Abstract
The backbone resonance assignments of an engineered splicing-inactive mini-RecA intein based on triple resonance experiments with [13C,15N]-labeled protein are reported. The construct contains inactivating mutations specifically designed to retain most catalytic residues, especially those that are potentially metal-coordinating. The assignments are essential for protein structure determination of a precursor with an active N-terminal catalytic cysteine and for investigation of the atomic details of splicing.
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Acknowledgments
This work was supported by NIH Biomolecular Science and Engineering training grant GM067545 (C.S.P.), NIH Grant GM44844 (M.B.), and NIH grant GM085006 (A.S.).
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Pearson, C.S., Belfort, G., Belfort, M. et al. Backbone assignments of mini-RecA intein with short native exteins and an active N-terminal catalytic cysteine. Biomol NMR Assign 9, 235–238 (2015). https://doi.org/10.1007/s12104-014-9581-z
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DOI: https://doi.org/10.1007/s12104-014-9581-z