Loading
PDBj
メニューPDBj@FacebookPDBj@X(formerly Twitter)PDBj@BlueSkyPDBj@YouTubewwPDB FoundationwwPDBDonate
RCSB PDBPDBeBMRBAdv. SearchSearch help

2LOY

Refined Miminal Constraint Solution NMR Structure of Translationally-controlled tumor protein (TCTP) from Caenorhabditis elegans, Northeast Structural Genomics Consortium Target WR73

2LOY の概要
エントリーDOI10.2210/pdb2loy/pdb
関連するPDBエントリー2KWB
NMR情報BMRB: 16833
分子名称Translationally-controlled tumor protein homolog (1 entity in total)
機能のキーワードstructural genomics, northeast structural genomics consortium (nesg), psi-biology, protein structure initiative, metal binding protein
由来する生物種Caenorhabditis elegans (nematode)
細胞内の位置Cytoplasm (By similarity): Q93573
タンパク質・核酸の鎖数1
化学式量合計21642.56
構造登録者
主引用文献Lange, O.F.,Rossi, P.,Sgourakis, N.G.,Song, Y.,Lee, H.W.,Aramini, J.M.,Ertekin, A.,Xiao, R.,Acton, T.B.,Montelione, G.T.,Baker, D.
Determination of solution structures of proteins up to 40 kDa using CS-Rosetta with sparse NMR data from deuterated samples.
Proc.Natl.Acad.Sci.USA, 109:10873-10878, 2012
Cited by
PubMed Abstract: We have developed an approach for determining NMR structures of proteins over 20 kDa that utilizes sparse distance restraints obtained using transverse relaxation optimized spectroscopy experiments on perdeuterated samples to guide RASREC Rosetta NMR structure calculations. The method was tested on 11 proteins ranging from 15 to 40 kDa, seven of which were previously unsolved. The RASREC Rosetta models were in good agreement with models obtained using traditional NMR methods with larger restraint sets. In five cases X-ray structures were determined or were available, allowing comparison of the accuracy of the Rosetta models and conventional NMR models. In all five cases, the Rosetta models were more similar to the X-ray structures over both the backbone and side-chain conformations than the "best effort" structures determined by conventional methods. The incorporation of sparse distance restraints into RASREC Rosetta allows routine determination of high-quality solution NMR structures for proteins up to 40 kDa, and should be broadly useful in structural biology.
PubMed: 22733734
DOI: 10.1073/pnas.1203013109
主引用文献が同じPDBエントリー
実験手法
SOLUTION NMR
構造検証レポート
Validation report summary of 2loy
検証レポート(詳細版)ダウンロードをダウンロード

252091

件を2026-04-15に公開中

PDB statisticsPDBj update infoContact PDBjnumon