NMR STRUCTURE OF THE FIBRONECTIN EDA DOMAIN, NMR, 20 STRUCTURES
NIDRPKGLAFTDVDVDSIKIAWESPQGQVSRYRVTYSSPEDGIHELFPAPDGEEDTAELQGLRPGSEYTVSVVALHDDME SQPLIGTQSTAIPA
THREE-DIMENSIONAL STRUCTURE IN SOLUTION REPRESENTED BY 20 CONFORMERS DETERMINED BY NUCLEAR MAGNETIC RESONANCE, TORSION ANGLE DYNAMICS AND RESTRAINED ENERGY REFINEMENT.
structures with the least restraint violations
THESE STRUCTURES CONSIST OF 1289 UPPER LIMITS ON DISTANCES OBTAINED FROM NOE MEASUREMENTS AND HTDROGEN EXCHANGE MEASUREMENTS AND 51 TORSION ANGLE CONSTRAINTS OBTAINED FROM COUPLING CONSTANT AND CHEMICAL SHIFT INDEX
2mM EDA U-15N,13C; 50mM phosphate buffer, 400mM sodium sulfate; 90% H2O, 10% D2O
EDA, FIBRONECTIN, TYPEIII DOMAIN, PROTEIN BINDING