BMRB Entry 15879
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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/BMR15879
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Title: Protein folding on a highly rugged landscape: Experimental observation of glassy dynamics and structural frustration PubMed: 19240216
Deposition date: 2008-07-18 Original release date: 2009-03-12
Authors: Sadqi, Mourad; de Alba, Eva; Perez-Jimenez, Raul; Sanchez-Ruiz, Jose; Munoz, Victor
Citation: Sadqi, Mourad; de Alba, Eva; Perez-Jimenez, Raul; Sanchez-Ruiz, Jose; Munoz, Victor. "A designed protein as experimental model of primordial folding" Proc. Natl. Acad. U.S.A. 106, 4127-4132 (2009).
Assembly members:
FSD_mod, polymer, 29 residues, 3854.456 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):
FSD_mod: GQQYTAXIKGRTFRNEKELR
DFIEKFXGR
- assigned_chemical_shifts
| Data type | Count |
| 13C chemical shifts | 23 |
| 1H chemical shifts | 216 |
Additional metadata:
Assembly:
| Entity Assembly ID | Entity Name | Entity ID |
|---|---|---|
| 1 | FSD_mod | 1 |
Entities:
Entity 1, FSD_mod 29 residues - 3854.456 Da.
| 1 | GLY | GLN | GLN | TYR | THR | ALA | NAL | ILE | LYS | GLY | ||||
| 2 | ARG | THR | PHE | ARG | ASN | GLU | LYS | GLU | LEU | ARG | ||||
| 3 | ASP | PHE | ILE | GLU | LYS | PHE | DNS | GLY | ARG |
Samples:
sample_1: FSD_mod 1 mM; DSS 0.05 mM; D2O, [U-99.9% 2H], 10%; H2O 90%
sample_conditions_1: ionic strength: 0 M; pH: 5.0; pressure: 1 atm; temperature: 323 K
Experiments:
| Name | Sample | Sample state | Sample conditions |
|---|---|---|---|
| 2D 1H-1H TOCSY | sample_1 | isotropic | sample_conditions_1 |
| 2D 1H-1H NOESY | sample_1 | isotropic | sample_conditions_1 |
| 2D DQF-COSY | sample_1 | isotropic | sample_conditions_1 |
Software:
NMRPipe, Delaglio, Grzesiek, Vuister, Zhu, Pfeifer and Bax - processing
TOPSPIN, Bruker Biospin - collection
SPARKY, Goddard - chemical shift assignment, data analysis, peak picking
X-PLOR NIH, Schwieters, Kuszewski, Tjandra and Clore - structure solution
TALOS, Cornilescu, Delaglio and Bax - data analysis
NMR spectrometers:
- Bruker DMX 500 MHz
- Bruker Avance 600 MHz
Related Database Links:
| PDB |