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. 2021 Mar 17;20:69. doi: 10.1186/s12934-021-01560-z

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© The Author(s) 2021

Open AccessThis 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/. The Creative Commons Public Domain Dedication waiver (http://creativecommons.org/publicdomain/zero/1.0/) applies to the data made available in this article, unless otherwise stated in a credit line to the data.

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Fig. 7 — Molecular docking model of myriocin-NFYA/RIOK2. a and b represent the models of myriocin-NFYA and myriocin-RIOK2, respectively. From left to right, ribbons, surfaces and detailed binding diagrams are shown. Left: rectangular boxes represent internal docking areas. Middle: detailed internal docking areas (the surface color of proteins is classified by aromaticity). Right: detailed the bonding of myriocin-NFYA/RIOK2. GLU90, ARG253, PRO119, LYS105, ASP246, GLY104, LEU190, PHE232, PRO195 and ILE235 are amino acid residues. Hydrogen bonds are shown in green dashed lines. Electrostatic are shown in orange dashed line. Hydrophobics are shown in pink dashed line