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. 2022 May 17;298(6):102040. doi: 10.1016/j.jbc.2022.102040

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© 2022 The Authors

This is an open access article under the CC BY license (http://creativecommons.org/licenses/by/4.0/).

PMC Copyright notice

MD simulations of SaTrmK.A, mean length of the salt bridge between Arg7 and either SAM or SAH. B, time-dependence of the RMSDs over SaTrmK, SaTrmK:SAM, and SaTrmK:SAH Cα. C, mean RMSF over Cα. D, Cα RMSFs of the top three dominant motions of SaTrmK, SaTrmK:SAM, and SaTrmK:SAH as revealed by principal component analysis. Percentages in brackets represent the relative eigenvalue contributed by each eigenvector in each structure. E, ribbon-diagram representation of each dominant motion. The width or delocalization of the ribbon regions corresponds to the motion amplitude. SaTrmK, S. aureus TrmK; TrmK, m1A22-tRNA methyltransferase; MD, molecular dynamics; RMSF, root-mean-square fluctuation.