BMRB Entry 31018
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PDB ID:
Entry in NMR Restraints Grid
Validation report in NRG-CING
Chem Shift validation: AVS_full
BMRB Entry DOI: doi:10.13018/BMR31018
MolProbity Validation Chart
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NMR-STAR v3 text file.
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Title: NMR solution structure of the De novo designed small beta-barrel protein 33_bp_sh3 PubMed: 36897987
Deposition date: 2022-05-04 Original release date: 2023-03-14
Authors: Peterson, F.; Kim, D.; Jensen, D.; Saleem, A.; Chow, C.; Volkman, B.; Baker, D.
Citation: Kim, D.; Jensen, D.; Feldman, D.; Tischer, D.; Saleem, A.; Chow, C.; Li, X.; Carter, L.; Milles, L.; Nguyen, H.; Kang, A.; Bera, A.; Peterson, F.; Volkman, B.; Ovchinnikov, S.; Baker, D.. "De novo design of small beta barrel proteins" Proc. Natl. Acad. Sci. U. S. A. 120, e2207974120-e2207974120 (2023).
Assembly members:
entity_1, polymer, 62 residues, 7175.926 Da.
Natural source: Common Name: not available Taxonomy ID: 32630 Superkingdom: not available Kingdom: not available Genus/species: synthetic construct
Experimental source: Production method: recombinant technology Host organism: Escherichia coli BL21(DE3) Vector: pET29a
Entity Sequences (FASTA):
entity_1: MDGFDRGADVTYTDSDGSKK
TYKVLSYSGDKVTVQDSDGR
TLTFDARLLRVKKWLEHHHH
HH
- assigned_chemical_shifts
- spectral_peak_list
Data type | Count |
13C chemical shifts | 245 |
15N chemical shifts | 60 |
1H chemical shifts | 389 |
Additional metadata:
Assembly:
Entity Assembly ID | Entity Name | Entity ID |
---|---|---|
1 | unit_1 | 1 |
Entities:
Entity 1, unit_1 62 residues - 7175.926 Da.
1 | MET | ASP | GLY | PHE | ASP | ARG | GLY | ALA | ASP | VAL | ||||
2 | THR | TYR | THR | ASP | SER | ASP | GLY | SER | LYS | LYS | ||||
3 | THR | TYR | LYS | VAL | LEU | SER | TYR | SER | GLY | ASP | ||||
4 | LYS | VAL | THR | VAL | GLN | ASP | SER | ASP | GLY | ARG | ||||
5 | THR | LEU | THR | PHE | ASP | ALA | ARG | LEU | LEU | ARG | ||||
6 | VAL | LYS | LYS | TRP | LEU | GLU | HIS | HIS | HIS | HIS | ||||
7 | HIS | HIS |
Samples:
sample_1: 33_bp_sh3, [U-13C; U-15N], 1.25 mM; sodium phosphate 50 mM; sodium chloride 50 mM; sodium azide 0.02 % w/v
sample_conditions_1: ionic strength: 132 mM; pH: 6.5; pressure: 1 atm; temperature: 298 K
Experiments:
Name | Sample | Sample state | Sample conditions |
---|---|---|---|
3D 1H-15N NOESY | sample_1 | isotropic | sample_conditions_1 |
3D 1H-13C NOESY aliphatic | sample_1 | isotropic | sample_conditions_1 |
3D 1H-13C NOESY aromatic | sample_1 | isotropic | sample_conditions_1 |
Software:
TopSpin v3.6, Bruker Biospin - data analysis
NMRPipe, Delaglio, Grzesiek, Vuister, Zhu, Pfeifer and Bax - processing
XEASY, Bartels et al. - data analysis
GARANT, Bartels, Guntert, Billeter and Wuthrich - chemical shift assignment
CYANA v3.98.13, Guntert, Mumenthaler and Wuthrich - refinement, structure calculation
X-PLOR NIH, Schwieters, Kuszewski, Tjandra and Clore - geometry optimization, refinement
TALOS, Cornilescu, Delaglio and Bax - data analysis
NMR spectrometers:
- Bruker AVANCE III HD 600 MHz
Download HSQC peak lists in one of the following formats:
CSV: Backbone
or all simulated shifts
SPARKY: Backbone
or all simulated shifts