GenomeNet

Database: PDB
Entry: 5CAE
LinkDB: 5CAE
Original site: 5CAE 
HEADER    LIGASE                                  29-JUN-15   5CAE              
TITLE     SUCCINATE BOUND TO PIG GTP-SPECIFIC SUCCINYL-COA SYNTHETASE           
COMPND    MOL_ID: 1;                                                            
COMPND   2 MOLECULE: SUCCINYL-COA LIGASE [ADP/GDP-FORMING] SUBUNIT ALPHA,       
COMPND   3 MITOCHONDRIAL;                                                       
COMPND   4 CHAIN: A;                                                            
COMPND   5 FRAGMENT: UNP RESIDUES 42-346;                                       
COMPND   6 SYNONYM: SUCCINYL-COA SYNTHETASE SUBUNIT ALPHA,SCS-ALPHA;            
COMPND   7 EC: 6.2.1.4,6.2.1.5;                                                 
COMPND   8 ENGINEERED: YES;                                                     
COMPND   9 MOL_ID: 2;                                                           
COMPND  10 MOLECULE: SUCCINYL-COA LIGASE [GDP-FORMING] SUBUNIT BETA,            
COMPND  11 MITOCHONDRIAL;                                                       
COMPND  12 CHAIN: B;                                                            
COMPND  13 FRAGMENT: UNP RESIDUES 40-433;                                       
COMPND  14 SYNONYM: GTP-SPECIFIC SUCCINYL-COA SYNTHETASE SUBUNIT BETA,SUCCINYL- 
COMPND  15 COA SYNTHETASE BETA-G CHAIN,SCS-BETAG;                               
COMPND  16 EC: 6.2.1.4;                                                         
COMPND  17 ENGINEERED: YES                                                      
SOURCE    MOL_ID: 1;                                                            
SOURCE   2 ORGANISM_SCIENTIFIC: SUS SCROFA;                                     
SOURCE   3 ORGANISM_COMMON: PIG;                                                
SOURCE   4 ORGANISM_TAXID: 9823;                                                
SOURCE   5 GENE: SUCLG1;                                                        
SOURCE   6 EXPRESSION_SYSTEM: ESCHERICHIA COLI;                                 
SOURCE   7 EXPRESSION_SYSTEM_TAXID: 469008;                                     
SOURCE   8 EXPRESSION_SYSTEM_STRAIN: BL21(DE3);                                 
SOURCE   9 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;                              
SOURCE  10 EXPRESSION_SYSTEM_PLASMID: PT7-7;                                    
SOURCE  11 MOL_ID: 2;                                                           
SOURCE  12 ORGANISM_SCIENTIFIC: SUS SCROFA;                                     
SOURCE  13 ORGANISM_COMMON: PIG;                                                
SOURCE  14 ORGANISM_TAXID: 9823;                                                
SOURCE  15 GENE: SUCLG2;                                                        
SOURCE  16 EXPRESSION_SYSTEM: ESCHERICHIA COLI;                                 
SOURCE  17 EXPRESSION_SYSTEM_TAXID: 469008;                                     
SOURCE  18 EXPRESSION_SYSTEM_STRAIN: BL21(DE3);                                 
SOURCE  19 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;                              
SOURCE  20 EXPRESSION_SYSTEM_PLASMID: PT7-7                                     
KEYWDS    LIGASE                                                                
EXPDTA    X-RAY DIFFRACTION                                                     
AUTHOR    J.HUANG,M.E.FRASER                                                    
REVDAT   5   01-NOV-17 5CAE    1       REMARK                                   
REVDAT   4   06-SEP-17 5CAE    1       REMARK                                   
REVDAT   3   17-AUG-16 5CAE    1       JRNL                                     
REVDAT   2   10-AUG-16 5CAE    1       JRNL                                     
REVDAT   1   29-JUN-16 5CAE    0                                                
JRNL        AUTH   J.HUANG,M.E.FRASER                                           
JRNL        TITL   STRUCTURAL BASIS FOR THE BINDING OF SUCCINATE TO             
JRNL        TITL 2 SUCCINYL-COA SYNTHETASE.                                     
JRNL        REF    ACTA CRYSTALLOGR D STRUCT     V.  72   912 2016              
JRNL        REF  2 BIOL                                                         
JRNL        REFN                   ISSN 2059-7983                               
JRNL        PMID   27487822                                                     
JRNL        DOI    10.1107/S2059798316010044                                    
REMARK   2                                                                      
REMARK   2 RESOLUTION.    2.20 ANGSTROMS.                                       
REMARK   3                                                                      
REMARK   3 REFINEMENT.                                                          
REMARK   3   PROGRAM     : PHENIX 1.9_1692                                      
REMARK   3   AUTHORS     : PAUL ADAMS,PAVEL AFONINE,VINCENT CHEN,IAN            
REMARK   3               : DAVIS,KRESHNA GOPAL,RALF GROSSE-KUNSTLEVE,           
REMARK   3               : LI-WEI HUNG,ROBERT IMMORMINO,TOM IOERGER,            
REMARK   3               : AIRLIE MCCOY,ERIK MCKEE,NIGEL MORIARTY,              
REMARK   3               : REETAL PAI,RANDY READ,JANE RICHARDSON,               
REMARK   3               : DAVID RICHARDSON,TOD ROMO,JIM SACCHETTINI,           
REMARK   3               : NICHOLAS SAUTER,JACOB SMITH,LAURENT                  
REMARK   3               : STORONI,TOM TERWILLIGER,PETER ZWART                  
REMARK   3                                                                      
REMARK   3    REFINEMENT TARGET : ML                                            
REMARK   3                                                                      
REMARK   3  DATA USED IN REFINEMENT.                                            
REMARK   3   RESOLUTION RANGE HIGH (ANGSTROMS) : 2.20                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 49.07                          
REMARK   3   MIN(FOBS/SIGMA_FOBS)              : 1.340                          
REMARK   3   COMPLETENESS FOR RANGE        (%) : 97.0                           
REMARK   3   NUMBER OF REFLECTIONS             : 33535                          
REMARK   3                                                                      
REMARK   3  FIT TO DATA USED IN REFINEMENT.                                     
REMARK   3   R VALUE     (WORKING + TEST SET) : 0.170                           
REMARK   3   R VALUE            (WORKING SET) : 0.165                           
REMARK   3   FREE R VALUE                     : 0.214                           
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 9.920                           
REMARK   3   FREE R VALUE TEST SET COUNT      : 3327                            
REMARK   3                                                                      
REMARK   3  FIT TO DATA USED IN REFINEMENT (IN BINS).                           
REMARK   3   BIN  RESOLUTION RANGE  COMPL.    NWORK NFREE   RWORK  RFREE        
REMARK   3     1 49.0848 -  6.3415    0.98     1322   131  0.1564 0.2084        
REMARK   3     2  6.3415 -  5.0351    0.98     1289   147  0.1852 0.1988        
REMARK   3     3  5.0351 -  4.3991    0.98     1294   138  0.1494 0.1856        
REMARK   3     4  4.3991 -  3.9971    0.98     1255   160  0.1380 0.1846        
REMARK   3     5  3.9971 -  3.7107    0.98     1278   123  0.1513 0.1905        
REMARK   3     6  3.7107 -  3.4920    0.98     1293   131  0.1517 0.2083        
REMARK   3     7  3.4920 -  3.3171    0.98     1259   151  0.1468 0.1839        
REMARK   3     8  3.3171 -  3.1728    0.98     1232   149  0.1532 0.1974        
REMARK   3     9  3.1728 -  3.0506    0.98     1293   145  0.1646 0.2343        
REMARK   3    10  3.0506 -  2.9454    0.97     1250   143  0.1561 0.2015        
REMARK   3    11  2.9454 -  2.8533    0.98     1275   131  0.1614 0.1943        
REMARK   3    12  2.8533 -  2.7717    0.98     1236   144  0.1647 0.2225        
REMARK   3    13  2.7717 -  2.6988    0.98     1269   128  0.1675 0.2220        
REMARK   3    14  2.6988 -  2.6329    0.97     1282   144  0.1639 0.2491        
REMARK   3    15  2.6329 -  2.5731    0.97     1236   152  0.1722 0.2388        
REMARK   3    16  2.5731 -  2.5183    0.97     1233   134  0.1769 0.2621        
REMARK   3    17  2.5183 -  2.4680    0.97     1258   148  0.1870 0.2507        
REMARK   3    18  2.4680 -  2.4214    0.97     1226   138  0.1804 0.2441        
REMARK   3    19  2.4214 -  2.3781    0.97     1290   141  0.1918 0.2311        
REMARK   3    20  2.3781 -  2.3378    0.96     1204   141  0.2025 0.2737        
REMARK   3    21  2.3378 -  2.3001    0.96     1257   134  0.1974 0.2629        
REMARK   3    22  2.3001 -  2.2647    0.95     1212   129  0.2135 0.2564        
REMARK   3    23  2.2647 -  2.2314    0.95     1254   132  0.2252 0.3146        
REMARK   3    24  2.2314 -  2.2000    0.93     1211   113  0.2132 0.2466        
REMARK   3                                                                      
REMARK   3  BULK SOLVENT MODELLING.                                             
REMARK   3   METHOD USED        : FLAT BULK SOLVENT MODEL                       
REMARK   3   SOLVENT RADIUS     : 1.11                                          
REMARK   3   SHRINKAGE RADIUS   : 0.90                                          
REMARK   3   K_SOL              : NULL                                          
REMARK   3   B_SOL              : NULL                                          
REMARK   3                                                                      
REMARK   3  ERROR ESTIMATES.                                                    
REMARK   3   COORDINATE ERROR (MAXIMUM-LIKELIHOOD BASED)     : 0.220            
REMARK   3   PHASE ERROR (DEGREES, MAXIMUM-LIKELIHOOD BASED) : 20.750           
REMARK   3                                                                      
REMARK   3  B VALUES.                                                           
REMARK   3   FROM WILSON PLOT           (A**2) : 26.81                          
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : 30.72                          
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  TWINNING INFORMATION.                                               
REMARK   3   FRACTION: NULL                                                     
REMARK   3   OPERATOR: NULL                                                     
REMARK   3                                                                      
REMARK   3  DEVIATIONS FROM IDEAL VALUES.                                       
REMARK   3                 RMSD          COUNT                                  
REMARK   3   BOND      :  0.003           5358                                  
REMARK   3   ANGLE     :  0.542           7241                                  
REMARK   3   CHIRALITY :  0.044            827                                  
REMARK   3   PLANARITY :  0.003            961                                  
REMARK   3   DIHEDRAL  : 10.813           3254                                  
REMARK   3                                                                      
REMARK   3  TLS DETAILS                                                         
REMARK   3   NUMBER OF TLS GROUPS  : NULL                                       
REMARK   3                                                                      
REMARK   3  NCS DETAILS                                                         
REMARK   3   NUMBER OF NCS GROUPS : NULL                                        
REMARK   3                                                                      
REMARK   3  OTHER REFINEMENT REMARKS: NULL                                      
REMARK   4                                                                      
REMARK   4 5CAE COMPLIES WITH FORMAT V. 3.30, 13-JUL-11                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 13-JUL-15.                  
REMARK 100 THE DEPOSITION ID IS D_1000211223.                                   
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : 20-SEP-14                          
REMARK 200  TEMPERATURE           (KELVIN) : 100                                
REMARK 200  PH                             : 7.0                                
REMARK 200  NUMBER OF CRYSTALS USED        : NULL                               
REMARK 200                                                                      
REMARK 200  SYNCHROTRON              (Y/N) : Y                                  
REMARK 200  RADIATION SOURCE               : CLSI                               
REMARK 200  BEAMLINE                       : 08B1-1                             
REMARK 200  X-RAY GENERATOR MODEL          : NULL                               
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M                                  
REMARK 200  WAVELENGTH OR RANGE        (A) : 0.97947                            
REMARK 200  MONOCHROMATOR                  : KOHZU DOUBLE CRYSTAL               
REMARK 200                                   MONOCHROMATOR (DCM)                
REMARK 200  OPTICS                         : NULL                               
REMARK 200                                                                      
REMARK 200  DETECTOR TYPE                  : CCD                                
REMARK 200  DETECTOR MANUFACTURER          : RAYONIX MX300HE                    
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : IMOSFLM                            
REMARK 200  DATA SCALING SOFTWARE          : SCALA 3.3.21                       
REMARK 200                                                                      
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 33544                              
REMARK 200  RESOLUTION RANGE HIGH      (A) : 2.200                              
REMARK 200  RESOLUTION RANGE LOW       (A) : 49.073                             
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : NULL                               
REMARK 200                                                                      
REMARK 200 OVERALL.                                                             
REMARK 200  COMPLETENESS FOR RANGE     (%) : 97.0                               
REMARK 200  DATA REDUNDANCY                : 3.600                              
REMARK 200  R MERGE                    (I) : NULL                               
REMARK 200  R SYM                      (I) : 0.09600                            
REMARK 200  <I/SIGMA(I)> FOR THE DATA SET  : 9.3000                             
REMARK 200                                                                      
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.                                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.20                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 2.32                     
REMARK 200  COMPLETENESS FOR SHELL     (%) : 94.6                               
REMARK 200  DATA REDUNDANCY IN SHELL       : 3.50                               
REMARK 200  R MERGE FOR SHELL          (I) : 0.46600                            
REMARK 200  R SYM FOR SHELL            (I) : 0.46600                            
REMARK 200  <I/SIGMA(I)> FOR SHELL         : 1.600                              
REMARK 200                                                                      
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH                              
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT        
REMARK 200 SOFTWARE USED: PHENIX 1.9_1692                                       
REMARK 200 STARTING MODEL: PDB ENTRY 4XX0                                       
REMARK 200                                                                      
REMARK 200 REMARK: NULL                                                         
REMARK 280                                                                      
REMARK 280 CRYSTAL                                                              
REMARK 280 SOLVENT CONTENT, VS   (%): 46.99                                     
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.32                     
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: PEG 3350, AMMONIUM SUCCINATE,            
REMARK 280  MAGNESIUM CHLORIDE, COA, HEPES, PH 7.0, VAPOR DIFFUSION, HANGING    
REMARK 280  DROP, TEMPERATURE 294K                                              
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY                                            
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 1 21 1                         
REMARK 290                                                                      
REMARK 290      SYMOP   SYMMETRY                                                
REMARK 290     NNNMMM   OPERATOR                                                
REMARK 290       1555   X,Y,Z                                                   
REMARK 290       2555   -X,Y+1/2,-Z                                             
REMARK 290                                                                      
REMARK 290     WHERE NNN -> OPERATOR NUMBER                                     
REMARK 290           MMM -> TRANSLATION VECTOR                                  
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY TRANSFORMATIONS                            
REMARK 290 THE FOLLOWING TRANSFORMATIONS OPERATE ON THE ATOM/HETATM             
REMARK 290 RECORDS IN THIS ENTRY TO PRODUCE CRYSTALLOGRAPHICALLY                
REMARK 290 RELATED MOLECULES.                                                   
REMARK 290   SMTRY1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 290   SMTRY1   2 -1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   2  0.000000  1.000000  0.000000       40.51000            
REMARK 290   SMTRY3   2  0.000000  0.000000 -1.000000        0.00000            
REMARK 290                                                                      
REMARK 290 REMARK: NULL                                                         
REMARK 300                                                                      
REMARK 300 BIOMOLECULE: 1                                                       
REMARK 300 SEE REMARK 350 FOR THE AUTHOR PROVIDED AND/OR PROGRAM                
REMARK 300 GENERATED ASSEMBLY INFORMATION FOR THE STRUCTURE IN                  
REMARK 300 THIS ENTRY. THE REMARK MAY ALSO PROVIDE INFORMATION ON               
REMARK 300 BURIED SURFACE AREA.                                                 
REMARK 300 REMARK: SDS-PAGE/GEL FILTRATION (G100 SEPHADEX) CONFIRMS THE         
REMARK 300 HETERODIMER.                                                         
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: DIMERIC                           
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: DIMERIC                    
REMARK 350 SOFTWARE USED: PISA                                                  
REMARK 350 TOTAL BURIED SURFACE AREA: 7130 ANGSTROM**2                          
REMARK 350 SURFACE AREA OF THE COMPLEX: 26920 ANGSTROM**2                       
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -46.0 KCAL/MOL                        
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, B                                  
REMARK 350   BIOMT1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 350   BIOMT2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 350   BIOMT3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 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     MET A   305                                                      
REMARK 465     LEU A   306                                                      
REMARK 465     LEU A   307                                                      
REMARK 465     VAL A   308                                                      
REMARK 465     HIS A   309                                                      
REMARK 465     HIS A   310                                                      
REMARK 465     HIS A   311                                                      
REMARK 465     HIS A   312                                                      
REMARK 465     HIS A   313                                                      
REMARK 465     HIS A   314                                                      
REMARK 465     LYS B   394                                                      
REMARK 465     LYS B   395                                                      
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   554     O    HOH A   623              2.15            
REMARK 500   O    HOH A   610     O    HOH A   625              2.18            
REMARK 500   O    HOH B   597     O    HOH B   619              2.18            
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    TYR A  79       57.36   -116.77                                   
REMARK 500    GLU A 140      -49.10   -132.07                                   
REMARK 500    ASP A 195     -169.72   -108.40                                   
REMARK 500    SER A 235     -130.97    -88.57                                   
REMARK 500    LYS A 238       57.07   -106.99                                   
REMARK 500    LEU B 346      -18.54   -144.47                                   
REMARK 500    GLU B 347       87.76     60.46                                   
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 620                                                                      
REMARK 620 METAL COORDINATION                                                   
REMARK 620 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;               
REMARK 620 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE):                             
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              MG B 401  MG                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 PO4 A 404   O4                                                     
REMARK 620 2 HOH A 547   O    97.1                                              
REMARK 620 3 HOH A 564   O    95.9  88.9                                        
REMARK 620 4 SIN B 402   O4   90.8 171.3  93.7                                  
REMARK 620 5 HOH B 528   O    96.1  91.2 167.8  84.5                            
REMARK 620 6 HOH A 505   O   176.1  85.7  86.9  86.2  81.0                      
REMARK 620 N                    1     2     3     4     5                       
REMARK 800                                                                      
REMARK 800 SITE                                                                 
REMARK 800 SITE_IDENTIFIER: AC1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue COA A 401                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue CL A 402                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue GOL A 403                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC4                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue PO4 A 404                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC5                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue MG B 401                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC6                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue SIN B 402                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC7                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue GOL B 403                 
REMARK 900                                                                      
REMARK 900 RELATED ENTRIES                                                      
REMARK 900 RELATED ID: 4XX0   RELATED DB: PDB                                   
REMARK 900 RELATED ID: 2FP4   RELATED DB: PDB                                   
REMARK 900 RELATED ID: 2FPI   RELATED DB: PDB                                   
REMARK 900 RELATED ID: 2FPG   RELATED DB: PDB                                   
REMARK 900 RELATED ID: 2FPP   RELATED DB: PDB                                   
REMARK 900 RELATED ID: 1EUC   RELATED DB: PDB                                   
REMARK 900 RELATED ID: 1EUD   RELATED DB: PDB                                   
DBREF  5CAE A    2   306  UNP    O19069   SUCA_PIG        42    346             
DBREF  5CAE B    2   395  UNP    P53590   SUCB2_PIG       40    433             
SEQADV 5CAE LEU A  307  UNP  O19069              EXPRESSION TAG                 
SEQADV 5CAE VAL A  308  UNP  O19069              EXPRESSION TAG                 
SEQADV 5CAE HIS A  309  UNP  O19069              EXPRESSION TAG                 
SEQADV 5CAE HIS A  310  UNP  O19069              EXPRESSION TAG                 
SEQADV 5CAE HIS A  311  UNP  O19069              EXPRESSION TAG                 
SEQADV 5CAE HIS A  312  UNP  O19069              EXPRESSION TAG                 
SEQADV 5CAE HIS A  313  UNP  O19069              EXPRESSION TAG                 
SEQADV 5CAE HIS A  314  UNP  O19069              EXPRESSION TAG                 
SEQADV 5CAE MET B    1  UNP  P53590              INITIATING METHIONINE          
SEQRES   1 A  313  SER TYR THR ALA SER ARG LYS HIS LEU TYR VAL ASP LYS          
SEQRES   2 A  313  ASN THR LYS VAL ILE CYS GLN GLY PHE THR GLY LYS GLN          
SEQRES   3 A  313  GLY THR PHE HIS SER GLN GLN ALA LEU GLU TYR GLY THR          
SEQRES   4 A  313  ASN LEU VAL GLY GLY THR THR PRO GLY LYS GLY GLY LYS          
SEQRES   5 A  313  THR HIS LEU GLY LEU PRO VAL PHE ASN THR VAL LYS GLU          
SEQRES   6 A  313  ALA LYS GLU GLN THR GLY ALA THR ALA SER VAL ILE TYR          
SEQRES   7 A  313  VAL PRO PRO PRO PHE ALA ALA ALA ALA ILE ASN GLU ALA          
SEQRES   8 A  313  ILE ASP ALA GLU VAL PRO LEU VAL VAL CYS ILE THR GLU          
SEQRES   9 A  313  GLY ILE PRO GLN GLN ASP MET VAL ARG VAL LYS HIS ARG          
SEQRES  10 A  313  LEU LEU ARG GLN GLY LYS THR ARG LEU ILE GLY PRO ASN          
SEQRES  11 A  313  CYS PRO GLY VAL ILE ASN PRO GLY GLU CYS LYS ILE GLY          
SEQRES  12 A  313  ILE MET PRO GLY HIS ILE HIS LYS LYS GLY ARG ILE GLY          
SEQRES  13 A  313  ILE VAL SER ARG SER GLY THR LEU THR TYR GLU ALA VAL          
SEQRES  14 A  313  HIS GLN THR THR GLN VAL GLY LEU GLY GLN SER LEU CYS          
SEQRES  15 A  313  VAL GLY ILE GLY GLY ASP PRO PHE ASN GLY THR ASP PHE          
SEQRES  16 A  313  THR ASP CYS LEU GLU ILE PHE LEU ASN ASP PRO ALA THR          
SEQRES  17 A  313  GLU GLY ILE ILE LEU ILE GLY GLU ILE GLY GLY ASN ALA          
SEQRES  18 A  313  GLU GLU ASN ALA ALA GLU PHE LEU LYS GLN HIS ASN SER          
SEQRES  19 A  313  GLY PRO LYS SER LYS PRO VAL VAL SER PHE ILE ALA GLY          
SEQRES  20 A  313  LEU THR ALA PRO PRO GLY ARG ARG MET GLY HIS ALA GLY          
SEQRES  21 A  313  ALA ILE ILE ALA GLY GLY LYS GLY GLY ALA LYS GLU LYS          
SEQRES  22 A  313  ILE THR ALA LEU GLN SER ALA GLY VAL VAL VAL SER MET          
SEQRES  23 A  313  SER PRO ALA GLN LEU GLY THR THR ILE TYR LYS GLU PHE          
SEQRES  24 A  313  GLU LYS ARG LYS MET LEU LEU VAL HIS HIS HIS HIS HIS          
SEQRES  25 A  313  HIS                                                          
SEQRES   1 B  395  MET ASN LEU GLN GLU TYR GLN SER LYS LYS LEU MET SER          
SEQRES   2 B  395  ASP ASN GLY VAL LYS VAL GLN ARG PHE PHE VAL ALA ASP          
SEQRES   3 B  395  THR ALA ASN GLU ALA LEU GLU ALA ALA LYS ARG LEU ASN          
SEQRES   4 B  395  ALA LYS GLU ILE VAL LEU LYS ALA GLN ILE LEU ALA GLY          
SEQRES   5 B  395  GLY ARG GLY LYS GLY VAL PHE SER SER GLY LEU LYS GLY          
SEQRES   6 B  395  GLY VAL HIS LEU THR LYS ASP PRO GLU VAL VAL GLY GLN          
SEQRES   7 B  395  LEU ALA LYS GLN MET ILE GLY TYR ASN LEU ALA THR LYS          
SEQRES   8 B  395  GLN THR PRO LYS GLU GLY VAL LYS VAL ASN LYS VAL MET          
SEQRES   9 B  395  VAL ALA GLU ALA LEU ASP ILE SER ARG GLU THR TYR LEU          
SEQRES  10 B  395  ALA ILE LEU MET ASP ARG SER CSS ASN GLY PRO VAL LEU          
SEQRES  11 B  395  VAL GLY SER PRO GLN GLY GLY VAL ASP ILE GLU GLU VAL          
SEQRES  12 B  395  ALA ALA SER ASN PRO GLU LEU ILE PHE LYS GLU GLN ILE          
SEQRES  13 B  395  ASP ILE ILE GLU GLY ILE LYS ASP SER GLN ALA GLN ARG          
SEQRES  14 B  395  MET ALA GLU ASN LEU GLY PHE LEU GLY PRO LEU GLN ASN          
SEQRES  15 B  395  GLN ALA ALA ASP GLN ILE LYS LYS LEU TYR ASN LEU PHE          
SEQRES  16 B  395  LEU LYS ILE ASP ALA THR GLN VAL GLU VAL ASN PRO PHE          
SEQRES  17 B  395  GLY GLU THR PRO GLU GLY GLN VAL VAL CYS PHE ASP ALA          
SEQRES  18 B  395  LYS ILE ASN PHE ASP ASP ASN ALA GLU PHE ARG GLN LYS          
SEQRES  19 B  395  ASP ILE PHE ALA MET ASP ASP LYS SER GLU ASN GLU PRO          
SEQRES  20 B  395  ILE GLU ASN GLU ALA ALA LYS TYR ASP LEU LYS TYR ILE          
SEQRES  21 B  395  GLY LEU ASP GLY ASN ILE ALA CYS PHE VAL ASN GLY ALA          
SEQRES  22 B  395  GLY LEU ALA MET ALA THR CYS ASP ILE ILE PHE LEU ASN          
SEQRES  23 B  395  GLY GLY LYS PRO ALA ASN PHE LEU ASP LEU GLY GLY GLY          
SEQRES  24 B  395  VAL LYS GLU SER GLN VAL TYR GLN ALA PHE LYS LEU LEU          
SEQRES  25 B  395  THR ALA ASP PRO LYS VAL GLU ALA ILE LEU VAL ASN ILE          
SEQRES  26 B  395  PHE GLY GLY ILE VAL ASN CYS ALA ILE ILE ALA ASN GLY          
SEQRES  27 B  395  ILE THR LYS ALA CYS ARG GLU LEU GLU LEU LYS VAL PRO          
SEQRES  28 B  395  LEU VAL VAL ARG LEU GLU GLY THR ASN VAL HIS GLU ALA          
SEQRES  29 B  395  GLN ASN ILE LEU THR ASN SER GLY LEU PRO ILE THR SER          
SEQRES  30 B  395  ALA VAL ASP LEU GLU ASP ALA ALA LYS LYS ALA VAL ALA          
SEQRES  31 B  395  SER VAL THR LYS LYS                                          
MODRES 5CAE CSS B  125  CYS  MODIFIED RESIDUE                                   
HET    CSS  B 125       7                                                       
HET    COA  A 401      48                                                       
HET     CL  A 402       1                                                       
HET    GOL  A 403       6                                                       
HET    PO4  A 404       5                                                       
HET     MG  B 401       1                                                       
HET    SIN  B 402       8                                                       
HET    GOL  B 403       6                                                       
HETNAM     CSS S-MERCAPTOCYSTEINE                                               
HETNAM     COA COENZYME A                                                       
HETNAM      CL CHLORIDE ION                                                     
HETNAM     GOL GLYCEROL                                                         
HETNAM     PO4 PHOSPHATE ION                                                    
HETNAM      MG MAGNESIUM ION                                                    
HETNAM     SIN SUCCINIC ACID                                                    
HETSYN     GOL GLYCERIN; PROPANE-1,2,3-TRIOL                                    
FORMUL   2  CSS    C3 H7 N O2 S2                                                
FORMUL   3  COA    C21 H36 N7 O16 P3 S                                          
FORMUL   4   CL    CL 1-                                                        
FORMUL   5  GOL    2(C3 H8 O3)                                                  
FORMUL   6  PO4    O4 P 3-                                                      
FORMUL   7   MG    MG 2+                                                        
FORMUL   8  SIN    C4 H6 O4                                                     
FORMUL  10  HOH   *250(H2 O)                                                    
HELIX    1 AA1 SER A    2  TYR A   11  5                                  10    
HELIX    2 AA2 GLY A   25  GLY A   39  1                                  15    
HELIX    3 AA3 THR A   63  GLY A   72  1                                  10    
HELIX    4 AA4 PRO A   81  ALA A   95  1                                  15    
HELIX    5 AA5 PRO A  108  LEU A  120  1                                  13    
HELIX    6 AA6 PRO A  147  HIS A  151  5                                   5    
HELIX    7 AA7 SER A  162  VAL A  176  1                                  15    
HELIX    8 AA8 ASP A  195  ASP A  206  1                                  12    
HELIX    9 AA9 ASN A  221  ASN A  234  1                                  14    
HELIX   10 AB1 GLY A  270  ALA A  281  1                                  12    
HELIX   11 AB2 SER A  288  ALA A  290  5                                   3    
HELIX   12 AB3 GLN A  291  ARG A  303  1                                  13    
HELIX   13 AB4 GLN B    4  ASN B   15  1                                  12    
HELIX   14 AB5 THR B   27  ASN B   39  1                                  13    
HELIX   15 AB6 GLY B   53  GLY B   57  5                                   5    
HELIX   16 AB7 ASP B   72  GLN B   82  1                                  11    
HELIX   17 AB8 ASP B  139  ASN B  147  1                                   9    
HELIX   18 AB9 PRO B  148  ILE B  151  5                                   4    
HELIX   19 AC1 LYS B  163  LEU B  174  1                                  12    
HELIX   20 AC2 LEU B  177  ILE B  198  1                                  22    
HELIX   21 AC3 ASP B  227  ARG B  232  5                                   6    
HELIX   22 AC4 GLN B  233  ALA B  238  1                                   6    
HELIX   23 AC5 GLU B  246  TYR B  255  1                                  10    
HELIX   24 AC6 GLY B  272  ASN B  286  1                                  15    
HELIX   25 AC7 LYS B  301  ASP B  315  1                                  15    
HELIX   26 AC8 ASN B  331  GLU B  345  1                                  15    
HELIX   27 AC9 ASN B  360  ASN B  370  1                                  11    
HELIX   28 AD1 ASP B  380  SER B  391  1                                  12    
SHEET    1 AA1 7 THR A  54  HIS A  55  0                                        
SHEET    2 AA1 7 LEU A  58  PHE A  61 -1  O  LEU A  58   N  HIS A  55           
SHEET    3 AA1 7 ASN A  41  THR A  46  1  N  GLY A  45   O  PHE A  61           
SHEET    4 AA1 7 LYS A  17  GLN A  21  1  N  VAL A  18   O  ASN A  41           
SHEET    5 AA1 7 ALA A  75  ILE A  78  1  O  VAL A  77   N  GLN A  21           
SHEET    6 AA1 7 LEU A  99  CYS A 102  1  O  VAL A 101   N  SER A  76           
SHEET    7 AA1 7 ARG A 126  ILE A 128  1  O  ILE A 128   N  VAL A 100           
SHEET    1 AA2 7 CYS A 141  GLY A 144  0                                        
SHEET    2 AA2 7 GLY A 134  ASN A 137 -1  N  ASN A 137   O  CYS A 141           
SHEET    3 AA2 7 GLN A 180  GLY A 185 -1  O  GLY A 185   N  GLY A 134           
SHEET    4 AA2 7 LYS A 153  SER A 160  1  N  ILE A 158   O  VAL A 184           
SHEET    5 AA2 7 GLY A 211  GLU A 217  1  O  ILE A 213   N  GLY A 157           
SHEET    6 AA2 7 VAL A 242  ALA A 247  1  O  VAL A 243   N  ILE A 212           
SHEET    7 AA2 7 VAL A 284  VAL A 285  1  O  VAL A 284   N  VAL A 242           
SHEET    1 AA3 4 PHE B  22  ALA B  25  0                                        
SHEET    2 AA3 4 VAL B 103  GLU B 107 -1  O  VAL B 105   N  PHE B  23           
SHEET    3 AA3 4 ILE B  43  ALA B  47 -1  N  LYS B  46   O  MET B 104           
SHEET    4 AA3 4 VAL B  67  THR B  70 -1  O  HIS B  68   N  LEU B  45           
SHEET    1 AA4 3 VAL B  58  PHE B  59  0                                        
SHEET    2 AA4 3 ASN B  87  ALA B  89 -1  O  ALA B  89   N  VAL B  58           
SHEET    3 AA4 3 VAL B  98  LYS B  99 -1  O  VAL B  98   N  LEU B  88           
SHEET    1 AA5 5 PHE B 152  GLN B 155  0                                        
SHEET    2 AA5 5 GLY B 127  SER B 133 -1  N  GLY B 132   O  PHE B 152           
SHEET    3 AA5 5 ARG B 113  ASP B 122 -1  N  ASP B 122   O  GLY B 127           
SHEET    4 AA5 5 ALA B 200  GLU B 210 -1  O  VAL B 205   N  LEU B 117           
SHEET    5 AA5 5 VAL B 216  CYS B 218 -1  O  VAL B 217   N  GLY B 209           
SHEET    1 AA6 5 PHE B 152  GLN B 155  0                                        
SHEET    2 AA6 5 GLY B 127  SER B 133 -1  N  GLY B 132   O  PHE B 152           
SHEET    3 AA6 5 ARG B 113  ASP B 122 -1  N  ASP B 122   O  GLY B 127           
SHEET    4 AA6 5 ALA B 200  GLU B 210 -1  O  VAL B 205   N  LEU B 117           
SHEET    5 AA6 5 ALA B 221  PHE B 225 -1  O  LYS B 222   N  GLU B 204           
SHEET    1 AA7 2 LYS B 258  GLY B 261  0                                        
SHEET    2 AA7 2 ASN B 292  ASP B 295 -1  O  PHE B 293   N  ILE B 260           
SHEET    1 AA8 4 ILE B 266  VAL B 270  0                                        
SHEET    2 AA8 4 ALA B 320  GLY B 327  1  O  LEU B 322   N  ALA B 267           
SHEET    3 AA8 4 LEU B 352  GLY B 358  1  O  VAL B 353   N  VAL B 323           
SHEET    4 AA8 4 ILE B 375  SER B 377  1  O  THR B 376   N  LEU B 352           
LINK         C   SER B 124                 N   CSS B 125     1555   1555  1.33  
LINK         C   CSS B 125                 N   ASN B 126     1555   1555  1.33  
LINK         O4  PO4 A 404                MG    MG B 401     1555   1555  2.06  
LINK        MG    MG B 401                 O   HOH A 547     1555   1555  2.14  
LINK        MG    MG B 401                 O   HOH A 564     1555   1555  2.08  
LINK        MG    MG B 401                 O4  SIN B 402     1555   1555  2.35  
LINK        MG    MG B 401                 O   HOH B 528     1555   1555  2.24  
LINK        MG    MG B 401                 O   HOH A 505     1555   1555  2.20  
CISPEP   1 GLY A  129    PRO A  130          0         9.13                     
CISPEP   2 ASN B  206    PRO B  207          0         2.32                     
SITE     1 AC1 26 GLY A  22  THR A  24  GLY A  25  LYS A  26                    
SITE     2 AC1 26 GLN A  27  PRO A  48  LYS A  50  TYR A  79                    
SITE     3 AC1 26 VAL A  80  PRO A  81  PRO A  82  ILE A 103                    
SITE     4 AC1 26 THR A 104  GLU A 105  ASN A 131  CYS A 132                    
SITE     5 AC1 26 PRO A 133  ILE A 145  HOH A 510  HOH A 513                    
SITE     6 AC1 26 HOH A 529  HOH A 552  HOH A 565  HOH A 581                    
SITE     7 AC1 26 GLY B 298  SIN B 402                                          
SITE     1 AC2  1 ARG A   7                                                     
SITE     1 AC3  8 ARG A 161  PRO A 190  ASN A 192  ALA A 222                    
SITE     2 AC3  8 HOH A 536  HOH A 537  HOH A 571  ARG B 123                    
SITE     1 AC4 11 SER A 162  GLY A 163  THR A 164  HIS A 259                    
SITE     2 AC4 11 HOH A 538  HOH A 564  GLY B 272  ALA B 273                    
SITE     3 AC4 11 GLY B 274   MG B 401  SIN B 402                               
SITE     1 AC5  6 PO4 A 404  HOH A 505  HOH A 547  HOH A 564                    
SITE     2 AC5  6 SIN B 402  HOH B 528                                          
SITE     1 AC6 14 ILE A 145  TYR A 167  COA A 401  PO4 A 404                    
SITE     2 AC6 14 HOH A 505  ASN B 271  GLY B 297  GLY B 298                    
SITE     3 AC6 14 GLY B 327  GLY B 328  ILE B 329  VAL B 330                    
SITE     4 AC6 14  MG B 401  HOH B 528                                          
SITE     1 AC7  3 GLY B  77  GLN B  78  HOH B 544                               
CRYST1   86.670   81.020   50.780  90.00 104.90  90.00 P 1 21 1      2          
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      0.011538  0.000000  0.003070        0.00000                         
SCALE2      0.000000  0.012343  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.020378        0.00000                         
(ATOM LINES ARE NOT SHOWN.)
END                                                                             
DBGET integrated database retrieval system