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. Author manuscript; available in PMC: 2012 Sep 20.
Published in final edited form as: Biochemistry. 2011 Aug 26;50(37):8018–8027. doi: 10.1021/bi201101t

Figure 2.

Figure 2

(a) Final |Fo| - |Fc| map of metal-free HAI contoured at 3.0σ (green) and −3.0σ (red). Only spurious noise peaks are observed, and none correspond to residual metal ions. A water molecule (red sphere), confirmed in a simulated annealing omit map contoured at 3.0σ (blue), is hydrogen bonded (green dashed lines) to D124, D128, and D232. Atoms are color-coded as follows: C = yellow, N = blue, O = red. (b) Superposition of chains A for metal-free HAI (pH 7.0, color-coded as in (a)) and Mn2+2-HAI (pH 7.5) (PDB 2PHA, all atoms and interactions colored light blue). Apart from small conformational changes of D232 and H101, protein residues in the apoenzyme are nearly pre-formed for ideal metal coordination interactions.