NMR structure of the protein NP_247299.1: comparison with the crystal structure

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

doi:10.1107/S1744309110005890

Figure 7
NMR evidence for slow conformational exchange between several locally different conformations formed by the polypeptide segment 36–39 (see also Fig. 6

c) and for the coexistence of two conformational species with distinct NMR signals for the polypeptide segments 64–66 and 101–104 (see also Fig. 8

). (a) 2D [¹⁵N,¹H]-HSQC spectrum of a 0.9 mM solution of NP_247299.1 recorded at 800 MHz and 313 K. The cross-peaks of the residues involved in the aforementioned conformational polymorphisms are identified with the following color code: blue, residues 36–39 and, for reference, Glu77, Ala81 and Val86 [see (b) and (c) below]; red, residues 64–66 and 101–103, which all show two signals (see Fig. 8

). (b, c) NMR line-shape analysis reveals slow conformational exchange between the different conformations of the polypeptide segment 36–39 shown in Fig. 6

(c). (b) and (c) show cross-sections along ω₂(¹H) and ω₁(¹⁵N), respectively, illustrating pronounced line broadening of the cross-peaks belonging to Lys36 (red), Ser37 (blue), Thr38 (green) and Lys39 (magenta) when compared with the reference peaks of Glu77 (black), Ala81 (black dashed line) and Val86 (black dashed/dotted line).

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ISSN: 2053-230X

Volume 66| Part 10| July 2010| Pages 1367-1380

doi:10.1107/S1744309110005890

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