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. 2023 Sep 16;14:5763. doi: 10.1038/s41467-023-41488-z

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© The Author(s) 2023

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. 10 — a–c Top panels: Ribbon diagrams showing the predicted poses of indicated peptides bound to CCL5. Chemokines are in grey, and the peptide poses in colour, with the top-ranked pose coloured green. Bottom panels: Corresponding heatmaps of weighted proximity scores mapped onto ribbon diagrams of CCL5. Chemokine structural features (α-helix, β-strands and 30s loop) are indicated. a Poses obtained following the previously reported HADDOCK⁷⁶ analysis of NMR chemical shift perturbation data of peptide Ev4E14N31 (Ev4Glu¹⁴-Asn³¹, EEEDDYTAYAPLTAYFTN) in complex with CCL5²⁸. b, c Poses obtained following AlphaFold2-Multimer (AFM) and AutoDock CrankPep (ADCP) analysis respectively of peptide HD2 (EEDDYTAYAPLTCYFT) docked to CCL5. d Heatmap scale for weighted proximity score. NMR nuclear magnetic resonance, AFM AlphaFold2-Multimer, ADCP AutoDock CrankPep, N N-terminus of the top-ranked pose, β1, β3: β-strands, α α-helix. Source data are provided as a Source Data file.