Journal
JOURNAL OF BIOMOLECULAR NMR
Volume 56, Issue 3, Pages 227-241Publisher
SPRINGER
DOI: 10.1007/s10858-013-9741-y
Keywords
Heteronuclear chemical shift; Secondary structure; Backbone and sidechain conformation; Dynamics; TALOS; Order parameter; Protein structure; SPARTA
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Funding
- NIDDK, NIH
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A new program, TALOS-N, is introduced for predicting protein backbone torsion angles from NMR chemical shifts. The program relies far more extensively on the use of trained artificial neural networks than its predecessor, TALOS+. Validation on an independent set of proteins indicates that backbone torsion angles can be predicted for a larger, a parts per thousand yen90 % fraction of the residues, with an error rate smaller than ca 3.5 %, using an acceptance criterion that is nearly two-fold tighter than that used previously, and a root mean square difference between predicted and crystallographically observed (I center dot, psi) torsion angles of ca 12A(0). TALOS-N also reports sidechain chi(1) rotameric states for about 50 % of the residues, and a consistency with reference structures of 89 %. The program includes a neural network trained to identify secondary structure from residue sequence and chemical shifts.
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