Comparison of NMR and crystal structures for the proteins TM1112 and TM1367

Mohanty, B.; Serrano, P.; Pedrini, B.; Jaudzems, K.; Geralt, M.; Horst, R.; Herrmann, T.; Elsliger, M.-A.; Wilson, I.A.; Wüthrich, K.

doi:10.1107/S1744309110020956

Figure 5
Per-residue $[\overline B]$ values for the backbone heavy atoms in CrystA and CrystB of TM1112, per-residue global backbone and all-heavy-atom displacements between CrystA and CrystB and mean values of the per-residue pairwise backbone displacements among the bundles of 20 conformers representing the NMR structure and the reference NMR and crystal structures. (a) Linear least-squares fit of the $[\overline B]$ values for the CrystA versus the corresponding displacements in the reference crystal structure, $[\overline D_{{\rm refCryst}A}]$ . The resulting representation of the $[\overline B]$ values by $[\overline {\langle \Delta x\rangle }]$ is used for comparisons with the $[\overline D]$ values for the other structures (Jaudzems et al., 2010

). (b)–(d) Plots of per-residue polypeptide backbone displacements versus the sequence. (b) CrystA and CrystB and reference crystal structure A. For crystal structure B, the same relation between $[\overline B]$ and $[\overline {\langle \Delta x\rangle }]$ was used as for CrystA. The locations of the regular secondary structures are indicated and asterisks identify the residues with solvent accessibility below 15% in the NMR structure. (c) NMR structure and reference NMR structure. (d) Backbone displacements between CrystA and CrystB in the crystal asymmetric unit. (e) All-heavy-atom displacements, $[\overline D_{\rm ha}]$ , between CrystA and CrystB. Residues with large $[\overline D_{\rm ha}]$ values are identified.

STRUCTURAL BIOLOGY
COMMUNICATIONS

ISSN: 2053-230X

Volume 66| Part 10| August 2010| Pages 1381-1392

doi:10.1107/S1744309110020956

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