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Entry: 2SCU
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HEADER    LIGASE                                  24-SEP-98   2SCU              
TITLE     A DETAILED DESCRIPTION OF THE STRUCTURE OF SUCCINYL-COA               
TITLE    2 SYNTHETASE FROM ESCHERICHIA COLI                                     
COMPND    MOL_ID: 1;                                                            
COMPND   2 MOLECULE: PROTEIN (SUCCINYL-COA LIGASE);                             
COMPND   3 CHAIN: A, D;                                                         
COMPND   4 SYNONYM: SCS;                                                        
COMPND   5 EC: 6.2.1.5;                                                         
COMPND   6 ENGINEERED: YES;                                                     
COMPND   7 OTHER_DETAILS: RESIDUES A246 AND D246 ARE                            
COMPND   8 PHOSPHOHISTIDINES;                                                   
COMPND   9 MOL_ID: 2;                                                           
COMPND  10 MOLECULE: PROTEIN (SUCCINYL-COA LIGASE);                             
COMPND  11 CHAIN: B, E;                                                         
COMPND  12 SYNONYM: SCS;                                                        
COMPND  13 EC: 6.2.1.5;                                                         
COMPND  14 ENGINEERED: YES;                                                     
COMPND  15 OTHER_DETAILS: RESIDUES A246 AND D246 ARE PHOSPHOHISTIDINES          
SOURCE    MOL_ID: 1;                                                            
SOURCE   2 ORGANISM_SCIENTIFIC: ESCHERICHIA COLI;                               
SOURCE   3 ORGANISM_TAXID: 562;                                                 
SOURCE   4 STRAIN: CR63;                                                        
SOURCE   5 EXPRESSION_SYSTEM: ESCHERICHIA COLI;                                 
SOURCE   6 EXPRESSION_SYSTEM_TAXID: 562;                                        
SOURCE   7 MOL_ID: 2;                                                           
SOURCE   8 ORGANISM_SCIENTIFIC: ESCHERICHIA COLI;                               
SOURCE   9 ORGANISM_TAXID: 562;                                                 
SOURCE  10 STRAIN: CR63;                                                        
SOURCE  11 EXPRESSION_SYSTEM: ESCHERICHIA COLI;                                 
SOURCE  12 EXPRESSION_SYSTEM_TAXID: 562                                         
KEYWDS    CITRIC ACID CYCLE, HETEROTETRAMER, LIGASE                             
EXPDTA    X-RAY DIFFRACTION                                                     
AUTHOR    M.E.FRASER,W.T.WOLODKO,M.N.G.JAMES,W.A.BRIDGER                        
REVDAT   3   24-FEB-09 2SCU    1       VERSN                                    
REVDAT   2   01-APR-03 2SCU    1       JRNL                                     
REVDAT   1   02-AUG-99 2SCU    0                                                
JRNL        AUTH   M.E.FRASER,M.N.JAMES,W.A.BRIDGER,W.T.WOLODKO                 
JRNL        TITL   A DETAILED STRUCTURAL DESCRIPTION OF ESCHERICHIA             
JRNL        TITL 2 COLI SUCCINYL-COA SYNTHETASE.                                
JRNL        REF    J.MOL.BIOL.                   V. 285  1633 1999              
JRNL        REFN                   ISSN 0022-2836                               
JRNL        PMID   9917402                                                      
JRNL        DOI    10.1006/JMBI.1998.2324                                       
REMARK   1                                                                      
REMARK   1 REFERENCE 1                                                          
REMARK   1  AUTH   W.T.WOLODKO,M.E.FRASER,M.N.G.JAMES,W.A.BRIDGER               
REMARK   1  TITL   THE CRYSTAL STRUCTURE OF SUCCINYL-COA SYNTHETASE             
REMARK   1  TITL 2 FROM ESCHERICHIA COLI AT 2.5 ANGSTROMS RESOLUTION            
REMARK   1  REF    J.BIOL.CHEM.                  V. 269 10883 1994              
REMARK   1  REFN                   ISSN 0021-9258                               
REMARK   1 REFERENCE 2                                                          
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. 259  5316 1984              
REMARK   1  REFN                   ISSN 0021-9258                               
REMARK   1 REFERENCE 3                                                          
REMARK   1  AUTH   D.L.BAILEY,M.E.FRASER,W.A.BRIDGER,M.N.G.JAMES,               
REMARK   1  AUTH 2 W.T.WOLODKO                                                  
REMARK   1  TITL   A DIMERIC FORM OF ESCHERICHIA COLI SUCCINYL-COA              
REMARK   1  TITL 2 SYNTHETASE PRODUCED BY SITE- DIRECTED MUTAGENESIS            
REMARK   1  REF    J.MOL.BIOL.                   V. 285  1655 1999              
REMARK   1  REFN                   ISSN 0022-2836                               
REMARK   1  DOI    10.1006/JMBI.1998.2325                                       
REMARK   2                                                                      
REMARK   2 RESOLUTION.    2.30 ANGSTROMS.                                       
REMARK   3                                                                      
REMARK   3 REFINEMENT.                                                          
REMARK   3   PROGRAM     : TNT V. 5-EB                                          
REMARK   3   AUTHORS     : TRONRUD,TEN EYCK,MATTHEWS                            
REMARK   3                                                                      
REMARK   3  DATA USED IN REFINEMENT.                                            
REMARK   3   RESOLUTION RANGE HIGH (ANGSTROMS) : 2.30                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 8.00                           
REMARK   3   DATA CUTOFF            (SIGMA(F)) : 0.000                          
REMARK   3   COMPLETENESS FOR RANGE        (%) : 93.0                           
REMARK   3   NUMBER OF REFLECTIONS             : 83411                          
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) : NULL                            
REMARK   3   R VALUE            (WORKING SET) : 0.195                           
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) : 0.1950                 
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) : 83411                  
REMARK   3                                                                      
REMARK   3  NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.                    
REMARK   3   PROTEIN ATOMS            : 9900                                    
REMARK   3   NUCLEIC ACID ATOMS       : 0                                       
REMARK   3   HETEROGEN ATOMS          : 106                                     
REMARK   3   SOLVENT ATOMS            : 502                                     
REMARK   3                                                                      
REMARK   3  WILSON B VALUE (FROM FCALC, A**2) : 32.000                          
REMARK   3                                                                      
REMARK   3  RMS DEVIATIONS FROM IDEAL VALUES.    RMS    WEIGHT  COUNT           
REMARK   3   BOND LENGTHS                 (A) : 0.020 ; 1.000 ; 10160           
REMARK   3   BOND ANGLES            (DEGREES) : 2.042 ; 1.000 ; 13710           
REMARK   3   TORSION ANGLES         (DEGREES) : 19.193; 0.000 ; 6206            
REMARK   3   PSEUDOROTATION ANGLES  (DEGREES) : NULL  ; NULL  ; NULL            
REMARK   3   TRIGONAL CARBON PLANES       (A) : 0.013 ; 2.000 ; 242             
REMARK   3   GENERAL PLANES               (A) : 0.023 ; 3.000 ; 1480            
REMARK   3   ISOTROPIC THERMAL FACTORS (A**2) : 2.854 ; 0.300 ; 10160           
REMARK   3   NON-BONDED CONTACTS          (A) : 0.036 ; 10.000; 313             
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 2SCU COMPLIES WITH FORMAT V. 3.15, 01-DEC-08                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 13-JUL-99.                  
REMARK 100 THE RCSB ID CODE IS RCSB001229.                                      
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : 01-MAR-95                          
REMARK 200  TEMPERATURE           (KELVIN) : 283                                
REMARK 200  PH                             : 7.2                                
REMARK 200  NUMBER OF CRYSTALS USED        : 23                                 
REMARK 200                                                                      
REMARK 200  SYNCHROTRON              (Y/N) : Y                                  
REMARK 200  RADIATION SOURCE               : PHOTON FACTORY                     
REMARK 200  BEAMLINE                       : BL-6A                              
REMARK 200  X-RAY GENERATOR MODEL          : NULL                               
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M                                  
REMARK 200  WAVELENGTH OR RANGE        (A) : 1.000                              
REMARK 200  MONOCHROMATOR                  : NULL                               
REMARK 200  OPTICS                         : NULL                               
REMARK 200                                                                      
REMARK 200  DETECTOR TYPE                  : IMAGE PLATE                        
REMARK 200  DETECTOR MANUFACTURER          : NULL                               
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : WEIS                               
REMARK 200  DATA SCALING SOFTWARE          : BIOMOL (KBRANI, KBAPLY)            
REMARK 200                                                                      
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 417950                             
REMARK 200  RESOLUTION RANGE HIGH      (A) : 2.300                              
REMARK 200  RESOLUTION RANGE LOW       (A) : 100.000                            
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : 0.000                              
REMARK 200                                                                      
REMARK 200 OVERALL.                                                             
REMARK 200  COMPLETENESS FOR RANGE     (%) : 92.7                               
REMARK 200  DATA REDUNDANCY                : 5.000                              
REMARK 200  R MERGE                    (I) : 0.09500                            
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) : 2.30                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 2.50                     
REMARK 200  COMPLETENESS FOR SHELL     (%) : NULL                               
REMARK 200  DATA REDUNDANCY IN SHELL       : NULL                               
REMARK 200  R MERGE FOR SHELL          (I) : 0.45000                            
REMARK 200  R SYM FOR SHELL            (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR SHELL         : NULL                               
REMARK 200                                                                      
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH                              
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MIR                          
REMARK 200 SOFTWARE USED: NULL                                                  
REMARK 200 STARTING MODEL: NULL                                                 
REMARK 200                                                                      
REMARK 200 REMARK: DATA WERE COLLECTED USING THE WEISSENBERG METHOD.            
REMARK 280                                                                      
REMARK 280 CRYSTAL                                                              
REMARK 280 SOLVENT CONTENT, VS   (%): 64.35                                     
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 3.45                     
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: PH 7.2                                   
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      201.88000            
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      302.82000            
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      100.94000            
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      201.88000            
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      100.94000            
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      302.82000            
REMARK 290                                                                      
REMARK 290 REMARK: NULL                                                         
REMARK 300                                                                      
REMARK 300 BIOMOLECULE: 1, 2                                                    
REMARK 300 SEE REMARK 350 FOR THE AUTHOR PROVIDED AND/OR PROGRAM                
REMARK 300 GENERATED ASSEMBLY INFORMATION FOR THE STRUCTURE IN                  
REMARK 300 THIS ENTRY. THE REMARK MAY ALSO PROVIDE INFORMATION ON               
REMARK 300 BURIED SURFACE AREA.                                                 
REMARK 350                                                                      
REMARK 350 COORDINATES FOR A COMPLETE MULTIMER REPRESENTING THE KNOWN           
REMARK 350 BIOLOGICALLY SIGNIFICANT OLIGOMERIZATION STATE OF THE                
REMARK 350 MOLECULE CAN BE GENERATED BY APPLYING BIOMT TRANSFORMATIONS          
REMARK 350 GIVEN BELOW.  BOTH NON-CRYSTALLOGRAPHIC AND                          
REMARK 350 CRYSTALLOGRAPHIC OPERATIONS ARE GIVEN.                               
REMARK 350                                                                      
REMARK 350 BIOMOLECULE: 1                                                       
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: TETRAMERIC                        
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: TETRAMERIC                 
REMARK 350 SOFTWARE USED: PISA                                                  
REMARK 350 TOTAL BURIED SURFACE AREA: 9390 ANGSTROM**2                          
REMARK 350 SURFACE AREA OF THE COMPLEX: 49910 ANGSTROM**2                       
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -69.0 KCAL/MOL                        
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, B                                  
REMARK 350   BIOMT1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 350   BIOMT2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 350   BIOMT3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 350   BIOMT1   2  0.000000  1.000000  0.000000        0.00000            
REMARK 350   BIOMT2   2  1.000000  0.000000  0.000000        0.00000            
REMARK 350   BIOMT3   2  0.000000  0.000000 -1.000000      100.94000            
REMARK 350                                                                      
REMARK 350 BIOMOLECULE: 2                                                       
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: TETRAMERIC                        
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: TETRAMERIC                 
REMARK 350 SOFTWARE USED: PISA                                                  
REMARK 350 TOTAL BURIED SURFACE AREA: 9530 ANGSTROM**2                          
REMARK 350 SURFACE AREA OF THE COMPLEX: 50000 ANGSTROM**2                       
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -65.0 KCAL/MOL                        
REMARK 350 APPLY THE FOLLOWING TO CHAINS: 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 350   BIOMT1   2  0.000000  1.000000  0.000000        0.00000            
REMARK 350   BIOMT2   2  1.000000  0.000000  0.000000        0.00000            
REMARK 350   BIOMT3   2  0.000000  0.000000 -1.000000      100.94000            
REMARK 375                                                                      
REMARK 375 SPECIAL POSITION                                                     
REMARK 375 THE FOLLOWING ATOMS ARE FOUND TO BE WITHIN 0.15 ANGSTROMS            
REMARK 375 OF A SYMMETRY RELATED ATOM AND ARE ASSUMED TO BE ON SPECIAL          
REMARK 375 POSITIONS.                                                           
REMARK 375                                                                      
REMARK 375 ATOM RES CSSEQI                                                      
REMARK 375      HOH B1166  LIES ON A SPECIAL POSITION.                          
REMARK 375      HOH D1288  LIES ON A SPECIAL POSITION.                          
REMARK 465                                                                      
REMARK 465 MISSING RESIDUES                                                     
REMARK 465 THE FOLLOWING RESIDUES WERE NOT LOCATED IN THE                       
REMARK 465 EXPERIMENT. (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN               
REMARK 465 IDENTIFIER; SSSEQ=SEQUENCE NUMBER; I=INSERTION CODE.)                
REMARK 465                                                                      
REMARK 465   M RES C SSSEQI                                                     
REMARK 465     LEU A   287                                                      
REMARK 465     LYS A   288                                                      
REMARK 465     GLU B   386                                                      
REMARK 465     GLY B   387                                                      
REMARK 465     LYS B   388                                                      
REMARK 465     LEU D   287                                                      
REMARK 465     LYS D   288                                                      
REMARK 465     GLU E   386                                                      
REMARK 465     GLY E   387                                                      
REMARK 465     LYS E   388                                                      
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 113   CG    GLU A 113   CD      0.095                       
REMARK 500    ALA B 222   CA    ALA B 222   CB     -0.140                       
REMARK 500    TRP E 248   CB    TRP E 248   CG     -0.137                       
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    ASP A   5   CB  -  CG  -  OD1 ANGL. DEV. =   6.8 DEGREES          
REMARK 500    ASP A  79   CB  -  CG  -  OD1 ANGL. DEV. =   6.4 DEGREES          
REMARK 500    LEU A 102   CB  -  CG  -  CD1 ANGL. DEV. = -12.2 DEGREES          
REMARK 500    ARG A 152   NE  -  CZ  -  NH1 ANGL. DEV. =   3.1 DEGREES          
REMARK 500    ARG B 116   NE  -  CZ  -  NH1 ANGL. DEV. =   3.7 DEGREES          
REMARK 500    ARG B 116   NE  -  CZ  -  NH2 ANGL. DEV. =  -3.8 DEGREES          
REMARK 500    PRO B 227   C   -  N   -  CD  ANGL. DEV. = -21.3 DEGREES          
REMARK 500    ARG B 233   NE  -  CZ  -  NH1 ANGL. DEV. =  -4.2 DEGREES          
REMARK 500    ARG B 297   NE  -  CZ  -  NH1 ANGL. DEV. =  -4.8 DEGREES          
REMARK 500    ARG B 297   NE  -  CZ  -  NH2 ANGL. DEV. =   3.2 DEGREES          
REMARK 500    CYS B 325   CB  -  CA  -  C   ANGL. DEV. =   8.9 DEGREES          
REMARK 500    LEU B 349   CB  -  CG  -  CD1 ANGL. DEV. = -10.3 DEGREES          
REMARK 500    LEU D 111   CB  -  CG  -  CD1 ANGL. DEV. = -14.5 DEGREES          
REMARK 500    THR D 128   N   -  CA  -  C   ANGL. DEV. = -16.8 DEGREES          
REMARK 500    VAL E 113   CB  -  CA  -  C   ANGL. DEV. = -11.5 DEGREES          
REMARK 500    ARG E 191   NE  -  CZ  -  NH1 ANGL. DEV. =  -4.7 DEGREES          
REMARK 500    ARG E 225   NE  -  CZ  -  NH1 ANGL. DEV. =   3.0 DEGREES          
REMARK 500    GLY E 257   N   -  CA  -  C   ANGL. DEV. = -16.8 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    LEU A   3      -63.43     65.79                                   
REMARK 500    LYS A   6       -9.86    -51.22                                   
REMARK 500    LEU A  48       36.04     34.52                                   
REMARK 500    TYR A  71       52.25   -119.29                                   
REMARK 500    THR A  96      123.63    -38.35                                   
REMARK 500    SER A 212       34.36   -147.28                                   
REMARK 500    TYR B  84       -4.50    -55.14                                   
REMARK 500    ASP B  87     -151.98    -83.75                                   
REMARK 500    THR B 140       46.96   -141.83                                   
REMARK 500    PRO B 141      -14.44    -40.39                                   
REMARK 500    PRO B 227      -53.02    -28.71                                   
REMARK 500    ASN B 285      160.06    177.07                                   
REMARK 500    ALA B 293       58.07    -57.58                                   
REMARK 500    LYS B 372       79.59   -104.63                                   
REMARK 500    LEU D   3      -59.28     52.26                                   
REMARK 500    ASP D   5     -169.82   -173.78                                   
REMARK 500    PHE D  15      -37.35    -39.53                                   
REMARK 500    TYR D  30        2.04    -63.33                                   
REMARK 500    PRO D  40      112.54    -32.36                                   
REMARK 500    THR D  63      -41.61   -143.48                                   
REMARK 500    THR D  96      129.84    -28.41                                   
REMARK 500    HIS D 140       29.79    -75.68                                   
REMARK 500    TYR D 167       18.33    -64.40                                   
REMARK 500    PHE D 169      -46.05    -21.41                                   
REMARK 500    SER D 172      -77.71    -70.15                                   
REMARK 500    ASN D 186     -155.49   -103.45                                   
REMARK 500    PHE D 187      -70.34    -66.61                                   
REMARK 500    SER D 212       24.64   -147.36                                   
REMARK 500    ALA D 267       30.41    -73.85                                   
REMARK 500    LEU D 276        9.45    -56.42                                   
REMARK 500    ASP D 278       31.62    -98.63                                   
REMARK 500    GLU E 197      106.43   -163.46                                   
REMARK 500    ASN E 258       16.74   -153.36                                   
REMARK 500    ALA E 293       63.79    -64.86                                   
REMARK 500    ALA E 313      157.97    179.65                                   
REMARK 500    VAL E 341      108.98    -50.50                                   
REMARK 500    ARG E 348      103.85   -162.30                                   
REMARK 500    ASN E 353       32.62     83.33                                   
REMARK 500    ASN E 367       45.65    -86.70                                   
REMARK 500    ALA E 384      -10.15    -35.24                                   
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: MAIN CHAIN PLANARITY                                       
REMARK 500                                                                      
REMARK 500 THE FOLLOWING RESIDUES HAVE A PSEUDO PLANARITY                       
REMARK 500 TORSION, C(I) - CA(I) - N(I+1) - O(I), GREATER                       
REMARK 500 10.0 DEGREES. (M=MODEL NUMBER; RES=RESIDUE NAME;                     
REMARK 500 C=CHAIN IDENTIFIER; SSEQ=SEQUENCE NUMBER;                            
REMARK 500 I=INSERTION CODE).                                                   
REMARK 500                                                                      
REMARK 500  M RES CSSEQI        ANGLE                                           
REMARK 500    THR A 106         10.90                                           
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 600                                                                      
REMARK 600 HETEROGEN                                                            
REMARK 600 SO4 400 IS ASSOCIATED WITH BETA SUBUNIT CHAIN B.                     
REMARK 600 SO4 401 IS ASSOCIATED WITH BETA SUBUNIT CHAIN E.                     
REMARK 800                                                                      
REMARK 800 SITE                                                                 
REMARK 800 SITE_IDENTIFIER: AC1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 B 400                 
REMARK 800 SITE_IDENTIFIER: AC2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 E 401                 
REMARK 800 SITE_IDENTIFIER: AC3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE COA A 300                 
REMARK 800 SITE_IDENTIFIER: AC4                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE COA D 301                 
REMARK 900                                                                      
REMARK 900 RELATED ENTRIES                                                      
REMARK 900 RELATED ID: 1SCU   RELATED DB: PDB                                   
REMARK 900 SUCCINYL-COA SYNTHETASE (SUCCINATE-COA LIGASE) (ADP-FORMING)         
REMARK 999                                                                      
REMARK 999 SEQUENCE                                                             
REMARK 999 AMINO-TERMINAL ANALYSIS OF THE ALPHA SUBUNIT INDICATES THAT          
REMARK 999  THE FIRST RESIDUE IS A SERINE                                       
REMARK 999 (W. A. BRIDGE, ENZYMES, 1974, 3RD ED. 10, 581-606). IN THE           
REMARK 999  GENE SEQUENCING PAPER, BUCK, SPENCER AND GUEST STATE THAT           
REMARK 999 [THE ASSUMPTION IS] THAT THE INITIATING FORMYLMETHIONINE             
REMARK 999 IS 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  2SCU A    1   288  UNP    P07459   SUCD_ECOLI       2    289             
DBREF  2SCU B    1   388  UNP    P07460   SUCC_ECOLI       1    388             
DBREF  2SCU D    1   288  UNP    P07459   SUCD_ECOLI       2    289             
DBREF  2SCU E    1   388  UNP    P07460   SUCC_ECOLI       1    388             
SEQADV 2SCU NEP A  246  UNP  P07459    HIS   247 MODIFIED RESIDUE               
SEQADV 2SCU NEP D  246  UNP  P07459    HIS   247 MODIFIED RESIDUE               
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 2SCU NEP A  246  HIS  N1-PHOSPHONOHISTIDINE                              
MODRES 2SCU NEP D  246  HIS  N1-PHOSPHONOHISTIDINE                              
HET    NEP  A 246      14                                                       
HET    NEP  D 246      14                                                       
HET    SO4  B 400       5                                                       
HET    SO4  E 401       5                                                       
HET    COA  A 300      48                                                       
HET    COA  D 301      48                                                       
HETNAM     NEP N1-PHOSPHONOHISTIDINE                                            
HETNAM     SO4 SULFATE ION                                                      
HETNAM     COA COENZYME A                                                       
FORMUL   1  NEP    2(C6 H10 N3 O5 P)                                            
FORMUL   5  SO4    2(O4 S 2-)                                                   
FORMUL   7  COA    2(C21 H36 N7 O16 P3 S)                                       
FORMUL   9  HOH   *502(H2 O)                                                    
HELIX    1   1 SER A   18  TYR A   30  1                                  13    
HELIX    2   2 VAL A   56  THR A   63  1                                   8    
HELIX    3   3 ALA A   74  ALA A   87  5                                  14    
HELIX    4   4 THR A  101  ALA A  114  1                                  14    
HELIX    5   5 GLY A  139  ILE A  141  5                                   3    
HELIX    6   6 GLY A  154  ASP A  166  1                                  13    
HELIX    7   7 PHE A  187  GLU A  195  1                                   9    
HELIX    8   8 ALA A  213  HIS A  224  1                                  12    
HELIX    9   9 ALA A  258  ALA A  267  1                                  10    
HELIX   10  10 LEU A  276  LYS A  284  5                                   9    
HELIX   11  11 GLU B    5  TYR B   15  1                                  11    
HELIX   12  12 PRO B   28  ILE B   38  1                                  11    
HELIX   13  13 LYS B   66  TRP B   76  1                                  11    
HELIX   14  14 ILE B  133  LEU B  143  1                                  11    
HELIX   15  15 PRO B  157  LYS B  166  1                                  10    
HELIX   16  16 GLY B  171  GLU B  190  5                                  20    
HELIX   17  17 GLY B  220  ARG B  225  5                                   6    
HELIX   18  18 PRO B  227  MET B  232  1                                   6    
HELIX   19  19 GLN B  235  GLN B  237  5                                   3    
HELIX   20  20 PRO B  240  TRP B  248  1                                   9    
HELIX   21  21 ALA B  266  LEU B  278  1                                  13    
HELIX   22  22 LYS B  295  SER B  307  1                                  13    
HELIX   23  23 CYS B  325  GLU B  338  1                                  14    
HELIX   24  24 ALA B  354  SER B  364  1                                  11    
HELIX   25  25 LEU B  374  ALA B  383  1                                  10    
HELIX   26  26 SER D   18  ALA D   29  1                                  12    
HELIX   27  27 VAL D   56  ALA D   61  1                                   6    
HELIX   28  28 ALA D   74  ASP D   86  5                                  13    
HELIX   29  29 THR D  101  GLU D  113  1                                  13    
HELIX   30  30 GLY D  139  ILE D  141  5                                   3    
HELIX   31  31 THR D  155  ASP D  166  1                                  12    
HELIX   32  32 PHE D  187  PHE D  194  1                                   8    
HELIX   33  33 ALA D  213  HIS D  224  1                                  12    
HELIX   34  34 ALA D  258  ALA D  268  1                                  11    
HELIX   35  35 ILE D  279  LYS D  284  1                                   6    
HELIX   36  36 GLU E    5  ARG E   14  1                                  10    
HELIX   37  37 PRO E   28  ILE E   38  1                                  11    
HELIX   38  38 LYS E   66  TRP E   76  1                                  11    
HELIX   39  39 ILE E  133  GLU E  139  1                                   7    
HELIX   40  40 PRO E  141  LEU E  143  5                                   3    
HELIX   41  41 PRO E  157  LYS E  166  1                                  10    
HELIX   42  42 GLY E  171  GLU E  190  5                                  20    
HELIX   43  43 GLY E  220  ARG E  225  5                                   6    
HELIX   44  44 PRO E  227  MET E  232  1                                   6    
HELIX   45  45 GLN E  235  GLN E  237  5                                   3    
HELIX   46  46 PRO E  240  TRP E  248  1                                   9    
HELIX   47  47 ALA E  266  LEU E  278  1                                  13    
HELIX   48  48 LYS E  295  ILE E  305  1                                  11    
HELIX   49  49 CYS E  325  VAL E  339  1                                  15    
HELIX   50  50 ALA E  354  ALA E  362  1                                   9    
HELIX   51  51 LEU E  374  ALA E  383  1                                  10    
SHEET    1   A 5 ARG A 117  ILE A 119  0                                        
SHEET    2   A 5 LEU A  91  THR A  94  1  N  ILE A  92   O  ARG A 117           
SHEET    3   A 5 ALA A  67  ILE A  70  1  N  SER A  68   O  LEU A  91           
SHEET    4   A 5 VAL A  10  GLN A  13  1  N  ILE A  11   O  ALA A  67           
SHEET    5   A 5 MET A  34  VAL A  38  1  N  VAL A  35   O  VAL A  10           
SHEET    1   B 2 THR A  45  HIS A  47  0                                        
SHEET    2   B 2 LEU A  50  VAL A  52 -1  N  VAL A  52   O  THR A  45           
SHEET    1   C 2 GLY A 125  THR A 128  0                                        
SHEET    2   C 2 CYS A 132  GLY A 135 -1  N  ILE A 134   O  VAL A 126           
SHEET    1   D 4 CYS A 174  GLY A 176  0                                        
SHEET    2   D 4 VAL A 147  SER A 151  1  N  ILE A 149   O  VAL A 175           
SHEET    3   D 4 ALA A 202  GLU A 208  1  N  ALA A 202   O  GLY A 148           
SHEET    4   D 4 PRO A 228  ALA A 234  1  N  PRO A 228   O  ILE A 203           
SHEET    1   E 4 GLY B  22  CYS B  25  0                                        
SHEET    2   E 4 ILE B  96  ALA B 100 -1  N  VAL B  98   O  TYR B  23           
SHEET    3   E 4 TRP B  43  CYS B  47 -1  N  LYS B  46   O  LEU B  97           
SHEET    4   E 4 VAL B  60  VAL B  63 -1  N  VAL B  63   O  TRP B  43           
SHEET    1   F 5 LYS B 215  ALA B 218  0                                        
SHEET    2   F 5 LEU B 193  ILE B 198 -1  N  GLU B 197   O  LYS B 215           
SHEET    3   F 5 TYR B 109  ASP B 115 -1  N  ALA B 112   O  ILE B 196           
SHEET    4   F 5 ARG B 120  SER B 126 -1  N  SER B 126   O  TYR B 109           
SHEET    5   F 5 ILE B 144  ALA B 148 -1  N  VAL B 147   O  PHE B 123           
SHEET    1   G 3 LEU B 209  CYS B 211  0                                        
SHEET    2   G 3 LEU B 201  THR B 204 -1  N  VAL B 202   O  ILE B 210           
SHEET    3   G 3 ILE B 104  LEU B 108 -1  N  LEU B 108   O  LEU B 201           
SHEET    1   H 2 LEU B 250  ALA B 254  0                                        
SHEET    2   H 2 ASN B 285  VAL B 289 -1  N  ASP B 288   O  ASN B 251           
SHEET    1   I 4 ILE B 259  VAL B 263  0                                        
SHEET    2   I 4 ALA B 313  PHE B 319  1  N  ALA B 313   O  GLY B 260           
SHEET    3   I 4 VAL B 345  GLU B 350  1  N  VAL B 346   O  VAL B 314           
SHEET    4   I 4 ILE B 368  ALA B 370  1  N  ILE B 369   O  VAL B 345           
SHEET    1   J 5 ARG D 117  ILE D 119  0                                        
SHEET    2   J 5 LEU D  91  THR D  94  1  N  ILE D  92   O  ARG D 117           
SHEET    3   J 5 ALA D  67  ILE D  70  1  N  SER D  68   O  LEU D  91           
SHEET    4   J 5 LYS D   9  GLN D  13  1  N  ILE D  11   O  ALA D  67           
SHEET    5   J 5 LYS D  33  VAL D  38  1  N  LYS D  33   O  VAL D  10           
SHEET    1   K 2 THR D  45  HIS D  47  0                                        
SHEET    2   K 2 LEU D  50  VAL D  52 -1  N  VAL D  52   O  THR D  45           
SHEET    1   L 6 CYS D 132  GLY D 135  0                                        
SHEET    2   L 6 GLY D 125  THR D 128 -1  N  THR D 128   O  CYS D 132           
SHEET    3   L 6 THR D 173  GLY D 176 -1  N  CYS D 174   O  ILE D 127           
SHEET    4   L 6 VAL D 147  SER D 151  1  N  ILE D 149   O  VAL D 175           
SHEET    5   L 6 ALA D 202  GLU D 208  1  N  ALA D 202   O  GLY D 148           
SHEET    6   L 6 PRO D 228  ALA D 234  1  N  PRO D 228   O  ILE D 203           
SHEET    1   M 4 GLY E  22  CYS E  25  0                                        
SHEET    2   M 4 ILE E  96  ALA E 100 -1  N  VAL E  98   O  TYR E  23           
SHEET    3   M 4 TRP E  43  CYS E  47 -1  N  LYS E  46   O  LEU E  97           
SHEET    4   M 4 VAL E  60  VAL E  63 -1  N  VAL E  63   O  TRP E  43           
SHEET    1   N 5 LYS E 215  ALA E 218  0                                        
SHEET    2   N 5 LEU E 193  ILE E 198 -1  N  GLU E 197   O  LYS E 215           
SHEET    3   N 5 TYR E 109  ASP E 115 -1  N  ALA E 112   O  ILE E 196           
SHEET    4   N 5 ARG E 120  SER E 126 -1  N  SER E 126   O  TYR E 109           
SHEET    5   N 5 ILE E 144  ALA E 148 -1  N  VAL E 147   O  PHE E 123           
SHEET    1   O 3 LEU E 209  CYS E 211  0                                        
SHEET    2   O 3 LEU E 201  THR E 204 -1  N  VAL E 202   O  ILE E 210           
SHEET    3   O 3 ILE E 104  LEU E 108 -1  N  LEU E 108   O  LEU E 201           
SHEET    1   P 2 LEU E 250  ALA E 254  0                                        
SHEET    2   P 2 ASN E 285  VAL E 289 -1  N  ASP E 288   O  ASN E 251           
SHEET    1   Q 2 GLY E 260  VAL E 263  0                                        
SHEET    2   Q 2 VAL E 314  ASN E 317  1  N  LEU E 315   O  GLY E 260           
SHEET    1   R 2 VAL E 345  VAL E 347  0                                        
SHEET    2   R 2 ILE E 368  ALA E 370  1  N  ILE E 369   O  VAL E 345           
LINK         C   GLY A 245                 N   NEP A 246     1555   1555  1.35  
LINK         C   NEP A 246                 N   ALA A 247     1555   1555  1.32  
LINK         C   GLY D 245                 N   NEP D 246     1555   1555  1.32  
LINK         C   NEP D 246                 N   ALA D 247     1555   1555  1.33  
CISPEP   1 GLY A  120    PRO A  121          0        16.05                     
CISPEP   2 GLY B   41    PRO B   42          0        -2.67                     
CISPEP   3 ASN B  199    PRO B  200          0        10.49                     
CISPEP   4 GLY D  120    PRO D  121          0         1.68                     
CISPEP   5 GLY E   41    PRO E   42          0         2.40                     
CISPEP   6 ASN E  199    PRO E  200          0        17.13                     
SITE     1 AC1  4 GLY B  53  ARG B  54  GLY B  55  ASP B 213                    
SITE     1 AC2  5 GLY E  53  ARG E  54  GLY E  55  ASP E 213                    
SITE     2 AC2  5 HOH E1365                                                     
SITE     1 AC3 29 GLY A  14  THR A  16  GLY A  17  SER A  18                    
SITE     2 AC3 29 GLN A  19  VAL A  38  PRO A  40  LYS A  42                    
SITE     3 AC3 29 TYR A  71  VAL A  72  PRO A  73  ILE A  95                    
SITE     4 AC3 29 THR A  96  GLU A  97  ASN A 122  CYS A 123                    
SITE     5 AC3 29 PRO A 124  HOH A1005  HOH A1006  HOH A1010                    
SITE     6 AC3 29 HOH A1031  HOH A1350  HOH A1355  HOH A1483                    
SITE     7 AC3 29 HOH B1173  ARG E  29  GLU E  33  SER E  36                    
SITE     8 AC3 29 LYS E  66                                                     
SITE     1 AC4 30 ARG B  29  GLU B  33  SER B  36  LYS B  66                    
SITE     2 AC4 30 HOH B1122  GLY D  14  THR D  16  GLY D  17                    
SITE     3 AC4 30 SER D  18  GLN D  19  VAL D  38  PRO D  40                    
SITE     4 AC4 30 LYS D  42  TYR D  71  VAL D  72  SER D  80                    
SITE     5 AC4 30 ILE D  95  THR D  96  GLU D  97  ASN D 122                    
SITE     6 AC4 30 CYS D 123  NEP D 246  HOH D1119  HOH D1253                    
SITE     7 AC4 30 HOH D1254  HOH D1255  HOH D1273  HOH D1277                    
SITE     8 AC4 30 HOH D1476  HOH D1485                                          
CRYST1   98.680   98.680  403.760  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      0.010134  0.000000  0.000000        0.00000                         
SCALE2      0.000000  0.010134  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.002477        0.00000                         
MTRIX1   1 -0.756672 -0.256354 -0.601439       90.27800    1                    
MTRIX2   1 -0.242056 -0.744706  0.621950       28.08100    1                    
MTRIX3   1 -0.607335  0.616195  0.501446       25.00900    1                    
MTRIX1   2 -0.756672 -0.256354 -0.601439       90.27800    1                    
MTRIX2   2 -0.242056 -0.744706  0.621950       28.08100    1                    
MTRIX3   2 -0.607335  0.616195  0.501446       25.00900    1                    
MTRIX1   3 -0.754283 -0.251541 -0.606452       90.59100    1                    
MTRIX2   3 -0.247007 -0.747110  0.617101       28.48600    1                    
MTRIX3   3 -0.608313  0.615267  0.501400       25.02700    1                    
MTRIX1   4 -0.754283 -0.251541 -0.606452       90.59100    1                    
MTRIX2   4 -0.247007 -0.747110  0.617101       28.48600    1                    
MTRIX3   4 -0.608313  0.615267  0.501400       25.02700    1                    
(ATOM LINES ARE NOT SHOWN.)
END                                                                             
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