Improved methodology for protein NMR structure calculation using hydrogen bond restraints and ANSURR validation: The SH2 domain of SH2B1
Improved methodology for protein NMR structure calculation using hydrogen bond restraints and ANSURR validation: The SH2 domain of SH2B1
复制标题
DOI：
10.1016/j.str.2023.05.012
复制
发表时间：
2023-08-03
期刊：
影响因子：
5.7
通讯作者：
Williamson，Mike P.
中科院分区：
文献类型：
--
作者：
Fowler，Nicholas J.;Albalwi，Marym F.;Williamson，Mike P.
使用NMR数据计算的蛋白质结构不太准确，也不太明确。在这里，我们使用程序ANSURR表明，这种缺陷至少部分是由于缺乏氢键的限制。我们描述了一个协议，以系统和透明的方式将氢键约束引入SH2B1的SH2结构域的结构计算中，并表明生成的结构更准确，更好地定义为结果。我们还表明，ANSURR可以作为一个指南，知道什么时候结构计算是足够好，停止。
Protein structures calculated using NMR data are less accurate and less well-defined than they could be. Here we use the program ANSURR to show that this deficiency is at least in part due to a lack of hydrogen bond restraints. We describe a protocol to introduce hydrogen bond restraints into the structure calculation of the SH2 domain from SH2B1 in a systematic and transparent way and show that the structures generated are more accurate and better defined as a result. We also show that ANSURR can be used as a guide to know when the structure calculation is good enough to stop.