BMRB Entry 30221
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PDB ID:
Entry in NMR Restraints Grid
Validation report in NRG-CING
Chem Shift validation: AVS_full, LACS
BMRB Entry DOI: doi:10.13018/BMR30221
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Title: Solution NMR Structure of NERD-S, a natively folded pentamutant of the B1 domain of streptococcal protein G (GB1) with a solvent-exposed Trp43 PubMed: 29058725
Deposition date: 2016-12-21 Original release date: 2017-08-16
Authors: Damry, A.; Davey, J.; Goto, N.; Chica, R.
Citation: Davey, J.; Damry, A.; Goto, N.; Chica, R.. "Rational design of proteins that exchange on functional timescales." Nat. Chem. Biol. 13, 1280-1285 (2017).
Assembly members:
entity_1, polymer, 56 residues, 6289.934 Da.
Natural source: Common Name: Streptococcus sp. GX7805 Taxonomy ID: 1325 Superkingdom: Bacteria Kingdom: not available Genus/species: Streptococcus Streptococcus sp. GX7805
Experimental source: Production method: recombinant technology Host organism: Escherichia coli
Entity Sequences (FASTA):
entity_1: MTFKLIINGKTLKGETTTEA
VDAATAEKVFKQYFNDNGID
GEWTYDDATKTFTITE
- assigned_chemical_shifts
- spectral_peak_list
| Data type | Count |
| 13C chemical shifts | 240 |
| 15N chemical shifts | 61 |
| 1H chemical shifts | 342 |
Additional metadata:
Assembly:
| Entity Assembly ID | Entity Name | Entity ID |
|---|---|---|
| 1 | entity_1 | 1 |
Entities:
Entity 1, entity_1 56 residues - 6289.934 Da.
| 1 | MET | THR | PHE | LYS | LEU | ILE | ILE | ASN | GLY | LYS | ||||
| 2 | THR | LEU | LYS | GLY | GLU | THR | THR | THR | GLU | ALA | ||||
| 3 | VAL | ASP | ALA | ALA | THR | ALA | GLU | LYS | VAL | PHE | ||||
| 4 | LYS | GLN | TYR | PHE | ASN | ASP | ASN | GLY | ILE | ASP | ||||
| 5 | GLY | GLU | TRP | THR | TYR | ASP | ASP | ALA | THR | LYS | ||||
| 6 | THR | PHE | THR | ILE | THR | GLU |
Samples:
sample_1: EDTA 100 uM; protein (GB1), [U-98% 15N], 1 mM; sodium azide 0.02%; sodium phosphate 10 mM
sample_2: EDTA 100 uM; protein (GB1), [U-99% 13C; U-98% 15N], 1 mM; sodium azide 0.02%; sodium phosphate 10 mM
sample_3: EDTA 100 uM; protein (GB1), [U-99% 13C; U-98% 15N], 1 mM; sodium azide 0.02%; sodium phosphate 10 mM
sample_conditions_1: ionic strength: 10 mM; pH: 7.4; 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_3 | isotropic | sample_conditions_1 |
| 3D 1H-13C NOESY aromatic | sample_3 | isotropic | sample_conditions_1 |
| 3D HNCACB | sample_2 | isotropic | sample_conditions_1 |
| 3D HNCO | sample_2 | isotropic | sample_conditions_1 |
| 2D 1H-13C HSQC | sample_3 | isotropic | sample_conditions_1 |
| 2D 1H-13C HSQC | sample_2 | isotropic | sample_conditions_1 |
| 2D 1H-15N HSQC | sample_1 | isotropic | sample_conditions_1 |
| 3D 1H-15N TOCSY | sample_1 | isotropic | sample_conditions_1 |
| 3D HCCH-COSY | sample_3 | isotropic | sample_conditions_1 |
| 3D HCCH-TOCSY | sample_3 | isotropic | sample_conditions_1 |
| 3D CCH-TOCSY | sample_3 | isotropic | sample_conditions_1 |
| 3D CBCA(CO)NH | sample_2 | isotropic | sample_conditions_1 |
Software:
CYANA, Guntert, Mumenthaler and Wuthrich - refinement, structure calculation
NMRPipe, Delaglio, Grzesiek, Vuister, Zhu, Pfeifer and Bax - processing
NMRView, Johnson, One Moon Scientific - chemical shift assignment, peak picking
TOPSPIN, Bruker Biospin - collection
VNMR, Varian - collection
NMR spectrometers:
- Bruker AVANCE III HD 600 MHz
- Varian Inova 500 MHz
Download simulated HSQC data in one of the following formats:
CSV: Backbone
or all simulated shifts
SPARKY: Backbone
or all simulated shifts