NMR and circular dichroism data for domain 2 of the HCV NS5A protein phosphorylated by the Casein Kinase II

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NMR and circular dichroism data for domain 2 of the HCV NS5A protein phosphorylated by the Casein Kinase II

Publication date: Available online 31 January 2018
Source:Data in Brief

Author(s): Luiza M. Bessa, Robert Schneider, Xavier Hanoulle

The Hepatitis C Virus (HCV) 1 1 HCV: Hepatitis C Virus; HSQC: heteronuclear single-quantum coherence; NS5A: nonstructural protein 5A; NS5A-D2: domain 2 of the nonstructural protein 5A; CKII: Casein kinase II, NS5A-D2_CKII: NS5A-D2 phosphorylated by CKII; CSP: combined chemical shift perturbations; THP: (Tris(hydroxypropyl)phosphine). nonstructural 5A protein (NS5A) is a phosphoprotein [1,2] composed of an N-terminal well-structured domain and two C-terminal intrinsically disordered domains [3–5]. So far, no precise molecular function has been identified for this viral protein [6] which is required for viral replication [7]. In this article, we present datasets of NMR and circular dichroism analyses of the domain 2 of the HCV NS5A protein (NS5A-D2) phosphorylated in vitro by the Casein Kinase II (CKII) [8–11]. We describe the in vitro phosphorylation of the serine 288 (pS288) of NS5A-D2 by CKII and report the circular dichroism spectrum of the phosphorylated domain (NS5-D2_CKII). This data article also contains the 1H, 15N and 13C NMR chemical shift assignments (HN, N, C?, C? and C’) for the phosphorylated NS5A-D2 domain, and an assigned 1H,15N-HSQC spectrum is shown. The NMR data have been acquired on an 800MHz spectrometer. These NMR data have been used to calculate both the 1H,15N combined chemical shift perturbations (CSP) induced by the phosphorylation of pS288 and the secondary structural propensity (SSP) scores that describe the structural tendencies in this intrinsically disordered domain. The circular dichroism spectrum and the SSP scores of NS5A-D2_CKII have been compared with those of unphosphorylated NS5A-D2 [12,13].







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