 | Acta Crystallographica Section F Acta Crystallographica Section F STRUCTURAL BIOLOGY COMMUNICATIONS |
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![[Figure 1]](wd5133fig1mag.jpg)
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Figure 1
Amino-acid sequence and NMR structure of the protein TM1112 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 for best fit of the polypeptide-backbone heavy atoms of residues 2–89 of the two molecules in the crystal asymmetric unit, CrystA and CrystB (black lines), with the bundle of 20 conformers that represent the NMR structure (brown). In generating this picture, CrystB was superimposed for best fit with CrystA and then each one in the ensemble of 20 NMR conformers was superimposed for best fit of the polypeptide-backbone heavy atoms with CrystA. (c) Amino-acid sequence. The locations of regular secondary structure are indicated above the sequence using the same color code as in (a). |
![[Figure 1]](wd5133fig1.jpg)
| STRUCTURAL BIOLOGY COMMUNICATIONS |
ISSN: 2053-230X
