Fig. 2
From: Molecular principles underlying dual RNA specificity in the Drosophila SNF protein
dSNF1-101 15N/1H backbone dynamics change upon RNA binding. a–c Values of ΔR2,eff, calculated from end points of a CPMG experiment; ΔR2,eff = R2,app(νCPMG50 Hz)–R2,app(νCPMG1000 Hz). Positions of secondary structure elements are shown on the top. a dSNF1-101, b dSNF1–101 bound to dU1SLII, c dSNF1-101 bound to dU2SLIV. Errors were determined from the propagation of base plane rms noise. In a, b and c, amides from residues L27 and I30 have no signal from exchange broadening, while in (a), amides from K44 and L46 are exchange-broadened and not quantifiable (orange labels). Prolines (orange labels) do not yield a signal. 50 mM KCl, 20 mM sodium cacodylate, pH 6.5, in 90% 1H2O, 10% 2H2O; 23 °C; 700 MHz. d Orthogonal views of ΔR2,eff values mapped onto the structure of dSNF1–96 in isolation (top), bound to dU1SLII (middle) and bound to dU2A′ and dU2SLIV (bottom). A scale bar is shown on the top. The orientation of the left panels relative to Fig. 1b is shown at the bottom
