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. 2020 Feb 25;11:1038. doi: 10.1038/s41467-020-14842-8

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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 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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Fig. 4 — a Overall structure of the docking model obtained by MDFF for MTBD, α-tubulin, and β-tubulin (colored magenta, dark gray, and light gray, respectively). b–d The close-up view of the interface of the (b) α-tubulin side, (c) H1 helix, and (d) H3 helix. The residues involved in intermolecular salt bridges are shown by stick models.