mdCATH:用于数据驱动计算生物物理学的大规模 MD 数据集。

ArXiv Pub Date : 2024-12-03
Antonio Mirarchi, Toni Giorgino, Gianni De Fabritiis
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引用次数: 0

摘要

蛋白质结构测定的最新进展正在彻底改变我们对蛋白质的理解。尽管如此,关注蛋白质动力学的综合数据集的可用性仍然存在重大差距,这对于理解蛋白质功能,折叠和相互作用至关重要。为了解决这一关键问题,我们引入了mdCATH,这是一个通过广泛的全原子分子动力学模拟生成的数据集,模拟了多种具有代表性的蛋白质结构域。该数据集包括5,398个域的全原子系统,用最先进的经典力场建模,并在320 K至450 K的五个温度下进行了五次重复模拟。mdCATH数据集记录坐标和力每1ns,超过62毫秒的累积模拟时间,有效地捕获各种类型的结构域的动态,并为蛋白质展开热力学和动力学的蛋白质组范围的统计分析提供独特的资源。我们概述了数据集结构,并通过四个易于重复的案例研究展示了它的潜力,突出了它在推进蛋白质科学方面的能力。
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mdCATH: A Large-Scale MD Dataset for Data-Driven Computational Biophysics.

Recent advancements in protein structure determination are revolutionizing our understanding of proteins. Still, a significant gap remains in the availability of comprehensive datasets that focus on the dynamics of proteins, which are crucial for understanding protein function, folding, and interactions. To address this critical gap, we introduce mdCATH, a dataset generated through an extensive set of all-atom molecular dynamics simulations of a diverse and representative collection of protein domains. This dataset comprises all-atom systems for 5,398 domains, modeled with a state-of-the-art classical force field, and simulated in five replicates each at five temperatures from 320 K to 450 K. The mdCATH dataset records coordinates and forces every 1 ns, for over 62 ms of accumulated simulation time, effectively capturing the dynamics of the various classes of domains and providing a unique resource for proteome-wide statistical analyses of protein unfolding thermodynamics and kinetics. We outline the dataset structure and showcase its potential through four easily reproducible case studies, highlighting its capabilities in advancing protein science.

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