 | Acta Crystallographica Section D Acta Crystallographica Section D BIOLOGICAL CRYSTALLOGRAPHY |
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![[Figure 4]](hv5133fig4mag.jpg)
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Figure 4
The native protein has two distinct loop conformations. (a) All 14 monomers from the asymmetric unit have been overlaid (r.m.s.d. < 1 Å for 180 main-chain atoms excluding residues proximal to the loop). (b) Chain A and chain N superimposed, highlighting the degree of side-chain movement between the alternative loop regions (r.m.s.d. = 0.095 Å for 180 main-chain atoms excluding residues proximal to the loop). Chain A is shown in light colours and chain N in dark colours; the side chains of Arg46, Ser45, Asn44 and Arg43 are shown in yellow, blue, red and green, respectively. |
![[Figure 4]](hv5133fig4.jpg)
| BIOLOGICAL CRYSTALLOGRAPHY |
ISSN: 1399-0047
