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. 2017 Jun 13;7:3385. doi: 10.1038/s41598-017-03457-7

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© The Author(s) 2017

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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Backbone dynamics of muPA. Displayed is the catalytic protease domain of muPA from the muPA:Nb7:EGR-cmk structure (Nb7 is removed for clarity) with EGR-cmk shown as sticks (red). Residues in muPA within contacts distance of EGR-cmk (<4 Å) are represented as spheres. Peptides included in the HDXMS analysis and their corresponding deuterium uptake plots are highlighted on the structure and boxed in different colors: 170s loop (black); β9-strand (teal); 180s loop (magenta); 220s loop (orange). The deuterium uptake plots show the 4 peptides from apo-muPA (blue), EGR-cmk-bound muPA (green) and Nb7-bound muPA (orange) respectively. The amino acid sequence and molecular masses are indicated for each peptide. The Y-axis is scaled to show the maximum uptake for each individual peptide. Error bars, s.d. (n = 3 independent measurements).