2M8W

Restrained CS-Rosetta Solution NMR Structure of Staphylococcus aureus protein SAV1430. Northeast Structural Genomics Target ZR18. Structure determination

2M8W の概要

• エントリーDOI: 10.2210/pdb2m8w/pdb
• 関連するPDBエントリー: 1PQX 2M6Q
• NMR情報: BMRB: 5844
• 分子名称: Uncharacterized protein (1 entity in total)
• 機能のキーワード: structural genomics, northeast structural genomics consortium, nesg, psi-biology, protein structure initiative, unknown function
• 由来する生物種: Staphylococcus aureus subsp. aureus
• タンパク質・核酸の鎖数: 1
• 化学式量合計: 10487.75

構造登録者

Mao, B.,Tejero, R.T.,Aramini, J.M.,Snyder, D.A.,Montelione, G.T.,Northeast Structural Genomics Consortium (NESG) (登録日: 2013-05-29, 公開日: 2013-08-21, 最終更新日: 2024-05-15)

主引用文献

Tejero, R.,Snyder, D.,Mao, B.,Aramini, J.M.,Montelione, G.T.
PDBStat: a universal restraint converter and restraint analysis software package for protein NMR.
J.Biomol.Nmr, 56:337-351, 2013

PubMed Abstract: The heterogeneous array of software tools used in the process of protein NMR structure determination presents organizational challenges in the structure determination and validation processes, and creates a learning curve that limits the broader use of protein NMR in biology. These challenges, including accurate use of data in different data formats required by software carrying out similar tasks, continue to confound the efforts of novices and experts alike. These important issues need to be addressed robustly in order to standardize protein NMR structure determination and validation. PDBStat is a C/C++ computer program originally developed as a universal coordinate and protein NMR restraint converter. Its primary function is to provide a user-friendly tool for interconverting between protein coordinate and protein NMR restraint data formats. It also provides an integrated set of computational methods for protein NMR restraint analysis and structure quality assessment, relabeling of prochiral atoms with correct IUPAC names, as well as multiple methods for analysis of the consistency of atomic positions indicated by their convergence across a protein NMR ensemble. In this paper we provide a detailed description of the PDBStat software, and highlight some of its valuable computational capabilities. As an example, we demonstrate the use of the PDBStat restraint converter for restrained CS-Rosetta structure generation calculations, and compare the resulting protein NMR structure models with those generated from the same NMR restraint data using more traditional structure determination methods. These results demonstrate the value of a universal restraint converter in allowing the use of multiple structure generation methods with the same restraint data for consensus analysis of protein NMR structures and the underlying restraint data.

PubMed: 23897031
DOI: 10.1007/s10858-013-9753-7

実験手法

SOLUTION NMR