Courtney Joseph M, Ye Qing, Nesbitt Anna E, Tang Ming, Tuttle Marcus D, Watt Eric D, Nuzzio Kristin M, Sperling Lindsay J, Comellas Gemma, Peterson Joseph R, Morrissey James H, Rienstra Chad M
Department of Chemistry, University of Illinois at Urbana-Champaign, Urbana, IL 61801, USA.
Center for Biophysics and Computational Biology, University of Illinois at Urbana-Champaign, Urbana, IL 61801, USA.
Structure. 2015 Oct 6;23(10):1958-1966. doi: 10.1016/j.str.2015.07.019. Epub 2015 Sep 10.
Standard methods for de novo protein structure determination by nuclear magnetic resonance (NMR) require time-consuming data collection and interpretation efforts. Here we present a qualitatively distinct and novel approach, called Comparative, Objective Measurement of Protein Architectures by Scoring Shifts (COMPASS), which identifies the best structures from a set of structural models by numerical comparison with a single, unassigned 2D (13)C-(13)C NMR spectrum containing backbone and side-chain aliphatic signals. COMPASS does not require resonance assignments. It is particularly well suited for interpretation of magic-angle spinning solid-state NMR spectra, but also applicable to solution NMR spectra. We demonstrate COMPASS with experimental data from four proteins--GB1, ubiquitin, DsbA, and the extracellular domain of human tissue factor--and with reconstructed spectra from 11 additional proteins. For all these proteins, with molecular mass up to 25 kDa, COMPASS distinguished the correct fold, most often within 1.5 Å root-mean-square deviation of the reference structure.
通过核磁共振（NMR）从头确定蛋白质结构的标准方法需要耗费大量时间进行数据收集和解读。在此，我们提出一种性质截然不同的新方法，称为通过评分位移比较客观地测量蛋白质结构（COMPASS），该方法通过与包含主链和侧链脂肪族信号的单个未归属二维（13）C-（13）C NMR谱进行数值比较，从一组结构模型中识别出最佳结构。COMPASS不需要共振归属。它特别适合于魔角旋转固态NMR谱的解读，但也适用于溶液NMR谱。我们用来自四种蛋白质（GB1、泛素、DsbA和人组织因子的细胞外结构域）的实验数据以及另外11种蛋白质的重建谱证明了COMPASS的有效性。对于所有这些分子量高达25 kDa的蛋白质，COMPASS能够区分出正确的折叠结构，大多数情况下与参考结构的均方根偏差在1.5 Å以内。
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