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. 2018 Jul 10;4:65. doi: 10.1038/s41420-018-0067-0

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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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Fig. 4 — a Optimal poses obtained inside RIP1 active site (grey) for compound Oxa12 (represented in stick model and coloured blue) compared with crystallographic ligand 1-aminoisoquinoline inhibitor (PDBID: 4NEU) (yellow). b Compound Oxa12 and 4NEU co-crystallized inhibitor interacting with Asp156, Leu157, Met67, and Met95. Docking calculations were performed using the X-ray structure obtained for RIP1 complexed with 1-aminoisoquinoline inhibitor at resolution of 2.57 Å, PDBID: 4NEU, by the GOLD 5.2 software