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. 2023 Aug 18;14:5020. doi: 10.1038/s41467-023-40736-6

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© This is a U.S. Government work and not under copyright protection in the US; foreign copyright protection may apply 2023

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Fig. 4 — a P1 phenyl side chain is oriented differently in FA 20mer (left panel) relative to FV 20mer (right panel). This is due to molecular cross-talks between peptide P1 and P2 residues and Ile152 and Tyr59 (missing) (see text and Fig. 3b). Overall, the network of hydrophobic (black dashed lines) and hydrogen bond (red dashed lines) interactions in the A and B pockets are different in these two structures. b The network of interactions in FA 8mer (left panel) and FV 8mer (right panel) are quite similar overall in these canonical structures, which is in contrast to FA and FV 20mer structures shown in panel a. Water molecules (shown as magenta balls) are involved in a network of hydrogen bonds.