Direct noe refinement of crambin from 2D NMR data using a slow-cooling annealing protocol. Determined by solution NMR. Released 31 Oct 1993.
Explore 1CCN in 3D Show helices and sheets RCSB PDB PDBe
1CCN contains 2 α-helices and 2 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 | 2-3 | 2 | 1 |
| α-helix | 7-16 | 10 | |
| α-helix | 23-30 | 8 | |
| β-strand | 33-34 | 2 | 1 |
| Molecule | Chains | Type | Length | Organism | UniProt |
|---|---|---|---|---|---|
| Crambin | A | protein | 46 | Crambe hispanica subsp. abyssinica | P01542 (AlphaFold model) |
>1CCN_1 CRAMBIN (chains A) TTCCPSIVARSNFNVCRLPGTPEALCATYTGCIIIPGATCPGDYAN
Direct NOE refinement of biomolecular structures using 2D NMR data. Bonvin, A.M.J.J., Boelens, R., Kaptein, R. J Biomol NMR (1991) 1:305-309. DOI 10.1007/BF01875523 · PubMed
Other PDB entries of the same protein (UniProt P01542 (AlphaFold model), which also has an AlphaFold model), best resolution first:
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