2N46

EC-NMR Structure of Human H-RasT35S mutant protein Determined by Combining Evolutionary Couplings (EC) and Sparse NMR Data

Summary for 2N46

• Entry DOI: 10.2210/pdb2n46/pdb
• Related: 2N42 2N44 2N45 2N47 2N48 2N49 2N4A 2N4B 2N4C 2N4D 2N4F
• NMR Information: BMRB: 17610
• Descriptor: GTPase HRas (1 entity in total)
• Functional Keywords: ec-nmr, northeast structural genomics consortium, nesg, protein structure initiative, psi-biology, structural genomics, signaling protein
• Biological source: Homo sapiens (human)
• Cellular location: Cell membrane. Isoform 2: Nucleus: P01112
• Total number of polymer chains: 1
• Total formula weight: 19387.71

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

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

Experimental method

SOLUTION NMR