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. 2022 May 18;13:820336. doi: 10.3389/fimmu.2022.820336

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Copyright © 2022 Yang, Lin, Sun, Chen, Yang, Lin, Guo, Wang, Wen, Zhang, Dai, He, Cao, Dong, Liu, Chen, Li, Zhao and Lu

This is an open-access article distributed under the terms of the Creative Commons Attribution License (CC BY). The use, distribution or reproduction in other forums is permitted, provided the original author(s) and the copyright owner(s) are credited and that the original publication in this journal is cited, in accordance with accepted academic practice. No use, distribution or reproduction is permitted which does not comply with these terms.

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The complex structure of Nb-007 bound to SARS-CoV-2 S-RBD. (A) A cartoon representation of the complex structure. Nb-007 is colored in lemon and S-RBD in cyan. The CDR1, CDR2 and CDR3 of Nb-007 are indicated with arrows and highlighted in magenta, gray and orange, respectively. The external subdomain and core subdomain of S-RBD, are roughly divided by a dashed line. (B) The multiple van der Waals (vdw) and hydrophobic interactions between Nb-007 and S-RBD. The left panel, amino acid interactions between CDR1 and CDR3 of Nb-007 and S-RBD. The right panel, amino acid interactions between framework region and CDR2 of Nb-007 and S-RBD. Those residues providing ≥2 contacts are shown (the distance cutoff is 4.5 Å). (C) Hydrophilic interactions (hydrogen bonds and salt bridges) between Nb-007 and S-RBD (the distance cutoff is 3.1 Å).