caa a22 4500 445325852 CHVBK 20180317142720.0 cr unu---uuuuu 170323e20110801xx s 000 0 eng 10.1007/s10858-011-9521-5 doi (NATIONALLICENCE)springer-10.1007/s10858-011-9521-5 Backbone resonance assignment and order tensor estimation using residual dipolar couplings [Elektronische Daten] [Paul Shealy, Yizhou Liu, Mikhail Simin, Homayoun Valafar] An NMR investigation of proteins with known X-ray structures is of interest in a number of endeavors. Performing these studies through nuclear magnetic resonance (NMR) requires the costly step of resonance assignment. The prevalent assignment strategy does not make use of existing structural information and requires uniform isotope labeling. Here we present a rapid and cost-effective method of assigning NMR data to an existing structure—either an X-ray or computationally modeled structure. The presented method, Exhaustively Permuted Assignment of RDCs (EPAR), utilizes unassigned residual dipolar coupling (RDC) data that can easily be obtained by NMR spectroscopy. The algorithm uses only the backbone N-H RDCs from multiple alignment media along with the amino acid type of the RDCs. It is inspired by previous work from Zweckstetter and provides several extensions. We present results on 13 synthetic and experimental datasets from 8 different structures, including two homodimers. Using just two alignment media, EPAR achieves an average assignment accuracy greater than 80%. With three media, the average accuracy is higher than 94%. The algorithm also outputs a prediction of the assignment accuracy, which has a correlation of 0.77 to the true accuracy. This prediction score can be used to establish the needed confidence in assignment accuracy. Springer Science+Business Media B.V., 2011 Assignment nationallicence Residual dipolar coupling nationallicence Refinement nationallicence Protein nationallicence Structure nationallicence RDC nationallicence NMR nationallicence Shealy Paul Department of Computer Science and Engineering, University of South Carolina, 315 Main Street, 29208, Columbia, SC, USA aut Liu Yizhou Complex Carbohydrate Research Center, University of Georgia, 30603, Athens, GA, USA aut Simin Mikhail Department of Computer Science and Engineering, University of South Carolina, 315 Main Street, 29208, Columbia, SC, USA aut Valafar Homayoun Department of Computer Science and Engineering, University of South Carolina, 315 Main Street, 29208, Columbia, SC, USA aut Journal of Biomolecular NMR Springer Netherlands 50/4(2011-08-01), 357-369 0925-2738 50:4<357 2011 50 10858 https://doi.org/10.1007/s10858-011-9521-5 text/html Onlinezugriff via DOI 1 research-article jats NATIONALLICENCE 856 40 https://doi.org/10.1007/s10858-011-9521-5 text/html Onlinezugriff via DOI NATIONALLICENCE 700 1- Shealy Paul Department of Computer Science and Engineering, University of South Carolina, 315 Main Street, 29208, Columbia, SC, USA aut NATIONALLICENCE 700 1- Liu Yizhou Complex Carbohydrate Research Center, University of Georgia, 30603, Athens, GA, USA aut NATIONALLICENCE 700 1- Simin Mikhail Department of Computer Science and Engineering, University of South Carolina, 315 Main Street, 29208, Columbia, SC, USA aut NATIONALLICENCE 700 1- Valafar Homayoun Department of Computer Science and Engineering, University of South Carolina, 315 Main Street, 29208, Columbia, SC, USA aut NATIONALLICENCE 773 0- Journal of Biomolecular NMR Springer Netherlands 50/4(2011-08-01), 357-369 0925-2738 50:4<357 2011 50 10858 Metadata rights reserved Springer special CC-BY-NC licence nationallicence BK010053 XK010053 XK010000 NATIONALLICENCE NATIONALLICENCE NL-springer