 | Acta Crystallographica Section F Acta Crystallographica Section F STRUCTURAL BIOLOGY COMMUNICATIONS |
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![[Figure 1]](wd5126fig1mag.jpg)
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Figure 1
Amino-acid sequence and NMR structure of protein NP_247299.1 and comparison of the NMR structure with the crystal structure. (a) Stereo ribbon diagram of the NMR conformer closest to the mean coordinates of the bundle of conformers in (b). Color code: β-strands, cyan; helices, red/yellow; nonregular secondary structure, gray. The individual regular secondary structures are identified and the two chain ends are marked N and C. (b) Stereoview of a superposition of the polypeptide backbone heavy atoms of residues 1–102 of the crystal structure (black line) with the 20 conformers representing the NMR structure (brown). The crystal structure was superimposed for best fit with the mean atomic coordinates of the 20 NMR conformers. (c) Amino-acid sequence. Residues −2 and −1 originate from the expression and purification tag at the TEV cleavage site and are not part of NP_247299.1. The locations of regular secondary structures are indicated above the sequence. |
![[Figure 1]](wd5126fig1.jpg)
| STRUCTURAL BIOLOGY COMMUNICATIONS |
ISSN: 2053-230X
