BMRB Entry 16187
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PDB ID:
Entry in NMR Restraints Grid
Validation report in NRG-CING
Chem Shift validation: AVS_full, SPARTA
BMRB Entry DOI: doi:10.13018/BMR16187
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Title: Backbone 1H Chemical Shift Assignments for FP1 PubMed: 19292861
Deposition date: 2009-02-26 Original release date: 2009-04-17
Authors: Araki, Mitsugu; Tamura, Atsuo
Citation: Araki, Mitsugu; Tamura, Atsuo. "Solubility-dependent structural formation of a 25-residue natively unfolded protein, induced by addition of a seven-residue peptide fragment" FEBS J. 276, 2336-2347 (2009).
Assembly members:
FP1, polymer, 32 residues, 3519.278 Da.
Natural source: Common Name: not available Taxonomy ID: not available Superkingdom: not available Kingdom: not available Genus/species: not available not available
Experimental source: Production method: chemical synthesis
Entity Sequences (FASTA):
FP1: YAFACPACPKRFMRSDALSK
HIKTAFIVVALG
- assigned_chemical_shifts
| Data type | Count |
| 1H chemical shifts | 225 |
Additional metadata:
Assembly:
| Entity Assembly ID | Entity Name | Entity ID |
|---|---|---|
| 1 | FP1 | 1 |
Entities:
Entity 1, FP1 32 residues - 3519.278 Da.
| 1 | TYR | ALA | PHE | ALA | CYS | PRO | ALA | CYS | PRO | LYS | ||||
| 2 | ARG | PHE | MET | ARG | SER | ASP | ALA | LEU | SER | LYS | ||||
| 3 | HIS | ILE | LYS | THR | ALA | PHE | ILE | VAL | VAL | ALA | ||||
| 4 | LEU | GLY |
Samples:
sample_1: FP1 3 mM; acetic acid, [U-100% 2H], 25 mM; sodium chloride 50 mM
sample_conditions_1: ionic strength: 50 mM; pH: 3.0; pressure: 1 atm; temperature: 293.15 K
Experiments:
| Name | Sample | Sample state | Sample conditions |
|---|---|---|---|
| 2D 1H-1H COSY | sample_1 | isotropic | sample_conditions_1 |
| 2D DQF-COSY | sample_1 | isotropic | sample_conditions_1 |
| 2D 1H-1H NOESY | sample_1 | isotropic | sample_conditions_1 |
| 2D 1H-1H TOCSY | sample_1 | isotropic | sample_conditions_1 |
Software:
DYANA v1.5, Guntert, Braun and Wuthrich - structure solution
NMRPipe, Delaglio, Grzesiek, Vuister, Zhu, Pfeifer and Bax - processing
SPARKY, Goddard - chemical shift assignment
NMR spectrometers:
- Bruker DMX 750 MHz
Related Database Links:
| PDB |