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Chemical shift assignments for the apo-form of the catalytic domain, the linker region, and the carbohydrate-binding domain of the cellulose-active lytic polysaccharide monooxygenase ScLPMO10C

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Abstract

The apo-form of the 21.4 kDa catalytic domain and the 10.7 kDa carbohydrate binding domain of the AA10 family lytic polysaccharide monooxygenase ScLPMO10C from Streptomyces coelicolor have been isotopically labeled and recombinantly expressed in Escherichia coli. In this paper, we report the 1H, 13C, and 15N chemical shift assignments of each individual domain as well as an ensemble of the assignment for the full-length protein, including its approximately 30-amino acid long linker.

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Acknowledgements

This work was financed by SO-funds from NTNU Norwegian University of Science and Technology and by the MARPOL project, the Norwegian NMR Platform, both from the Research Council of Norway (grant numbers 221576, 226244, respectively).

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Authors and Affiliations

  1. NOBIPOL, Department of Biotechnology and Food Science, NTNU Norwegian University of Science and Technology, Sem Sælands vei 6/8, 7491, Trondheim, Norway

    Gaston Courtade & Finn L. Aachmann

  2. Faculty of Chemistry, Biotechnology and Food Science, Norwegian University of Life Sciences, 1432, Ås, Norway

    Zarah Forsberg, Gustav Vaaje-Kolstad & Vincent G. H. Eijsink

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  1. Gaston Courtade
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  2. Zarah Forsberg
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  3. Gustav Vaaje-Kolstad
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  4. Vincent G. H. Eijsink
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  5. Finn L. Aachmann
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Correspondence to Finn L. Aachmann.

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Courtade, G., Forsberg, Z., Vaaje-Kolstad, G. et al. Chemical shift assignments for the apo-form of the catalytic domain, the linker region, and the carbohydrate-binding domain of the cellulose-active lytic polysaccharide monooxygenase ScLPMO10C. Biomol NMR Assign 11, 257–264 (2017). https://doi.org/10.1007/s12104-017-9759-2

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  • DOI: https://doi.org/10.1007/s12104-017-9759-2

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