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. 2023 Jul 13;51(16):8643–8662. doi: 10.1093/nar/gkad589

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© The Author(s) 2023. Published by Oxford University Press on behalf of Nucleic Acids Research.

This is an Open Access article distributed under the terms of the Creative Commons Attribution License (https://creativecommons.org/licenses/by/4.0/), which permits unrestricted reuse, distribution, and reproduction in any medium, provided the original work is properly cited.

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Figure 7. — Modelling studies on the RAD51-RAD54-WT interaction. (A) RMSD of the RAD51-RAD54-WT complex over 500 ns. (B) Distance based hydrogen bond analysis: (1) GLU371-HIS244 (black), ARG374-ASP198 (red), GLU378-LYS64 (green), ARG691-GLU29 (blue). (C) Principal component analysis (PCA) for RAD51-RAD54-WT (red), black marker as the reference complex structure and RAD51-RAD54-T700D -Mutant (green), blue marker as the reference complex structure. (D) RMSF of the RAD51-RAD54-WT complex over 500 ns. (E) Initial state of RAD51-RAD54-WT complex at the beginning of 500 ns. (F) Final state of RAD51-RAD54-WT complex at the end of 500 ns. (G) Residue level interaction between RAD51 and the RAD54, Arg683-Glu29, Arg691-Gln30, Ser701-Asn34, Asp698-Ser701, Glu379-Asn62, Arg382-Asn62, Gln375-Met243 and Arg374-Glu37.