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. 2022 Oct 7;8:104. doi: 10.1038/s41421-022-00463-6

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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 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. 5 — a Close-up view of the interaction between FD01 and Omicron. The Omicron S RBD is displayed in pink surface. 16L9 and GW01 are shown as cartoons colored green and medium-blue, respectively. b The interactions between S RBD and 16L9. c The detailed interaction between RBD and the heavy chain of 16L9. The residues involved in interactions are represented as sticks. The polar interactions are indicated as dotted lines. The hydrophobic interactions are highlighted by red circles. d The detailed interaction between RBD and the light chain of 16L9. e The detailed interaction between RBD and GW01. f Epitope mapping of FD01. g Conservancy analysis of FD01 epitope. h Surface representation of RBD showing the buried binding site, including 16L9 (green), GW01 (purple), and 16L9 epitope overlapping with GW01 region (blue); goldenrod dotted line indicates receptor-binding site.