EFFICIENT COMPUTATION OF 3-DIMENSIONAL PROTEIN STRUCTURES IN SOLUTION FROM NUCLEAR-MAGNETIC-RESONANCE DATA USING THE PROGRAM DIANA AND THE SUPPORTING PROGRAMS CALIBA, HABAS AND GLOMSA
EFFICIENT COMPUTATION OF 3-DIMENSIONAL PROTEIN STRUCTURES IN SOLUTION FROM NUCLEAR-MAGNETIC-RESONANCE DATA USING THE PROGRAM DIANA AND THE SUPPORTING PROGRAMS CALIBA, HABAS AND GLOMSA
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DOI：
10.1016/0022-2836(91)90754-t
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发表时间：
1991-02-05
影响因子：
5.6
通讯作者：
WUTHRICH, K
中科院分区：
文献类型：
--
作者：
GUNTERT, P;BRAUN, W;WUTHRICH, K
本文介绍了一种基于DIANA程序，结合CALIBA、HABAS和GLOMSA等辅助程序，利用核磁共振（n.m.r）数据在溶液中高效计算蛋白质三维结构的新方法。本文第一部分介绍了DIANA、CALIBA和GLOMSA三个新项目。DIANA是一种新的、完全矢量化的可变目标函数算法，用于从核磁共振数据中计算蛋白质结构。与以前使用可变目标函数算法的程序相比，它的主要优点是大大减少了计算时间，并且对涉及未单独分配的非对映异构体氢原子群的实验距离约束进行了新颖的处理。CALIBA将测量到的核过大效应转换为距离上限，从而为前面描述的程序HABAS和DIANA准备输入。通过将实验约束与结构计算的初步结果进行比较，利用GLOMSA对非对映异构体取代基对进行个别赋值。目前使用的四个程序的组合，以其一般的费用，是特别友好的。在论文的第二部分，初步结果提出了对非对映位质子的新型DIANA处理对所得到的结构质量的影响，并系统地研究了在一系列不同的、常用的计算机上计算相同蛋白质结构所需的中央处理单元时间。
A novel procedure for efficient computation of three-dimensional protein structures from nuclear magnetic resonance (n.m.r.) data in solution is described, which is based on using the program DIANA in combination with the supporting programs CALIBA, HABAS and GLOMSA. The first part of this paper describes the new programs DIANA, CALIBA and GLOMSA. DIANA is a new, fully vectorized implementation of the variable target function algorithm for the computation of protein structures from n.m.r. data. Its main advantages, when compared to previously available programs using the variable target function algorithm, are a significant reduction of the computation time, and a novel treatment of experimental distance constraints involving diastereotopic groups of hydrogen atoms that were not individually assigned. CALIBA converts the measured nuclear Overhauser effects into upper distance limits and thus prepares the input for the previously described program HABAS and for DIANA. GLOMSA is used for obtaining individual assignments for pairs of diastereotopic substituents by comparison of the experimental constraints with preliminary results of the structure calculations. With its general outlay, the presently used combination of the four programs is particularly user-friendly. In the second part of the paper, initial results are presented on the influence of the novel DIANA treatment of diastereotopic protons on the quality of the structures obtained, and a systematic study of the central processing unit times needed for the same protein structure calculation on a range of different, commonly available computers is described.