VAM3P N-TERMINAL DOMAIN SOLUTION STRUCTURE
Vam3p structure reveals conserved and divergent properties of syntaxins.
TNQKTKELSNLIETFAEQSRVLEKECTKIGSKRDSKELRYKIETELIPNCTSVRDKIESNILIHQNGKLSADFKNLKTKY QSLQQSYNQRKSLFPLK
The structure was determined using triple-resonance spectroscopy
1771 total experimental restraints, 1565 NOE distance restraints, 130 hydrogen bond restraints, 76 dihedral angle restraints
0.9 mM 15N-labeled Vam3p N-terminal domain; 20 mM phosphate pH 6.0, 30 C
0.8 mM 15N,13C-labeled Vam3p N-terminal domain; 20 mM phosphate pH 6.0, 30 C
up-and-down three-helix bundle insertion preceding proline in an alpha-helix, ENDOCYTOSIS-EXOCYTOSIS COMPLEX
MSFFDIEAQSSKGNSQQEPQFSTNQKTKELSNLIETFAEQSRVLEKECTKIGSKRDSKELRYKIETELIPNCTSVRDKIE SNILIHQNGKLSADFKNLKTKYQSLQQSYNQRKSLFPLKTPISPGTSKERKDIHPRTEAVRQDPESSYISIKVNEQSPLL HNEGQHQLQLQEEQEQQQQGLSQEELDFQTIIHQERSQQIGRIHTAVQEVNAIFHQLGSLVKEQGEQVTTIDENISHLHD NMQNANKQLTRADQHQRDRNKCGKVTLIIIIVVCMVVLLAVLS