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. 2021 Jan 25;12:559. doi: 10.1038/s41467-020-20879-6

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© The Author(s) 2021

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. 6 — a H3-3I14; b H3-FI6v3; c H3-39.29; d H1-3.1. All V_H3-30-derived antibodies recognize the hydrophobic groove between helix A and the fusion peptide. CDRs are shown as cartoons with residues interacting with sub-pockets (labeled as 1 through 5) shown as sticks. The fusion peptide is colored cyan with Trp21 shown as sticks; helix A is colored red and HA1 is colored orange. e Sequences for antibody CDRs, which have at least one residue that interacts with a sub-pocket. Highlighted residues coincide with which HA subpocket the interaction occurs: pocket 1-red; pocket 2-cyan; pocket 3-green; pocket 4-yellow; and pocket 5-purple.