB  -  CA  -  C   ANGL. DEV. =   8.3 DEGREES          
REMARK 500    MET A  91   CG  -  SD  -  CE  ANGL. DEV. =  10.3 DEGREES          
REMARK 500    ILE A  92   O   -  C   -  N   ANGL. DEV. = -10.4 DEGREES          
REMARK 500    THR A  93   C   -  N   -  CA  ANGL. DEV. = -15.5 DEGREES          
REMARK 500    MET A  98   CG  -  SD  -  CE  ANGL. DEV. =   9.9 DEGREES          
REMARK 500    ALA A 106   CA  -  C   -  N   ANGL. DEV. = -14.7 DEGREES          
REMARK 500    ALA A 106   O   -  C   -  N   ANGL. DEV. =  14.1 DEGREES          
REMARK 500    MET A 112   CG  -  SD  -  CE  ANGL. DEV. =  10.2 DEGREES          
REMARK 500    ARG A 116   NE  -  CZ  -  NH2 ANGL. DEV. =   4.0 DEGREES          
REMARK 500    CYS A 137   CB  -  CA  -  C   ANGL. DEV. =  15.8 DEGREES          
REMARK 500    CYS A 137   CA  -  CB  -  SG  ANGL. DEV. = -17.8 DEGREES          
REMARK 500    CYS A 137   CA  -  C   -  N   ANGL. DEV. = -14.7 DEGREES          
REMARK 500    CYS A 137   O   -  C   -  N   ANGL. DEV. =  13.8 DEGREES          
REMARK 500    MET A 139   CG  -  SD  -  CE  ANGL. DEV. =   9.7 DEGREES          
REMARK 500    VAL A 140   CA  -  C   -  N   ANGL. DEV. = -13.4 DEGREES          
REMARK 500    VAL A 140   O   -  C   -  N   ANGL. DEV. =  13.0 DEGREES          
REMARK 500    GLU A 152   CB  -  CA  -  C   ANGL. DEV. =  19.4 DEGREES          
REMARK 500    GLU A 152   O   -  C   -  N   ANGL. DEV. = -11.2 DEGREES          
REMARK 500    ARG A 154   CB  -  CA  -  C   ANGL. DEV. =  13.9 DEGREES          
REMARK 500    ARG A 154   NE  -  CZ  -  NH2 ANGL. DEV. =   3.6 DEGREES          
REMARK 500    ASP A 161   O   -  C   -  N   ANGL. DEV. =  12.8 DEGREES          
REMARK 500    PRO A 168   O   -  C   -  N   ANGL. DEV. =  10.0 DEGREES          
REMARK 500    ILE A 169   O   -  C   -  N   ANGL. DEV. =  11.3 DEGREES          
REMARK 500    ARG A 171   NE  -  CZ  -  NH2 ANGL. DEV. =   3.2 DEGREES          
REMARK 500    GLY A 172   O   -  C   -  N   ANGL. DEV. =   9.8 DEGREES          
REMARK 500    LEU A 178   CB  -  CA  -  C   ANGL. DEV. = -14.6 DEGREES          
REMARK 500    GLU A 179   CB  -  CA  -  C   ANGL. DEV. =  16.4 DEGREES          
REMARK 500    LEU A 178   O   -  C   -  N   ANGL. DEV. =  10.5 DEGREES          
REMARK 500    GLY A 180   CA  -  C   -  N   ANGL. DEV. = -13.5 DEGREES          
REMARK 500    GLY A 180   O   -  C   -  N   ANGL. DEV. =  11.9 DEGREES          
REMARK 500    ALA A 182   CA  -  C   -  N   ANGL. DEV. = -14.8 DEGREES          
REMARK 500    ALA A 182   O   -  C   -  N   ANGL. DEV. =  14.2 DEGREES          
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    LYS A   9      151.56     64.70                                   
REMARK 500    VAL A  20       82.25    142.80                                   
REMARK 500    ASP A  21      -27.03    133.21                                   
REMARK 500    PRO A  72        5.00    -69.92                                   
REMARK 500    THR A  93      -95.02    -67.48                                   
REMARK 500    ALA A  96      -58.43     87.24                                   
REMARK 500    GLN A  97      120.16     56.18                                   
REMARK 500    ALA A 107      -36.31    -30.13                                   
REMARK 500    ASP A 109     -136.28    -95.87                                   
REMARK 500    VAL A 127       95.05    -62.69                                   
REMARK 500    LYS A 136       47.70    134.29                                   
REMARK 500    MET A 139       22.15   -162.32                                   
REMARK 500    ASP A 142       89.00    152.68                                   
REMARK 500    ASP A 161      -95.46   -147.99                                   
REMARK 500    PHE A 162      161.70    -44.55                                   
REMARK 500    PRO A 163      -75.49    -50.63                                   
REMARK 500    ASP A 165      -71.84    -99.70                                   
REMARK 500    SER A 173      109.78   -168.61                                   
REMARK 500    ALA A 182      162.04    147.45                                   
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: NON-CIS, NON-TRANS                                         
REMARK 500                                                                      
REMARK 500 THE FOLLOWING PEPTIDE BONDS DEVIATE SIGNIFICANTLY FROM BOTH          
REMARK 500 CIS AND TRANS CONFORMATION.  CIS BONDS, IF ANY, ARE LISTED           
REMARK 500 ON CISPEP RECORDS.  TRANS IS DEFINED AS 180 +/- 30 AND               
REMARK 500 CIS IS DEFINED AS 0 +/- 30 DEGREES.                                  
REMARK 500                                 MODEL     OMEGA                      
REMARK 500 ILE A  102     LEU A  103                 -148.97                    
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 620                                                                      
REMARK 620 METAL COORDINATION                                                   
REMARK 620  (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;              
REMARK 620  SSEQ=SEQUENCE NUMBER; I=INSERTION CODE):                            
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              MG A 394  MG                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 GDP A 395   O1B                                                    
REMARK 620 2 THR A  25   OG1  61.6                                              
REMARK 620 N                    1                                               
REMARK 800                                                                      
REMARK 800 SITE                                                                 
REMARK 800 SITE_IDENTIFIER: AC1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MG A 394                  
REMARK 800 SITE_IDENTIFIER: AC2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE GDP A 395                 
REMARK 999                                                                      
REMARK 999 SEQUENCE                                                             
REMARK 999                                                                      
REMARK 999 EF-TU IS CODED FOR BY TWO DIFFERENT GENES.  THE SEQUENCE             
REMARK 999 STRUCTURE ANALYSIS CARRIED OUT ON THIS MIXTURE SHOWS THAT            
REMARK 999 THE C-TERMINAL RESIDUE OCCURS AS GLY/SER IN THE RATIO OF             
REMARK 999 3/1.  THIS RESIDUE IS IDENTIFIED AS GLY ON THE *SEQRES*              
REMARK 999 RECORDS BELOW.                                                       
DBREF  1ETU A    1   393  UNP    P0A6N1   EFTU_ECOLI       1    392             
SEQRES   1 A  393  SER 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 GLY                                                  
HET     MG  A 394       1                                                       
HET    GDP  A 395      28                                                       
HETNAM      MG MAGNESIUM ION                                                    
HETNAM     GDP GUANOSINE-5'-DIPHOSPHATE                                         
FORMUL   2   MG    MG 2+                                                        
FORMUL   3  GDP    C10 H15 N5 O11 P2                                            
HELIX    1   1 GLY A   23  GLY A   40  1                                  18    
HELIX    2   2 GLY A   83  THR A   93  1                                  11    
HELIX    3   3 MET A  112  GLY A  126  1                                  15    
HELIX    4   4 ASP A  142  ASP A  161  1                                  20    
HELIX    5   5 SER A  173  GLY A  180  1                                   8    
HELIX    6   6 ALA A  182  ILE A  199  1                                  18    
SHEET    1   A 6 SER A  65  ASP A  70  0                                        
SHEET    2   A 6 HIS A  75  ASP A  80 -1  N  TYR A  76   O  TYR A  69           
SHEET    3   A 6 HIS A  11  ILE A  17  1  O  VAL A  12   N  ALA A  77           
SHEET    4   A 6 GLY A 100  VAL A 105  1  O  GLY A 100   N  GLY A  15           
SHEET    5   A 6 TYR A 129  ASN A 135  1  O  TYR A 129   N  ALA A 101           
SHEET    6   A 6 ILE A 169  GLY A 172  1  O  VAL A 170   N  LEU A 134           
LINK         OD1 ASP A 138                 N2  GDP A 395     1555   1555  1.97  
LINK        MG    MG A 394                 O1B GDP A 395     1555   1555  3.04  
LINK        MG    MG A 394                 OG1 THR A  25     1555   1555  2.09  
SITE     1 AC1  2 THR A  25  GDP A 395                                          
SITE     1 AC2 12 ASP A  21  HIS A  22  GLY A  23  LYS A  24                    
SITE     2 AC2 12 THR A  25  THR A  26  ASN A 135  MET A 139                    
SITE     3 AC2 12 SER A 173  ALA A 174  LEU A 175   MG A 394                    
CRYST1   98.200  100.800  160.800  90.00  90.00  90.00 C 2 2 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      0.010183  0.000000  0.000000        0.00000                         
SCALE2      0.000000  0.009921  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.006219        0.00000                         
(ATOM LINES ARE NOT SHOWN.)
END                                                                             
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