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Among the four viral proteins encoded by HBV, the X protein (HBx) has remained resistant to atomic-level characterization. HBx is a small, non-structural protein that interacts with various human host proteins. It is essential for HBV replication and implicated in HBV-induced carcinogenesis. Here, we present the sequential backbone resonance assignments of a C-terminally truncated HBx isoform (residues 1\u2013120), which is frequently found in chronically infected patients. Three-dimensional NMR experiments were recorded in the presence of residual urea (1\u00a0M), and the assignments of amide moieties were subsequently transferred to a low-urea condition (&lt;\u20090.2\u00a0M) compatible with HBx interaction studies. We compare manual assignments with automated predictions using the ARTINA software. These results reveal secondary structure propensities in the truncated HBx isoform and lay the groundwork for future NMR-based studies of HBx interactions in solution.<\/jats:p>","DOI":"10.1007\/s12104-025-10255-0","type":"journal-article","created":{"date-parts":[[2025,11,8]],"date-time":"2025-11-08T03:19:16Z","timestamp":1762571956000},"update-policy":"https:\/\/doi.org\/10.1007\/springer_crossmark_policy","source":"Crossref","is-referenced-by-count":3,"title":["Sequential backbone chemical shift assignments of a cancer-associated isoform of the HBx protein from human hepatitis B virus"],"prefix":"10.1007","volume":"20","author":[{"given":"Alexis","family":"Clavier","sequence":"first","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Toshinobu","family":"Shida","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Maxim A.","family":"Droemer","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Julian","family":"Holzinger","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Anne K.","family":"Sch\u00fctz","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]}],"member":"297","published-online":{"date-parts":[[2025,11,8]]},"reference":[{"key":"10255_CR32","doi-asserted-by":"publisher","first-page":"106842","DOI":"10.1016\/j.pep.2025.106842","volume":"2025","author":"A Clavier","year":"2025","unstructured":"Clavier A, G\u00f3mez-Evain S, Shida T, Abanti RR, Hammerstein F, Kielkowski P, Leuthold M, Sch\u00fctz AK (2025) Expression, purification and functional validation of a cancer-associated isoform of the HBc protein from human hepatitis B virus. Protein Expr Purif 2025:106842. https:\/\/doi.org\/10.1016\/j.pep.2025.106842","journal-title":"Protein Expression and Purification"},{"key":"10255_CR1","doi-asserted-by":"publisher","first-page":"277","DOI":"10.1007\/BF00197809","volume":"6","author":"F Delaglio","year":"1995","unstructured":"Delaglio F, Grzesiek S, Vuister GW, Zhu G, Pfeifer J, Bax A (1995) NMRPipe: a multidimensional spectral processing system based on UNIX pipes. J Biomol NMR 6:277\u2013293. https:\/\/doi.org\/10.1007\/BF00197809","journal-title":"J Biomol NMR"},{"key":"10255_CR2","doi-asserted-by":"publisher","first-page":"827","DOI":"10.1038\/s41573-019-0037-0","volume":"18","author":"GC Fanning","year":"2019","unstructured":"Fanning GC, Zoulim F, Hou J, Bertoletti A (2019) Therapeutic strategies for hepatitis B virus infection: towards a cure. 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