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2N4C

EC-NMR Structure of Agrobacterium tumefaciens Atu1203 Determined by Combining Evolutionary Couplings (EC) and Sparse NMR Data. Northeast Structural Genomics Consortium target AtT10

Summary for 2N4C
Entry DOI10.2210/pdb2n4c/pdb
Related2N42 2N44 2N45 2N46 2N47 2N48 2N49 2N4A 2N4B 2N4D 2N4F
DescriptorUncharacterized protein Atu1203 (1 entity in total)
Functional Keywordsputative metal-binding domain atu1203, ec-nmr, northeast structural genomics consortium, nesg, protein structure initiative, psi-biology, structural genomics, unknown function, ontario centre for structural proteomics, ocsp
Biological sourceAgrobacterium fabrum str. C58 (Agrobacterium Tumefaciens)
Total number of polymer chains1
Total formula weight8766.73
Authors
Primary citationTang, 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: 26121406
DOI: 10.1038/nmeth.3455
PDB entries with the same primary citation
Experimental method
SOLUTION NMR
Structure validation

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