Backbone Conformational Constraints in a Microcrystalline U-15N-Labeled Protein by 3D Dipolar-Shift Solid-State NMR Spectroscopy. Determined by X-ray diffraction at 1.14 Å resolution. Released 25 Apr 2006.
Explore 2GI9 in 3D Show helices and sheets RCSB PDB PDBe
2GI9 contains 1 α-helix and 4 β-strands across 1 chain. Residue ranges use author residue numbering, as in the PDB file, from PDBe. To see them in 3D, choose the Cartoon representation with Secondary structure coloring: helices, sheets and coils get different colors.
| Element | Residues | Length | Sheet |
|---|---|---|---|
| β-strand | 2-8 | 7 | 1 |
| β-strand | 13-19 | 7 | 1 |
| α-helix | 23-36 | 14 | |
| β-strand | 42-46 | 5 | 1 |
| β-strand | 51-55 | 5 | 1 |
| Molecule | Chains | Type | Length | Organism | UniProt |
|---|---|---|---|---|---|
| Immunoglobulin B1 binding domain of protein G | A | protein | 56 | Staphylococcus aureus | P19909 (AlphaFold model) |
>2GI9_1 Immunoglobulin B1 binding domain of protein G (chains A) MQYKLILNGKTLKGETTTEAVDAATAEKVFKQYANDNGVDGEWTYDDATKTFTVTE
Backbone Conformational Constraints in a Microcrystalline U-15N-Labeled Protein by 3D Dipolar-Shift Solid-State NMR Spectroscopy. Franks, W.T., Wylie, B.J., Stellfox, S.A. et al. J Am Chem Soc (2006) 128:3154-3155. DOI 10.1021/ja058292x · PubMed
Other PDB entries of the same protein (UniProt P19909 (AlphaFold model), which also has an AlphaFold model), best resolution first:
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