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. 2010 Jul 6;66(Pt 10):1367–1380. doi: 10.1107/S1744309110005890

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© Jaudzems et al. 2010

This is an open-access article distributed under the terms of the Creative Commons Attribution Licence, which permits unrestricted use, distribution, and reproduction in any medium, provided the original authors and source are cited.

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Comparison of crystallographic B values and NMR displacements (). (a) Linear least-squares fit of the crystallographic values (2) versus the corresponding displacements (1) in the reference crystal structure, yielding the c value in (3) for NP_247299.1, with c = 1/87. (b) Plots of the per-residue polypeptide backbone displacements versus the NP_247299.1 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 values with (2) and (3). For the NMR structure and the two reference structures, the data correspond to the per-residue displacements calculated with (1). The locations of regular secondary structures are indicated at the bottom of the upper panel.

Inline graphic — Comparison of crystallographic B values and NMR displacements (). (a) Linear least-squares fit of the crystallographic values (2) versus the corresponding displacements (1) in the reference crystal structure, yielding the c value in (3) for NP_247299.1, with c = 1/87. (b) Plots of the per-residue polypeptide backbone displacements versus the NP_247299.1 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 values with (2) and (3). For the NMR structure and the two reference structures, the data correspond to the per-residue displacements calculated with (1). The locations of regular secondary structures are indicated at the bottom of the upper panel.