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. Author manuscript; available in PMC: 2019 Mar 1.
Published in final edited form as: Nature. 2018 Feb 21;555(7694):61–66. doi: 10.1038/nature25762

Extended Data Table 1.

Sequences of protein constructs and fluorescently labeled variants of H1 and ProTα.(top) Sequences of H1 and ProTα wildtype and variants used. Bold yellow-shaded residues are positions mutated to Cys for fluorophore conjugation. Residues in red are part of protease recognition sites used to cleave the HisTag with thrombin (GGPR or GC) or HRV-3C (GP). (Note that the wt sequence of H1 starts with "T"; the preceding Cys residue (−1) was added for labeling.) The underlined H1 sequence indicates the globular domain (GD), identified based on a sequence alignment with the G. gallus homolog20 (PDB access code 1HST, 82% sequence identity). Surface-exposed residues (as shown in Fig. 1a and 5b) are shaded in light blue. The net charge of each variant is indicated in parentheses. aC-terminal disordered region. bN-terminal disordered region including GD. (bottom) Labeled variants of H1 and ProTα. cFörster radius of the corresponding dye pair.

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