Supplementary Figure 2: Human YL1-Z is intrinsically disordered.
From: Structural basis of H2A.Z recognition by SRCAP chromatin-remodeling subunit YL1
(a), 1H–15N heteronuclear single quantum coherence (HSQC) spectra of human YL1-Z in histone-free form. The backbone 1H–15N resonances of hYL1 residue 1–77 were fully assigned and the peaks representing YL1-Z residues were labeled. (b), The hYL1-Z backbone Cα chemical shift deviations corresponding to random coil values are presented. The results show that hYL1-Z largely remains as a disordered polypeptide.
