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. 2023 Mar 30;10:1148653. doi: 10.3389/fmolb.2023.1148653

FIGURE 2.

FIGURE 2

PYM1–160 is an intrinsically unfolded protein. (A) 15N-HSQC spectrum of PYM1–160 with peak assignments. The limited dispersion of the HN chemical shifts is indicative of a largely unfolded protein. (B) The lowest energy structure of PYM1–160. The β-domain, emulating a β-strand–turn–β-strand motif, is in blue (aa 16–33), the region comprising stretches 9–16 and 34–65, where long-range NOEs are observed, is in cyan, and the helix 68–81 is in red. The most C-terminal stretch is not shown, as it is completely disordered. (C) Three representative structures of the region 13–65, with the detected long-range NOEs shown as black dashed lines. (D) Overlay of helix 68–81 in the 20 lowest-energy structures. The lowest energy structure is in red and all other structures are in grey. (E) Three representative conformations of the stretch 68–86 (the lowest-energy structure is in red, the other structures are in grey).