Work

Improved methodology for protein NMR structure calculation using hydrogen bond restraints and ANSURR validation: the SH2 domain of SH2B1

Year: 2022

Type: preprint

Abstract: Protein 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.

Source: bioRxiv (Cold Spring Harbor Laboratory)

DOI: 10.1101/2022.08.29.505644

Authors: Nicholas J. Fowler, Marym F. Albalwi, Subin Lee, Andrea M. Hounslow, Mike P. Williamson

Institution: University of Sheffield

Language: English

Topic: Protein Structure and Dynamics

Subfield: Molecular Biology

Field: Biochemistry, Genetics and Molecular Biology

Domain: Life Sciences

Open Access status: green

Funders: Directorate for Biological Sciences, Biotechnology and Biological Sciences Research Council

Awards: Validation of NMR protein structures using FIRST and RCI, Upgrade to 600 MHz NMR spectrometer