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. 2020 Nov 12;25(22):5268. doi: 10.3390/molecules25225268

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© 2020 by the authors.

Licensee MDPI, Basel, Switzerland. This article is an open access article distributed under the terms and conditions of the Creative Commons Attribution (CC BY) license (http://creativecommons.org/licenses/by/4.0/).

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Pre-hydrolytic states using the system BmrA-E504A (catalytically inhibited). Percentage of ADP (Δ) and ATP (○) in the presence of the mutant BmrA-E504A (symbol filled in blue) or of the mutant, which does not bind the nucleotide, BmrA-K380A (symbol filled in green). BmrA-K380A was chosen as a negative control in order to exclude the possibility of an ATPase contaminant in the sample (A). ³¹P 1D CP spectrum of BmrA-E504A:ATP (B). The overly of the alanine region of ¹³C-¹³C-DARR spectra of BmrA-E504A (blue) and BmrA-E504A:ATP (red) (C). Results in panels (A) and (B) are original, and spectra in (C) were adapted from Lacabanne et al. 2019 [92] (http://creativecommons.org/licenses/by/4.0/.).