N-15, C-13, AND H-1-NMR ASSIGNMENTS AND SECONDARY STRUCTURE FOR T4-LYSOZYME

Sequence-specific H-1, C-13, and N-15 backbone assignments and H-1 and C-13 side-chain assignments have been identified for T4-1ysozyme (164 residues, MW = 18.7 kDa). A variety of double- and triple-resonance 3D techniques were used, Some of these methods were applied in unconventional ways and a detailed description of the advantages and disadvantages of these approaches is given. Complete backbone resonances for 162 of the 164 residues and partial assignments for the remaining 2 residues were obtained. The H-1 and N-15 assignments are in agreement with those obtained previously by McIntosh et al, who used selective labeling (L. P. McIntosh et al., Biochemistuy 29, 6341 (1990)). Complete proton and carbon side-chain assignments were made for 120 residues and partial side-chain assignments were made for 42 additional residues. A qualitative analysis of the medium-range NOESY data reveals a secondary structure consistent with the X-ray crystallographic structure. (C) 1995 Academic Press, Inc.