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Figure 9
Local precision of the TM1081 structures along the sequence. (a) Linear least-squares fit of the crystallographic per-residue [\overline B] values versus the corresponding per-residue displacements in the reference crystal structure, [\overline D_{\rm RefCrystal}], yielding c = 1/69 in equation (3) of Jaudzems et al. (2010BB16). (b) Plots of the per-residue polypeptide-backbone displacements versus the sequence. Upper panel, crystal structure and reference crystal structure. Lower panel, NMR structure and reference NMR structure. For the crystal structure, per-residue displacements were calculated from the [\overline B] values using the relation in (a). For the NMR structure and the two reference structures the data correspond to the global per-residue displacements calculated for bundles of 20 conformers (Billeter et al., 1989BB4). The locations of regular secondary structures are indicated in the upper panel and conserved residues in anti-σ factor antagonists are shaded (see text).

Journal logoSTRUCTURAL BIOLOGY
COMMUNICATIONS
ISSN: 2053-230X
Volume 66| Part 10| September 2010| Pages 1393-1405
doi:10.1107/S1744309110033658
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