2KS6
NMR solution structure of ALG13 --- obtained with iterative CS-Rosetta from backbone NMR data.
Summary for 2KS6
| Entry DOI | 10.2210/pdb2ks6/pdb |
| Related | 2jzc |
| Descriptor | UDP-N-acetylglucosamine transferase subunit ALG13 (1 entity in total) |
| Functional Keywords | cs-rosetta, cyclic n-oxides, endoplasmic reticulum, glycosyltransferase, transferase |
| Biological source | Saccharomyces cerevisiae (brewer's yeast,lager beer yeast,yeast) |
| Cellular location | Endoplasmic reticulum: P53178 |
| Total number of polymer chains | 1 |
| Total formula weight | 22552.82 |
| Authors | Lange, O.F.,Wang, X.,Prestegard, J.H.,Baker, D. (deposition date: 2009-12-29, release date: 2011-01-12, Last modification date: 2024-05-01) |
| Primary citation | Raman, S.,Lange, O.F.,Rossi, P.,Tyka, M.,Wang, X.,Aramini, J.,Liu, G.,Ramelot, T.A.,Eletsky, A.,Szyperski, T.,Kennedy, M.A.,Prestegard, J.,Montelione, G.T.,Baker, D. NMR structure determination for larger proteins using backbone-only data. Science, 327:1014-1018, 2010 Cited by PubMed Abstract: Conventional protein structure determination from nuclear magnetic resonance data relies heavily on side-chain proton-to-proton distances. The necessary side-chain resonance assignment, however, is labor intensive and prone to error. Here we show that structures can be accurately determined without nuclear magnetic resonance (NMR) information on the side chains for proteins up to 25 kilodaltons by incorporating backbone chemical shifts, residual dipolar couplings, and amide proton distances into the Rosetta protein structure modeling methodology. These data, which are too sparse for conventional methods, serve only to guide conformational search toward the lowest-energy conformations in the folding landscape; the details of the computed models are determined by the physical chemistry implicit in the Rosetta all-atom energy function. The new method is not hindered by the deuteration required to suppress nuclear relaxation processes for proteins greater than 15 kilodaltons and should enable routine NMR structure determination for larger proteins. PubMed: 20133520DOI: 10.1126/science.1183649 PDB entries with the same primary citation |
| Experimental method | SOLUTION NMR |
Structure validation
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