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Database: PDB
Entry: 1SCU
LinkDB: 1SCU
Original site: 1SCU 
HEADER    LIGASE (ATP-BINDING)                    18-NOV-93   1SCU              
TITLE     THE CRYSTAL STRUCTURE OF SUCCINYL-COA SYNTHETASE FROM                 
TITLE    2 ESCHERICHIA COLI AT 2.5 ANGSTROMS RESOLUTION                         
COMPND    MOL_ID: 1;                                                            
COMPND   2 MOLECULE: SUCCINYL-COA SYNTHETASE, ALPHA SUBUNIT;                    
COMPND   3 CHAIN: A, D;                                                         
COMPND   4 EC: 6.2.1.5;                                                         
COMPND   5 ENGINEERED: YES;                                                     
COMPND   6 MOL_ID: 2;                                                           
COMPND   7 MOLECULE: SUCCINYL-COA SYNTHETASE, BETA SUBUNIT;                     
COMPND   8 CHAIN: B, E;                                                         
COMPND   9 EC: 6.2.1.5;                                                         
COMPND  10 ENGINEERED: YES                                                      
SOURCE    MOL_ID: 1;                                                            
SOURCE   2 ORGANISM_SCIENTIFIC: ESCHERICHIA COLI;                               
SOURCE   3 ORGANISM_TAXID: 562;                                                 
SOURCE   4 MOL_ID: 2;                                                           
SOURCE   5 ORGANISM_SCIENTIFIC: ESCHERICHIA COLI;                               
SOURCE   6 ORGANISM_TAXID: 562                                                  
KEYWDS    LIGASE (ATP-BINDING)                                                  
EXPDTA    X-RAY DIFFRACTION                                                     
AUTHOR    W.T.WOLODKO,M.E.FRASER,M.N.G.JAMES,W.A.BRIDGER                        
REVDAT   4   21-APR-09 1SCU    1       MODRES                                   
REVDAT   3   24-FEB-09 1SCU    1       VERSN                                    
REVDAT   2   01-APR-03 1SCU    1       JRNL                                     
REVDAT   1   20-APR-95 1SCU    0                                                
JRNL        AUTH   W.T.WOLODKO,M.E.FRASER,M.N.JAMES,W.A.BRIDGER                 
JRNL        TITL   THE CRYSTAL STRUCTURE OF SUCCINYL-COA SYNTHETASE             
JRNL        TITL 2 FROM ESCHERICHIA COLI AT 2.5-A RESOLUTION.                   
JRNL        REF    J.BIOL.CHEM.                  V. 269 10883 1994              
JRNL        REFN                   ISSN 0021-9258                               
JRNL        PMID   8144675                                                      
REMARK   1                                                                      
REMARK   1 REFERENCE 1                                                          
REMARK   1  AUTH   W.T.WOLODKO,M.N.G.JAMES,W.A.BRIDGER                          
REMARK   1  TITL   CRYSTALLIZATION OF SUCCINYL-COA SYNTHETASE FROM              
REMARK   1  TITL 2 ESCHERICHIA COLI                                             
REMARK   1  REF    J.BIOL.CHEM.                  V. 249  5316 1984              
REMARK   1  REFN                   ISSN 0021-9258                               
REMARK   2                                                                      
REMARK   2 RESOLUTION.    2.50 ANGSTROMS.                                       
REMARK   3                                                                      
REMARK   3 REFINEMENT.                                                          
REMARK   3   PROGRAM     : TNT, X-PLOR                                          
REMARK   3   AUTHORS     : TRONRUD,TEN EYCK,MATTHEWS                            
REMARK   3                                                                      
REMARK   3  DATA USED IN REFINEMENT.                                            
REMARK   3   RESOLUTION RANGE HIGH (ANGSTROMS) : 2.50                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 100.00                         
REMARK   3   DATA CUTOFF            (SIGMA(F)) : 0.000                          
REMARK   3   COMPLETENESS FOR RANGE        (%) : NULL                           
REMARK   3   NUMBER OF REFLECTIONS             : 67272                          
REMARK   3                                                                      
REMARK   3  USING DATA ABOVE SIGMA CUTOFF.                                      
REMARK   3   CROSS-VALIDATION METHOD          : NULL                            
REMARK   3   FREE R VALUE TEST SET SELECTION  : NULL                            
REMARK   3   R VALUE     (WORKING + TEST SET) : 0.216                           
REMARK   3   R VALUE            (WORKING SET) : 0.216                           
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                                                                      
REMARK   3  USING ALL DATA, NO SIGMA CUTOFF.                                    
REMARK   3   R VALUE   (WORKING + TEST SET, NO CUTOFF) : NULL                   
REMARK   3   R VALUE          (WORKING SET, NO CUTOFF) : NULL                   
REMARK   3   FREE R VALUE                  (NO CUTOFF) : NULL                   
REMARK   3   FREE R VALUE TEST SET SIZE (%, NO CUTOFF) : NULL                   
REMARK   3   FREE R VALUE TEST SET COUNT   (NO CUTOFF) : NULL                   
REMARK   3   TOTAL NUMBER OF REFLECTIONS   (NO CUTOFF) : NULL                   
REMARK   3                                                                      
REMARK   3  NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.                    
REMARK   3   PROTEIN ATOMS            : 9982                                    
REMARK   3   NUCLEIC ACID ATOMS       : 0                                       
REMARK   3   HETEROGEN ATOMS          : 96                                      
REMARK   3   SOLVENT ATOMS            : 110                                     
REMARK   3                                                                      
REMARK   3  WILSON B VALUE (FROM FCALC, A**2) : NULL                            
REMARK   3                                                                      
REMARK   3  RMS DEVIATIONS FROM IDEAL VALUES.    RMS    WEIGHT  COUNT           
REMARK   3   BOND LENGTHS                 (A) : NULL  ; NULL  ; NULL            
REMARK   3   BOND ANGLES            (DEGREES) : NULL  ; NULL  ; NULL            
REMARK   3   TORSION ANGLES         (DEGREES) : NULL  ; NULL  ; NULL            
REMARK   3   PSEUDOROTATION ANGLES  (DEGREES) : NULL  ; NULL  ; NULL            
REMARK   3   TRIGONAL CARBON PLANES       (A) : NULL  ; NULL  ; NULL            
REMARK   3   GENERAL PLANES               (A) : NULL  ; NULL  ; NULL            
REMARK   3   ISOTROPIC THERMAL FACTORS (A**2) : NULL  ; NULL  ; NULL            
REMARK   3   NON-BONDED CONTACTS          (A) : NULL  ; NULL  ; NULL            
REMARK   3                                                                      
REMARK   3  INCORRECT CHIRAL-CENTERS (COUNT) : NULL                             
REMARK   3                                                                      
REMARK   3  BULK SOLVENT MODELING.                                              
REMARK   3   METHOD USED : NULL                                                 
REMARK   3   KSOL        : NULL                                                 
REMARK   3   BSOL        : NULL                                                 
REMARK   3                                                                      
REMARK   3  RESTRAINT LIBRARIES.                                                
REMARK   3   STEREOCHEMISTRY : NULL                                             
REMARK   3   ISOTROPIC THERMAL FACTOR RESTRAINTS : NULL                         
REMARK   3                                                                      
REMARK   3  OTHER REFINEMENT REMARKS: NULL                                      
REMARK   4                                                                      
REMARK   4 1SCU 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: X-PLOR                                                
REMARK 200 STARTING MODEL: NULL                                                 
REMARK 200                                                                      
REMARK 200 REMARK: NULL                                                         
REMARK 280                                                                      
REMARK 280 CRYSTAL                                                              
REMARK 280 SOLVENT CONTENT, VS   (%): 63.93                                     
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 3.41                     
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: NULL                                     
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY                                            
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 43 2 2                         
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   -Y,X,Z+3/4                                              
REMARK 290       4555   Y,-X,Z+1/4                                              
REMARK 290       5555   -X,Y,-Z                                                 
REMARK 290       6555   X,-Y,-Z+1/2                                             
REMARK 290       7555   Y,X,-Z+1/4                                              
REMARK 290       8555   -Y,-X,-Z+3/4                                            
REMARK 290                                                                      
REMARK 290     WHERE NNN -> OPERATOR NUMBER                                     
REMARK 290           MMM -> TRANSLATION VECTOR                                  
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY TRANSFORMATIONS                            
REMARK 290 THE FOLLOWING TRANSFORMATIONS OPERATE ON THE ATOM/HETATM             
REMARK 290 RECORDS IN THIS ENTRY TO PRODUCE CRYSTALLOGRAPHICALLY                
REMARK 290 RELATED MOLECULES.                                                   
REMARK 290   SMTRY1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 290   SMTRY1   2 -1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   2  0.000000 -1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   2  0.000000  0.000000  1.000000      200.30000            
REMARK 290   SMTRY1   3  0.000000 -1.000000  0.000000        0.00000            
REMARK 290   SMTRY2   3  1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY3   3  0.000000  0.000000  1.000000      300.45000            
REMARK 290   SMTRY1   4  0.000000  1.000000  0.000000        0.00000            
REMARK 290   SMTRY2   4 -1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY3   4  0.000000  0.000000  1.000000      100.15000            
REMARK 290   SMTRY1   5 -1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   5  0.000000  1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   5  0.000000  0.000000 -1.000000        0.00000            
REMARK 290   SMTRY1   6  1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   6  0.000000 -1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   6  0.000000  0.000000 -1.000000      200.30000            
REMARK 290   SMTRY1   7  0.000000  1.000000  0.000000        0.00000            
REMARK 290   SMTRY2   7  1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY3   7  0.000000  0.000000 -1.000000      100.15000            
REMARK 290   SMTRY1   8  0.000000 -1.000000  0.000000        0.00000            
REMARK 290   SMTRY2   8 -1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY3   8  0.000000  0.000000 -1.000000      300.45000            
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 APPLY THE FOLLOWING TO CHAINS: A, B, D, E                            
REMARK 350   BIOMT1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 350   BIOMT2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 350   BIOMT3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: 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   CA   LEU B   189     O    HOH B   408              1.27            
REMARK 500   CA   TRP B   248     O    HOH B   418              1.43            
REMARK 500   O    HOH B   402     O    HOH B   403              1.47            
REMARK 500   C    LEU B   189     O    HOH B   408              1.54            
REMARK 500   O    LYS D   284     CG   LYS D   288              1.59            
REMARK 500   CG2  THR D   237     OD1  ASP E   274              1.65            
REMARK 500   C    TRP B   248     O    HOH B   418              1.67            
REMARK 500   N    MET D   118     O    HOH D   300              1.68            
REMARK 500   N    LEU B   189     O    HOH B   408              1.69            
REMARK 500   O    HOH E   397     O    HOH E   418              1.71            
REMARK 500   O    PRO B    42     O    HOH B   390              1.78            
REMARK 500   O    ASP E    87     N    ASN E    89              1.82            
REMARK 500   CB   MET B   270     O    HOH B   419              1.88            
REMARK 500   O    ILE D     2     O    HOH D   293              1.90            
REMARK 500   C    PHE B   188     O    HOH B   408              1.90            
REMARK 500   O    ILE B   304     OG   SER B   307              1.91            
REMARK 500   O    PHE B   188     O    HOH B   408              1.93            
REMARK 500   O    LYS D   284     CD   LYS D   288              1.93            
REMARK 500   O    ILE D   203     CG2  VAL D   229              1.95            
REMARK 500   C    ILE D     2     O    HOH D   293              1.96            
REMARK 500   OD1  ASP D   259     NH2  ARG D   274              2.00            
REMARK 500   O    GLY D   139     N    ILE D   141              2.01            
REMARK 500   OD2  ASP B   274     O    HOH B   420              2.03            
REMARK 500   O    ASP E   150     O    THR E   153              2.04            
REMARK 500   CG   ASP E   115     O    HOH E   395              2.05            
REMARK 500   O    ASP E   326     N    ILE E   328              2.05            
REMARK 500   O    ALA E   383     N    GLU E   386              2.07            
REMARK 500   O    LEU B   223     NH1  ARG B   230              2.08            
REMARK 500   O    THR B   140     N    LEU B   143              2.10            
REMARK 500   O    GLN A   163     N    THR A   165              2.10            
REMARK 500   CA   MET B   270     O    HOH B   419              2.13            
REMARK 500   OE1  GLN D   163     O    ALA D   277              2.13            
REMARK 500   O    LEU B   189     O    HOH B   408              2.13            
REMARK 500   O    GLU D   266     N    GLY D   269              2.13            
REMARK 500   CB   TRP B   248     O    HOH B   418              2.14            
REMARK 500   O    ALA B   222     N    ARG B   225              2.14            
REMARK 500   O    THR D   165     N    GLY D   168              2.14            
REMARK 500   O    ASP A   197     NZ   LYS A   227              2.15            
REMARK 500   O    SER A   212     OE1  GLU A   215              2.15            
REMARK 500   OD1  ASP A     5     N    ASN A     7              2.15            
REMARK 500   O    ILE D   203     N    VAL D   230              2.15            
REMARK 500   OE2  GLU B   249     NH2  ARG E    70              2.17            
REMARK 500   O    ALA E   246     N    TRP E   248              2.17            
REMARK 500   OD1  ASP B   150     N    LEU B   152              2.18            
REMARK 500   OD1  ASP E   239     N    ARG E   241              2.18            
REMARK 500   O    ALA E   246     N    GLU E   249              2.18            
REMARK 500   OD1  ASP B   326     ND2  ASN B   353              2.19            
REMARK 500   O    THR D   157     CG2  VAL D   161              2.19            
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    GLU A  25   CD    GLU A  25   OE2     0.077                       
REMARK 500    GLU A  58   CD    GLU A  58   OE2     0.074                       
REMARK 500    GLU A  97   CD    GLU A  97   OE2     0.086                       
REMARK 500    GLU A 113   CD    GLU A 113   OE2     0.074                       
REMARK 500    GLU A 131   CD    GLU A 131   OE2     0.066                       
REMARK 500    GLU A 159   CD    GLU A 159   OE2     0.074                       
REMARK 500    GLU A 201   CD    GLU A 201   OE1     0.069                       
REMARK 500    GLU A 214   CD    GLU A 214   OE2     0.084                       
REMARK 500    GLU A 215   CD    GLU A 215   OE2     0.069                       
REMARK 500    GLU A 216   CD    GLU A 216   OE2     0.069                       
REMARK 500    GLU A 223   CD    GLU A 223   OE1     0.090                       
REMARK 500    GLU A 260   CD    GLU A 260   OE2     0.068                       
REMARK 500    GLU A 266   CD    GLU A 266   OE2     0.083                       
REMARK 500    GLU A 281   CD    GLU A 281   OE2     0.068                       
REMARK 500    GLU B   5   CD    GLU B   5   OE2     0.083                       
REMARK 500    GLU B  32   CD    GLU B  32   OE2     0.087                       
REMARK 500    GLU B  33   CD    GLU B  33   OE2     0.068                       
REMARK 500    GLU B  74   CD    GLU B  74   OE2     0.079                       
REMARK 500    GLU B 128   CD    GLU B 128   OE1     0.072                       
REMARK 500    GLU B 132   CD    GLU B 132   OE2     0.074                       
REMARK 500    GLU B 134   CD    GLU B 134   OE2     0.069                       
REMARK 500    GLU B 138   CD    GLU B 138   OE2     0.070                       
REMARK 500    GLU B 139   CD    GLU B 139   OE2     0.075                       
REMARK 500    GLU B 162   CD    GLU B 162   OE2     0.114                       
REMARK 500    GLU B 170   CD    GLU B 170   OE2     0.076                       
REMARK 500    GLU B 190   CD    GLU B 190   OE2     0.068                       
REMARK 500    GLU B 197   CD    GLU B 197   OE2     0.082                       
REMARK 500    GLU B 231   CD    GLU B 231   OE2     0.075                       
REMARK 500    GLU B 238   CD    GLU B 238   OE2     0.073                       
REMARK 500    GLU B 242   CD    GLU B 242   OE2     0.079                       
REMARK 500    GLU B 249   CD    GLU B 249   OE2     0.083                       
REMARK 500    GLU B 282   CD    GLU B 282   OE2     0.073                       
REMARK 500    GLU B 296   CD    GLU B 296   OE2     0.069                       
REMARK 500    GLU B 300   CD    GLU B 300   OE2     0.078                       
REMARK 500    GLU B 338   CD    GLU B 338   OE2     0.083                       
REMARK 500    GLU B 386   CD    GLU B 386   OE1     0.067                       
REMARK 500    GLU D  25   CD    GLU D  25   OE2     0.071                       
REMARK 500    GLU D  58   CD    GLU D  58   OE2     0.106                       
REMARK 500    GLU D  97   CD    GLU D  97   OE1     0.076                       
REMARK 500    GLU D 113   CD    GLU D 113   OE2     0.073                       
REMARK 500    GLU D 131   CD    GLU D 131   OE2     0.070                       
REMARK 500    GLU D 159   CD    GLU D 159   OE2     0.078                       
REMARK 500    GLU D 192   CD    GLU D 192   OE2     0.083                       
REMARK 500    GLU D 195   CD    GLU D 195   OE2     0.071                       
REMARK 500    GLU D 208   CD    GLU D 208   OE2     0.085                       
REMARK 500    GLU D 215   CD    GLU D 215   OE2     0.079                       
REMARK 500    GLU D 216   CD    GLU D 216   OE2     0.068                       
REMARK 500    GLU D 223   CD    GLU D 223   OE2     0.069                       
REMARK 500    GLU D 260   CD    GLU D 260   OE2     0.071                       
REMARK 500    GLU D 266   CD    GLU D 266   OE2     0.085                       
REMARK 500                                                                      
REMARK 500 THIS ENTRY HAS      71 BOND DEVIATIONS.                              
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    LEU A   3   C   -  N   -  CA  ANGL. DEV. = -16.9 DEGREES          
REMARK 500    ASP A   5   CB  -  CG  -  OD1 ANGL. DEV. =   6.1 DEGREES          
REMARK 500    HIS A  23   CA  -  CB  -  CG  ANGL. DEV. = -13.9 DEGREES          
REMARK 500    VAL A  56   CA  -  CB  -  CG1 ANGL. DEV. = -10.6 DEGREES          
REMARK 500    VAL A  69   CB  -  CA  -  C   ANGL. DEV. = -12.5 DEGREES          
REMARK 500    VAL A  69   CA  -  CB  -  CG2 ANGL. DEV. =  -9.5 DEGREES          
REMARK 500    CYS A  77   CA  -  CB  -  SG  ANGL. DEV. = -13.6 DEGREES          
REMARK 500    ASP A  79   CB  -  CG  -  OD1 ANGL. DEV. =   8.8 DEGREES          
REMARK 500    ASP A  79   CB  -  CG  -  OD2 ANGL. DEV. =  -7.9 DEGREES          
REMARK 500    THR A 101   CA  -  CB  -  CG2 ANGL. DEV. = -11.7 DEGREES          
REMARK 500    GLN A 137   N   -  CA  -  CB  ANGL. DEV. = -13.0 DEGREES          
REMARK 500    VAL A 150   CB  -  CA  -  C   ANGL. DEV. = -11.4 DEGREES          
REMARK 500    ARG A 152   NE  -  CZ  -  NH1 ANGL. DEV. =   3.8 DEGREES          
REMARK 500    ARG A 152   NE  -  CZ  -  NH2 ANGL. DEV. =  -5.2 DEGREES          
REMARK 500    ASP A 166   CB  -  CG  -  OD1 ANGL. DEV. =   5.8 DEGREES          
REMARK 500    ASP A 166   CB  -  CG  -  OD2 ANGL. DEV. =  -7.9 DEGREES          
REMARK 500    ASP A 180   CB  -  CG  -  OD1 ANGL. DEV. =   6.1 DEGREES          
REMARK 500    PRO A 183   C   -  N   -  CD  ANGL. DEV. = -18.0 DEGREES          
REMARK 500    ASP A 189   CB  -  CG  -  OD2 ANGL. DEV. =  -5.8 DEGREES          
REMARK 500    VAL A 204   CA  -  CB  -  CG1 ANGL. DEV. =  -9.7 DEGREES          
REMARK 500    GLY A 210   C   -  N   -  CA  ANGL. DEV. = -12.9 DEGREES          
REMARK 500    ALA A 213   N   -  CA  -  CB  ANGL. DEV. = -13.3 DEGREES          
REMARK 500    ALA A 219   CB  -  CA  -  C   ANGL. DEV. = -10.8 DEGREES          
REMARK 500    SER A 275   N   -  CA  -  CB  ANGL. DEV. =  11.2 DEGREES          
REMARK 500    ASP A 278   CB  -  CG  -  OD1 ANGL. DEV. =   5.7 DEGREES          
REMARK 500    ASP A 278   CB  -  CG  -  OD2 ANGL. DEV. =  -6.1 DEGREES          
REMARK 500    ARG B  14   NE  -  CZ  -  NH1 ANGL. DEV. =   4.2 DEGREES          
REMARK 500    ASP B  68   CB  -  CG  -  OD1 ANGL. DEV. =   5.4 DEGREES          
REMARK 500    ASP B  68   CB  -  CG  -  OD2 ANGL. DEV. =  -7.0 DEGREES          
REMARK 500    ARG B  70   NE  -  CZ  -  NH1 ANGL. DEV. =   4.6 DEGREES          
REMARK 500    VAL B 113   CB  -  CA  -  C   ANGL. DEV. = -12.4 DEGREES          
REMARK 500    ASP B 115   CB  -  CG  -  OD2 ANGL. DEV. =  -6.2 DEGREES          
REMARK 500    PRO B 141   C   -  N   -  CD  ANGL. DEV. = -30.7 DEGREES          
REMARK 500    ASP B 150   CB  -  CG  -  OD1 ANGL. DEV. =   5.6 DEGREES          
REMARK 500    GLY B 154   C   -  N   -  CA  ANGL. DEV. = -13.5 DEGREES          
REMARK 500    ARG B 191   NE  -  CZ  -  NH1 ANGL. DEV. =  -3.3 DEGREES          
REMARK 500    ILE B 196   CB  -  CA  -  C   ANGL. DEV. = -12.9 DEGREES          
REMARK 500    ASP B 213   CB  -  CG  -  OD2 ANGL. DEV. =  -5.5 DEGREES          
REMARK 500    ASP B 219   CB  -  CG  -  OD1 ANGL. DEV. =   5.7 DEGREES          
REMARK 500    ARG B 225   CD  -  NE  -  CZ  ANGL. DEV. =   8.9 DEGREES          
REMARK 500    ARG B 225   NE  -  CZ  -  NH1 ANGL. DEV. =   4.6 DEGREES          
REMARK 500    ARG B 230   NE  -  CZ  -  NH1 ANGL. DEV. =   3.0 DEGREES          
REMARK 500    ASP B 256   CB  -  CG  -  OD2 ANGL. DEV. =  -5.8 DEGREES          
REMARK 500    ASP B 288   CB  -  CG  -  OD1 ANGL. DEV. =   6.1 DEGREES          
REMARK 500    ASP B 288   CB  -  CG  -  OD2 ANGL. DEV. =  -7.1 DEGREES          
REMARK 500    ARG B 297   NE  -  CZ  -  NH1 ANGL. DEV. =   3.0 DEGREES          
REMARK 500    ARG B 297   NE  -  CZ  -  NH2 ANGL. DEV. =  -3.3 DEGREES          
REMARK 500    ASP B 308   CB  -  CG  -  OD2 ANGL. DEV. =  -6.2 DEGREES          
REMARK 500    ASP B 309   CB  -  CG  -  OD2 ANGL. DEV. =  -5.7 DEGREES          
REMARK 500    CYS B 325   CB  -  CA  -  C   ANGL. DEV. =  14.4 DEGREES          
REMARK 500                                                                      
REMARK 500 THIS ENTRY HAS     121 ANGLE DEVIATIONS.                             
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    ILE A   2      -51.19   -128.73                                   
REMARK 500    PHE A  22      -75.36    -36.37                                   
REMARK 500    PRO A  40      124.94    -37.34                                   
REMARK 500    LEU A  48       29.02     46.88                                   
REMARK 500    ALA A  74      -67.17    -22.45                                   
REMARK 500    LYS A  78      -39.97    -38.99                                   
REMARK 500    THR A  96      141.27    -35.73                                   
REMARK 500    PRO A 121     -165.36   -100.73                                   
REMARK 500    GLN A 137      133.46    -31.82                                   
REMARK 500    HIS A 140        3.16    -54.62                                   
REMARK 500    LEU A 156      -57.54    -29.06                                   
REMARK 500    ALA A 160      -74.02    -28.92                                   
REMARK 500    VAL A 161      -71.35    -32.94                                   
REMARK 500    LYS A 162      -64.62    -29.86                                   
REMARK 500    GLN A 163      -91.66    -48.06                                   
REMARK 500    THR A 164      -40.68    -21.57                                   
REMARK 500    SER A 172      -73.50    -77.78                                   
REMARK 500    PHE A 187      -73.57    -39.95                                   
REMARK 500    ILE A 188      -71.80    -36.15                                   
REMARK 500    ASP A 189      -45.98    -21.45                                   
REMARK 500    ALA A 213      -76.16      5.61                                   
REMARK 500    GLU A 214      -72.93    -44.72                                   
REMARK 500    ALA A 218      -70.19    -28.28                                   
REMARK 500    ALA A 219      -89.04    -25.20                                   
REMARK 500    TYR A 220      -78.86    -27.28                                   
REMARK 500    ILE A 221      -75.66    -20.54                                   
REMARK 500    HIS A 224       -1.88   -157.56                                   
REMARK 500    LYS A 227      160.13    -46.53                                   
REMARK 500    ALA A 252     -135.44    -60.04                                   
REMARK 500    GLU A 281      -85.54    -38.82                                   
REMARK 500    ALA A 282      -46.10    -26.87                                   
REMARK 500    LYS A 284      -57.70    -26.15                                   
REMARK 500    THR A 285      -90.44    -55.05                                   
REMARK 500    VAL A 286      -22.87    -36.70                                   
REMARK 500    ASP B  87     -130.63    -66.24                                   
REMARK 500    ALA B 105      -70.21    -80.50                                   
REMARK 500    LEU B 108     -164.90   -101.87                                   
REMARK 500    LYS B 135      -79.19    -66.89                                   
REMARK 500    VAL B 136      -57.74    -21.06                                   
REMARK 500    GLU B 139       -2.64   -144.04                                   
REMARK 500    THR B 140       29.87   -140.71                                   
REMARK 500    PRO B 141      -31.64    -24.32                                   
REMARK 500    GLN B 206       -4.56    -53.39                                   
REMARK 500    ASP B 234       73.06   -117.44                                   
REMARK 500    GLU B 249       40.29     38.69                                   
REMARK 500    LEU B 255     -156.96   -119.52                                   
REMARK 500    HIS B 279       40.20    -80.59                                   
REMARK 500    ASN B 285      166.26    174.65                                   
REMARK 500    ALA B 293       61.50    -54.85                                   
REMARK 500    ASP B 309       -5.04    -54.04                                   
REMARK 500    PHE B 319      -86.55   -125.21                                   
REMARK 500    ASN B 342       41.96    -99.14                                   
REMARK 500    ASP B 363      -15.02    -46.34                                   
REMARK 500    LYS B 372      -91.56    -69.60                                   
REMARK 500    LEU B 374      -82.48    -30.13                                   
REMARK 500    ALA B 378      -72.74    -37.87                                   
REMARK 500    ALA B 383      -96.93    -34.98                                   
REMARK 500    ALA B 384      -43.33    -27.79                                   
REMARK 500    ILE D   2     -161.23   -125.83                                   
REMARK 500    LEU D   3      -38.11     -7.45                                   
REMARK 500    PHE D  15      -51.74    -29.45                                   
REMARK 500    SER D  18      -75.12    -47.13                                   
REMARK 500    PHE D  22      -72.37    -51.65                                   
REMARK 500    HIS D  23      -19.81    -45.14                                   
REMARK 500    LYS D  33       72.42    -69.83                                   
REMARK 500    VAL D  35       -7.74   -150.04                                   
REMARK 500    ALA D  61      -70.25    -62.95                                   
REMARK 500    ALA D  62       -7.43    -48.34                                   
REMARK 500    ALA D  74      -51.10    -24.40                                   
REMARK 500    THR D  96      144.36    -22.83                                   
REMARK 500    PRO D 129      134.81    -37.93                                   
REMARK 500    GLU D 131      -71.35    -92.55                                   
REMARK 500    GLN D 137      157.89    -42.20                                   
REMARK 500    HIS D 140        9.40    -25.73                                   
REMARK 500    SER D 153      134.58   -170.42                                   
REMARK 500    ALA D 160      -70.43    -41.02                                   
REMARK 500    VAL D 161      -78.83    -27.45                                   
REMARK 500    LYS D 162      -65.59    -24.83                                   
REMARK 500    GLN D 163      -70.46    -43.58                                   
REMARK 500    PHE D 169      -83.97    -37.84                                   
REMARK 500    SER D 172      -70.41    -65.76                                   
REMARK 500    PHE D 187      -73.52    -44.61                                   
REMARK 500    LEU D 191      -72.11    -52.64                                   
REMARK 500    GLU D 192      -62.98    -26.95                                   
REMARK 500    SER D 212       -2.17   -163.04                                   
REMARK 500    ALA D 218     -100.80    -43.08                                   
REMARK 500    ALA D 219      -49.31    -17.42                                   
REMARK 500    TYR D 220      -71.92    -51.53                                   
REMARK 500    LYS D 227      154.59    -37.74                                   
REMARK 500    ALA D 249       76.29   -119.76                                   
REMARK 500    ALA D 252      103.76    -59.57                                   
REMARK 500    ALA D 263      -79.29    -52.61                                   
REMARK 500    ALA D 264      -40.80    -23.17                                   
REMARK 500    ALA D 268        6.64    -69.97                                   
REMARK 500    ALA D 277      -72.33    -43.53                                   
REMARK 500    ASP D 278       29.36    -66.04                                   
REMARK 500    LYS D 284      -46.08    -25.15                                   
REMARK 500    THR D 285      -86.05    -59.33                                   
REMARK 500    LEU D 287       41.54    -91.60                                   
REMARK 500    THR E  27      138.83   -171.21                                   
REMARK 500    ALA E  35      -37.63    -37.45                                   
REMARK 500    PRO E  42      175.84    -58.32                                   
REMARK 500    THR E  86     -157.32    -92.22                                   
REMARK 500    ALA E  88      -10.63     45.61                                   
REMARK 500    GLU E 128       54.21    -68.47                                   
REMARK 500    GLU E 132      100.41    -54.34                                   
REMARK 500    LYS E 135      -75.75    -52.26                                   
REMARK 500    THR E 140       38.97    171.44                                   
REMARK 500    PRO E 141      -16.77    -38.54                                   
REMARK 500    GLU E 197      107.89   -161.88                                   
REMARK 500    GLN E 206       -3.94    -55.15                                   
REMARK 500    GLN E 226       56.78   -157.09                                   
REMARK 500    GLN E 247       -5.65    -44.43                                   
REMARK 500    GLU E 249       46.06     72.50                                   
REMARK 500    VAL E 253      113.43   -160.03                                   
REMARK 500    LEU E 255     -144.00   -126.46                                   
REMARK 500    ASN E 258       14.60   -144.00                                   
REMARK 500    ALA E 269      -79.69    -40.68                                   
REMARK 500    ALA E 293       64.03    -64.24                                   
REMARK 500    LYS E 295      -77.45    -22.15                                   
REMARK 500    ALA E 313      157.10    171.52                                   
REMARK 500    PHE E 319     -113.86    -94.66                                   
REMARK 500    VAL E 323      -96.59   -106.36                                   
REMARK 500    ARG E 324      124.34    155.92                                   
REMARK 500    CYS E 325      -74.96    -16.12                                   
REMARK 500    ASP E 326      -78.74    -58.53                                   
REMARK 500    LEU E 327      -40.91    -20.47                                   
REMARK 500    ASP E 330      -72.67    -43.86                                   
REMARK 500    ALA E 337      -87.56    -61.29                                   
REMARK 500    GLU E 338      -67.63    -22.81                                   
REMARK 500    ASN E 352       99.12    -36.10                                   
REMARK 500    LYS E 372      -74.83    -74.29                                   
REMARK 500    ALA E 383      -78.53    -59.40                                   
REMARK 500    ALA E 384      -68.36    -10.50                                   
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: CHIRAL CENTERS                                             
REMARK 500                                                                      
REMARK 500 UNEXPECTED CONFIGURATION OF THE FOLLOWING CHIRAL                     
REMARK 500 CENTER(S) USING IMPROPER CA--C--CB--N CHIRALITY                      
REMARK 500 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: (11X,I3,1X,A3,1X,A1,I4,A1,6X,F5.1,6X,A1,10X,A1,3X,A16)       
REMARK 500                                                                      
REMARK 500   M RES CSSEQI    IMPROPER   EXPECTED   FOUND DETAILS                
REMARK 500     LEU A  48        21.9      L          L   OUTSIDE RANGE          
REMARK 500     ALA A  74        21.8      L          L   OUTSIDE RANGE          
REMARK 500     ILE A 134        20.9      L          L   OUTSIDE RANGE          
REMARK 500     ILE A 136        24.8      L          L   OUTSIDE RANGE          
REMARK 500     PHE A 169        24.2      L          L   OUTSIDE RANGE          
REMARK 500     VAL A 175        22.2      L          L   OUTSIDE RANGE          
REMARK 500     SER A 275        20.3      L          L   OUTSIDE RANGE          
REMARK 500     LEU A 287        22.9      L          L   OUTSIDE RANGE          
REMARK 500     GLU B  32        23.0      L          L   OUTSIDE RANGE          
REMARK 500     ALA B  34        24.3      L          L   OUTSIDE RANGE          
REMARK 500     ASN B  64        -3.2      L          D   EXPECTING SP3          
REMARK 500     THR B 102        22.0      L          L   OUTSIDE RANGE          
REMARK 500     ILE B 104        23.8      L          L   OUTSIDE RANGE          
REMARK 500     ALA B 112        24.6      L          L   OUTSIDE RANGE          
REMARK 500     GLU B 134        23.1      L          L   OUTSIDE RANGE          
REMARK 500     ALA B 222        21.0      L          L   OUTSIDE RANGE          
REMARK 500     ASP B 256        24.7      L          L   OUTSIDE RANGE          
REMARK 500     CYS B 325        14.2      L          L   OUTSIDE RANGE          
REMARK 500     ASN B 352        24.1      L          L   OUTSIDE RANGE          
REMARK 500     LEU D   3        18.7      L          L   OUTSIDE RANGE          
REMARK 500     ALA D  74        15.4      L          L   OUTSIDE RANGE          
REMARK 500     LYS D 133        23.5      L          L   OUTSIDE RANGE          
REMARK 500     ILE D 177        23.5      L          L   OUTSIDE RANGE          
REMARK 500     ASP D 197        20.4      L          L   OUTSIDE RANGE          
REMARK 500     ILE D 203        22.2      L          L   OUTSIDE RANGE          
REMARK 500     VAL D 225        19.9      L          L   OUTSIDE RANGE          
REMARK 500     VAL D 229        23.8      L          L   OUTSIDE RANGE          
REMARK 500     ARG D 243        16.9      L          L   OUTSIDE RANGE          
REMARK 500     ASN E  64         4.2      L          D   EXPECTING SP3          
REMARK 500     GLU E  99        24.2      L          L   OUTSIDE RANGE          
REMARK 500     THR E 153        46.4      L          L   OUTSIDE RANGE          
REMARK 500     ALA E 243        23.0      L          L   OUTSIDE RANGE          
REMARK 500     ASP E 256        -6.4      L          D   EXPECTING SP3          
REMARK 500     LEU E 287         4.8      L          D   EXPECTING SP3          
REMARK 500     ASP E 288        24.8      L          L   OUTSIDE RANGE          
REMARK 500     LYS E 312        22.4      L          L   OUTSIDE RANGE          
REMARK 500     CYS E 325       -20.8      L          D   OUTSIDE RANGE          
REMARK 500     ASN E 352        -6.0      L          D   EXPECTING SP3          
REMARK 500     LYS E 388        14.6      L          L   OUTSIDE RANGE          
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 800                                                                      
REMARK 800 SITE                                                                 
REMARK 800 SITE_IDENTIFIER: AC1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE COA A 289                 
REMARK 800 SITE_IDENTIFIER: AC2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE COA D 289                 
REMARK 999                                                                      
REMARK 999 SEQUENCE                                                             
REMARK 999 AMINO-TERMINAL ANALYSIS OF THE ALPHA SUBUNIT INDICATES THAT          
REMARK 999 THE FIRST RESIDUE IS A SERINE (W. A. BRIDGE, ENZYMES,                
REMARK 999 3RD ED. 10, 581-606 (1974)).  IN THE GENE SEQUENCING                 
REMARK 999 PAPER, BUCK, SPENCER AND GUEST STATE THAT "[THE                      
REMARK 999 ASSUMPTION IS] THAT THE INITIATING FORMYLMETHIONINE IS               
REMARK 999 REMOVED POSTTRANSLATIONALLY FROM THE ALPHA BUT NOT FROM              
REMARK 999 THE BETA SUBUNIT" (D. BUCK, M. E. SPENCER, AND J. R. GUEST,          
REMARK 999 BIOCHEMISTRY 24, 6245-6252 (1985)).                                  
DBREF  1SCU A    1   288  UNP    P07459   SUCD_ECOLI       1    288             
DBREF  1SCU B    1   388  UNP    P0A836   SUCC_ECOLI       1    388             
DBREF  1SCU D    1   288  UNP    P07459   SUCD_ECOLI       1    288             
DBREF  1SCU E    1   388  UNP    P0A836   SUCC_ECOLI       1    388             
SEQRES   1 A  288  SER ILE LEU ILE ASP LYS ASN THR LYS VAL ILE CYS GLN          
SEQRES   2 A  288  GLY PHE THR GLY SER GLN GLY THR PHE HIS SER GLU GLN          
SEQRES   3 A  288  ALA ILE ALA TYR GLY THR LYS MET VAL GLY GLY VAL THR          
SEQRES   4 A  288  PRO GLY LYS GLY GLY THR THR HIS LEU GLY LEU PRO VAL          
SEQRES   5 A  288  PHE ASN THR VAL ARG GLU ALA VAL ALA ALA THR GLY ALA          
SEQRES   6 A  288  THR ALA SER VAL ILE TYR VAL PRO ALA PRO PHE CYS LYS          
SEQRES   7 A  288  ASP SER ILE LEU GLU ALA ILE ASP ALA GLY ILE LYS LEU          
SEQRES   8 A  288  ILE ILE THR ILE THR GLU GLY ILE PRO THR LEU ASP MET          
SEQRES   9 A  288  LEU THR VAL LYS VAL LYS LEU ASP GLU ALA GLY VAL ARG          
SEQRES  10 A  288  MET ILE GLY PRO ASN CYS PRO GLY VAL ILE THR PRO GLY          
SEQRES  11 A  288  GLU CYS LYS ILE GLY ILE GLN PRO GLY HIS ILE HIS LYS          
SEQRES  12 A  288  PRO GLY LYS VAL GLY ILE VAL SER ARG SER GLY THR LEU          
SEQRES  13 A  288  THR TYR GLU ALA VAL LYS GLN THR THR ASP TYR GLY PHE          
SEQRES  14 A  288  GLY GLN SER THR CYS VAL GLY ILE GLY GLY ASP PRO ILE          
SEQRES  15 A  288  PRO GLY SER ASN PHE ILE ASP ILE LEU GLU MET PHE GLU          
SEQRES  16 A  288  LYS ASP PRO GLN THR GLU ALA ILE VAL MET ILE GLY GLU          
SEQRES  17 A  288  ILE GLY GLY SER ALA GLU GLU GLU ALA ALA ALA TYR ILE          
SEQRES  18 A  288  LYS GLU HIS VAL THR LYS PRO VAL VAL GLY TYR ILE ALA          
SEQRES  19 A  288  GLY VAL THR ALA PRO LYS GLY LYS ARG MET GLY NEP ALA          
SEQRES  20 A  288  GLY ALA ILE ILE ALA GLY GLY LYS GLY THR ALA ASP GLU          
SEQRES  21 A  288  LYS PHE ALA ALA LEU GLU ALA ALA GLY VAL LYS THR VAL          
SEQRES  22 A  288  ARG SER LEU ALA ASP ILE GLY GLU ALA LEU LYS THR VAL          
SEQRES  23 A  288  LEU LYS                                                      
SEQRES   1 B  388  MET ASN LEU HIS GLU TYR GLN ALA LYS GLN LEU PHE ALA          
SEQRES   2 B  388  ARG TYR GLY LEU PRO ALA PRO VAL GLY TYR ALA CYS THR          
SEQRES   3 B  388  THR PRO ARG GLU ALA GLU GLU ALA ALA SER LYS ILE GLY          
SEQRES   4 B  388  ALA GLY PRO TRP VAL VAL LYS CYS GLN VAL HIS ALA GLY          
SEQRES   5 B  388  GLY ARG GLY LYS ALA GLY GLY VAL LYS VAL VAL ASN SER          
SEQRES   6 B  388  LYS GLU ASP ILE ARG ALA PHE ALA GLU ASN TRP LEU GLY          
SEQRES   7 B  388  LYS ARG LEU VAL THR TYR GLN THR ASP ALA ASN GLY GLN          
SEQRES   8 B  388  PRO VAL ASN GLN ILE LEU VAL GLU ALA ALA THR ASP ILE          
SEQRES   9 B  388  ALA LYS GLU LEU TYR LEU GLY ALA VAL VAL ASP ARG SER          
SEQRES  10 B  388  SER ARG ARG VAL VAL PHE MET ALA SER THR GLU GLY GLY          
SEQRES  11 B  388  VAL GLU ILE GLU LYS VAL ALA GLU GLU THR PRO HIS LEU          
SEQRES  12 B  388  ILE HIS LYS VAL ALA LEU ASP PRO LEU THR GLY PRO MET          
SEQRES  13 B  388  PRO TYR GLN GLY ARG GLU LEU ALA PHE LYS LEU GLY LEU          
SEQRES  14 B  388  GLU GLY LYS LEU VAL GLN GLN PHE THR LYS ILE PHE MET          
SEQRES  15 B  388  GLY LEU ALA THR ILE PHE LEU GLU ARG ASP LEU ALA LEU          
SEQRES  16 B  388  ILE GLU ILE ASN PRO LEU VAL ILE THR LYS GLN GLY ASP          
SEQRES  17 B  388  LEU ILE CYS LEU ASP GLY LYS LEU GLY ALA ASP GLY ASN          
SEQRES  18 B  388  ALA LEU PHE ARG GLN PRO ASP LEU ARG GLU MET ARG ASP          
SEQRES  19 B  388  GLN SER GLN GLU ASP PRO ARG GLU ALA GLN ALA ALA GLN          
SEQRES  20 B  388  TRP GLU LEU ASN TYR VAL ALA LEU ASP GLY ASN ILE GLY          
SEQRES  21 B  388  CYS MET VAL ASN GLY ALA GLY LEU ALA MET GLY THR MET          
SEQRES  22 B  388  ASP ILE VAL LYS LEU HIS GLY GLY GLU PRO ALA ASN PHE          
SEQRES  23 B  388  LEU ASP VAL GLY GLY GLY ALA THR LYS GLU ARG VAL THR          
SEQRES  24 B  388  GLU ALA PHE LYS ILE ILE LEU SER ASP ASP LYS VAL LYS          
SEQRES  25 B  388  ALA VAL LEU VAL ASN ILE PHE GLY GLY ILE VAL ARG CYS          
SEQRES  26 B  388  ASP LEU ILE ALA ASP GLY ILE ILE GLY ALA VAL ALA GLU          
SEQRES  27 B  388  VAL GLY VAL ASN VAL PRO VAL VAL VAL ARG LEU GLU GLY          
SEQRES  28 B  388  ASN ASN ALA GLU LEU GLY ALA LYS LYS LEU ALA ASP SER          
SEQRES  29 B  388  GLY LEU ASN ILE ILE ALA ALA LYS GLY LEU THR ASP ALA          
SEQRES  30 B  388  ALA GLN GLN VAL VAL ALA ALA VAL GLU GLY LYS                  
SEQRES   1 D  288  SER ILE LEU ILE ASP LYS ASN THR LYS VAL ILE CYS GLN          
SEQRES   2 D  288  GLY PHE THR GLY SER GLN GLY THR PHE HIS SER GLU GLN          
SEQRES   3 D  288  ALA ILE ALA TYR GLY THR LYS MET VAL GLY GLY VAL THR          
SEQRES   4 D  288  PRO GLY LYS GLY GLY THR THR HIS LEU GLY LEU PRO VAL          
SEQRES   5 D  288  PHE ASN THR VAL ARG GLU ALA VAL ALA ALA THR GLY ALA          
SEQRES   6 D  288  THR ALA SER VAL ILE TYR VAL PRO ALA PRO PHE CYS LYS          
SEQRES   7 D  288  ASP SER ILE LEU GLU ALA ILE ASP ALA GLY ILE LYS LEU          
SEQRES   8 D  288  ILE ILE THR ILE THR GLU GLY ILE PRO THR LEU ASP MET          
SEQRES   9 D  288  LEU THR VAL LYS VAL LYS LEU ASP GLU ALA GLY VAL ARG          
SEQRES  10 D  288  MET ILE GLY PRO ASN CYS PRO GLY VAL ILE THR PRO GLY          
SEQRES  11 D  288  GLU CYS LYS ILE GLY ILE GLN PRO GLY HIS ILE HIS LYS          
SEQRES  12 D  288  PRO GLY LYS VAL GLY ILE VAL SER ARG SER GLY THR LEU          
SEQRES  13 D  288  THR TYR GLU ALA VAL LYS GLN THR THR ASP TYR GLY PHE          
SEQRES  14 D  288  GLY GLN SER THR CYS VAL GLY ILE GLY GLY ASP PRO ILE          
SEQRES  15 D  288  PRO GLY SER ASN PHE ILE ASP ILE LEU GLU MET PHE GLU          
SEQRES  16 D  288  LYS ASP PRO GLN THR GLU ALA ILE VAL MET ILE GLY GLU          
SEQRES  17 D  288  ILE GLY GLY SER ALA GLU GLU GLU ALA ALA ALA TYR ILE          
SEQRES  18 D  288  LYS GLU HIS VAL THR LYS PRO VAL VAL GLY TYR ILE ALA          
SEQRES  19 D  288  GLY VAL THR ALA PRO LYS GLY LYS ARG MET GLY NEP ALA          
SEQRES  20 D  288  GLY ALA ILE ILE ALA GLY GLY LYS GLY THR ALA ASP GLU          
SEQRES  21 D  288  LYS PHE ALA ALA LEU GLU ALA ALA GLY VAL LYS THR VAL          
SEQRES  22 D  288  ARG SER LEU ALA ASP ILE GLY GLU ALA LEU LYS THR VAL          
SEQRES  23 D  288  LEU LYS                                                      
SEQRES   1 E  388  MET ASN LEU HIS GLU TYR GLN ALA LYS GLN LEU PHE ALA          
SEQRES   2 E  388  ARG TYR GLY LEU PRO ALA PRO VAL GLY TYR ALA CYS THR          
SEQRES   3 E  388  THR PRO ARG GLU ALA GLU GLU ALA ALA SER LYS ILE GLY          
SEQRES   4 E  388  ALA GLY PRO TRP VAL VAL LYS CYS GLN VAL HIS ALA GLY          
SEQRES   5 E  388  GLY ARG GLY LYS ALA GLY GLY VAL LYS VAL VAL ASN SER          
SEQRES   6 E  388  LYS GLU ASP ILE ARG ALA PHE ALA GLU ASN TRP LEU GLY          
SEQRES   7 E  388  LYS ARG LEU VAL THR TYR GLN THR ASP ALA ASN GLY GLN          
SEQRES   8 E  388  PRO VAL ASN GLN ILE LEU VAL GLU ALA ALA THR ASP ILE          
SEQRES   9 E  388  ALA LYS GLU LEU TYR LEU GLY ALA VAL VAL ASP ARG SER          
SEQRES  10 E  388  SER ARG ARG VAL VAL PHE MET ALA SER THR GLU GLY GLY          
SEQRES  11 E  388  VAL GLU ILE GLU LYS VAL ALA GLU GLU THR PRO HIS LEU          
SEQRES  12 E  388  ILE HIS LYS VAL ALA LEU ASP PRO LEU THR GLY PRO MET          
SEQRES  13 E  388  PRO TYR GLN GLY ARG GLU LEU ALA PHE LYS LEU GLY LEU          
SEQRES  14 E  388  GLU GLY LYS LEU VAL GLN GLN PHE THR LYS ILE PHE MET          
SEQRES  15 E  388  GLY LEU ALA THR ILE PHE LEU GLU ARG ASP LEU ALA LEU          
SEQRES  16 E  388  ILE GLU ILE ASN PRO LEU VAL ILE THR LYS GLN GLY ASP          
SEQRES  17 E  388  LEU ILE CYS LEU ASP GLY LYS LEU GLY ALA ASP GLY ASN          
SEQRES  18 E  388  ALA LEU PHE ARG GLN PRO ASP LEU ARG GLU MET ARG ASP          
SEQRES  19 E  388  GLN SER GLN GLU ASP PRO ARG GLU ALA GLN ALA ALA GLN          
SEQRES  20 E  388  TRP GLU LEU ASN TYR VAL ALA LEU ASP GLY ASN ILE GLY          
SEQRES  21 E  388  CYS MET VAL ASN GLY ALA GLY LEU ALA MET GLY THR MET          
SEQRES  22 E  388  ASP ILE VAL LYS LEU HIS GLY GLY GLU PRO ALA ASN PHE          
SEQRES  23 E  388  LEU ASP VAL GLY GLY GLY ALA THR LYS GLU ARG VAL THR          
SEQRES  24 E  388  GLU ALA PHE LYS ILE ILE LEU SER ASP ASP LYS VAL LYS          
SEQRES  25 E  388  ALA VAL LEU VAL ASN ILE PHE GLY GLY ILE VAL ARG CYS          
SEQRES  26 E  388  ASP LEU ILE ALA ASP GLY ILE ILE GLY ALA VAL ALA GLU          
SEQRES  27 E  388  VAL GLY VAL ASN VAL PRO VAL VAL VAL ARG LEU GLU GLY          
SEQRES  28 E  388  ASN ASN ALA GLU LEU GLY ALA LYS LYS LEU ALA ASP SER          
SEQRES  29 E  388  GLY LEU ASN ILE ILE ALA ALA LYS GLY LEU THR ASP ALA          
SEQRES  30 E  388  ALA GLN GLN VAL VAL ALA ALA VAL GLU GLY LYS                  
MODRES 1SCU NEP A  246  HIS  N1-PHOSPHONOHISTIDINE                              
MODRES 1SCU NEP D  246  HIS  N1-PHOSPHONOHISTIDINE                              
HET    NEP  A 246      14                                                       
HET    NEP  D 246      14                                                       
HET    COA  A 289      48                                                       
HET    COA  D 289      48                                                       
HETNAM     NEP N1-PHOSPHONOHISTIDINE                                            
HETNAM     COA COENZYME A                                                       
FORMUL   1  NEP    2(C6 H10 N3 O5 P)                                            
FORMUL   5  COA    2(C21 H36 N7 O16 P3 S)                                       
FORMUL   7  HOH   *110(H2 O)                                                    
HELIX    1   1 GLY A   17  GLY A   31  1                                  15    
HELIX    2   2 THR A   55  GLY A   64  1                                  10    
HELIX    3   3 PRO A   73  GLY A   88  1                                  16    
HELIX    4   4 PRO A  100  GLY A  115  1                                  16    
HELIX    5   5 PRO A  138  HIS A  142  5                                   5    
HELIX    6   6 SER A  153  TYR A  167  1                                  15    
HELIX    7   7 ASN A  186  ASP A  197  1                                  12    
HELIX    8   8 SER A  212  GLU A  223  1                                  12    
HELIX    9   9 THR A  257  ALA A  268  1                                  12    
HELIX   10  10 SER A  275  ALA A  277  5                                   3    
HELIX   11  11 ASP A  278  LYS A  288  1                                  11    
HELIX   12  12 HIS B    4  GLY B   16  1                                  13    
HELIX   13  13 THR B   27  GLY B   39  1                                  13    
HELIX   14  14 GLY B   53  GLY B   58  1                                   6    
HELIX   15  15 SER B   65  LEU B   77  1                                  13    
HELIX   16  16 GLU B  132  THR B  140  1                                   9    
HELIX   17  17 PRO B  141  ILE B  144  5                                   4    
HELIX   18  18 PRO B  157  GLY B  168  1                                  12    
HELIX   19  19 GLY B  171  ARG B  191  1                                  21    
HELIX   20  20 GLY B  220  ARG B  225  5                                   6    
HELIX   21  21 GLN B  226  MET B  232  1                                   7    
HELIX   22  22 ARG B  233  ARG B  233  5                                   1    
HELIX   23  23 ASP B  234  GLU B  238  5                                   5    
HELIX   24  24 ASP B  239  GLN B  247  1                                   9    
HELIX   25  25 GLY B  265  HIS B  279  1                                  15    
HELIX   26  26 THR B  294  ASP B  308  1                                  15    
HELIX   27  27 ARG B  324  GLY B  340  1                                  17    
HELIX   28  28 ASN B  353  SER B  364  1                                  12    
HELIX   29  29 GLY B  373  LYS B  388  1                                  16    
SHEET    1   A 7 THR A  46  HIS A  47  0                                        
SHEET    2   A 7 LEU A  50  PHE A  53 -1  N  LEU A  50   O  HIS A  47           
SHEET    3   A 7 LYS A  33  VAL A  38  1  O  GLY A  37   N  PHE A  53           
SHEET    4   A 7 LYS A   9  GLN A  13  1  O  VAL A  10   N  VAL A  35           
SHEET    5   A 7 ALA A  67  ILE A  70  1  O  ALA A  67   N  ILE A  11           
SHEET    6   A 7 LEU A  91  THR A  94  1  O  LEU A  91   N  SER A  68           
SHEET    7   A 7 ARG A 117  ILE A 119  1  O  ARG A 117   N  ILE A  92           
SHEET    1   B 7 CYS A 132  GLY A 135  0                                        
SHEET    2   B 7 GLY A 125  THR A 128 -1  N  VAL A 126   O  ILE A 134           
SHEET    3   B 7 GLN A 171  GLY A 176 -1  N  CYS A 174   O  ILE A 127           
SHEET    4   B 7 VAL A 147  SER A 151  1  O  VAL A 147   N  SER A 172           
SHEET    5   B 7 ALA A 202  GLU A 208  1  O  ALA A 202   N  GLY A 148           
SHEET    6   B 7 VAL A 229  ALA A 234  1  O  VAL A 230   N  MET A 205           
SHEET    7   B 7 LYS A 271  THR A 272  1  O  LYS A 271   N  GLY A 231           
SHEET    1   C 4 GLY B  22  CYS B  25  0                                        
SHEET    2   C 4 ILE B  96  ALA B 100 -1  O  ILE B  96   N  CYS B  25           
SHEET    3   C 4 TRP B  43  CYS B  47 -1  N  VAL B  44   O  GLU B  99           
SHEET    4   C 4 VAL B  60  VAL B  63 -1  O  LYS B  61   N  VAL B  45           
SHEET    1   D 2 ARG B  80  LEU B  81  0                                        
SHEET    2   D 2 GLN B  91  PRO B  92 -1  N  GLN B  91   O  LEU B  81           
SHEET    1   E 5 HIS B 145  ALA B 148  0                                        
SHEET    2   E 5 ARG B 120  SER B 126 -1  O  PHE B 123   N  VAL B 147           
SHEET    3   E 5 ILE B 104  ASP B 115 -1  N  TYR B 109   O  SER B 126           
SHEET    4   E 5 LEU B 193  THR B 204 -1  N  ILE B 196   O  ALA B 112           
SHEET    5   E 5 LEU B 209  CYS B 211 -1  O  ILE B 210   N  VAL B 202           
SHEET    1   F 5 HIS B 145  ALA B 148  0                                        
SHEET    2   F 5 ARG B 120  SER B 126 -1  O  PHE B 123   N  VAL B 147           
SHEET    3   F 5 ILE B 104  ASP B 115 -1  N  TYR B 109   O  SER B 126           
SHEET    4   F 5 LEU B 193  THR B 204 -1  N  ILE B 196   O  ALA B 112           
SHEET    5   F 5 LEU B 216  ALA B 218 -1  O  GLY B 217   N  ALA B 194           
SHEET    1   G 2 LEU B 250  ALA B 254  0                                        
SHEET    2   G 2 ASN B 285  VAL B 289 -1  N  PHE B 286   O  VAL B 253           
SHEET    1   H 4 ILE B 259  VAL B 263  0                                        
SHEET    2   H 4 ALA B 313  ASN B 317  1  O  ALA B 313   N  GLY B 260           
SHEET    3   H 4 VAL B 345  ARG B 348  1  O  VAL B 346   N  VAL B 316           
SHEET    4   H 4 ILE B 368  ALA B 370  1  N  ILE B 369   O  VAL B 345           
LINK         C   GLY A 245                 N   NEP A 246     1555   1555  1.32  
LINK         C   NEP A 246                 N   ALA A 247     1555   1555  1.29  
LINK         C   GLY D 245                 N   NEP D 246     1555   1555  1.30  
LINK         C   NEP D 246                 N   ALA D 247     1555   1555  1.27  
CISPEP   1 GLY A  120    PRO A  121          0         6.20                     
CISPEP   2 GLY B   41    PRO B   42          0        -3.75                     
CISPEP   3 ASN B  199    PRO B  200          0        11.34                     
CISPEP   4 GLY D  120    PRO D  121          0         0.77                     
CISPEP   5 GLY E   41    PRO E   42          0        -5.29                     
CISPEP   6 ASN E  199    PRO E  200          0         5.04                     
SITE     1 AC1 26 GLY A  14  THR A  16  GLY A  17  SER A  18                    
SITE     2 AC1 26 GLN A  19  VAL A  38  THR A  39  PRO A  40                    
SITE     3 AC1 26 LYS A  42  TYR A  71  VAL A  72  PRO A  73                    
SITE     4 AC1 26 SER A  80  ILE A  95  THR A  96  GLU A  97                    
SITE     5 AC1 26 ASN A 122  CYS A 123  PRO A 124  HOH A 293                    
SITE     6 AC1 26 HOH A 294  ARG B 161  ARG E  29  GLU E  33                    
SITE     7 AC1 26 SER E  36  LYS E  66                                          
SITE     1 AC2 22 GLU B  33  SER B  36  LYS B  66  GLY D  14                    
SITE     2 AC2 22 THR D  16  GLY D  17  SER D  18  GLN D  19                    
SITE     3 AC2 22 VAL D  38  PRO D  40  LYS D  42  TYR D  71                    
SITE     4 AC2 22 VAL D  72  PRO D  73  SER D  80  ILE D  95                    
SITE     5 AC2 22 THR D  96  GLU D  97  ASN D 122  CYS D 123                    
SITE     6 AC2 22 HOH D 298  HOH D 303                                          
CRYST1   98.470   98.470  400.600  90.00  90.00  90.00 P 43 2 2     16          
ORIGX1      1.000000  0.000000  0.000000        0.00000                         
ORIGX2      0.000000  1.000000  0.000000        0.00000                         
ORIGX3      0.000000  0.000000  1.000000        0.00000                         
SCALE1      0.010155  0.000000  0.000000        0.00000                         
SCALE2      0.000000  0.010155  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.002496        0.00000                         
(ATOM LINES ARE NOT SHOWN.)
END                                                                             
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