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![[Figure 3]](nz5018fig3mag.jpg)
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Figure 3
Histogram distributions of backbone covalent bond angles from AlphaFold2 prediction residues with low pLDDT, low packing and high outlier density (these residues are barbed wire-like, but without explicit selection for angle outliers). The x axis is σ from the target angle value, with bins of 0.1σ. The y axis is the count of residues falling in the bin. The target (0σ) is marked with a light blue bar; the outlier threshold (−4σ) is marked with a red bar. The underflow bin is ≤−10σ; the overflow bin is >+4σ (the other outlier threshold). All three of these bond angles show frequent geometric distortions, with the distortion of the C—N—CA angle being systematic, and its distribution recentered almost exactly on the −4σ outlier threshold (a). This angle partially spans the peptide bond, and its systematic distortion suggests errors in how AlphaFold forms peptide bonds in barbed wire. |
![[Figure 3]](nz5018fig3.jpg)
 | STRUCTURAL BIOLOGY |
ISSN: 2059-7983
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