2N4A

EC-NMR Structure of Ralstonia metallidurans Rmet_5065 Determined by Combining Evolutionary Couplings (EC) and Sparse NMR Data. Northeast Structural Genomics Consortium target CrR115

2N4A の概要

• エントリーDOI: 10.2210/pdb2n4a/pdb
• 関連するPDBエントリー: 2N42 2N44 2N45 2N46 2N47 2N48 2N49 2N4B 2N4C 2N4D 2N4F
• 分子名称: Uncharacterized protein (1 entity in total)
• 機能のキーワード: ahsa1, cog3832, pf08327, start domain, ec-nmr, structural genomics, unknown function, psi-biology, northeast structural genomics consortium, nesg
• 由来する生物種: Cupriavidus metallidurans CH34
• タンパク質・核酸の鎖数: 1
• 化学式量合計: 16136.81

構造登録者

Tang, Y.,Huang, Y.J.,Hopf, T.A.,Sander, C.,Marks, D.,Montelione, G.T.,Northeast Structural Genomics Consortium (NESG) (登録日: 2015-06-17, 公開日: 2015-07-01, 最終更新日: 2024-05-15)

主引用文献

Tang, Y.,Huang, Y.J.,Hopf, T.A.,Sander, C.,Marks, D.S.,Montelione, G.T.
Protein structure determination by combining sparse NMR data with evolutionary couplings.
Nat.Methods, 12:751-754, 2015

PubMed Abstract: Accurate determination of protein structure by NMR spectroscopy is challenging for larger proteins, for which experimental data are often incomplete and ambiguous. Evolutionary sequence information together with advances in maximum entropy statistical methods provide a rich complementary source of structural constraints. We have developed a hybrid approach (evolutionary coupling-NMR spectroscopy; EC-NMR) combining sparse NMR data with evolutionary residue-residue couplings and demonstrate accurate structure determination for several proteins 6-41 kDa in size.

PubMed: 26121406
DOI: 10.1038/nmeth.3455

実験手法

SOLUTION NMR