IntAct European Bioinformatics Institute IntAct intact http://www.ebi.ac.uk/ http://www.ebi.ac.uk/intact/query/${ac} EBI-[0-9]+|IA:[0-9]+ INTerAction database (IntAct) provides an open source database and toolkit for the storage, presentation and analysis of molecular interactions. http://www.ebi.ac.uk/intact European Bioinformatics Institute; Wellcome Trust Genome Campus; Hinxton, Cambridge; CB10 1SD; United Kingdom http://www.ebi.ac.uk/intact/ Crystal structure of SARS-CoV-2 main protease provides a basis for design of improved α-ketoamide inhibitors. Crystal structure of SARS-CoV-2 main protease provides a basis for design of improved α-ketoamide inhibitors. Science (New York, N.Y.) 2020 imex curation Zhang L., Lin D., Sun X., Curth U., Drosten C., Sauerhering L., Becker S., Rox K., Hilgenfeld R. Virus - Publications including interactions involving viral proteins Coronavirus - Interactions investigated in the context of Coronavirus There are several Methods for an Enzyme Assay (protein cleavage), but NO RESULTS/Figures other than the text:- "Compound 13b inhibits the purified recombinant SARS-CoV-2 Mpro with IC50 = 0.67 ± 0.18 μM. The corresponding IC50 values for inhibition of the SARS-CoV Mpro and the MERS-CoV Mpro are 0.90 ± 0.29 μM and 0.58 ± 0.22 μM, respectively." I decided not to enter any of this as I can see no experimental data, and there is no mention of any MERS construct elsewhere in the publication, so these may be results from another publication. rolf.hilgenfeld@uni-luebeck.de Only protein-protein interactions imex curation in vitro In vitro x-ray diffraction x-ray crystallography X-ray X-ray x-ray diffraction predetermined predetermined participant predetermined Zhang L., Lin D., Sun X., Curth U., Drosten C., Sauerhering L., Becker S., Rox K., Hilgenfeld R. Virus - Publications including interactions involving viral proteins There are several Methods for an Enzyme Assay (protein cleavage), but NO RESULTS/Figures other than the text:- "Compound 13b inhibits the purified recombinant SARS-CoV-2 Mpro with IC50 = 0.67 ± 0.18 μM. The corresponding IC50 values for inhibition of the SARS-CoV Mpro and the MERS-CoV Mpro are 0.90 ± 0.29 μM and 0.58 ± 0.22 μM, respectively." I decided not to enter any of this as I can see no experimental data, and there is no mention of any MERS construct elsewhere in the publication, so these may be results from another publication. rolf.hilgenfeld@uni-luebeck.de Accepted 2020-MAY-27 AT 07:48 BST AT 07:48 BST by KALPANAP Science (New York, N.Y.) 2020 Only protein-protein interactions imex curation imex curation Crystal structure of SARS-CoV-2 main protease provides a basis for design of improved α-ketoamide inhibitors. Crystal structure of SARS-CoV-2 main protease provides a basis for design of improved α-ketoamide inhibitors. Science (New York, N.Y.) 2020 imex curation Zhang L., Lin D., Sun X., Curth U., Drosten C., Sauerhering L., Becker S., Rox K., Hilgenfeld R. Virus - Publications including interactions involving viral proteins Coronavirus - Interactions investigated in the context of Coronavirus There are several Methods for an Enzyme Assay (protein cleavage), but NO RESULTS/Figures other than the text:- "Compound 13b inhibits the purified recombinant SARS-CoV-2 Mpro with IC50 = 0.67 ± 0.18 μM. The corresponding IC50 values for inhibition of the SARS-CoV Mpro and the MERS-CoV Mpro are 0.90 ± 0.29 μM and 0.58 ± 0.22 μM, respectively." I decided not to enter any of this as I can see no experimental data, and there is no mention of any MERS construct elsewhere in the publication, so these may be results from another publication. rolf.hilgenfeld@uni-luebeck.de Only protein-protein interactions imex curation in vitro In vitro solution sedimentati cosedimentation in solution solution sedimentati predetermined predetermined participant predetermined Zhang L., Lin D., Sun X., Curth U., Drosten C., Sauerhering L., Becker S., Rox K., Hilgenfeld R. Virus - Publications including interactions involving viral proteins There are several Methods for an Enzyme Assay (protein cleavage), but NO RESULTS/Figures other than the text:- "Compound 13b inhibits the purified recombinant SARS-CoV-2 Mpro with IC50 = 0.67 ± 0.18 μM. The corresponding IC50 values for inhibition of the SARS-CoV Mpro and the MERS-CoV Mpro are 0.90 ± 0.29 μM and 0.58 ± 0.22 μM, respectively." I decided not to enter any of this as I can see no experimental data, and there is no mention of any MERS construct elsewhere in the publication, so these may be results from another publication. Info on SARS-CoV M pro is stated to be given in Refs. 14 and 20. Ref 14 states that "production and purification of SARS-CoV Mpro with authentic N and C termini ..." and references Xue-2007 which is Ref. 20 in this publication. The sequence was confirmed by reference to PDBe entry 1uk3, from Ref. 14. rolf.hilgenfeld@uni-luebeck.de Accepted 2020-MAY-27 AT 07:48 BST AT 07:48 BST by KALPANAP Science (New York, N.Y.) 2020 Only protein-protein interactions imex curation imex curation p0dtd1-pro_0000449623 3C-like proteinase nsp5 rep ORF1ab polyprotein 1a-1b protein protein SARS-CoV-2 SARS-CoV-2 SARS-CoV-2 Severe acute respiratory syndrome coronavirus 2 2019-nCoV SGFRKMAFPSGKVEGCMVQVTCGTTTLNGLWLDDVVYCPRHVICTSEDMLNPNYEDLLIRKSNHNFLVQAGNVQLRVIGHSMQNCVLKLKVDTANPKTPKYKFVRIQPGQTFSVLACYNGSPSGVYQCAMRPNFTIKGSFLNGSCGSVGFNIDYDCVSFCYMHHMELPTGVHAGTDLEGNFYGPFVDRQTAQAAGTDTTITVNVLAWLYAAVINGDRWFLNRFTTTLNDFNLVAMKYNYEPLTQDHVDILGPLSAQTGIAVLDMCASLKELLQNGMNGRTILGSALLEDEFTPFDVVRQCSGVTFQ 3264 3569 p0c6x7-pro_0000037312 3C-like proteinase nsp5 rep ORF1ab polyprotein 1a-1b protein protein sars-cov Human SARS coronavirus SARS-CoV Severe acute respiratory syndrome coronavirus SGFRKMAFPSGKVEGCMVQVTCGTTTLNGLWLDDTVYCPRHVICTAEDMLNPNYEDLLIRKSNHSFLVQAGNVQLRVIGHSMQNCLLRLKVDTSNPKTPKYKFVRIQPGQTFSVLACYNGSPSGVYQCAMRPNHTIKGSFLNGSCGSVGFNIDYDCVSFCYMHHMELPTGVHAGTDLEGKFYGPFVDRQTAQAAGTDTTITLNVLAWLYAAVINGDRWFLNRFTTTLNDFNLVAMKYNYEPLTQDHVDILGPLSAQTGIAVLDMCAALKELLQNGMNGRTILGSTILEDEFTPFDVVRQCSGVTFQ 3241 3546 8A3486F9E1A9A89D tert-butyl n-{1-[(1s)-1-{[(1r,2s)-1-(benzylcarbamoyl)-1-hydroxy-3-[(3s)-2-oxopyrrolidin-3-yl]propan-2-yl]carbamoyl}-2-cyclopropylethyl]-2-oxopyridin-3-yl}carbamate tert-butyl N-{1-[(1S)-1-{[(1R,2S)-1-(benzylcarbamoyl)-1-hydroxy-3-[(3S)-2-oxopyrrolidin-3-yl]propan-2-yl]carbamoyl}-2-cyclopropylethyl]-2-oxopyridin-3-yl}carbamate tert-butyl {1-[(2S)-1-({(2S,3R)-4-(benzylamino)-3-hydroxy-4-oxo-1-[(3S)-2-oxopyrrolidin-3-yl]butan-2-yl}amino)-3-cyclopropyl-1-oxopropan-2-yl]-2-oxo-1,2-dihydropyridin-3-yl}carbamate small molecule small molecule chemical synthesis Chemical synthesis (Chemical synthesis) rep-95 1 3 unspecified role unspecified role neutral component neutral component purified purified ecoli Escherichia coli (strain K12) direct interaction direct interaction Supp. Table 2 rep-96 1 5 unspecified role unspecified role neutral component neutral component chemical synthesis Chemical synthesis (Chemical synthesis) 3 unspecified role unspecified role neutral component neutral component purified purified ecoli Escherichia coli (strain K12) direct interaction direct interaction Supp. Table 2 rep-tert_butyl n_{1_[(1s)_1_{[(1r,2s)_1_(benzylcarbamoyl)_1_hydroxy_3_[(3s)_2_oxopyrrolidin_3_yl]propan_2_yl]carbamoyl}_2_cyclopropylethyl]_2_oxopyridin_3_yl}carbamate-1 1 5 unspecified role unspecified role neutral component neutral component chemical synthesis Chemical synthesis (Chemical synthesis) 3 unspecified role unspecified role neutral component neutral component purified purified ecoli Escherichia coli (strain K12) direct interaction direct interaction Supp. Table 2 rep-97 2 3 unspecified role unspecified role neutral component neutral component purified purified ecoli Escherichia coli (strain K12) direct interaction direct interaction Supp. Figure 10 A/C/D rep-98 2 4 unspecified role unspecified role neutral component neutral component purified purified ecoli Escherichia coli (strain K12) direct interaction direct interaction Supp. Figure 10 B/C/E