Abstract
AbstractProtein structures calculated using NMR data are less accurate and less well defined than they could be. Here we use the program ANSURR to show that this deficiency is at least in part due to a lack of hydrogen bond restraints. We then describe a protocol to introduce hydrogen bond restraints into the structure calculation of the SH2 domain from SH2B1 in a systematic and transparent way, and show that the structures generated are more accurate and better defined as a result. We also show that ANSURR can be used as a guide to know when the structure calculation is good enough to stop.
Publisher
Cold Spring Harbor Laboratory
Reference52 articles.
1. A method for validating the accuracy of NMR protein structures;Nature Comms,2020
2. The accuracy of NMR protein structures in the Protein Data Bank;Structure,2021
3. The accuracy of protein structures in solution determined by AlphaFold and NMR;Structure,2022
4. Neuhaus, D. ; Williamson, M. P. , The nuclear Overhauser effect in structural and conformational analysis. 2nd ed.; Wiley-VCH: New York, 2000
5. Protein backbone and sidechain torsion angles predicted from NMR chemical shifts using artificial neural networks