 | Acta Crystallographica Section D Acta Crystallographica Section D BIOLOGICAL CRYSTALLOGRAPHY |
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![[Figure 1]](kw5080fig1mag.jpg)
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Figure 1
Superposition of the region surrounding the aromatic ring of Phe59 from the two non-equivalent monomers in the 1.90 Å resolution structure of the P3121 crystal form of the cysteine-free variant of FKBP12.6. The C atoms of the molecule A structure are shown in yellow, while those of molecule B are indicated in green. In (a), the electron-density grid (2mFo − DFc at a contour level of 0.0114 e Å−3 = 1σ) for molecule A is also illustrated, indicating that the aromatic ring of Phe59 from this molecule is oriented perpendicular to that from molecule B. In the latter case, the plane of the ring forms the base of the active-site cleft, as seen in previously reported crystal structures of FKBP proteins. Among the residues lying beneath the ring of Phe59 (b), only Val101 Cγ2 lies within van der Waals contact with either the Cδ or C∊ atoms of the Phe59 ring for the two orientations in the P3121 crystal form. The side chains of Ala63 and Leu74 Cδ are approximately 1 Å beyond van der Waals contact. |
![[Figure 1]](kw5080fig1.jpg)
| BIOLOGICAL CRYSTALLOGRAPHY |
ISSN: 1399-0047
