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. 2016 May 18;44(13):6452–6470. doi: 10.1093/nar/gkw438

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© The Author(s) 2016. Published by Oxford University Press on behalf of Nucleic Acids Research.

This is an Open Access article distributed under the terms of the Creative Commons Attribution License (http://creativecommons.org/licenses/by-nc/4.0/), which permits non-commercial re-use, distribution, and reproduction in any medium, provided the original work is properly cited. For commercial re-use, please contact journals.permissions@oup.com

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Figure 3. — Time development of heavy atom distances of specific intermolecular H-bond interactions in selected SRSF1 protein / RNA complex (PDB: 2m8d) simulations: 1. G5(N1)/Ala150(O); 2. G5(O6)/Ala150(N); 3. G6(N1)/Asp139(OD); 4. G6(N2)/Asp139(OD); 5. G6(O4')/Gln135(NE2); 6. G6(O6)/Arg142(sc); 7. A7(N6)/Asp136(OD); 8. A7(N1)/Ser133(OG). The H-bonds written in bold are present in the experimental NMR ensemble structures with over 90% occurrence. The H-bond ‘6’ is present in just one structure of the NMR ensemble but it is frequently observed in our simulations. The remaining simulations are summarized in Supplementary Figure S3.