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. 2018 Sep 5;8:13266. doi: 10.1038/s41598-018-31480-9

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© The Author(s) 2018

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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Certain MTBD residues made most of the contacts with E-hooks. (a) Histogram of the number of E-hook B contacts each residue of the MTBD makes constants at various MTBD-microtubule distances (see legend). (b) Histogram of the number of E-hook D contacts each residue of the MTBD makes constants at various MTBD-microtubule distances (see legend). In each panel, the number of contacts was normalized by the total number of contacts each particular distance over the 3 independent runs of 2000 total frames each (see Methods). Note that no results are shown here for distances larger than 35 Å because there are few contacts, however these numbers are provided in supplementary material. The right panels show the MTBD at distance = 15 Å with electrostatic potential mapped onto its surface, and the α-/β- tubulin dimer with A, B, C, D chains E-hooks highlighted (red). Note, a frame was chosen in which the E-hooks are shown not making contact with the MTBD for clarity. The residues of MTBD making most of the contacts with E-hooks are labeled.