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 targ

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.
PDB ID: 2N45Download
MMDB ID: 130405
PDB Deposition Date: 2015/6/17
Updated in MMDB: 2015/08
Experimental Method:
solution nmr
Source Organism:
Similar Structures:
Biological Unit for 2N45: monomeric; determined by author
Molecular Components in 2N45
Label Count Molecule
Protein (1 molecule)
Maltose-binding Periplasmic Protein(Gene symbol: malE)
Molecule annotation
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Citing MMDB