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Automatic structure-based NMR methyl resonance assignment in large proteins

Authors :
T. Reid Alderson
Iva Pritišanac
Peter Güntert
Julia M. Würz
Source :
Nature Communications, Vol 10, Iss 1, Pp 1-12 (2019), Nature Communications, Nature Communications, 10 (1)
Publication Year :
2019
Publisher :
Nature Publishing Group, 2019.

Abstract

Isotopically labeled methyl groups provide NMR probes in large, otherwise deuterated proteins. However, the resonance assignment constitutes a bottleneck for broader applicability of methyl-based NMR. Here, we present the automated MethylFLYA method for the assignment of methyl groups that is based on methyl-methyl nuclear Overhauser effect spectroscopy (NOESY) peak lists. MethylFLYA is applied to five proteins (28–358 kDa) comprising a total of 708 isotope-labeled methyl groups, of which 612 contribute NOESY cross peaks. MethylFLYA confidently assigns 488 methyl groups, i.e. 80% of those with NOESY data. Of these, 459 agree with the reference, 6 were different, and 23 were without reference assignment. MethylFLYA assigns significantly more methyl groups than alternative algorithms, has an average error rate of 1%, modest runtimes of 0.4–1.2 h, and can handle arbitrary isotope labeling patterns and data from other types of NMR spectra.<br />Nature Communications, 10 (1)<br />ISSN:2041-1723

Details

Language :
English
ISSN :
20411723
Volume :
10
Issue :
1
Database :
OpenAIRE
Journal :
Nature Communications
Accession number :
edsair.doi.dedup.....b153e8ae4395e41f74bcebb35de7a552
Full Text :
https://doi.org/10.1038/s41467-019-12837-8