Fig. S1.

Substrate interactions with NTD. Chemical shift perturbations (CSPs), plotted by residue number, of [¹H, ¹⁵N]-labeled monomeric NTD upon binding to 3 molar equivalents of (A) chemically denatured firefly luciferase (FFL) aggregates, (B) heat-induced malate dehydrogenase (MDH) aggregates, (C) green fluorescent protein (GFP), (D) DnaK, (E) α-casein, (F) peptide B1, (G–K) reduced alkaline phosphatase (PhoA) fragments, (L) Src residues 1–85, (M) Sic1, (N) c-Jun, and (O) p13 (KLDSLIVFLREEA). CSPs were defined by the relation, $\mathrm{CSP}=\sqrt{{\left(\mathrm{\Delta }{\delta }_{\mathrm{H}}\right)}^2+{\left(\mathrm{\Delta }{\delta }_{\mathrm{N}}/5\right)}^2}$ , where Δδ_H and Δδ_N are proton and nitrogen chemical shift changes between apo and bound forms of the protein.