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. 2022 Jun 22;12:10601. doi: 10.1038/s41598-022-14790-x

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© The Author(s) 2022

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 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/.

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nsP4-CHIKV three-dimensional model by AlphaFold. (A) nsP4-CHIKV AlphaFold model colored according to pLDDT. At the top right are shown the pLDDT color scales. (B) Model of nsP4-CHIKV colored according to domain assignment. The N-terminal helixes, finger, palm and thumb domains are colored in purple, dark blue, green and red, respectively. A detailed view of predicted catalytic aspartic residues is presented in the inset. (C) Electrostatic potential projected on the surface charge of nsP4-CHIKV, calculated with APBS. Positive regions are colored in blue and negative regions are in red. (D) ConSurf analysis of nsP4-CHIKV model. The amino acids are colored by their conservation grades using the color-coding bar, with green-through-purple indicating variable-through-conserved.