NMR assignments of ¹H, ¹³C and ¹⁵N spectra of methionine sulfoxide reductase B1 from Mus musculus

Authors

Lena S. Sal, Norwegian University of Science and Technology
Finn L. Aachmann, Norwegian University of Science and Technology
Hwa-Young Kim, Department of Biochemistry and Molecular Biology, Yeungnam University College of Medicine, Daegu, 705-717, South KoreaFollow
Vadim N. Gladyshev, University of Nebraska-LincolnFollow
Alexander Dikiy, Norwegian University of Science and Technology

Date of this Version

July 2007

Comments

Published in Biomolecular NMR Assignments 1 (2007), pp. 131–133; doi 10.1007/s12104-007-9039-7. Copyright © 2007 Springer Science+Business Media B.V. Used by permission. http://www.springerlink.com/content/0m51520154233372/

Abstract

Isotopically labeled, ¹⁵N and ¹⁵N/¹³C forms of recombinant methionine-R-sulfoxide reductase 1 (MsrB1, SelR) from Mus musculus were produced, in which catalytic selenocysteine was replaced with cysteine. We report here the ¹H, ¹⁵N and ¹³C NMR assignment of the reduced form of this mammalian protein.