2N45
EC-NMR Structure of Escherichia coli Maltose-binding protein Determined by Combining Evolutionary Couplings (EC) and Sparse NMR Data with a second set of RDC data simulated for an alternative alignment tensor. Northeast Structural Genomics Consortium target ER690
Summary for 2N45
| Entry DOI | 10.2210/pdb2n45/pdb |
| Related | 2N42 2N44 2N46 2N47 2N48 2N49 2N4A 2N4B 2N4C 2N4D 2N4F |
| NMR Information | BMRB: 25237 |
| Descriptor | Maltose-binding periplasmic protein (1 entity in total) |
| Functional Keywords | ec-nmr, periplasmic binding protein, structural genomics, northeast structural genomics consortium, nesg, psi-biology, protein structure initiative |
| Biological source | Escherichia coli |
| Cellular location | Periplasm: P0AEX9 |
| Total number of polymer chains | 1 |
| Total formula weight | 40753.15 |
| Authors | Tang, Y.,Huang, Y.J.,Hopf, T.A.,Sander, C.,Marks, D.,Montelione, G.T.,Northeast Structural Genomics Consortium (NESG) (deposition date: 2015-06-17, release date: 2015-07-01, Last modification date: 2024-05-15) |
| Primary citation | Tang, Y.,Huang, Y.J.,Hopf, T.A.,Sander, C.,Marks, D.S.,Montelione, G.T. Protein structure determination by combining sparse NMR data with evolutionary couplings. Nat.Methods, 12:751-754, 2015 Cited by PubMed Abstract: Accurate determination of protein structure by NMR spectroscopy is challenging for larger proteins, for which experimental data are often incomplete and ambiguous. Evolutionary sequence information together with advances in maximum entropy statistical methods provide a rich complementary source of structural constraints. We have developed a hybrid approach (evolutionary coupling-NMR spectroscopy; EC-NMR) combining sparse NMR data with evolutionary residue-residue couplings and demonstrate accurate structure determination for several proteins 6-41 kDa in size. PubMed: 26121406DOI: 10.1038/nmeth.3455 PDB entries with the same primary citation |
| Experimental method | SOLUTION NMR |
Structure validation
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