Supplementary Figure 4: Analysis of cSnu17p monomer, cSnu17p–cPml1p dimer, cSnu17p–cBud13p dimer and cRES dynamics.
From: Cooperative structure of the heterotrimeric pre-mRNA retention and splicing complex
(a) Plot of residue specific hydrogen-deuterium exchange half-life H-D1/2 for cRES (black), cSnu17p–cPml1p dimer (yellow), cSnu17p–cBud13p dimer (blue), cSnu17p monomer (red). (b) R2 (black) and R1ρ (grey) plots (left panel) for the aforementioned complexes. Rex estimates derived from R2 and R1ρ difference (right panel). Positions marked with an asterisk correspond to the five most broadened peaks in c). (c) Normalized intensity vs 1H full width at half maximum (FWHM) of 1H, 15N HSQC peaks for the aforementioned complexes and cSnu17p monomer. Intensity values are offset between each group by 1. Please note that both cRES and cSnu17p–cBud13p dimer experience a decrease in the overall tumbling due to apparent increase in size related to peptide binding and/or the presence of C-terminal α-helix. This effect is small in cSnu17p–cPml1p dimer since cPml1p is shorter and C-terminal α-helix is folded. (d) S2 order parameter derived from the chemical shift for the aforementioned complexes.
