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. 2021 May 26;8:679915. doi: 10.3389/fmolb.2021.679915

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Copyright © 2021 D’Amico, Bosken, O’Rourke, Murray, Admasu, Chang and Boehr.

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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Molecular modeling reveals four positions with stronger interdomain interactions in A198W TS. (A) Electrostatic link between alpha residues αGln65, αAsn66 and beta residues βSer161, βGly162, βAsp168, and βAsn171 (also see Supplementary Figure 11). (B) Hydrophobic cluster between αLeu177, αPhe212, and βIle20 observed in A198W TS (also see Supplementary Figure 9). (C) αAsn104 forms consistent hydrogen bonds with βGln 288/βGly 292 in A198W TS (D) Consistent hydrogen bond between αThr183 and αArg175 may contribute to closed αL6 conformation (also see Supplementary 11A).