ArticleJournal of biomolecular NMR2014
Robust and highly accurate automatic NOESY assignment and structure determination with Rosetta.
Article in Journal of biomolecular NMR, 2014. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 19 papers.
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Who cites it
19 citing papers in PubMed.
- Recent Advances in NMR Protein Structure Prediction with ROSETTA.International journal of molecular sciences · 2023Review
- High-throughput mutagenesis reveals unique structural features of human ADAR1.Nature communications · 2020Article
- CS-ROSETTA.Methods in enzymology · 2019Article
- POTENCI: prediction of temperature, neighbor and pH-corrected chemical shifts for intrinsically disordered proteins.Journal of biomolecular NMR · 2018Article
- Automated NMR resonance assignments and structure determination using a minimal set of 4D spectra.Nature communications · 2018Article
- Web-accessible molecular modeling with Rosetta: The Rosetta Online Server that Includes Everyone (ROSIE).Protein science : a publication of the Protein Society · 2018Article
- Modern Technologies of Solution Nuclear Magnetic Resonance Spectroscopy for Three-dimensional Structure Determination of Proteins Open Avenues for Life Scientists.Computational and structural biotechnology journal · 2017Review
- Protocols for Molecular Modeling with Rosetta3 and RosettaScripts.Biochemistry · 2016Review
- Guiding automated NMR structure determination using a global optimization metric, the NMR DP score.Journal of biomolecular NMR · 2015Article
- NMR data-driven structure determination using NMR-I-TASSER in the CASD-NMR experiment.Journal of biomolecular NMR · 2015Article
- Combined automated NOE assignment and structure calculation with CYANA.Journal of biomolecular NMR · 2015Article
- Improved reliability, accuracy and quality in automated NMR structure calculation with ARIA.Journal of biomolecular NMR · 2015Article
- CASD-NMR 2: robust and accurate unsupervised analysis of raw NOESY spectra and protein structure determination with UNIO.Journal of biomolecular NMR · 2015Article
- Analysis of the performance of the CHESHIRE and YAPP methods at CASD-NMR round 3.Journal of biomolecular NMR · 2015Article
- The second round of Critical Assessment of Automated Structure Determination of Proteins by NMR: CASD-NMR-2013.Journal of biomolecular NMR · 2015Article
- Systematic evaluation of combined automated NOE assignment and structure calculation with CYANA.Journal of biomolecular NMR · 2015Article
- Article
- High-resolution structure of the Shigella type-III secretion needle by solid-state NMR and cryo-electron microscopy.Nature communications · 2014Article
- Automatic NOESY assignment in CS-RASREC-Rosetta.Journal of biomolecular NMR · 2014Article
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Authors and funding
4 authors.
Funding
No grant is acknowledged in the PubMed record.
Abstract
We have developed a novel and robust approach for automatic and unsupervised simultaneous nuclear Overhauser effect (NOE) assignment and structure determination within the CS-Rosetta framework. Starting from unassigned peak lists and chemical shift assignments, autoNOE-Rosetta determines NOE cross-peak assignments and generates structural models. The approach tolerates incomplete and raw NOE peak lists as well as incomplete or partially incorrect chemical shift assignments, and its performance has been tested on 50 protein targets ranging from 50 to 200 residues in size. We find a significantly improved performance compared to established programs, particularly for larger proteins and for NOE data obtained on perdeuterated protein samples. X-ray crystallographic structures allowed comparison of Rosetta and conventional, PDB-deposited, NMR models in 20 of 50 test cases. The unsupervised autoNOE-Rosetta models were often of significantly higher accuracy than the corresponding expert-supervised NMR models deposited in the PDB. We also tested the method with unrefined peak lists and found that performance was nearly as good as for refined peak lists. Finally, demonstrating our method's remarkable robustness against problematic input data, we provided correct models for an incorrect PDB-deposited NMR solution structure.
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