ArticleJournal of biomolecular NMR2012
An automated system designed for large scale NMR data deposition and annotation: application to over 600 assigned chemical shift data entries to the BioMagResBank from the Riken Structural Genomics/Proteomics Initiative internal database.
Article in Journal of biomolecular NMR, 2012. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 15 papers.
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Who cites it
15 citing papers in PubMed.
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- Mechanisms of helix induction by the closed loop.Protein science : a publication of the Protein Society · 2025Article
- The 100-protein NMR spectra dataset: A resource for biomolecular NMR data analysis.Scientific data · 2024Article
- Presence of β-Turn Structure in Recombinant Spider Silk Dissolved in Formic Acid Revealed with NMR.Molecules (Basel, Switzerland) · 2022Article
- Mechanism of hERG inhibition by gating-modifier toxin, APETx1, deduced by functional characterization.BMC molecular and cell biology · 2021Article
- NMR Analysis on Molecular Interaction of Lignin with Amino Acid Residues of Carbohydrate-Binding Module from Trichoderma reesei Cel7A.Scientific reports · 2019Article
- Plastic roles of phenylalanine and tyrosine residues of TLS/FUS in complex formation with the G-quadruplexes of telomeric DNA and TERRA.Scientific reports · 2018Article
- NMR Detection of Semi-Specific Antibody Interactions in Serum Environments.Molecules (Basel, Switzerland) · 2017Article
- Structural Insight into the Recognition of r(UAG) by Musashi-1 RBD2, and Construction of a Model of Musashi-1 RBD1-2 Bound to the Minimum Target RNA.Molecules (Basel, Switzerland) · 2017Article
- 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
- The helical propensity of the extracellular loop is responsible for the substrate specificity of Fe(III)-phytosiderophore transporters.FEBS letters · 2016Article
- The impact of structural genomics: the first quindecennial.Journal of structural and functional genomics · 2016Review
- Solution structure of the ubiquitin-associated (UBA) domain of human autophagy receptor NBR1 and its interaction with ubiquitin and polyubiquitin.The Journal of biological chemistry · 2014Article
- Crystal structure of higher plant heme oxygenase-1 and its mechanism of interaction with ferredoxin.The Journal of biological chemistryArticle
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11 authors.
Funding
Abstract
Biomolecular NMR chemical shift data are key information for the functional analysis of biomolecules and the development of new techniques for NMR studies utilizing chemical shift statistical information. Structural genomics projects are major contributors to the accumulation of protein chemical shift information. The management of the large quantities of NMR data generated by each project in a local database and the transfer of the data to the public databases are still formidable tasks because of the complicated nature of NMR data. Here we report an automated and efficient system developed for the deposition and annotation of a large number of data sets including (1)H, (13)C and (15)N resonance assignments used for the structure determination of proteins. We have demonstrated the feasibility of our system by applying it to over 600 entries from the internal database generated by the RIKEN Structural Genomics/Proteomics Initiative (RSGI) to the public database, BioMagResBank (BMRB). We have assessed the quality of the deposited chemical shifts by comparing them with those predicted from the PDB coordinate entry for the corresponding protein. The same comparison for other matched BMRB/PDB entries deposited from 2001-2011 has been carried out and the results suggest that the RSGI entries greatly improved the quality of the BMRB database. Since the entries include chemical shifts acquired under strikingly similar experimental conditions, these NMR data can be expected to be a promising resource to improve current technologies as well as to develop new NMR methods for protein studies.
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