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Database: PDB
Entry: 1JKJ
LinkDB: 1JKJ
Original site: 1JKJ 
HEADER    LIGASE                                  12-JUL-01   1JKJ              
TITLE     E. 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                                                      
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, ROSSMANN   
KEYWDS   2 FOLD                                                                 
EXPDTA    X-RAY DIFFRACTION                                                     
AUTHOR    M.E.FRASER                                                            
REVDAT   3   13-JUL-11 1JKJ    1       VERSN                                    
REVDAT   2   24-FEB-09 1JKJ    1       VERSN                                    
REVDAT   1   30-JAN-02 1JKJ    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 BETA, ARE  
JRNL        TITL 2 CRUCIAL FOR PHOSPHORYLATION AND DEPHOSPHORYLATION OF THE     
JRNL        TITL 3 ACTIVE-SITE HISTIDINE 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   2                                                                      
REMARK   2 RESOLUTION.    2.35 ANGSTROMS.                                       
REMARK   3                                                                      
REMARK   3 REFINEMENT.                                                          
REMARK   3   PROGRAM     : CNS 1.0                                              
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) : 2.35                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 19.64                          
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)   (%) : 87.7                           
REMARK   3   NUMBER OF REFLECTIONS             : 68151                          
REMARK   3                                                                      
REMARK   3  FIT TO DATA USED IN REFINEMENT.                                     
REMARK   3   CROSS-VALIDATION METHOD          : THROUGHOUT.  STARTED WITH 10%   
REMARK   3                                      OF THE DATA, REDUCED THIS TO    
REMARK   3                                      JUST OVER 1000 REFLECTIONS      
REMARK   3                                      NEAR THE END OF THE REFINEMENT. 
REMARK   3   FREE R VALUE TEST SET SELECTION  : RANDOM. BUT THE REFLECTIONS     
REMARK   3                                      CHOSEN ARE CONSISTENT AMONG     
REMARK   3                                      ALL DATA SETS FOR THIS CRYSTAL  
REMARK   3                                      FORM.                           
REMARK   3   R VALUE            (WORKING SET) : 0.192                           
REMARK   3   FREE R VALUE                     : 0.238                           
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : NULL                            
REMARK   3   FREE R VALUE TEST SET COUNT      : 1063                            
REMARK   3   ESTIMATED ERROR OF FREE R VALUE  : NULL                            
REMARK   3                                                                      
REMARK   3  FIT IN THE HIGHEST RESOLUTION BIN.                                  
REMARK   3   TOTAL NUMBER OF BINS USED           : NULL                         
REMARK   3   BIN RESOLUTION RANGE HIGH       (A) : 2.35                         
REMARK   3   BIN RESOLUTION RANGE LOW        (A) : 2.46                         
REMARK   3   BIN COMPLETENESS (WORKING+TEST) (%) : 70.00                        
REMARK   3   REFLECTIONS IN BIN    (WORKING SET) : 6483                         
REMARK   3   BIN R VALUE           (WORKING SET) : 0.2690                       
REMARK   3   BIN FREE R VALUE                    : 0.2690                       
REMARK   3   BIN FREE R VALUE TEST SET SIZE  (%) : 1.00                         
REMARK   3   BIN FREE R VALUE TEST SET COUNT     : 96                           
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            : 9931                                    
REMARK   3   NUCLEIC ACID ATOMS       : 0                                       
REMARK   3   HETEROGEN ATOMS          : 167                                     
REMARK   3   SOLVENT ATOMS            : 593                                     
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) : 0.25                            
REMARK   3   ESD FROM SIGMAA              (A) : 0.27                            
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) : 0.33                            
REMARK   3   ESD FROM C-V SIGMAA          (A) : 0.38                            
REMARK   3                                                                      
REMARK   3  RMS DEVIATIONS FROM IDEAL VALUES.                                   
REMARK   3   BOND LENGTHS                 (A) : 0.016                           
REMARK   3   BOND ANGLES            (DEGREES) : 1.90                            
REMARK   3   DIHEDRAL ANGLES        (DEGREES) : 24.40                           
REMARK   3   IMPROPER ANGLES        (DEGREES) : 1.05                            
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) : 2.500 ; 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        : 0.35                                                 
REMARK   3   BSOL        : 25.43                                                
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 1JKJ COMPLIES WITH FORMAT V. 3.15, 01-DEC-08                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 18-JUL-01.                  
REMARK 100 THE RCSB ID CODE IS RCSB013878.                                      
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : 18-JAN-99                          
REMARK 200  TEMPERATURE           (KELVIN) : 100                                
REMARK 200  PH                             : 7.4                                
REMARK 200  NUMBER OF CRYSTALS USED        : 1                                  
REMARK 200                                                                      
REMARK 200  SYNCHROTRON              (Y/N) : Y                                  
REMARK 200  RADIATION SOURCE               : CHESS                              
REMARK 200  BEAMLINE                       : A1                                 
REMARK 200  X-RAY GENERATOR MODEL          : NULL                               
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M                                  
REMARK 200  WAVELENGTH OR RANGE        (A) : 0.935                              
REMARK 200  MONOCHROMATOR                  : CYLINDRICALLY-BENT SILICON         
REMARK 200                                   CRYSTAL, CYLINDRICALLY BENT        
REMARK 200                                   RHODIUM-COATED SILICON MIRROR      
REMARK 200  OPTICS                         : NULL                               
REMARK 200                                                                      
REMARK 200  DETECTOR TYPE                  : CCD                                
REMARK 200  DETECTOR MANUFACTURER          : ADSC QUANTUM 4                     
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : DENZO                              
REMARK 200  DATA SCALING SOFTWARE          : SCALEPACK                          
REMARK 200                                                                      
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 68244                              
REMARK 200  RESOLUTION RANGE HIGH      (A) : 2.400                              
REMARK 200  RESOLUTION RANGE LOW       (A) : 20.000                             
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : 0.000                              
REMARK 200                                                                      
REMARK 200 OVERALL.                                                             
REMARK 200  COMPLETENESS FOR RANGE     (%) : 89.4                               
REMARK 200  DATA REDUNDANCY                : 2.300                              
REMARK 200  R MERGE                    (I) : 0.05300                            
REMARK 200  R SYM                      (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR THE DATA SET  : 14.0000                            
REMARK 200                                                                      
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.                                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.40                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 2.44                     
REMARK 200  COMPLETENESS FOR SHELL     (%) : 73.5                               
REMARK 200  DATA REDUNDANCY IN SHELL       : NULL                               
REMARK 200  R MERGE FOR SHELL          (I) : 0.32400                            
REMARK 200  R SYM FOR SHELL            (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR SHELL         : 2.500                              
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: 2SCU                                                 
REMARK 200                                                                      
REMARK 200 REMARK: NULL                                                         
REMARK 280                                                                      
REMARK 280 CRYSTAL                                                              
REMARK 280 SOLVENT CONTENT, VS   (%): 61.23                                     
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 3.17                     
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: POTASSIUM PHOSPHATE, AMMONIUM SULFATE,   
REMARK 280  PH 7.4, MICRODIALYSIS, 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      193.40000            
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      290.10000            
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       96.70000            
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      193.40000            
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       96.70000            
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      290.10000            
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       96.70000            
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       96.70000            
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    HOH A  1798     O    HOH A  1802              2.05            
REMARK 500   OE2  GLU B   128     O    HOH B  1958              2.07            
REMARK 500   OD2  ASP E    68     O    HOH E  1959              2.10            
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: CLOSE CONTACTS                                             
REMARK 500                                                                      
REMARK 500 THE FOLLOWING ATOMS THAT ARE RELATED BY CRYSTALLOGRAPHIC             
REMARK 500 SYMMETRY ARE IN CLOSE CONTACT.  AN ATOM LOCATED WITHIN 0.15          
REMARK 500 ANGSTROMS OF A SYMMETRY RELATED ATOM IS ASSUMED TO BE ON A           
REMARK 500 SPECIAL POSITION AND IS, THEREFORE, LISTED IN REMARK 375             
REMARK 500 INSTEAD OF REMARK 500.  ATOMS WITH NON-BLANK ALTERNATE               
REMARK 500 LOCATION INDICATORS ARE NOT INCLUDED IN THE CALCULATIONS.            
REMARK 500                                                                      
REMARK 500 DISTANCE CUTOFF:                                                     
REMARK 500 2.2 ANGSTROMS FOR CONTACTS NOT INVOLVING HYDROGEN ATOMS              
REMARK 500 1.6 ANGSTROMS FOR CONTACTS INVOLVING HYDROGEN ATOMS                  
REMARK 500                                                                      
REMARK 500  ATM1  RES C  SSEQI   ATM2  RES C  SSEQI  SSYMOP   DISTANCE          
REMARK 500   O    HOH A  1753     O    HOH B  2072     7555     2.16            
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 174   CB    CYS A 174   SG     -0.100                       
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    VAL D 150   CB  -  CA  -  C   ANGL. DEV. = -12.7 DEGREES          
REMARK 500    LEU E 201   N   -  CA  -  C   ANGL. DEV. = -16.7 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      -58.11     64.36                                   
REMARK 500    THR A  96      133.75    -38.81                                   
REMARK 500    PRO A 121     -159.69    -81.09                                   
REMARK 500    SER A 212       24.63   -140.63                                   
REMARK 500    HIS B 279       33.54    -96.74                                   
REMARK 500    VAL B 289       35.86    -75.19                                   
REMARK 500    ALA B 293       56.12    -54.11                                   
REMARK 500    ASN B 353       31.51     77.60                                   
REMARK 500    LEU D   3      -56.59     60.41                                   
REMARK 500    THR D  96      131.11    -37.24                                   
REMARK 500    SER D 212       24.86   -143.90                                   
REMARK 500    MET D 244       75.53   -100.51                                   
REMARK 500    ALA E  88       -9.05    -59.39                                   
REMARK 500    GLU E 128       48.45    -84.18                                   
REMARK 500    HIS E 279       32.17    -96.66                                   
REMARK 500    ALA E 293       56.14    -56.89                                   
REMARK 500    ASN E 353       32.06     78.99                                   
REMARK 500    ALA E 384      -17.26    -47.71                                   
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: PLANAR GROUPS                                              
REMARK 500                                                                      
REMARK 500 PLANAR GROUPS IN THE FOLLOWING RESIDUES HAVE A TOTAL                 
REMARK 500 RMS DISTANCE OF ALL ATOMS FROM THE BEST-FIT PLANE                    
REMARK 500 BY MORE THAN AN EXPECTED VALUE OF 6*RMSD, WITH AN                    
REMARK 500 RMSD 0.02 ANGSTROMS, OR AT LEAST ONE ATOM HAS                        
REMARK 500 AN RMSD GREATER THAN THIS VALUE                                      
REMARK 500 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;               
REMARK 500 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).                             
REMARK 500                                                                      
REMARK 500  M RES CSSEQI        RMS     TYPE                                    
REMARK 500    TYR A 232         0.07    SIDE CHAIN                              
REMARK 500    TYR D 232         0.07    SIDE CHAIN                              
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 525                                                                      
REMARK 525 SOLVENT                                                              
REMARK 525                                                                      
REMARK 525 THE SOLVENT MOLECULES HAVE CHAIN IDENTIFIERS THAT                    
REMARK 525 INDICATE THE POLYMER CHAIN WITH WHICH THEY ARE MOST                  
REMARK 525 CLOSELY ASSOCIATED. THE REMARK LISTS ALL THE SOLVENT                 
REMARK 525 MOLECULES WHICH ARE MORE THAN 5A AWAY FROM THE                       
REMARK 525 NEAREST POLYMER CHAIN (M = MODEL NUMBER;                             
REMARK 525 RES=RESIDUE NAME; C=CHAIN IDENTIFIER; SSEQ=SEQUENCE                  
REMARK 525 NUMBER; I=INSERTION CODE):                                           
REMARK 525                                                                      
REMARK 525  M RES CSSEQI                                                        
REMARK 525    HOH B2014        DISTANCE =  5.74 ANGSTROMS                       
REMARK 525    HOH B2078        DISTANCE =  5.09 ANGSTROMS                       
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 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                                                                      
REMARK 800 SITE_IDENTIFIER: AC2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 B 1400                
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 B 1500                
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC4                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE PO4 D 1601                
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC5                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 E 1401                
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC6                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 E 1501                
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC7                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE COA A 1300                
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC8                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE COA D 1301                
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC9                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE COA B 1903                
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: BC1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE COA E 1904                
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: BC2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE GOL A 1700                
REMARK 900                                                                      
REMARK 900 RELATED ENTRIES                                                      
REMARK 900 RELATED ID: 2SCU   RELATED DB: PDB                                   
REMARK 900 2SCU 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  1JKJ A    1   288  UNP    P07459   SUCD_ECOLI       1    288             
DBREF  1JKJ D    1   288  UNP    P07459   SUCD_ECOLI       1    288             
DBREF  1JKJ B    1   388  UNP    P0A836   SUCC_ECOLI       1    388             
DBREF  1JKJ E    1   388  UNP    P0A836   SUCC_ECOLI       1    388             
SEQRES   1 A  288  SER ILE LEU ILE ASP LYS ASN THR LYS VAL ILE CYS GLN          
SEQRES   2 A  288  GLY PHE THR GLY SER GLN GLY THR PHE HIS SER GLU GLN          
SEQRES   3 A  288  ALA ILE ALA TYR GLY THR LYS MET VAL GLY GLY VAL THR          
SEQRES   4 A  288  PRO GLY LYS GLY GLY THR THR HIS LEU GLY LEU PRO VAL          
SEQRES   5 A  288  PHE ASN THR VAL ARG GLU ALA VAL ALA ALA THR GLY ALA          
SEQRES   6 A  288  THR ALA SER VAL ILE TYR VAL PRO ALA PRO PHE CYS LYS          
SEQRES   7 A  288  ASP SER ILE LEU GLU ALA ILE ASP ALA GLY ILE LYS LEU          
SEQRES   8 A  288  ILE ILE THR ILE THR GLU GLY ILE PRO THR LEU ASP MET          
SEQRES   9 A  288  LEU THR VAL LYS VAL LYS LEU ASP GLU ALA GLY VAL ARG          
SEQRES  10 A  288  MET ILE GLY PRO ASN CYS PRO GLY VAL ILE THR PRO GLY          
SEQRES  11 A  288  GLU CYS LYS ILE GLY ILE GLN PRO GLY HIS ILE HIS LYS          
SEQRES  12 A  288  PRO GLY LYS VAL GLY ILE VAL SER ARG SER GLY THR LEU          
SEQRES  13 A  288  THR TYR GLU ALA VAL LYS GLN THR THR ASP TYR GLY PHE          
SEQRES  14 A  288  GLY GLN SER THR CYS VAL GLY ILE GLY GLY ASP PRO ILE          
SEQRES  15 A  288  PRO GLY SER ASN PHE ILE ASP ILE LEU GLU MET PHE GLU          
SEQRES  16 A  288  LYS ASP PRO GLN THR GLU ALA ILE VAL MET ILE GLY GLU          
SEQRES  17 A  288  ILE GLY GLY SER ALA GLU GLU GLU ALA ALA ALA TYR ILE          
SEQRES  18 A  288  LYS GLU HIS VAL THR LYS PRO VAL VAL GLY TYR ILE ALA          
SEQRES  19 A  288  GLY VAL THR ALA PRO LYS GLY LYS ARG MET GLY 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 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 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 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                  
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      48                                                       
HET    COA  D1301      48                                                       
HET    COA  B1903      27                                                       
HET    COA  E1904       8                                                       
HET    GOL  A1700       6                                                       
HETNAM     PO4 PHOSPHATE ION                                                    
HETNAM     SO4 SULFATE ION                                                      
HETNAM     COA COENZYME A                                                       
HETNAM     GOL GLYCEROL                                                         
HETSYN     GOL GLYCERIN; PROPANE-1,2,3-TRIOL                                    
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  GOL    C3 H8 O3                                                     
FORMUL  16  HOH   *593(H2 O)                                                    
HELIX    1   1 GLY A   17  GLY A   31  1                                  15    
HELIX    2   2 THR A   55  GLY A   64  1                                  10    
HELIX    3   3 PRO A   73  PRO A   75  5                                   3    
HELIX    4   4 PHE A   76  ALA A   87  1                                  12    
HELIX    5   5 PRO A  100  GLY A  115  1                                  16    
HELIX    6   6 SER A  153  TYR A  167  1                                  15    
HELIX    7   7 ASN A  186  LYS A  196  1                                  11    
HELIX    8   8 SER A  212  VAL A  225  1                                  14    
HELIX    9   9 THR A  257  ALA A  268  1                                  12    
HELIX   10  10 SER A  275  ALA A  277  5                                   3    
HELIX   11  11 ASP A  278  LEU A  287  1                                  10    
HELIX   12  12 HIS B    4  TYR B   15  1                                  12    
HELIX   13  13 THR B   27  GLY B   39  1                                  13    
HELIX   14  14 SER B   65  LEU B   77  1                                  13    
HELIX   15  15 GLU B  132  THR B  140  1                                   9    
HELIX   16  16 MET B  156  LEU B  167  1                                  12    
HELIX   17  17 GLY B  171  ARG B  191  1                                  21    
HELIX   18  18 GLY B  220  ARG B  225  5                                   6    
HELIX   19  19 GLN B  226  MET B  232  1                                   7    
HELIX   20  20 ARG B  233  ARG B  233  5                                   1    
HELIX   21  21 ASP B  234  GLU B  238  5                                   5    
HELIX   22  22 ASP B  239  TRP B  248  1                                  10    
HELIX   23  23 GLY B  265  HIS B  279  1                                  15    
HELIX   24  24 THR B  294  SER B  307  1                                  14    
HELIX   25  25 ARG B  324  VAL B  339  1                                  16    
HELIX   26  26 ASN B  353  ASP B  363  1                                  11    
HELIX   27  27 GLY B  373  ALA B  384  1                                  12    
HELIX   28  28 GLY D   17  GLY D   31  1                                  15    
HELIX   29  29 THR D   55  GLY D   64  1                                  10    
HELIX   30  30 PRO D   73  PRO D   75  5                                   3    
HELIX   31  31 PHE D   76  ALA D   87  1                                  12    
HELIX   32  32 PRO D  100  GLY D  115  1                                  16    
HELIX   33  33 SER D  153  TYR D  167  1                                  15    
HELIX   34  34 ASN D  186  LYS D  196  1                                  11    
HELIX   35  35 SER D  212  VAL D  225  1                                  14    
HELIX   36  36 THR D  257  ALA D  268  1                                  12    
HELIX   37  37 SER D  275  ALA D  277  5                                   3    
HELIX   38  38 ASP D  278  LEU D  287  1                                  10    
HELIX   39  39 HIS E    4  TYR E   15  1                                  12    
HELIX   40  40 THR E   27  GLY E   39  1                                  13    
HELIX   41  41 SER E   65  LEU E   77  1                                  13    
HELIX   42  42 GLU E  132  THR E  140  1                                   9    
HELIX   43  43 PRO E  141  ILE E  144  5                                   4    
HELIX   44  44 MET E  156  LEU E  167  1                                  12    
HELIX   45  45 GLY E  171  ARG E  191  1                                  21    
HELIX   46  46 GLY E  220  ARG E  225  5                                   6    
HELIX   47  47 GLN E  226  ARG E  233  1                                   8    
HELIX   48  48 ASP E  234  GLU E  238  5                                   5    
HELIX   49  49 ASP E  239  TRP E  248  1                                  10    
HELIX   50  50 GLY E  265  HIS E  279  1                                  15    
HELIX   51  51 THR E  294  SER E  307  1                                  14    
HELIX   52  52 ARG E  324  VAL E  339  1                                  16    
HELIX   53  53 ASN E  353  ASP E  363  1                                  11    
HELIX   54  54 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  O  LEU A  50   N  HIS A  47           
SHEET    3   A 7 LYS A  33  VAL A  38  1  O  GLY A  37   N  PHE A  53           
SHEET    4   A 7 LYS A   9  GLN A  13  1  O  VAL A  10   N  VAL A  35           
SHEET    5   A 7 ALA A  67  ILE A  70  1  O  ALA A  67   N  ILE A  11           
SHEET    6   A 7 LEU A  91  THR A  94  1  O  LEU A  91   N  SER A  68           
SHEET    7   A 7 ARG A 117  ILE A 119  1  O  ARG A 117   N  ILE A  92           
SHEET    1   B 7 CYS A 132  GLY A 135  0                                        
SHEET    2   B 7 GLY A 125  THR A 128 -1  O  VAL A 126   N  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  O  VAL B  44   N  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  O  GLN B  91   N  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  GLU 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 4 ILE B 259  VAL B 263  0                                        
SHEET    2   H 4 ALA B 313  PHE B 319  1  O  ALA B 313   N  GLY B 260           
SHEET    3   H 4 VAL B 345  GLU B 350  1  O  VAL B 346   N  VAL B 316           
SHEET    4   H 4 ILE B 368  ALA B 370  1  O  ILE B 369   N  VAL B 347           
SHEET    1   I 7 THR D  46  HIS D  47  0                                        
SHEET    2   I 7 LEU D  50  PHE D  53 -1  O  LEU D  50   N  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  GLY D 135  0                                        
SHEET    2   J 7 GLY D 125  THR D 128 -1  O  VAL D 126   N  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  N  LYS D 271   O  VAL D 229           
SHEET    1   K 4 GLY E  22  CYS E  25  0                                        
SHEET    2   K 4 ILE E  96  ALA E 100 -1  N  ILE E  96   O  CYS E  25           
SHEET    3   K 4 TRP E  43  CYS E  47 -1  O  VAL E  44   N  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  O  GLN E  91   N  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  N  LYS E 215   O  GLU 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 4 ILE E 259  VAL E 263  0                                        
SHEET    2   P 4 ALA E 313  PHE E 319  1  O  ALA E 313   N  GLY E 260           
SHEET    3   P 4 VAL E 345  GLU E 350  1  O  VAL E 346   N  VAL E 316           
SHEET    4   P 4 ILE E 368  ALA E 370  1  O  ILE E 369   N  VAL E 347           
LINK         SG  CYS B 325                 S1P COA B1903     1555   1555  2.04  
LINK         SG  CYS E 325                 S1P COA E1904     1555   1555  2.05  
CISPEP   1 GLY A  120    PRO A  121          0         0.27                     
CISPEP   2 GLY B   41    PRO B   42          0        -0.32                     
CISPEP   3 ASN B  199    PRO B  200          0         0.87                     
CISPEP   4 GLY D  120    PRO D  121          0         0.38                     
CISPEP   5 GLY E   41    PRO E   42          0        -0.66                     
CISPEP   6 ASN E  199    PRO E  200          0         0.42                     
SITE     1 AC1  8 SER A 153  GLY A 154  THR A 155  HIS A 246                    
SITE     2 AC1  8 HOH A1733  GLY B 265  ALA B 266  GLY B 267                    
SITE     1 AC2  6 GLY B  52  GLY B  53  ARG B  54  GLY B  55                    
SITE     2 AC2  6 ASP B 213  HOH B2019                                          
SITE     1 AC3  5 ARG A 243  MET B   1  GLY B 220  ARG B 233                    
SITE     2 AC3  5 HOH B1930                                                     
SITE     1 AC4  8 SER D 153  GLY D 154  THR D 155  HIS D 246                    
SITE     2 AC4  8 HOH D1644  GLY E 265  ALA E 266  GLY E 267                    
SITE     1 AC5  6 GLY E  52  GLY E  53  ARG E  54  GLY E  55                    
SITE     2 AC5  6 ASP E 213  HOH E1931                                          
SITE     1 AC6  5 ARG D 243  MET E   1  GLY E 220  ARG E 233                    
SITE     2 AC6  5 HOH E2006                                                     
SITE     1 AC7 31 GLY A  14  THR A  16  GLY A  17  SER A  18                    
SITE     2 AC7 31 GLN A  19  VAL A  38  PRO A  40  LYS A  42                    
SITE     3 AC7 31 TYR A  71  VAL A  72  PRO A  73  SER A  80                    
SITE     4 AC7 31 ILE A  95  THR A  96  GLU A  97  ASN A 122                    
SITE     5 AC7 31 CYS A 123  PRO A 124  ILE A 136  HOH A1703                    
SITE     6 AC7 31 HOH A1705  HOH A1706  HOH A1710  HOH A1764                    
SITE     7 AC7 31 HOH A1770  HOH A1784  HOH A1788  GLU E  33                    
SITE     8 AC7 31 SER E  36  LYS E  66  HOH E1907                               
SITE     1 AC8 34 ARG B  29  GLU B  33  SER B  36  LYS B  66                    
SITE     2 AC8 34 HOH B1921  GLY D  14  THR D  16  GLY D  17                    
SITE     3 AC8 34 SER D  18  GLN D  19  VAL D  38  PRO D  40                    
SITE     4 AC8 34 LYS D  42  TYR D  71  VAL D  72  PRO D  73                    
SITE     5 AC8 34 SER D  80  ILE D  95  THR D  96  GLU D  97                    
SITE     6 AC8 34 ASN D 122  CYS D 123  PRO D 124  ILE D 136                    
SITE     7 AC8 34 HOH D1604  HOH D1606  HOH D1611  HOH D1612                    
SITE     8 AC8 34 HOH D1629  HOH D1645  HOH D1661  HOH D1672                    
SITE     9 AC8 34 HOH D1673  HOH D1692                                          
SITE     1 AC9  8 PHE A  22  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  6 GLY E 320  GLY E 321  VAL E 323  CYS E 325                    
SITE     2 BC1  6 GLU E 350  ASN E 352                                          
SITE     1 BC2  6 VAL A 225  THR A 226  LYS A 227  VAL A 229                    
SITE     2 BC2  6 ALA A 268  GLY A 269                                          
CRYST1   96.630   96.630  386.800  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      0.010349  0.000000  0.000000        0.00000                         
SCALE2      0.000000  0.010349  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.002585        0.00000                         
(ATOM LINES ARE NOT SHOWN.)
END                                                                             
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