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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. 1 — a Representation of the domains of ANP32A. Blue surface shows the LRR domain, pale blue ribbon-disordered IDD (100 or 132 amino acids). Sequence distribution of IDDs shown on right. Red = acidic, blue = basic and beige = hydrophobic or polar. AvIDD contains a 33 amino acids insert (horizontal line) comprising an avian-unique hexapeptide (H). b Chemical shift titration of 627(K) into ¹⁵N-labelled IDD of hANP32A. hANP32A was 25 μM throughout. 627(K) concentrations were 0 (blue), 25 (green), 50 (grey-blue), 100 (orange) and 200 (red) μM. Measurement at 850 MHz, 293 K (see ‘Methods’ section). c ¹⁵N rotating frame relaxation (R_1ρ) of free (blue) ¹⁵N-labelled IDD of hANP32A at 300 μM, and upon mixing with 627(K) at 1:1 (orange) and 1:4 (red) ratio. Measurement at 850 MHz, 293 K. d ¹⁵N rotating frame relaxation (R_1ρ) of free (blue) ¹⁵N-labelled IDD of avANP32A at 300 μM, and upon mixing with 627(E) at 1:1 (orange) and 1:4 (red) ratio. Maximum effect is seen at the equivalent motif, 33 amino acids downstream, from hANP32A. e Chemical shift perturbation (CSP) of full-length avANP32A upon addition of 627(E) (orange), NLS (red) and 627-NLS(E) (blue). Concentration of avANP32A was 25 μM and the partner 50 μM throughout. Resonances from the LRR were not observable at this low concentration. f ¹⁵N rotating frame relaxation (R_1ρ) of free (red) ¹⁵N-labelled full-length hANP32A at 300 μM, and upon mixing with 627-NLS(K) at 1:1 ratio (blue). Measurement at 850 MHz, 293 K. g CSP of full-length hANP32A upon addition of 627-NLS(K) (blue). Concentration of hANP32A was 300 μM and 627-NLS(K) 600 μM. The cross-interaction between hANP32A and 627-NLS(E) is shown for comparison at the same stoichiometric ratio (orange). h ¹⁵N rotating frame relaxation (R_1ρ) of free (red) ¹⁵N-labelled full-length avANP32A at 300 μM, and upon mixing with 627-NLS(E) at 1:1 ratio (blue). Measurement at 850 MHz, 293 K. i CSP of full-length avANP32A upon addition of 627-NLS(E) (blue). Concentration of avANP32A was 300 μM and 627-NLS(E) 600 μM. The cross-interaction between hANP32A and 627-NLS(E) is shown for comparison at the same stoichiometric ratio (orange). The avian-specific insert is highlighted by shifting data from hANP32A from residues following the beginning of the insert by 33 amino acids.