NMR structure of the domain 527-651 of the SARS-CoV nonstructural protein nsp3
Joint Center for Structural Genomics (JCSG)
Nuclear magnetic resonance structure shows that the severe acute respiratory syndrome coronavirus-unique domain contains a macrodomain fold.
Non-structural protein 3 (Domain 527-651): Residues 1345-1469
pp1ab, ORF1ab polyprotein [includes: Replicase polyprotein 1a, Non-structural proteins 1,2,3,4, 3C-like proteinase, Non-structural proteins 6,7,8,9,10, RNA-directed RNA polymerase, Helicase, Exoribonuclease, Uridylate-specific endoribonuclease, Putative 2'-O-methyl transferase]
GSHMGTVSWNLREMLAHAEETRKLMPICMDVRAIMATIQRKYKGIKIQEGIVDYGVRFFFYTSKEPVASIITKLNSLNEP LVTMPIGYVTHGFNLEEAARCMRSLKAPAVVSVSSPDAVTTYNGYLTSS
NMR assignment of the domain 527-651 from the SARS-CoV nonstructural protein nsp3
NMR assignment of the domain 513-651 from the SARS-CoV nonstructural protein nsp3
NMR structure of the domain 527-651 of the SARS-CoV nonstructural protein nsp3, single conformer
NMR structure of the domain 513-651 of the SARS-CoV nonstructural protein nsp3, single conformer
NMR structure of the domain 513-651 of the SARS-CoV nonstructural protein nsp3, ensemble of twenty energy minimized structures
1.4 mM [U-99% 13C; U-98% 15N] nsp3(527-651), 25 mM sodium phosphate, 150 mM sodium chloride, 2 mM sodium azide, 10 % D2O, 90% H2O/10% D2O
SARS-CoV, SARS-unique domain, nonstructural protein, nsp3, nsp3c, Functional and Structural Proteomics of SARS-CoV-Related Proteins, FSPS, PSI-2, Protein Structure Initiative, Joint Center for Structural Genomics, JCSG, ATP-binding, Cytoplasm, Endonuclease, Exonuclease, Helicase, Hydrolase, Membrane, Metal-binding, Nuclease, Nucleotide-binding, Nucleotidyltransferase, Protease, Ribosomal frameshift, RNA replication, RNA-binding, RNA-directed RNA polymerase, Thiol protease, Transferase, Transmembrane, Zinc, Zinc-finger, VIRAL PROTEIN
GTVSWNLREMLAHAEETRKLMPICMDVRAIMATIQRKYKGIKIQEGIVDYGVRFFFYTSKEPVASIITKLNSLNEPLVTM PIGYVTHGFNLEEAARCMRSLKAPAVVSVSSPDAVTTYNGYLTSS