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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]. Residues 140-155_CT (176-196seq) of the 140s_CT loop are colored magenta. The amides of residues corresponding to resonances experiencing μs-ms dynamics in both thrombin-TM456 and apo-thrombin are shown as violet spheres. Sidechains are shown for the catalytic triad (cyan). (b) Deuterium uptake plots for the peptides spanning residues 132-144_CT (168-180seq; MH + 1378.723) and 145-155_CT (181-196seq; MH + 1714.912). The colors are the same as in previous figures. (c) CPMG plots for thrombin resonances corresponding to residues Asn 149B_CT (187seq) and Lys 149E_CT (190seq). The colors of the curves are the same as in previous figures. CPMG data could not be obtained from the 600 MHz spectra for Thr 149_CT (187seq). (d) Examples of thrombin-TM456 HSQC (red) doublet resonances compared to apo-thrombin (blue) resonances for residues in the 140s_CT loop.