1H and 15N assignments and secondary structure of the Src SH3 domain.
The 1H and 15N sequential assignments of the Src SH3 domain have been determined through a combination of 2D and 3D Nuclear Magnetic Resonance (NMR) methods. The secondary structure of the protein has been identified based on long-range NOE patterns. The SH3 domain of Src consists largely of six beta-strands that form two anti-parallel beta-sheets.
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Department of Chemistry, Harvard University, Cambridge, MA 02138.
Rosen
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Schreiber
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D000595:Amino Acid Sequence; D003001:Cloning, Molecular; D004926:Escherichia coli / Q000235:genetics; D016391:Genes, src; D005982:Glutathione Transferase / Q000737:chemistry / Q000235:genetics; D006859:Hydrogen; D009682:Magnetic Resonance Spectroscopy / Q000379:methods; D008958:Models, Molecular; D008969:Molecular Sequence Data; D009587:Nitrogen Isotopes; D017510:Protein Folding; D017433:Protein Structure, Secondary; D011505:Protein-Tyrosine Kinases / Q000737:chemistry*; D011993:Recombinant Fusion Proteins / Q000737:chemistry; D017386:Sequence Homology, Amino Acid
D009587:Nitrogen Isotopes; D011993:Recombinant Fusion Proteins; D006859:Hydrogen; D005982:Glutathione Transferase; D011505:Protein-Tyrosine Kinases