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. 2021 Apr 30;11:9354. doi: 10.1038/s41598-021-88432-z

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© The Author(s) 2021

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) Structure of thrombin (wheat) bound to TM456 (light blue) [PDB ID: 1DX5]. The residues corresponding to resonances missing from the thrombin-TM456 HSQC are colored black. The residues corresponding to multiplet resonances (teal spheres), resonances experiencing increased μs-ms dynamics in thrombin-TM456 compared to apo-thrombin (pink spheres), and resonances experiencing similar μs-ms dynamics in thrombin-TM456 and apo-thrombin (violet spheres) and the catalytic triad (cyan sticks) are shown. (b) Deuterium uptake plot for the peptide spanning residues 106-114_CT (139-147seq; MH + 1061.654). (c) CPMG plots for resonances in the thrombin N-terminal β-barrel (symbols as in Fig. 1). (d) Examples of thrombin-TM456 HSQC (red) doublet resonances compared to apo-thrombin (blue) resonances for residues in the N-terminal β-barrel.