2MZU

Extending the eNOE data set of large proteins by evaluation of NOEs with unresolved diagonals

2MZU の概要

• エントリーDOI: 10.2210/pdb2mzu/pdb
• NMR情報: BMRB: 25502
• 分子名称: Peptidyl-prolyl cis-trans isomerase A (1 entity in total)
• 機能のキーワード: cyclophilin a, isomerase
• 由来する生物種: Homo sapiens (human)
• 細胞内の位置: Cytoplasm : P62937
• タンパク質・核酸の鎖数: 1
• 化学式量合計: 18036.50

構造登録者

Chi, C.N.,Strotz, D.,Riek, R.,Voegeli, B. (登録日: 2015-02-24, 公開日: 2015-04-22, 最終更新日: 2024-05-15)

主引用文献

Chi, C.N.,Strotz, D.,Riek, R.,Vogeli, B.
Extending the eNOE data set of large proteins by evaluation of NOEs with unresolved diagonals.
J.Biomol.Nmr, 62:63-69, 2015

PubMed Abstract: The representation of a protein's spatial sampling at atomic resolution is fundamental for understanding its function. NMR has been established as the best-suited technique toward this goal for small proteins. However, the accessible information content rapidly deteriorates with increasing protein size. We have recently demonstrated that for small proteins distance restraints with an accuracy smaller than 0.1 Å can be obtained by replacing traditional semi-quantitative Nuclear Overhauser Effects (NOEs) with exact NOEs (eNOE). The high quality of the data allowed us to calculate structural ensembles of the small model protein GB3 consisting of multiple rather than a single state. The analysis has been limited to small proteins because NOEs of spins with unresolved diagonal peaks cannot be used. Here we propose a simple approach to translate such NOEs into correct upper distance restraints, which opens access to larger biomolecules. We demonstrate that for 16 kDa cyclophilin A the collection of such restraints extends the original 1254 eNOEs to 3471.

PubMed: 25749872
DOI: 10.1007/s10858-015-9917-8

実験手法

SOLUTION NMR