8CHG

SH3 domain solved by the exact solid-state method from the Bruker Dynamics Center using the correction for dipolar truncation with PDB 2NUZ

Summary for 8CHG

• Entry DOI: 10.2210/pdb8chg/pdb
• Related: 2NUZ
• NMR Information: BMRB: 34785
• Descriptor: Spectrin alpha chain, non-erythrocytic 1 (1 entity in total)
• Functional Keywords: solid-state nmr spectroscopy, structure elucidation, integrated structural biology, protein dynamics, peptide binding protein
• Biological source: Gallus gallus (chicken)
• Total number of polymer chains: 1
• Total formula weight: 7229.24

Authors

Soeldner, B. (deposition date: 2023-02-08, release date: 2023-03-08, Last modification date: 2024-06-19)

Primary citation

Soldner, B.,Grohe, K.,Neidig, P.,Auch, J.,Blach, S.,Klein, A.,Vasa, S.K.,Schafer, L.V.,Linser, R.
Integrated Assessment of the Structure and Dynamics of Solid Proteins.
J Phys Chem Lett, 14:1725-1731, 2023

PubMed Abstract: Understanding macromolecular function, interactions, and stability hinges on detailed assessment of conformational ensembles. For solid proteins, accurate elucidation of the spatial aspects of dynamics at physiological temperatures is limited by the qualitative character or low abundance of solid-state nuclear magnetic resonance internuclear distance information. Here, we demonstrate access to abundant proton-proton internuclear distances for integrated structural biology and chemistry with unprecedented accuracy. Apart from highest-resolution single-state structures, the exact distances enable molecular dynamics (MD) ensemble simulations orchestrated by a dense network of experimental interproton distance boundaries gathered in the context of their physical lattices. This direct embedding of experimental ensemble distances into MD will provide access to representative, atomic-level spatial details of conformational dynamics in supramolecular assemblies, crystalline and lipid-embedded proteins, and beyond.

PubMed: 36757335
DOI: 10.1021/acs.jpclett.2c03398

Experimental method

SOLID-STATE NMR