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Figure 6
(a) The 28 independent Hyp-1 molecules forming the asymmetric unit of the crystal packing (with molecules A and B labelled), arranged in a dimeric pattern with a sevenfold repeat around a noncrystallographic 21 screw axis along the crystallographic c direction. The ANS ligands are shown as black ball-and-stick models. (b) Arrangement of Hyp-1 dimers (labelled by protein chain identifiers A, B…, b) in two rows (AB, …, MN and ab, …, OP) along c. Protein copies translated along c are marked with a prime. Centroid distances between consecutive Hyp-1 molecules are marked in Å. Cross-linking of consecutive Hyp-1 pairs through an interstitial ANS molecule is marked by *. NCS symmetry of the dimers is indicated by the degree of rotation between the two chains. The rotation required for the best superposition of molecule A onto the remaining Hyp-1 Cα traces is given for each chain, with the corresponding r.m.s.d. (in Å) boxed. All rotations (in °) were calculated in ALIGN (Cohen, 1997BB9).

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ISSN: 2059-7983
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