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Herein, we present nearly complete <jats:sup>1<\/jats:sup>H, <jats:sup>15<\/jats:sup>N, and <jats:sup>13<\/jats:sup>C backbone and <jats:sup>1<\/jats:sup>H, <jats:sup>13<\/jats:sup>C isoleucine, valine, and leucine methyl resonance assignment of the apo S135A catalytically inactive variant of the DENV 2 protease enzyme folded as a tandem formed between the serine protease domain NS3pro and the cofactor NS2B, as well as the secondary structure prediction of this complex based on the assigned chemical shifts using the TALOS-N software. 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