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. 2021 Nov 16;11:22365. doi: 10.1038/s41598-021-01530-w

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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 licence, and indicate if changes were made. The images or other third party material in this article are included in the article's Creative Commons licence, unless indicated otherwise in a credit line to the material. If material is not included in the article's Creative Commons licence 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 licence, visit http://creativecommons.org/licenses/by/4.0/.

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Amino acid sequence alignment of VL and VH of rbt4A11 with the closest human germline acceptor frameworks for humanization. The variable light chain (VL) and heavy chain (VH) domain of rbt4A11 was aligned with its closets human germlines to specify the different (letter) and identical (dot) amino acid residues in framework regions (FWR) and complementarity-determining regions (CDRs) by Kabat numbering scheme⁶. Six CDRs (box) and fifteen framework residues at Vernier zone (black fill) of rbt4A11 were fused in-frame to individual human germline acceptor framework for shuffling. Three positions (19, 79, 81) at the heavy chain framework guided by structure complex analysis were residues used to modulate antibody function (asterisk). The positions with sequence deletion and undefined heavy chain germline CDR3 were shown in blanks.