id	author	title	date	pages	extension	mime	words	sentences	flesch	summary	cache	txt
cord-294410-iy57tjx5	Zhang, Shengnan	(1)H, (13)C and (15)N resonance assignments of SARS-CoV main protease N-terminal domain	2010-12-23		.txt	text/plain	1013	60	65	title: (1)H, (13)C and (15)N resonance assignments of SARS-CoV main protease N-terminal domain The main protease (M(pro)) of severe acute respiratory syndrome coronavirus (SARS-CoV) plays an essential role in the extensive proteolytic processing of the viral polyproteins (pp1a and pp1ab), and it is an important target for anti-SARS drug development. Here, we reported the NMR assignments of the SARS-CoV M(pro) N-terminal domain alone, which are essential for its solution structure determination. The backbone resonance chemical shift assignments were based on 2D 1 H-15 N HSQC, 3D HNCA, HN(CO)CA, HNCACB, CBCA(CO)HN, HNCO, HN(CA)CO and HBHA(CO)NH NMR spectra. The side chain resonance chemical shift assignments were based on 3D HCCH-COSY, HCCH-TOCSY, (H)CCH-COSY, and (H)CCH-TOCSY NMR experiments data. Without its n-finger, SARS-CoV main protease can form a novel dimer through its C-terminal domain C-terminal domain of SARS-CoV main protease can form a 3D domain-swapped dimer	./cache/cord-294410-iy57tjx5.txt	./txt/cord-294410-iy57tjx5.txt