1H, 13C, 15N chemical shift assignments for oxidised ERp18

Rowe, Michelle L. and Alanen, Heli I. and Ruddock, Lloyd W. and Kelly, Geoff and Schmidt, Jürgen M. and Williamson, Richard A. and Howard, Mark J. (2009) 1H, 13C, 15N chemical shift assignments for oxidised ERp18. Biological Magnetic Resonance Data Bank (BMRB), Madison, Wisconsin, USA NMR-STAR formatted text file. 102kB. Located at: http://www.bmrb.wisc.edu/data_library/generate_summary.php?bmrbId=15964. BMRB entry 15964. (The full text of this publication is not available from this repository)

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Abstract

Citation: Rowe, Michelle, L.; Ruddock, Lloyd, W.; Kelly, Geoff; Schmidt, Jürgen, M.; Williamson, Richard, A.; Howard, Mark, J.; "Solution Structure and Dynamics of ERp18: a Small ER Resident Oxidoreductase," Biochemistry 48(21), 4596-4606 (2009). PubMed: 19361226. DOI: 10.1021/bi9003342. System Studied: ERp18. System Components: ERp18, Polymer, 157 residues, 17771 Da. Molecular Description: Classification: Oxidoreductase, Structure Weight: 17801.10 Da, Molecule: Thioredoxin domain-containing protein 12, Polymer: 1, Type: polypeptide(L), Length: 157, Chains: A, EC#: 1.8.4.2, Fragment: UNP residues 24-172. Natural Source: Common Name: Human. Taxonomy ID: 9606. Superkingdom: Eukaryota. Kingdom: Metazoa. Genus/species: Homo sapiens. Source: Scientific Name: Homo sapiens, Common Name: Human, Expression System: Escherichia coli. Experimental Data: NMR parameters. Type: Assigned Chemical Shifts. Number of Values: 1760. Sets: 1.

Item Type: Datasets / databases
Subjects: Q Science
Q Science > QD Chemistry
Q Science > QC Physics
Divisions: Faculties > Science Technology and Medical Studies > School of Biosciences
Faculties > Science Technology and Medical Studies > School of Biosciences > Protein Science Group
Depositing User: Jurgen M Schmidt
Date Deposited: 12 Feb 2011 09:23
Last Modified: 24 Jun 2014 11:00
Resource URI: http://kar.kent.ac.uk/id/eprint/26329 (The current URI for this page, for reference purposes)
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