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. 2020 Jul 31;11:3862. doi: 10.1038/s41467-020-17618-2

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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 — Ligands in active sites are colored by blue, and ligands in allosteric sites are colored by yellow. One of the highest weight pathways identified by Ohm is shown as green consecutive cylinders for each protein. Resides with high, moderate, low, and extremely low ACI values are colored by yellow, green, and blue, respectively. Ohm analysis results for all 20 proteins are provided in Supplementary Data 3.