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. 2020 Jul 21;11:3656. doi: 10.1038/s41467-020-17407-x

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© The Author(s) 2020

Open Access This article is licensed under a Creative Commons Attribution 4.0 International License, which permits use, sharing, adaptation, distribution and reproduction in any medium or format, as long as you give appropriate credit to the original author(s) and the source, provide a link to the Creative Commons license, and indicate if changes were made. The images or other third party material in this article are included in the article’s Creative Commons license, unless indicated otherwise in a credit line to the material. If material is not included in the article’s Creative Commons license and your intended use is not permitted by statutory regulation or exceeds the permitted use, you will need to obtain permission directly from the copyright holder. To view a copy of this license, visit http://creativecommons.org/licenses/by/4.0/.

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Fig. 4 — a Average distance difference matrix, showing the average difference (d_hh − d_avav) in distance between amino acid positions in the IDD of ANP32A (x-axis) and the 627-NLS domains (y-axis) over the two ensembles. The colour code shown on the right is measured in Å. b Representation of the key interactions between hANP32A and 627-NLS(K). Polyvalent interactions between 627 and the IDD localise the disordered domain in the vicinity of the basic patch on the surface of 627 (see Fig. 3). The different IDD chains are shown to represent different binding modes and are truncated at residue 200 for clarity. Red positions in the IDD indicate the acidic sidechains. Note that this representation illustrates the tendency over the entire ensemble that is highly disperse (see d and e). c Representation of the key interactions between avANP32A and 627-NLS(E). In this case, the average distance between the IDD and the surface of 627 is larger, but in general closer to the NLS domain, in particular the hexapaptide of ANP32A, and the linker between 627 and NLS. The two IDD chains represent reduced polyvalency compared to hANP32A and 627-NLS(K), and are again truncated at residue 200 for clarity. d Representative ensemble of conformations describing the conformational space sampled by the hANP32A:627-NLS(K) complex. The NLS domain has been removed for clarity, and the IDD truncated at residue 210. The position of residue 190 is indicated as a red sphere. e Representative ensemble of conformations describing the conformational space sampled by the avANP32A:627-NLS(E) complex. Representation as in d.