THREE-DIMENSIONAL SOLUTION STRUCTURE OF THE E3-BINDING DOMAIN OF THE DIHYDROLIPOAMIDE SUCCINYLTRANSFERASE CORE FROM THE 2-OXOGLUTARATE DEHYDROGENASE MULTIENZYME COMPLEX OF ESCHERICHIA COLI
DETAILS OF THE STRUCTURE DETERMINATION AND ALL STRUCTURAL STATISTICS ARE GIVEN IN THE PAPER CITED ON *JRNL* RECORDS ABOVE. THE STRUCTURES ARE BASED ON 630 INTERPROTON DISTANCE RESTRAINTS DERIVED FROM NOE MEASUREMENTS; AND 46 PHI AND 35 PSI BACKBONE TORSION ANGLE RESTRAINTS AND 20 CHI1 SIDE CHAIN TORSION ANGLE RESTRAINTS DERIVED FROM COUPLING CONSTANTS AND NOE DATA. THE LATTER ARE OBTAINED USING THE CONFORMATIONAL GRID SEARCH PROGRAM STEREOSEARCH (M.NILGES,G.M.CLORE,A.M.GRONENBORN (1990) BIOPOLYMERS 29, 813-822). THE METHOD USED TO DETERMINE THE STRUCTURES IS THE HYBRID METRIC MATRIX DISTANCE GEOMETRY-DYNAMICAL SIMULATED ANNEALING METHOD (M.NILGES,G.M.CLORE, A.M.GRONENBORN, FEBS LETT. 229, 317-324 (1988)). THIS ENTRY CONTAINS THE SIMULATED ANNEALING RESONANCE MINIMIZED AVERAGE STRUCTURE. THE COORDINATES OF 56 INDIVIDUAL STRUCTURES ARE PRESENTED IN PROTEIN DATA BANK ENTRY 1BAL. (SA)R RESTRAINED MINIMIZED MEAN STRUCTURE WAS DERIVED BY AVERAGING THE COORDINATES OF THE INDIVIDUAL SA STRUCTURES BEST FITTED TO RESIDUES 14 - 30 AND 39 - 47, AND SUBJECTING THE RESULTING COORDINATES TO RESTRAINED MINIMIZATION. RESIDUES 1 - 11 AND 48 - 51 ARE COMPLETELY DISORDERED AND ARE NOT INCLUDED IN THE COORDINATE SET. THE QUANTITY PRESENTED IN COLUMNS 61 - 66 OF THIS ENTRY HAS NO MEANING. THE QUANTITY PRESENTED IN COLUMNS 61 - 66 OF ENTRY 1BAL REPRESENTS THE ATOMIC RMS DEVIATIONS OF THE 56 INDIVIDUAL STRUCTURES ABOUT THE MEAN STRUCTURE. ALL THE INTERPROTON DISTANCE AND TORSION ANGLE RESTRAINTS ARE PRESENTED IN PROTEIN DATA BANK ENTRY R1BBLMR.
SSVDILVPDLPESVADATVATWHKKPGDAVVRDEVLVEIETDKVVLEVPASADGILDAVLEDEGTTVTSRQILGRLREGN SAGKETSAKSEEKASTPAQRQQASLEEQNNDALSPAIRRLLAEHNLDASAIKGTGVGGRLTREDVEKHLAKAPAKESAPA AAAPAAQPALAARSEKRVPMTRLRKRVAERLLEAKNSTAMLTTFNEVNMKPIMDLRKQYGEAFEKRHGIRLGFMSFYVKA VVEALKRYPEVNASIDGDDVVYHNYFDVSMAVSTPRGLVTPVLRDVDTLGMADIEKKIKELAVKGRDGKLTVEDLTGGNF TITNGGVFGSLMSTPIINPPQSAILGMHAIKDRPMAVNGQVEILPMMYLALSYDHRLIDGRESVGFLVTIKELLEDPTRL LLDV