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. 2017 Nov 30;8:1877. doi: 10.1038/s41467-017-01858-w

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© The Author(s) 2017

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. 3 — 5C4 forms few hydrogen bonds to RSV F main-chain atoms. a Two pre-F protomers are shown as dark and light gray surfaces, and the third protomer is shown as ribbons with F1 colored green and F2 colored blue. 5C4 heavy and light chains are shown as ribbons with the heavy and light chains colored pink and white, respectively. Antibody complementarity-determining regions (CDRs) involved in molecular recognition are labeled. Main-chain and side-chain atoms involved in molecular recognition are shown in stick representation with oxygen atoms colored red and nitrogen atoms colored blue. Hydrogen bonds and salt bridges are depicted as black dotted lines. b Linear sequence of antigenic site Ø for both RSV subtypes with the F2 β2–α1 loop on the left and the F1 α4 helix on the right. Subtype-specific residues in site Ø are colored blue in the subtype B consensus sequence. RSV F residues that make hydrogen bonds to 5C4 and D25 are denoted with symbols (side-chain hydrogen bonds, main-chain hydrogen bonds, or side-chain and main-chain hydrogen bonds are represented as open, filled, or partially filled diamonds, respectively)