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. 2002 Oct;11(10):2427–2436. doi: 10.1110/ps.0212502

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Fig. 1. — The location of individual cysteine residues in the full-length NarL and the carboxy-terminal NarL domain (NarL^C) used for copper phenanthroline attachment. The amino acids chosen for replacement in A, NarL^C (top) and B, NarL (bottom) are numbered relative to the amino-terminal methionine as residue number 1.

Fig. 1. — The location of individual cysteine residues in the full-length NarL and the carboxy-terminal NarL domain (NarL^C) used for copper phenanthroline attachment. The amino acids chosen for replacement in A, NarL^C (top) and B, NarL (bottom) are numbered relative to the amino-terminal methionine as residue number 1.