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Database: PDB
Entry: 1JLL
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Original site: 1JLL 
HEADER    LIGASE                                  16-JUL-01   1JLL              
TITLE     CRYSTAL STRUCTURE ANALYSIS OF THE E197BETAA MUTANT OF E.              
TITLE    2 COLI SCS                                                             
COMPND    MOL_ID: 1;                                                            
COMPND   2 MOLECULE: SUCCINYL-COA SYNTHETASE ALPHA SUBUNIT;                     
COMPND   3 CHAIN: A, D;                                                         
COMPND   4 SYNONYM: SCS-ALPHA;                                                  
COMPND   5 EC: 6.2.1.5;                                                         
COMPND   6 ENGINEERED: YES;                                                     
COMPND   7 MOL_ID: 2;                                                           
COMPND   8 MOLECULE: SUCCINYL-COA SYNTHETASE BETA SUBUNIT;                      
COMPND   9 CHAIN: B, E;                                                         
COMPND  10 SYNONYM: SCS-BETA;                                                   
COMPND  11 EC: 6.2.1.5;                                                         
COMPND  12 ENGINEERED: YES;                                                     
COMPND  13 MUTATION: YES                                                        
SOURCE    MOL_ID: 1;                                                            
SOURCE   2 ORGANISM_SCIENTIFIC: ESCHERICHIA COLI;                               
SOURCE   3 ORGANISM_TAXID: 562;                                                 
SOURCE   4 EXPRESSION_SYSTEM: ESCHERICHIA COLI;                                 
SOURCE   5 EXPRESSION_SYSTEM_TAXID: 562;                                        
SOURCE   6 MOL_ID: 2;                                                           
SOURCE   7 ORGANISM_SCIENTIFIC: ESCHERICHIA COLI;                               
SOURCE   8 ORGANISM_TAXID: 562;                                                 
SOURCE   9 EXPRESSION_SYSTEM: ESCHERICHIA COLI;                                 
SOURCE  10 EXPRESSION_SYSTEM_TAXID: 562                                         
KEYWDS    CITRIC ACID CYCLE, HETEROTETRAMER, LIGASE, ATP-GRASP FOLD,            
KEYWDS   2 ROSSMANN FOLD                                                        
EXPDTA    X-RAY DIFFRACTION                                                     
AUTHOR    M.E.FRASER                                                            
REVDAT   2   24-FEB-09 1JLL    1       VERSN                                    
REVDAT   1   30-JAN-02 1JLL    0                                                
JRNL        AUTH   M.E.FRASER,M.A.JOYCE,D.G.RYAN,W.T.WOLODKO                    
JRNL        TITL   TWO GLUTAMATE RESIDUES, GLU 208 ALPHA AND GLU 197            
JRNL        TITL 2 BETA, ARE CRUCIAL FOR PHOSPHORYLATION AND                    
JRNL        TITL 3 DEPHOSPHORYLATION OF THE ACTIVE-SITE HISTIDINE               
JRNL        TITL 4 RESIDUE IN SUCCINYL-COA SYNTHETASE.                          
JRNL        REF    BIOCHEMISTRY                  V.  41   537 2002              
JRNL        REFN                   ISSN 0006-2960                               
JRNL        PMID   11781092                                                     
JRNL        DOI    10.1021/BI011518Y                                            
REMARK   1                                                                      
REMARK   2                                                                      
REMARK   2 RESOLUTION.    2.69 ANGSTROMS.                                       
REMARK   3                                                                      
REMARK   3 REFINEMENT.                                                          
REMARK   3   PROGRAM     : CNS                                                  
REMARK   3   AUTHORS     : BRUNGER,ADAMS,CLORE,DELANO,GROS,GROSSE-              
REMARK   3               : KUNSTLEVE,JIANG,KUSZEWSKI,NILGES, PANNU,             
REMARK   3               : READ,RICE,SIMONSON,WARREN                            
REMARK   3                                                                      
REMARK   3  REFINEMENT TARGET : ENGH & HUBER                                    
REMARK   3                                                                      
REMARK   3  DATA USED IN REFINEMENT.                                            
REMARK   3   RESOLUTION RANGE HIGH (ANGSTROMS) : 2.69                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 34.38                          
REMARK   3   DATA CUTOFF            (SIGMA(F)) : 0.000                          
REMARK   3   DATA CUTOFF HIGH         (ABS(F)) : NULL                           
REMARK   3   DATA CUTOFF LOW          (ABS(F)) : NULL                           
REMARK   3   COMPLETENESS (WORKING+TEST)   (%) : 90.5                           
REMARK   3   NUMBER OF REFLECTIONS             : 48023                          
REMARK   3                                                                      
REMARK   3  FIT TO DATA USED IN REFINEMENT.                                     
REMARK   3   CROSS-VALIDATION METHOD          : THROUGHOUT. STARTED WITH        
REMARK   3                                      10% OF THE DATA, REDUCED        
REMARK   3                                      THIS TO JUST OVER 1000          
REMARK   3                                      REFLECTIONS NEAR THE END OF     
REMARK   3                                      THE REFINEMENT.                 
REMARK   3   FREE R VALUE TEST SET SELECTION  : RANDOM. BUT THE                 
REMARK   3                                      REFLECTIONS CHOSEN ARE          
REMARK   3                                      CONSISTENT AMONG ALL DATA       
REMARK   3                                      SETS FOR THIS CRYSTAL FORM.     
REMARK   3   R VALUE            (WORKING SET) : 0.222                           
REMARK   3   FREE R VALUE                     : 0.259                           
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : NULL                            
REMARK   3   FREE R VALUE TEST SET COUNT      : 1000                            
REMARK   3   ESTIMATED ERROR OF FREE R VALUE  : NULL                            
REMARK   3                                                                      
REMARK   3  FIT IN THE HIGHEST RESOLUTION BIN.                                  
REMARK   3   TOTAL NUMBER OF BINS USED           : 4                            
REMARK   3   BIN RESOLUTION RANGE HIGH       (A) : 2.70                         
REMARK   3   BIN RESOLUTION RANGE LOW        (A) : 2.82                         
REMARK   3   BIN COMPLETENESS (WORKING+TEST) (%) : 78.20                        
REMARK   3   REFLECTIONS IN BIN    (WORKING SET) : NULL                         
REMARK   3   BIN R VALUE           (WORKING SET) : 0.3400                       
REMARK   3   BIN FREE R VALUE                    : 0.3390                       
REMARK   3   BIN FREE R VALUE TEST SET SIZE  (%) : NULL                         
REMARK   3   BIN FREE R VALUE TEST SET COUNT     : 153                          
REMARK   3   ESTIMATED ERROR OF BIN FREE R VALUE : 0.027                        
REMARK   3                                                                      
REMARK   3  NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.                    
REMARK   3   PROTEIN ATOMS            : 9923                                    
REMARK   3   NUCLEIC ACID ATOMS       : 0                                       
REMARK   3   HETEROGEN ATOMS          : 139                                     
REMARK   3   SOLVENT ATOMS            : 193                                     
REMARK   3                                                                      
REMARK   3  B VALUES.                                                           
REMARK   3   FROM WILSON PLOT           (A**2) : NULL                           
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : NULL                           
REMARK   3   OVERALL ANISOTROPIC B VALUE.                                       
REMARK   3    B11 (A**2) : NULL                                                 
REMARK   3    B22 (A**2) : NULL                                                 
REMARK   3    B33 (A**2) : NULL                                                 
REMARK   3    B12 (A**2) : NULL                                                 
REMARK   3    B13 (A**2) : NULL                                                 
REMARK   3    B23 (A**2) : NULL                                                 
REMARK   3                                                                      
REMARK   3  ESTIMATED COORDINATE ERROR.                                         
REMARK   3   ESD FROM LUZZATI PLOT        (A) : 0.33                            
REMARK   3   ESD FROM SIGMAA              (A) : 0.40                            
REMARK   3   LOW RESOLUTION CUTOFF        (A) : 5.00                            
REMARK   3                                                                      
REMARK   3  CROSS-VALIDATED ESTIMATED COORDINATE ERROR.                         
REMARK   3   ESD FROM C-V LUZZATI PLOT    (A) : 0.40                            
REMARK   3   ESD FROM C-V SIGMAA          (A) : 0.60                            
REMARK   3                                                                      
REMARK   3  RMS DEVIATIONS FROM IDEAL VALUES.                                   
REMARK   3   BOND LENGTHS                 (A) : 0.017                           
REMARK   3   BOND ANGLES            (DEGREES) : 2.00                            
REMARK   3   DIHEDRAL ANGLES        (DEGREES) : 24.50                           
REMARK   3   IMPROPER ANGLES        (DEGREES) : 1.19                            
REMARK   3                                                                      
REMARK   3  ISOTROPIC THERMAL MODEL : NULL                                      
REMARK   3                                                                      
REMARK   3  ISOTROPIC THERMAL FACTOR RESTRAINTS.    RMS    SIGMA                
REMARK   3   MAIN-CHAIN BOND              (A**2) : 1.280 ; NULL                 
REMARK   3   MAIN-CHAIN ANGLE             (A**2) : NULL  ; NULL                 
REMARK   3   SIDE-CHAIN BOND              (A**2) : NULL  ; NULL                 
REMARK   3   SIDE-CHAIN ANGLE             (A**2) : NULL  ; NULL                 
REMARK   3                                                                      
REMARK   3  BULK SOLVENT MODELING.                                              
REMARK   3   METHOD USED : CNS BULK SOLVENT MODEL USED                          
REMARK   3   KSOL        : 0.38                                                 
REMARK   3   BSOL        : 43.63                                                
REMARK   3                                                                      
REMARK   3  NCS MODEL : NULL                                                    
REMARK   3                                                                      
REMARK   3  NCS RESTRAINTS.                         RMS   SIGMA/WEIGHT          
REMARK   3   GROUP  1  POSITIONAL            (A) : NULL  ; NULL                 
REMARK   3   GROUP  1  B-FACTOR           (A**2) : NULL  ; NULL                 
REMARK   3                                                                      
REMARK   3  PARAMETER FILE  1  : NULL                                           
REMARK   3  TOPOLOGY FILE  1   : NULL                                           
REMARK   3                                                                      
REMARK   3  OTHER REFINEMENT REMARKS: NULL                                      
REMARK   4                                                                      
REMARK   4 1JLL COMPLIES WITH FORMAT V. 3.15, 01-DEC-08                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 20-JUL-01.                  
REMARK 100 THE RCSB ID CODE IS RCSB013912.                                      
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : 20-NOV-00                          
REMARK 200  TEMPERATURE           (KELVIN) : 100                                
REMARK 200  PH                             : 7.6                                
REMARK 200  NUMBER OF CRYSTALS USED        : 1                                  
REMARK 200                                                                      
REMARK 200  SYNCHROTRON              (Y/N) : Y                                  
REMARK 200  RADIATION SOURCE               : SSRL                               
REMARK 200  BEAMLINE                       : BL9-1                              
REMARK 200  X-RAY GENERATOR MODEL          : NULL                               
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M                                  
REMARK 200  WAVELENGTH OR RANGE        (A) : 0.979                              
REMARK 200  MONOCHROMATOR                  : SI(311) BENT MONOCHROMATOR         
REMARK 200  OPTICS                         : FLAT MIRROR (VERTICAL              
REMARK 200                                   FOCUSING); SINGLE CRYSTAL          
REMARK 200                                   SI(311) BENT MONOCHROMATOR         
REMARK 200                                   (HORIZONTAL FOCUSING)              
REMARK 200                                                                      
REMARK 200  DETECTOR TYPE                  : IMAGE PLATE                        
REMARK 200  DETECTOR MANUFACTURER          : MARRESEARCH                        
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : DENZO                              
REMARK 200  DATA SCALING SOFTWARE          : SCALEPACK                          
REMARK 200                                                                      
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 48720                              
REMARK 200  RESOLUTION RANGE HIGH      (A) : 2.700                              
REMARK 200  RESOLUTION RANGE LOW       (A) : 50.000                             
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : 0.000                              
REMARK 200                                                                      
REMARK 200 OVERALL.                                                             
REMARK 200  COMPLETENESS FOR RANGE     (%) : 91.0                               
REMARK 200  DATA REDUNDANCY                : 3.100                              
REMARK 200  R MERGE                    (I) : 0.04100                            
REMARK 200  R SYM                      (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR THE DATA SET  : 28.0000                            
REMARK 200                                                                      
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.                                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.70                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 2.75                     
REMARK 200  COMPLETENESS FOR SHELL     (%) : 61.7                               
REMARK 200  DATA REDUNDANCY IN SHELL       : NULL                               
REMARK 200  R MERGE FOR SHELL          (I) : 0.33800                            
REMARK 200  R SYM FOR SHELL            (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR SHELL         : 2.600                              
REMARK 200                                                                      
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH                              
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: FOURIER SYNTHESIS            
REMARK 200 SOFTWARE USED: CNS                                                   
REMARK 200 STARTING MODEL: 1JKJ, PARTIALLY REFINED                              
REMARK 200                                                                      
REMARK 200 REMARK: NULL                                                         
REMARK 280                                                                      
REMARK 280 CRYSTAL                                                              
REMARK 280 SOLVENT CONTENT, VS   (%): 61.88                                     
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 3.23                     
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: BICINE, AMMONIUM SULFATE, PH 7.6,        
REMARK 280  VAPOR DIFFUSION, HANGING DROP, TEMPERATURE 294K                     
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      194.80000            
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      292.20000            
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       97.40000            
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      194.80000            
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       97.40000            
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      292.20000            
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 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       97.40000            
REMARK 350                                                                      
REMARK 350 BIOMOLECULE: 2                                                       
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: TETRAMERIC                        
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       97.40000            
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     LYS A   288                                                      
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: 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   O    GLY B   291     N    ALA B   293              2.08            
REMARK 500   ND2  ASN E    64     O    HOH E  1924              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    CYS A  77   CB    CYS A  77   SG     -0.143                       
REMARK 500    CYS D  77   CB    CYS D  77   SG     -0.100                       
REMARK 500    GLU E 132   CG    GLU E 132   CD      0.098                       
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    PRO A 124   C   -  N   -  CA  ANGL. DEV. =  -9.1 DEGREES          
REMARK 500    GLY A 139   N   -  CA  -  C   ANGL. DEV. =  15.3 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      -50.23     58.17                                   
REMARK 500    THR A  96      131.81    -36.56                                   
REMARK 500    PRO A 121     -154.38    -84.72                                   
REMARK 500    ASN A 122       79.17     63.86                                   
REMARK 500    PRO A 124     -157.36    -62.15                                   
REMARK 500    SER A 172      -70.22    -67.79                                   
REMARK 500    GLU A 208     -179.75   -172.36                                   
REMARK 500    SER A 212       28.59   -140.11                                   
REMARK 500    ASP A 278       35.76    -97.98                                   
REMARK 500    THR A 285     -102.40    -61.20                                   
REMARK 500    VAL A 286      -28.22    -31.83                                   
REMARK 500    GLU B 138      -76.21    -65.49                                   
REMARK 500    GLU B 139      -75.82    -46.31                                   
REMARK 500    THR B 140       73.28   -112.08                                   
REMARK 500    GLU B 249       48.94     72.02                                   
REMARK 500    HIS B 279       49.15    -99.80                                   
REMARK 500    ASN B 285     -179.62   -173.57                                   
REMARK 500    VAL B 289      -66.90    -94.57                                   
REMARK 500    ALA B 293       51.48    -51.84                                   
REMARK 500    THR B 294     -179.25    -62.23                                   
REMARK 500    ASP B 309       -7.73    -49.35                                   
REMARK 500    ALA B 313      152.78    175.94                                   
REMARK 500    PHE B 319       84.16   -163.81                                   
REMARK 500    CYS B 325      -12.04    -39.51                                   
REMARK 500    ASN B 342       32.45    -99.45                                   
REMARK 500    ASN B 353       33.34     70.57                                   
REMARK 500    LYS B 359      -73.94    -73.54                                   
REMARK 500    LYS B 360      -37.45    -29.05                                   
REMARK 500    ILE B 369     -167.85    -77.09                                   
REMARK 500    ALA B 370       82.88   -164.81                                   
REMARK 500    LYS B 372       72.96   -113.60                                   
REMARK 500    LEU B 374      -62.13    -90.96                                   
REMARK 500    ALA B 378      -75.65    -65.56                                   
REMARK 500    ALA B 384        8.23    -42.87                                   
REMARK 500    GLU B 386       93.60    -29.86                                   
REMARK 500    LEU D   3      -49.16     54.56                                   
REMARK 500    THR D  96      131.52    -32.28                                   
REMARK 500    PRO D 121     -157.47    -81.89                                   
REMARK 500    ASN D 122       79.26     65.45                                   
REMARK 500    PRO D 124     -154.62    -63.15                                   
REMARK 500    GLU D 131      -61.00    -90.47                                   
REMARK 500    PRO D 138       70.39   -100.98                                   
REMARK 500    SER D 172      -70.14    -66.45                                   
REMARK 500    SER D 212       27.08   -141.68                                   
REMARK 500    ASP D 278       36.51    -96.77                                   
REMARK 500    THR D 285     -104.87    -62.60                                   
REMARK 500    VAL D 286      -26.97    -29.97                                   
REMARK 500    GLU E 249       48.14     70.47                                   
REMARK 500    HIS E 279       48.10    -96.08                                   
REMARK 500    VAL E 289      -61.32    -93.17                                   
REMARK 500    ALA E 293       53.42    -61.92                                   
REMARK 500    ASP E 309       -8.60    -54.03                                   
REMARK 500    ALA E 313      153.25    178.36                                   
REMARK 500    PHE E 319       86.97   -166.78                                   
REMARK 500    CYS E 325      -12.22    -41.51                                   
REMARK 500    ASN E 353       31.12     70.08                                   
REMARK 500    LYS E 359      -75.67    -70.17                                   
REMARK 500    LYS E 360      -41.32    -25.74                                   
REMARK 500    ILE E 369     -167.49    -77.66                                   
REMARK 500    ALA E 370       84.40   -165.60                                   
REMARK 500    LYS E 372       74.92   -112.25                                   
REMARK 500    ALA E 378      -71.83    -65.85                                   
REMARK 500    ALA E 384        9.83    -42.80                                   
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 610                                                                      
REMARK 610 MISSING HETEROATOM                                                   
REMARK 610 THE FOLLOWING RESIDUES HAVE MISSING ATOMS (M=MODEL NUMBER;           
REMARK 610 RES=RESIDUE NAME; C=CHAIN IDENTIFIER; SSEQ=SEQUENCE NUMBER;          
REMARK 610 I=INSERTION CODE):                                                   
REMARK 610   M RES C SSEQI                                                      
REMARK 610     COA A 1300                                                       
REMARK 610     COA D 1301                                                       
REMARK 610     COA B 1903                                                       
REMARK 610     COA E 1904                                                       
REMARK 800                                                                      
REMARK 800 SITE                                                                 
REMARK 800 SITE_IDENTIFIER: AC1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE PO4 A 1600                
REMARK 800 SITE_IDENTIFIER: AC2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 B 1400                
REMARK 800 SITE_IDENTIFIER: AC3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 B 1500                
REMARK 800 SITE_IDENTIFIER: AC4                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE PO4 D 1601                
REMARK 800 SITE_IDENTIFIER: AC5                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 E 1401                
REMARK 800 SITE_IDENTIFIER: AC6                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 E 1501                
REMARK 800 SITE_IDENTIFIER: AC7                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE COA A 1300                
REMARK 800 SITE_IDENTIFIER: AC8                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE COA D 1301                
REMARK 800 SITE_IDENTIFIER: AC9                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE COA B 1903                
REMARK 800 SITE_IDENTIFIER: BC1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE COA E 1904                
REMARK 900                                                                      
REMARK 900 RELATED ENTRIES                                                      
REMARK 900 RELATED ID: 1JKJ   RELATED DB: PDB                                   
REMARK 900 1JKJ IS E. COLI SCS, DEPHOSPHORYLATED AND AT 100K                    
REMARK 900 RELATED ID: 2SCU   RELATED DB: PDB                                   
REMARK 900 1SCU IS THE PHOSPHORYLATED PROTEIN COLLECTED AT ROOM                 
REMARK 900 TEMPERATURE                                                          
REMARK 900 RELATED ID: 1CQI   RELATED DB: PDB                                   
REMARK 900 1CQI IS THE SAME PROTEIN COMPLEXED WITH ADP AND MAGNESIUM            
REMARK 900 IONS, COLLECTED AT ROOM TEMPERATURE                                  
REMARK 900 RELATED ID: 1CQJ   RELATED DB: PDB                                   
REMARK 900 1CQJ IS THE SAME PROTEIN AT ROOM TEMPERATURE                         
REMARK 900 RELATED ID: 1EUC   RELATED DB: PDB                                   
REMARK 900 1EUC IS GTP-SPECIFIC SUCCINYL-COA SYNTHETASE, NOT                    
REMARK 900 PHOSPHORYLATED AND AT ROOM TEMPERATURE                               
REMARK 900 RELATED ID: 1EUD   RELATED DB: PDB                                   
REMARK 900 1EUD IS GTP-SPECIFIC SUCCINYL-COA SYNTHETASE,                        
REMARK 900 PHOSPHORYLATED AND AT ROOM TEMPERATURE                               
DBREF  1JLL A    1   288  UNP    P07459   SUCD_ECOLI       1    288             
DBREF  1JLL D    1   288  UNP    P07459   SUCD_ECOLI       1    288             
DBREF  1JLL B    1   388  UNP    P0A836   SUCC_ECOLI       1    388             
DBREF  1JLL E    1   388  UNP    P0A836   SUCC_ECOLI       1    388             
SEQADV 1JLL ALA B  197  UNP  P0A836    GLU   197 ENGINEERED                     
SEQADV 1JLL ALA E  197  UNP  P0A836    GLU   197 ENGINEERED                     
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 HIS 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 ALA 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 HIS 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 ALA 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                  
HET    PO4  A1600       5                                                       
HET    SO4  B1400       5                                                       
HET    SO4  B1500       5                                                       
HET    PO4  D1601       5                                                       
HET    SO4  E1401       5                                                       
HET    SO4  E1501       5                                                       
HET    COA  A1300      42                                                       
HET    COA  D1301      42                                                       
HET    COA  B1903      17                                                       
HET    COA  E1904       8                                                       
HETNAM     PO4 PHOSPHATE ION                                                    
HETNAM     SO4 SULFATE ION                                                      
HETNAM     COA COENZYME A                                                       
FORMUL   5  PO4    2(O4 P 3-)                                                   
FORMUL   6  SO4    4(O4 S 2-)                                                   
FORMUL  11  COA    4(C21 H36 N7 O16 P3 S)                                       
FORMUL  15  HOH   *193(H2 O)                                                    
HELIX    1   1 GLY A   17  TYR A   30  1                                  14    
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 GLY A  154  TYR A  167  1                                  14    
HELIX    6   6 ASN A  186  LYS A  196  1                                  11    
HELIX    7   7 SER A  212  VAL A  225  1                                  14    
HELIX    8   8 THR A  257  ALA A  267  1                                  11    
HELIX    9   9 ASP A  278  LEU A  287  1                                  10    
HELIX   10  10 HIS B    4  TYR B   15  1                                  12    
HELIX   11  11 THR B   27  GLY B   39  1                                  13    
HELIX   12  12 SER B   65  LEU B   77  1                                  13    
HELIX   13  13 GLU B  132  THR B  140  1                                   9    
HELIX   14  14 MET B  156  LEU B  167  1                                  12    
HELIX   15  15 GLY B  171  ARG B  191  1                                  21    
HELIX   16  16 GLY B  220  ARG B  225  5                                   6    
HELIX   17  17 GLN B  226  MET B  232  1                                   7    
HELIX   18  18 ARG B  233  ARG B  233  5                                   1    
HELIX   19  19 ASP B  234  GLU B  238  5                                   5    
HELIX   20  20 ASP B  239  TRP B  248  1                                  10    
HELIX   21  21 GLY B  265  HIS B  279  1                                  15    
HELIX   22  22 THR B  294  SER B  307  1                                  14    
HELIX   23  23 ASP B  326  VAL B  339  1                                  14    
HELIX   24  24 ASN B  353  GLY B  365  1                                  13    
HELIX   25  25 GLY B  373  ALA B  384  1                                  12    
HELIX   26  26 GLY D   17  TYR D   30  1                                  14    
HELIX   27  27 THR D   55  GLY D   64  1                                  10    
HELIX   28  28 PRO D   73  ALA D   87  1                                  15    
HELIX   29  29 PRO D  100  GLY D  115  1                                  16    
HELIX   30  30 GLY D  154  TYR D  167  1                                  14    
HELIX   31  31 ASN D  186  LYS D  196  1                                  11    
HELIX   32  32 SER D  212  VAL D  225  1                                  14    
HELIX   33  33 ILE D  251  LYS D  255  5                                   5    
HELIX   34  34 THR D  257  ALA D  267  1                                  11    
HELIX   35  35 ASP D  278  LEU D  287  1                                  10    
HELIX   36  36 HIS E    4  TYR E   15  1                                  12    
HELIX   37  37 THR E   27  GLY E   39  1                                  13    
HELIX   38  38 SER E   65  LEU E   77  1                                  13    
HELIX   39  39 GLU E  132  THR E  140  1                                   9    
HELIX   40  40 PRO E  141  ILE E  144  5                                   4    
HELIX   41  41 MET E  156  LEU E  167  1                                  12    
HELIX   42  42 GLY E  171  ARG E  191  1                                  21    
HELIX   43  43 GLY E  220  ARG E  225  5                                   6    
HELIX   44  44 GLN E  226  MET E  232  1                                   7    
HELIX   45  45 ARG E  233  ARG E  233  5                                   1    
HELIX   46  46 ASP E  234  GLU E  238  5                                   5    
HELIX   47  47 ASP E  239  TRP E  248  1                                  10    
HELIX   48  48 GLY E  265  HIS E  279  1                                  15    
HELIX   49  49 THR E  294  SER E  307  1                                  14    
HELIX   50  50 ASP E  326  GLY E  340  1                                  15    
HELIX   51  51 ASN E  353  GLY E  365  1                                  13    
HELIX   52  52 GLY E  373  ALA E  384  1                                  12    
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  ILE A 134  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  N  VAL A 230   O  ILE A 203           
SHEET    7   B 7 LYS A 271  THR A 272  1  N  LYS A 271   O  VAL A 229           
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 ILE B 144  ALA B 148  0                                        
SHEET    2   E 5 ARG B 120  SER B 126 -1  N  PHE B 123   O  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  O  ALA B 194   N  VAL B 114           
SHEET    5   E 5 LEU B 209  CYS B 211 -1  O  ILE B 210   N  VAL B 202           
SHEET    1   F 5 ILE B 144  ALA B 148  0                                        
SHEET    2   F 5 ARG B 120  SER B 126 -1  N  PHE B 123   O  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  O  ALA B 194   N  VAL B 114           
SHEET    5   F 5 LYS B 215  ALA B 218 -1  N  LYS B 215   O  ALA B 197           
SHEET    1   G 2 ASN B 251  ALA B 254  0                                        
SHEET    2   G 2 ASN B 285  ASP B 288 -1  O  PHE B 286   N  VAL B 253           
SHEET    1   H 3 ILE B 259  VAL B 263  0                                        
SHEET    2   H 3 ALA B 313  ASN B 317  1  O  ALA B 313   N  GLY B 260           
SHEET    3   H 3 VAL B 345  ARG B 348  1  O  VAL B 346   N  VAL B 316           
SHEET    1   I 7 THR D  45  HIS D  47  0                                        
SHEET    2   I 7 LEU D  50  PHE D  53 -1  N  LEU D  50   O  HIS D  47           
SHEET    3   I 7 LYS D  33  VAL D  38  1  O  GLY D  37   N  PHE D  53           
SHEET    4   I 7 LYS D   9  GLN D  13  1  O  VAL D  10   N  VAL D  35           
SHEET    5   I 7 ALA D  67  ILE D  70  1  O  ALA D  67   N  ILE D  11           
SHEET    6   I 7 LEU D  91  THR D  94  1  O  LEU D  91   N  SER D  68           
SHEET    7   I 7 ARG D 117  ILE D 119  1  O  ARG D 117   N  ILE D  92           
SHEET    1   J 7 CYS D 132  ILE D 134  0                                        
SHEET    2   J 7 GLY D 125  THR D 128 -1  N  VAL D 126   O  ILE D 134           
SHEET    3   J 7 GLN D 171  GLY D 176 -1  N  CYS D 174   O  ILE D 127           
SHEET    4   J 7 VAL D 147  SER D 151  1  O  VAL D 147   N  SER D 172           
SHEET    5   J 7 ALA D 202  GLU D 208  1  O  ALA D 202   N  GLY D 148           
SHEET    6   J 7 VAL D 229  ALA D 234  1  N  VAL D 230   O  ILE D 203           
SHEET    7   J 7 LYS D 271  THR D 272  1  O  LYS D 271   N  GLY D 231           
SHEET    1   K 4 GLY E  22  CYS E  25  0                                        
SHEET    2   K 4 ILE E  96  ALA E 100 -1  O  ILE E  96   N  CYS E  25           
SHEET    3   K 4 TRP E  43  CYS E  47 -1  N  VAL E  44   O  GLU E  99           
SHEET    4   K 4 VAL E  60  VAL E  63 -1  O  LYS E  61   N  VAL E  45           
SHEET    1   L 2 ARG E  80  LEU E  81  0                                        
SHEET    2   L 2 GLN E  91  PRO E  92 -1  N  GLN E  91   O  LEU E  81           
SHEET    1   M 5 HIS E 145  ALA E 148  0                                        
SHEET    2   M 5 ARG E 120  SER E 126 -1  N  PHE E 123   O  VAL E 147           
SHEET    3   M 5 ILE E 104  ASP E 115 -1  N  TYR E 109   O  SER E 126           
SHEET    4   M 5 LEU E 193  THR E 204 -1  O  ALA E 194   N  VAL E 114           
SHEET    5   M 5 LEU E 209  CYS E 211 -1  O  ILE E 210   N  VAL E 202           
SHEET    1   N 5 HIS E 145  ALA E 148  0                                        
SHEET    2   N 5 ARG E 120  SER E 126 -1  N  PHE E 123   O  VAL E 147           
SHEET    3   N 5 ILE E 104  ASP E 115 -1  N  TYR E 109   O  SER E 126           
SHEET    4   N 5 LEU E 193  THR E 204 -1  O  ALA E 194   N  VAL E 114           
SHEET    5   N 5 LYS E 215  ALA E 218 -1  O  LYS E 215   N  ALA E 197           
SHEET    1   O 2 ASN E 251  ALA E 254  0                                        
SHEET    2   O 2 ASN E 285  ASP E 288 -1  O  PHE E 286   N  VAL E 253           
SHEET    1   P 3 ILE E 259  VAL E 263  0                                        
SHEET    2   P 3 ALA E 313  ASN E 317  1  O  ALA E 313   N  GLY E 260           
SHEET    3   P 3 VAL E 345  ARG E 348  1  O  VAL E 346   N  VAL E 316           
LINK         SG  CYS B 325                 S1P COA B1903     1555   1555  2.04  
LINK         SG  CYS E 325                 S1P COA E1904     1555   1555  2.04  
CISPEP   1 GLY A  120    PRO A  121          0         0.05                     
CISPEP   2 GLY B   41    PRO B   42          0        -0.35                     
CISPEP   3 ASN B  199    PRO B  200          0         1.40                     
CISPEP   4 GLY D  120    PRO D  121          0         0.06                     
CISPEP   5 GLY E   41    PRO E   42          0        -0.64                     
CISPEP   6 ASN E  199    PRO E  200          0         1.03                     
SITE     1 AC1  7 SER A 153  GLY A 154  THR A 155  HIS A 246                    
SITE     2 AC1  7 GLY B 265  ALA B 266  GLY B 267                               
SITE     1 AC2  5 GLY B  52  GLY B  53  ARG B  54  GLY B  55                    
SITE     2 AC2  5 ASP B 213                                                     
SITE     1 AC3  4 ARG A 243  MET B   1  GLY B 220  ARG B 233                    
SITE     1 AC4  7 SER D 153  GLY D 154  THR D 155  HIS D 246                    
SITE     2 AC4  7 GLY E 265  ALA E 266  GLY E 267                               
SITE     1 AC5  5 GLY E  52  GLY E  53  ARG E  54  GLY E  55                    
SITE     2 AC5  5 ASP E 213                                                     
SITE     1 AC6  4 ARG D 243  MET E   1  GLY E 220  ARG E 233                    
SITE     1 AC7 25 GLY A  14  THR A  16  GLY A  17  SER A  18                    
SITE     2 AC7 25 GLN A  19  VAL A  38  PRO A  40  LYS A  42                    
SITE     3 AC7 25 TYR A  71  VAL A  72  PRO A  73  SER A  80                    
SITE     4 AC7 25 THR A  96  GLU A  97  CYS A 123  HOH A1605                    
SITE     5 AC7 25 HOH A1610  HOH A1635  HOH A1643  HOH A1647                    
SITE     6 AC7 25 ARG B 161  ARG E  29  GLU E  33  SER E  36                    
SITE     7 AC7 25 LYS E  66                                                     
SITE     1 AC8 24 ARG B  29  GLU B  33  SER B  36  LYS B  66                    
SITE     2 AC8 24 HOH B1926  HOH B1932  GLY D  14  THR D  16                    
SITE     3 AC8 24 GLY D  17  SER D  18  GLN D  19  VAL D  38                    
SITE     4 AC8 24 PRO D  40  LYS D  42  TYR D  71  VAL D  72                    
SITE     5 AC8 24 PRO D  73  SER D  80  THR D  96  GLU D  97                    
SITE     6 AC8 24 CYS D 123  HOH D1630  HOH D1631  ARG E 161                    
SITE     1 AC9  8 ILE B 318  GLY B 320  GLY B 321  ILE B 322                    
SITE     2 AC9  8 VAL B 323  CYS B 325  GLU B 350  ASN B 352                    
SITE     1 BC1  9 ILE E 318  GLY E 320  GLY E 321  ILE E 322                    
SITE     2 BC1  9 VAL E 323  CYS E 325  GLU E 350  GLY E 351                    
SITE     3 BC1  9 ASN E 352                                                     
CRYST1   97.060   97.060  389.600  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      0.010303  0.000000  0.000000        0.00000                         
SCALE2      0.000000  0.010303  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.002567        0.00000                         
(ATOM LINES ARE NOT SHOWN.)
END                                                                             
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