Related Experiment Video
Updated: Mar 31, 2026
Atomic Scale Structural Studies of Macromolecular Assemblies by Solid-state Nuclear Magnetic Resonance Spectroscopy
Published on: September 17, 2017
NMRe: a web server for NMR protein structure refinement with high-quality structure validation scores
Hyojung Ryu1, GyuTae Lim1, Bong Hyun Sung2
1Korean Bioinformation Center (KOBIC), Korea Research Institute of Bioscience and Biotechnology, Yuseong-gu, Daejeon 305-806, the Republic of Korea, Department of Nanobiotechnology and Bioinformatics, University of Science and Technology, Yuseong-Gu, Daejeon 305-350, the Republic of Korea and.
NMRe is a new web server that refines nuclear magnetic resonance (NMR) structures using the Statistical Torsion Angle Potential (STAP) energy function. It improves NMR structure quality using NOE data or generated NOE-like restraints.
Area of Science:
- Structural Biology
- Biophysics
- Computational Biology
Background:
- Protein structure refinement is crucial for understanding protein function.
- Nuclear Magnetic Resonance (NMR) structures often require refinement compared to X-ray crystallographic structures.
Purpose of the Study:
- To present NMRe, a novel web-based server for refining NMR structures.
- To enhance the quality of NMR-derived protein structures.
Main Methods:
- Utilized the knowledge-based Statistical Torsion Angle Potential (STAP) energy function for refinement.
- Implemented two refinement protocols: one using Nuclear Overhauser Effect (NOE) data and another generating NOE-like restraints from input structures.
- Validated NMRe on 20 NMR structures.
Main Results:
- Most quality assessment scores for refined NMR structures showed improvement over original structures.
- NMRe provides comprehensive refinement results including 3D structure views, secondary structure schemes, and validation scores.
Conclusions:
- NMRe effectively refines NMR structures, leading to improved quality.
- The server offers a valuable tool for structural biologists studying protein function through NMR data.
