EC-NMR Structure of Escherichia coli YiaD Determined by Combining Evolutionary Couplings (EC) and Sparse NMR Data. Northeast Structural Genomics Consortium target ER553
Northeast Structural Genomics Consortium (NESG)
Protein structure determination by combining sparse NMR data with evolutionary couplings.
YYMDVQEAKLRDKMRGTGVSVTRSGDNIILNMPNNVTFDSSSATLKPAGANTLTGVAMVLKEYPKTAVNVIGYTDSTGGH DLNMRLSQQRADSVASALITQGVDASRIRTQGLGPANPIASNSTAEGKAQNRRVEITLSPLLEHHHHHH
residues 59-199 of YiaD, lipoprotein, function unknown. Homolog of OmpA-like C-terminal domain.
Northeast Structural Genomics Consortium
THIS ENTRY 2N48 REFLECTS AN ALTERNATIVE MODELING OF THE ORIGINAL STRUCTURAL DATA IN 2K1S DETERMINED BY AUTHORS: T.A.RAMELOT,L.ZHAO,K.HAMILTON,M.MAGLAQUI,R.XIAO,J.LIU,M.C.BARAN,G.SWAPNA,T.B.ACTON,B.ROST,G.T.MONTELIONE,M.A.KENNEDY,NORTHEAST STRUCTURAL GENOMICS CONSORTIUM (NESG)
AUTHOR USED THE EXPERIMENTAL DATA FROM ENTRY 2K1S.
Protons from the Rosetta models were removed and added back using Reduce.
Guntert, P., Mumenthaler, C. and Wuthrich, K.
EC-NMR, NORTHEAST STRUCTURAL GENOMICS CONSORTIUM, NESG, Protein Structure Initiative, PSI-Biology, Structural Genomics, LIPID BINDING PROTEIN
YYMDVQEAKLRDKMRGTGVSVTRSGDNIILNMPNNVTFDSSSATLKPAGANTLTGVAMVLKEYPKTAVNVIGYTDSTGGH DLNMRLSQQRADSVASALITQGVDASRIRTQGLGPANPIASNSTAEGKAQNRRVEITLSPL