Soares Rosemberg O, Torres Pedro H M, da Silva Manuela L, Pascutti Pedro G
Instituto de Biofísica Carlos Chagas Filho (IBCCF), Universidade Federal do Rio de Janeiro (UFRJ), Rio de Janeiro, Brazil; Diretoria de Metrologia Aplicada às Ciências da Vida (DIMAV), Instituto Nacional de Metrologia Qualidade e Tecnologia (INMETRO), Xerém, Brazil.
Instituto de Biofísica Carlos Chagas Filho (IBCCF), Universidade Federal do Rio de Janeiro (UFRJ), Rio de Janeiro, Brazil.
Data Brief. 2016 Jul 25;8:1144-50. doi: 10.1016/j.dib.2016.07.040. eCollection 2016 Sep.
The data described here supports the research article "Unraveling HIV Protease Flaps Dynamics by Constant pH Molecular Dynamics Simulations" (Soares et al., 2016) [1]. The data involves both standard Molecular Dynamics (MD) and Constant pH Molecular Dynamics (CpHMD) to elucidate the effect of protonation states of catalytic dyad on the HIV-PR conformation. The data obtained from MD simulation demonstrate that the protonation state of the two aspartic acids (Asp25/Asp25') has a strong influence on the dynamics of the HIV-PR. Regarding the CpHMD simulation, we performed pka calculations for HIV-PR and the data indicate that only one catalytic aspartate should be protonated.
此处描述的数据支持研究论文《通过恒定pH分子动力学模拟解析HIV蛋白酶的瓣片动力学》（索阿雷斯等人，2016年）[1]。该数据涉及标准分子动力学（MD）和恒定pH分子动力学（CpHMD），以阐明催化二元组的质子化状态对HIV-PR构象的影响。从MD模拟获得的数据表明，两个天冬氨酸（Asp25/Asp25'）的质子化状态对HIV-PR的动力学有强烈影响。关于CpHMD模拟，我们对HIV-PR进行了pKa计算，数据表明只有一个催化天冬氨酸应该被质子化。
