The Nsp9 Replicase Protein of Sars-Coronavirus, Structure and Functional Insights
PP1AB, ORF1AB, REPLICASE POLYPROTEIN 1AB
MSYYHHHHHHLESTSLYKKAGFLEVLFQGPNNELSPVALRQMSCAAGTTQTACTDDNALAYYNNSKGGRFVLALLSDHQD LKWARFPKSDGTGTIYTELEPPCRFVTDTPKGPKVKYLYFIKGLNNLNRGMVLGSLAATVRLQ
100MM CITRATE/PHOSPHATE PH3.8, 20% PEG 8000, PROTEIN CONCENTRATION 10MG/ML SITTING DROP 100NL + 100NL, pH 3.80
CORONAVIRUS MAIN PROTEINASE (3CLPRO) STRUCTURE : BASIS FORDESIGN OF ANTI-SARS DRUGS
3C-LIKE PROTEINASE DOMAIN STRUCTURE OF HUMAN CORONAVIRUS(STRAIN SARS) MODELED IN-SILICO
CRYSTAL STRUCTURE OF SARS CORONAVIRUS MAIN PROTEINASE(3CLPRO)
CRYSTAL STRUCTURE OF SARS CORONAVIRUS MAIN PROTEINASE(3CLPRO) AT PH8.0
CRYSTAL STRUCTURE OF SARS CORONAVIRUS MAIN PROTEINASE(3CLPRO) AT PH7.6
CRYSTAL STRUCTURE OF SARS CORONAVIRUS MAIN PROTEINASE(3CLPRO) COMPLEXED WITH AN INHIBITOR
THE 30 N-TERMINAL RESIDUES ARE THE N-TERMINAL TAG. THE FIRST NINE RESIDUES OF THE ENTRY CORRESPOND TO PART OF THE N-TERMINAL TAG ADDED TO FACILITATE PURIFICATION AND ARE NOT PART OF THE NATIVE PROTEIN.
VIRUS, VIRAL PROTEIN, REPLICASE PROTEIN, SARS, CORONAVIRUS, RNA-BINDING