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. Author manuscript; available in PMC: 2008 Nov 16.
Published in final edited form as: Cell. 2007 Nov 16;131(4):756–769. doi: 10.1016/j.cell.2007.09.039

Figure 2. Strategy for the assignment of methyl correlations of SecA.

Figure 2

Each column in the figure displays a structural model of one of the protomers of SecA with the domain or fragment studied in isolation being highlighted, along with the corresponding 1H-13C HMQC of Ile-δ1 methyls (displayed as spheres in the model) and the backbone 1H-15N HSQC.

(A) PBD (residues 220-379).

(B) SecAΔC/ΔIRA2 (residues 1-420, comprising NBD and PBD).

(C) SecAΔC (residues 1-610, comprising NBD, PBD and IRA2).

(D) Full-length SecA (residues 1-901). Only few resonances for the backbone of the full-length SecA are visible (Figure S9).