Various methods for understanding the structural and dynamic properties of proteins rely on the analysis of their NMR chemical shifts. These methods require the initial assignment of NMR signals to particular atoms in the sequence of the protein, a step that can be very time-consuming. The probabilistic interaction network of evidence (PINE) algorithm for automated assignment of backbone and side chain chemical shifts utilizes a Bayesian probabilistic network model that analyzes sequence data and peak lists from multiple NMR experiments. PINE, which is one of the most popular and reliable automated chemical shift assignment algorithms, has been available to the protein NMR community for longer than a decade. We announce here a new web server version of PINE, called Integrative PINE (I-PINE), which supports more types of NMR experiments than PINE (including three-dimensional nuclear Overhauser enhancement and four-dimensional J-coupling experiments) along with more comprehensive visualization of chemical shift based analysis of protein structure and dynamics. The I-PINE server is freely accessible at http://i-pine.nmrfam.wisc.edu . Help pages and tutorial including browser capability are available at: http://i-pine.nmrfam.wisc.edu/instruction.html . Sample data that can be used for testing the web server are available at: http://i-pine.nmrfam.wisc.edu/examples.html .

中文翻译：

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I-PINE Web 服务器：蛋白质的综合概率 NMR 分配系统。

了解蛋白质结构和动态特性的各种方法都依赖于对其 NMR 化学位移的分析。这些方法需要将 NMR 信号初始分配给蛋白质序列中的特定原子，这一步骤可能非常耗时。用于自动分配主链和侧链化学位移的概率相互作用证据网络 (PINE) 算法利用贝叶斯概率网络模型来分析来自多个 NMR 实验的序列数据和峰列表。PINE 是最流行、最可靠的自动化学位移分配算法之一，已在蛋白质 NMR 社区中使用了十多年。我们在此发布 PINE 的新 Web 服务器版本，称为 Integrative PINE (I-PINE)，它支持比 PINE 更多类型的 NMR 实验（包括三维核 Overhauser 增强和四维 J 耦合实验）以及更全面的功能基于化学位移的蛋白质结构和动力学分析的可视化。I-PINE 服务器可通过 http://i-pine.nmrfam.wisc.edu 免费访问。帮助页面和教程（包括浏览器功能）可从以下网址获取：http://i-pine.nmrfam.wisc.edu/instruction.html。可用于测试 Web 服务器的示例数据位于：http://i-pine.nmrfam.wisc.edu/examples.html。