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. 2018 Jan 12;8:581. doi: 10.1038/s41598-017-18951-1

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© The Author(s) 2018

Open Access This article is licensed under a Creative Commons Attribution 4.0 International License, which permits use, sharing, adaptation, distribution and reproduction in any medium or format, as long as you give appropriate credit to the original author(s) and the source, provide a link to the Creative Commons license, and indicate if changes were made. The images or other third party material in this article are included in the article’s Creative Commons license, unless indicated otherwise in a credit line to the material. If material is not included in the article’s Creative Commons license and your intended use is not permitted by statutory regulation or exceeds the permitted use, you will need to obtain permission directly from the copyright holder. To view a copy of this license, visit http://creativecommons.org/licenses/by/4.0/.

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Amino acid sequence of the metal binding domains of ATP7B (A) and a fingerprint 1H,15N-HSQC spectrum of MBD1 (B). (A) Conserved residues are shown in red. Cysteine residues in the copper binding motif of the MBDs are marked by an asterisk. The invariant glycine, which is a target of the Wilson disease causing mutation in MBD1 (G85V), is shown by the arrow. (B) The sequential amino acid assignments in MBD1 are shown. In the protein construct used for structure determination, residues 1–4 are from the purification tag, and Q5 corresponds to Q56 in the full length ATP7B.