Biomolecular NMR Assignments

, Volume 11, Issue 2, pp 257–264 | Cite as

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

  • Gaston Courtade
  • Zarah Forsberg
  • Gustav Vaaje-Kolstad
  • Vincent G. H. Eijsink
  • Finn L. Aachmann


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.


Lytic polysaccharide monooxygenase LPMO AA10 Cellulose Linker CBM2 



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).

Compliance with ethical standards

Conflict of interest

The authors declare that they have no conflict of interest.


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Copyright information

© Springer Science+Business Media B.V. 2017

Authors and Affiliations

  1. 1.NOBIPOL, Department of Biotechnology and Food ScienceNTNU Norwegian University of Science and TechnologyTrondheimNorway
  2. 2.Faculty of Chemistry, Biotechnology and Food ScienceNorwegian University of Life SciencesÅsNorway

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