Fig. 2: Resonance assignment of the coilin peptide (clp).

a Assigned Hα-HN region from the 2D 1H−1H TOCSY spectrum. The intra-residue peaks in the TOCSY were used for amino-acid residue-typing while the additional peaks apparent in the 2D 1H-1H NOESY spectrum provided inter-residue information (see also Supplementary Figs. 3–5). b Secondary structure propensities determined from the assigned chemical shifts via TALOS-N (top). Propensity for helix (red) and extended (blue) structures are shown respectively on positive and negative sides of Y-axis. Source data are provided as a Source Data file.