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. 2020 Oct 28;10:18530. doi: 10.1038/s41598-020-75409-7

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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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Free energy profiles of the opening of the central β-sheet for the N-SH2 domain in apo state (no ligand), bound to a truncated peptide (SPGEpYVNI), or bound to a full-length peptide (SPGEpYVNIEFGS). The opening of the central β-sheet was quantified as the distance between the backbone N and C atoms of residues Gly³⁹ and Asn⁵⁸, respectively.