Figure 3.

Titration of wild type and C-terminal truncated PTN with CSE dp6 A) ¹⁵N-edited HSQC overlay of wild type PTN at different concentrations of CSE dp6. Residues with large chemical shift changes are labeled and their movements are illustrated with arrows. B) Normalized CSE dp6-induced chemical shift changes of amide proton and nitrogen for each residue in wild type PTN. Schematic illustration of PTN’s secondary structure is shown on the top of the plot. C) Binding curves of residues C15 (NTD) and R92 (CTD) used to calculate the CSE dp6 binding Kd of each domain. D) Magnitudes of chemical shift perturbation mapped onto the ribbon diagram of PTN. Coloring scale is shown on the bottom. E) ¹⁵N-edited HSQC overlay of C-terminal truncated PTN (residues 1 to 114) at different concentrations of CSE dp6. F) Normalized CSE dp6-induced chemical shift changes of amide proton and nitrogen for each residue in truncated PTN. G) Binding curves of residues C15 (NTD) and R92 (CTD) used to calculate the CSE dp6 binding Kd of each domain. H) Magnitudes of chemical shift perturbation mapped onto the ribbon diagram of PTN. Coloring scale is shown on the bottom.