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![[Figure 1]](rr5136fig1mag.jpg)
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Figure 1
Sequence corrections to the N14 model. The top row shows the originally assigned sequences (Met4L, Thr8L and Pro84L) and the row below the corrected side chains (Leu4L, Pro8L and the split Ser84H in two conformations). The ball-and-stick models are displayed in 2mFo − DFc electron density displayed at 1σ (blue grid) and mFo − DFc difference density (2.8σ; green and red grid for positive and negative difference density, respectively) after refinement of the original N14C3 model (Met4L, Thr8L and Pro84H) with REFMAC (Murshudov et al., 2011  ) and are rendered in Coot (Emsley et al., 2010). Note how the unusual non-Pro cis-peptide indicated by the red plane indicator reverts to a common pre-Pro cis conformation (green) and how the incorrectly sequenced ProH84 causes a clash (red spikes) with, and displaces, the adjacent water atom, which is also consistent with the difference density. The atom contacts were calculated with the MolProbity suite (Chen et al., 2010). |
![[Figure 1]](rr5136fig1.jpg)
 | STRUCTURAL BIOLOGY |
ISSN: 2059-7983
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