PED 2027 发布：整合实验与预测的蛋白质构象集合
PED in 2027: integrating experimental and predicted protein conformational ensembles at scale
蛋白质构象集合数据库 PED 发布 2027 版本（2026 年 9 月上线），在原有实验解析的构象集合之外，整合了明确标注来源的计算预测集合。新版本包含面向 3319 个 DisProt 蛋白和 2452 个人工整理无序区的多方法集合，以及覆盖 10 022 个含 IDR 人类蛋白的 AlphaFlex 集合；同一序列的不同预测作为独立记录保留，并标注各自方法来源，便于跨方法比较。数据库提供可扩展的提交流程，兼顾单项实验研究与蛋白质组规模集合，并保留质量控制和策展审核；受控词表统一描述实验数据获取、计算生成、筛选与精修。
来源：Nucleic Acids Research · doi.org
数据库把实验解析与计算预测的构象集合分开标注并保留方法来源，便于比较不同生成方式得到的构象集合。
The Protein Ensemble Database (PED; https://proteinensemble.org) is the primary deposition resource for structural ensembles of intrinsically disordered proteins (IDPs) and intrinsically disordered regions (IDRs). PED 2027 (released in September 2026) substantially expands its scope by integrating ensembles determined or refined using experimental data with clearly identified collections of computational predictions. The release introduces a multi-method collection targeting 3319 DisProt proteins and 2452 manually curated disordered regions, together with AlphaFlex ensembles for 10 022 human proteins containing IDRs. Alternative predictions for the same sequence are retained as independent records with method-specific provenance, enabling comparison across ensemble-generation approaches. A scalable deposition workflow accommodates individual experimental studies and proteome-scale collections while preserving quality control and curator oversight. The PED controlled vocabulary standardizes experimental data acquisition, computational generation, selection, and refinement. Precomputed IDPEnsembleTools and CIDER analyses provide structural and sequence-derived descriptors directly on ensemble pages. A redesigned interface and extended REST API support discovery, visualization, download and programmatic access. Interoperability with UniProt, DisProt, MobiDB, and experimental-data repositories connects ensembles with sequences, annotations, and supporting measurements. PED 2027 therefore provides an interoperable, analysis-ready platform for studying IDP/IDR conformational behaviour.