Dimeric conformation of MERS-CoV N-NTD (Figure S1); LibDock pose of dimeric MERS-CoV N-NTD with potent compounds (Figure S2); P3-induced aggregation of the MERS-CoV N protein sequesters the RNA-binding region on the N-CTD dimer (Figure S3); potential target sites for broad-spectrum antiviral compound development (Figure S4); antiviral activity of P3 against MHV (mouse hepatitis virus) (Figure S5); crystallographic data collection and refinement statistics (Table S1); pW43 docking pose with chemical structures, docking scores, and biochemical properties of 17 potential hits (Table S2); primers used for mutagenesis in this study (Table S3); molecular formula strings (PDF)