Data from: Formation of beta-strands in the extramembrane controls dimerization of transmembrane helices in amyloid precursor protein C99 intrinsically disordered domains

Within this data set are 1) Conformations of the 99-residue C-terminal domain of Amyloid Precursor Protein (C99), which is processed to form amyloid beta, in a POPC lipid bilayer and 150 mM NaCl aqueous solvent. 2) Input parameters for gREST simulations of C99 monomer and homodimer in the GENESIS molecular dynamics simulation package. 3) NMR peak intensity ratios (I/I0) due to addition of paramagnetic probes measured at dilute C99 concentrations.本数据集包含如下内容： 1) 99残基的淀粉样前体蛋白（Amyloid Precursor Protein, APP）C端结构域（C99）的构象数据；该结构域经蛋白水解剪切后可生成β淀粉样蛋白（amyloid beta, Aβ），相关构象数据采集于1-棕榈酰-2-油酰-sn-甘油-3-磷酸胆碱（POPC）脂质双分子层与150 mM氯化钠水溶液溶剂体系中。 2) 适配GENESIS分子动力学模拟软件包的、用于C99单体与同二聚体的广义副本交换溶质温控（Generalized Replica Exchange with Solute Tempering, gREST）模拟输入参数。 3) 在低浓度C99体系中测得的、因添加顺磁探针而产生的核磁共振（Nuclear Magnetic Resonance, NMR）峰强比（I/I0）数据。