 | Acta Crystallographica Section D Acta Crystallographica Section D BIOLOGICAL CRYSTALLOGRAPHY |
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![[Figure 2]](dw5120fig2mag.jpg)
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Figure 2
Heparin molecules bound in the (APLP1 E2)2–(heparin)2 complex structure. The orientation corresponds to Fig. 1 ![[link]](../../../../../../logos/arrows/d_arr.gif) (b) rotated by 90° around the z and x axes (left). The heparin-binding sites (right) are shown perpendicular to the twofold noncrystallographic symmetry axis of the antiparallel (APLP1 E2)2 assembly. APLP1 E2 is shown as transparent cartoon representation and individual protein chains are coloured magenta (chain a) and cyan (chain b). The C atoms of individual heparin chains are coloured likewise. The heparin chains are consecutively numbered, starting with the nonreducing end positioned in the centre of the APLP1 E2 assembly. The 2Fo − Fc simulated-annealing composite OMIT electron-density map is contoured at 1σ (green and grey mesh, respectively). The grey parts of the 2Fo − Fc simulated-annealing composite OMIT electron-density map highlight a region at the reducing end of heparin chain a that was ambiguous and hence was not included in the model. The reducing ends of both heparin chains (C1 positions) are marked with red arrowheads. Black arrowheads mark substituents of sugar residues that were modelled with an occupancy of 0 owing to weak electron density. |
![[Figure 2]](dw5120fig2.jpg)
| BIOLOGICAL CRYSTALLOGRAPHY |
ISSN: 1399-0047
