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. 2020 Nov 11;10:19574. doi: 10.1038/s41598-020-76522-3

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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 licence, and indicate if changes were made. The images or other third party material in this article are included in the article's Creative Commons licence, unless indicated otherwise in a credit line to the material. If material is not included in the article's Creative Commons licence 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 licence, visit http://creativecommons.org/licenses/by/4.0/.

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(A) Neighbor-corrected secondary structure propensity (ncSSP) values obtained through the online ncSSP tool (https://st-protein02.chem.au.dk/ncSPC/)³² using the chemical shift values reported in Supplementary Table S2. Positive and negative values correspond to α-helical and β-strand propensities, respectively. The light cyan box represents the ± 0.05 value. Few regions display a moderate α-helix propensity (SSP > 0.2) while most of the protein is largely disordered. (B) ¹⁵N R₂ values reported as a function of residue number. The light cyan box indicates the modal value.