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. 2023 May 15;14:2782. doi: 10.1038/s41467-023-38108-1

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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. 3 — A DH270 clonal tree highlighting the I5, I3, and I4 intermediate antibodies. B Top views of the I3 and I4 contact sites. Alpha-carbons (Cα) of heavy and light chain mutations are presented as spheres. C (left) The N332-glycan D1 arm contact with the I5 V_H/V_L cleft. (right) The N332-glycan D1 arm contact with the I3 V_H/V_L cleft. D Structure of the I3 intermediate at the R87T site near potential N156-glycan contacts. E Aligned I5 and I3 V_H domains highlighting the change in elbow angle (magenta). F (left) Map and fit coordinates of the new N332-glycan contact formed at the I4 HCDR3 S108Y mutation site. (right) Aligned I5 and I4 V_H domains showing HCDR3 loop arrangements.