1XPW

Solution NMR Structure of human protein HSPCO34. Northeast Structural Genomics Target HR1958

1XPW の概要

• エントリーDOI: 10.2210/pdb1xpw/pdb
• 関連するPDBエントリー: 1TVG
• NMR情報: BMRB: 6344
• 分子名称: LOC51668 protein (1 entity in total)
• 機能のキーワード: gene pp25, locus loc51668, c1orf41, homo sapiens, nesgc cluster id 3237, target hr1958, structural genomics, apc10-related protein, northeast structural genomics consortium, protein structure initiative, psi, jellyroll, beta-sandwich, unknown function
• 由来する生物種: Homo sapiens (human)
• タンパク質・核酸の鎖数: 1
• 化学式量合計: 17442.54

構造登録者

Ramelot, T.A.,Xiao, R.,Ma, L.C.,Acton, T.B.,Montelione, G.T.,Kennedy, M.A.,Northeast Structural Genomics Consortium (NESG) (登録日: 2004-10-09, 公開日: 2004-11-09, 最終更新日: 2024-05-22)

主引用文献

Ramelot, T.A.,Raman, S.,Kuzin, A.P.,Xiao, R.,Ma, L.C.,Acton, T.B.,Hunt, J.F.,Montelione, G.T.,Baker, D.,Kennedy, M.A.
Improving NMR protein structure quality by Rosetta refinement: a molecular replacement study.
Proteins, 75:147-167, 2009

PubMed Abstract: The structure of human protein HSPC034 has been determined by both solution nuclear magnetic resonance (NMR) spectroscopy and X-ray crystallography. Refinement of the NMR structure ensemble, using a Rosetta protocol in the absence of NMR restraints, resulted in significant improvements not only in structure quality, but also in molecular replacement (MR) performance with the raw X-ray diffraction data using MOLREP and Phaser. This method has recently been shown to be generally applicable with improved MR performance demonstrated for eight NMR structures refined using Rosetta (Qian et al., Nature 2007;450:259-264). Additionally, NMR structures of HSPC034 calculated by standard methods that include NMR restraints have improvements in the RMSD to the crystal structure and MR performance in the order DYANA, CYANA, XPLOR-NIH, and CNS with explicit water refinement (CNSw). Further Rosetta refinement of the CNSw structures, perhaps due to more thorough conformational sampling and/or a superior force field, was capable of finding alternative low energy protein conformations that were equally consistent with the NMR data according to the Recall, Precision, and F-measure (RPF) scores. On further examination, the additional MR-performance shortfall for NMR refined structures as compared with the X-ray structure were attributed, in part, to crystal-packing effects, real structural differences, and inferior hydrogen bonding in the NMR structures. A good correlation between a decrease in the number of buried unsatisfied hydrogen-bond donors and improved MR performance demonstrates the importance of hydrogen-bond terms in the force field for improving NMR structures. The superior hydrogen-bond network in Rosetta-refined structures demonstrates that correct identification of hydrogen bonds should be a critical goal of NMR structure refinement. Inclusion of nonbivalent hydrogen bonds identified from Rosetta structures as additional restraints in the structure calculation results in NMR structures with improved MR performance.

PubMed: 18816799
DOI: 10.1002/prot.22229

実験手法

SOLUTION NMR