SpringerImages - 2D [15N, 1H]-HSQC spectrum of uniformly [13C, 15N]-labeled nsp3(1066–1181) (protein concentration 1.4 mM, 50 mM phosphate buffer at pH 6.5, 50 mM NaCl, 2 mM NaN3). The spectrum was recorded at a 1H frequency of 600 MHz, T = 25°C, with 256 increments in the 15N dimension and 4 scans/increment. Resonance assignments are indicated by the sequence numbers in the presently studied construct, which correspond to the residues 1066–1181 of nsp3 (see text). Side chain amide resonances were assigned for eight residues of asparagine and glutamine; these are connected by horizontal lines

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Fig 1

2D [¹⁵N, ¹H]-HSQC spectrum of uniformly [¹³C, ¹⁵N]-labeled nsp3(1066–1181) (protein concentration 1.4 mM, 50 mM phosphate buffer at pH 6.5, 50 mM NaCl, 2 mM NaN₃). The spectrum was recorded at a ¹H frequency of 600 MHz, T = 25°C, with 256 increments in the ¹⁵N dimension and 4 scans/increment. Resonance assignments are indicated by the sequence numbers in the presently studied construct, which correspond to the residues 1066–1181 of nsp3 (see text). Side chain amide resonances were assigned for eight residues of asparagine and glutamine; these are connected by horizontal lines

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The numbers above the sequence represent the numbering in the full-length nsp3 protein, and below the sequence the numbering for the construct used in this study is given, which is also used in the Figs. 1 and 2 .

High-quality NMR data were obtained, as illustrated by the [ ¹⁵ N, ¹ H]-HSQC spectrum shown in Fig. 1 .

The chemical shifts of the side chain amide groups of eight of the eleven Asn and Gln residues were also assigned, as is indicated in Fig. 1 .

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