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![[Figure 2]](mv5032fig2mag.jpg)
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Figure 2
Comparison of MST3(1–303) models. (a) The seven crystallographically independent structures are superimposed on the basis of Cα positions in the C lobe. The significant conformational variations in the N lobe, as illustrated here in a slightly different view from Fig. 1 ![[link]](../../../../../../logos/arrows/d_arr.gif) , can be attributed to rigid-body rotations anchored at the hinge and roughly about a line extending from the hinge to the C-terminal end of the C helix. (b) The models of the N lobe are superimposed and viewed approximately through the inter-lobal interface. Although most of the Cα atoms are well matched, deviations in the N-terminal region, including the glycine-rich loop, are prominent. The model of the native type I crystal is shown in blue, those of the native type II crystals are shown in lemon and cyan, the type II–ADP models are shown in green and aquamarine, the type III–adenine model is shown in magenta and the type III–Mn-ADP model is shown in red. |
![[Figure 2]](mv5032fig2.jpg)
 | STRUCTURAL BIOLOGY |
ISSN: 2059-7983
