Research workbench
Direct noe refinement of crambin from 2D NMR data using a slow-cooling annealing protocol
Analyse Direct noe refinement of crambin from 2D NMR data using a slow-cooling… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 1CCN
- Type
- protein
- Length
- 46 residues
- Chains
- 1
- Method
- solution nmr
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- UniProt
- P01542
Structure
solution nmr · 1 distinct chain.
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | — | protein | 46 | — | P01542 |
Compared structures
- 1CCN · Direct noe refinement of crambin from 2D NMR data using a slow-cooling annealing protocol · the same entry in another collection · chain A against A, TM-score 1.00
- P01542 · AlphaFold monomer V2.0 prediction for crambin (P01542) · a predicted model of the same protein · chain A against A, TM-score 0.88
Analyse
- Open in the research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides and crosslinks on the 3D structure
- Every structure of UniProt P01542
- Elsewhere: RCSB PDB 1CCN · PDBe 1CCN · UniProt P01542
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