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. 2021 May 11;12:2623. doi: 10.1038/s41467-021-22926-2

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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. 2 — a The overall P4A1-Fab-RBD complex structure superimposed with the hACE2-RBD complex. The P4A1 heavy chain (colored slate blue), light chain (colored salmon red), and hACE (colored pale green) are displayed in cartoon representation. The SARS-CoV-2 RBD is colored in gray and displayed in surface representation. b The epitope of P4A1 shown in surface representation. The CDR loops of heavy chain (HCDR) and light chain (LCDR) are colored in purple and magenta, respectively. The epitopes from the heavy chain and light chain are colored in slate blue and salmon red, respectively. The only residue K417, which contacts with both heavy chain and light chain, is colored in pink. The light-chain frame region 3 (LFR3) is colored in orange. The identical residues on RBD shared in P4A1 and hACE2 binding are labeled in red. The residues are numbered according to SARS-CoV-2 RBD. c The detailed interactions between SARS-CoV-2 RBD with HCDR, LCDR, and LFR3. The residues are shown in sticks with identical colors to (b).