ITC data for HIV-1 RevFL interaction with NPM1 variants.

Ka, association constant; Kd, dissociation constant; ΔH, enthalpy; n, binding stoichiometry (number of binding sites). HIV-1 RevFL did not show any binding to the RNA-binding domain (RBD) of NPM1. All measurements were performed at 25°C.a Kd values were calculated from Kd = 1/Ka.ITC data for HIV-1 RevFL interaction with NPM1 variants.

Ka（association constant，结合常数）；Kd（dissociation constant，解离常数）；ΔH（enthalpy，焓）；n为结合化学计量数（即结合位点数）。HIV-1 RevFL未表现出与NPM1的RNA结合结构域（RNA-binding domain, RBD）的结合。所有测定均在25℃条件下完成。注a：Kd值通过公式Kd = 1/Ka计算得到。本数据集包含HIV-1 RevFL与NPM1变体相互作用的等温滴定量热（Isothermal Titration Calorimetry, ITC）实验数据。