The NMR sample was supplied with 5% (v/v) D2O. All NMR spectra were acquired at 298 K on a Bruker 800 MHz AVANCE III spectrometer. Data were processed using NMRPipe (Delaglio et al. 1995) software and analyzed with CCPNMR Analysis (Vranken et al. 2005). Backbone resonance assignments were determined using the 15N–1H-HSQC spectrum (Fig. 1) together with a set of triple resonance experiments: HNCO, HN(CA)CO, HNCA, CBCA(CO)NH, HNCACB, and HBHA(CO)NH. Side-chain resonance assignments were performed using 13C-HSQC, (H)CCH-TOCSY, HCCH-TOCSY, and 15N and 13C-NOESY-HSQC experiments. The chemical shift of water proton was used as an internal reference for 1H while 13C and 15N chemical shifts were referenced indirectly to water (Wishart et al. 1995).

15N–1H-HSQC spectrum of the N-terminal domain (residues 56 to 193) of the nucleocapsid protein of hCoV-HKU1. Peak assignments are indicated by residue number and the one-letter amino acid code

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