2K0P
Determination of a Protein Structure in the Solid State from NMR Chemical Shifts
Summary for 2K0P
| Entry DOI | 10.2210/pdb2k0p/pdb |
| Related | 2ju6 |
| Descriptor | Immunoglobulin G-binding protein G (1 entity in total) |
| Functional Keywords | solid-state, chemical shift restraints, gb1, cell wall, igg-binding protein, peptidoglycan-anchor, secreted, protein binding |
| Biological source | Streptococcus sp. group G |
| Cellular location | Secreted, cell wall; Peptidoglycan-anchor (Potential): P06654 |
| Total number of polymer chains | 1 |
| Total formula weight | 6228.81 |
| Authors | Robustelli, P.,Cavalli, A.,Salvatella, X.,Vendruscolo, M. (deposition date: 2008-02-11, release date: 2009-03-03, Last modification date: 2024-05-29) |
| Primary citation | Robustelli, P.,Cavalli, A.,Vendruscolo, M. Determination of protein structures in the solid state from NMR chemical shifts. Structure, 16:1764-1769, 2008 Cited by PubMed Abstract: Solid-state NMR spectroscopy does not require proteins to form crystalline or soluble samples and can thus be applied under a variety of conditions, including precipitates, gels, and microcrystals. It has recently been shown that NMR chemical shifts can be used to determine the structures of the native states of proteins in solution. By considering the cases of two proteins, GB1 and SH3, we provide an initial demonstration here that this type of approach can be extended to the use of solid-state NMR chemical shifts to obtain protein structures in the solid state without the need for measuring interatomic distances. PubMed: 19081052DOI: 10.1016/j.str.2008.10.016 PDB entries with the same primary citation |
| Experimental method | SOLID-STATE NMR |
Structure validation
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