Fig. 6
Structural analysis of the pentameric Npm unbound and bound to H2A/H2B. a 1H-15N HSQC of the full-length Npm (red) overlaid with the tail alone (blue) under the same buffer and temperature conditions. Residues with significant differences in chemical shift values or those broadened in the full-length protein are labeled. b Ratio of 1H line widths of well-separated residues of the full-length protein compared to the tail domain alone. Ratio of 1 indicates peaks that are not broadened in the full-length spectrum. c SAXS curve (purple circles) of the core+A2:H2A/H2B complex. Top NMR-restrained SAXS hybrid model fit to the scattering curve (black line). d SAXS ab initio envelope of the core+A2:H2A/H2B complex (purple). Top NMR-restrained SAXS hybrid model fit into the envelope. Npm, H2A, and H2B colored gray, yellow, and red, respectively
