BMRB Entry 15408
Chem Shift validation: AVS_full, LACS
BMRB Entry DOI: doi:10.13018/BMR15408
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Title: NMR-detected conformational exchange observed in a computationally designed variant of protein Gb1 PubMed: 18586670
Deposition date: 2007-07-29 Original release date: 2008-08-18
Authors: Crowhurst, Karin; Mayo, Stephen
Citation: Crowhurst, Karin; Mayo, Stephen. "NMR-detected conformational exchange observed in a computationally designed variant of protein Gb1" Protein Eng. Des. Sel. 21, 577-587 (2008).
Assembly members:
delta1.5, polymer, 57 residues, 6342 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: recombinant technology Host organism: Escherichia coli
Entity Sequences (FASTA):
delta1.5: MTTFKLIINGKTLKGETTTE
AVDAATAEKVLKQYINDNGI
DGEWTYDDATKTWTVTE
- assigned_chemical_shifts
- heteronucl_T1_relaxation
- heteronucl_T2_relaxation
- H_exch_protection_factors
Data type | Count |
13C chemical shifts | 241 |
15N chemical shifts | 61 |
1H chemical shifts | 371 |
H exchange protection factors | 55 |
T1 relaxation values | 54 |
T2 relaxation values | 55 |
Additional metadata:
Assembly:
Entity Assembly ID | Entity Name | Entity ID |
---|---|---|
1 | delta1.5 | 1 |
Entities:
Entity 1, delta1.5 57 residues - 6342 Da.
1 | MET | THR | THR | PHE | LYS | LEU | ILE | ILE | ASN | GLY | ||||
2 | LYS | THR | LEU | LYS | GLY | GLU | THR | THR | THR | GLU | ||||
3 | ALA | VAL | ASP | ALA | ALA | THR | ALA | GLU | LYS | VAL | ||||
4 | LEU | LYS | GLN | TYR | ILE | ASN | ASP | ASN | GLY | ILE | ||||
5 | ASP | GLY | GLU | TRP | THR | TYR | ASP | ASP | ALA | THR | ||||
6 | LYS | THR | TRP | THR | VAL | THR | GLU |
Samples:
sample_1: delta1.5, [U-13C; U-15N], 1.5 mM; sodium phosphate 50 mM; DSS 0.2 mM; H2O 90%; D2O 10%
sample_2: delta1.5, [U-13C; U-15N], 2.2 mM; sodium phosphate 50 mM; DSS 0.2 mM; D2O 100%
sample_3: delta1.5, [U-15N], 2.6 mM; sodium phosphate 50 mM; DSS 0.2 mM; H2O 90%; D2O 10%
sample_4: delta1.5, [U-15N; U-2H], 2.6 mM; sodium phosphate 50 mM; DSS 0.2 mM; H2O 90%; D2O 10%
sample_conditions_1: ionic strength: 0.3 M; pH: 6; pressure: 1 atm; temperature: 298.15 K
sample_conditions_2: ionic strength: 0.3 M; pH*: 6.3; pressure: 1 atm; temperature: 298.15 K
Experiments:
Name | Sample | Sample state | Sample conditions |
---|---|---|---|
2D 1H-15N HSQC | sample_1 | isotropic | sample_conditions_1 |
2D 1H-13C HSQC | sample_1 | isotropic | sample_conditions_1 |
3D HNCACB | sample_1 | isotropic | sample_conditions_1 |
3D HNCO | sample_1 | isotropic | sample_conditions_1 |
3D HCCH-TOCSY | sample_1 | isotropic | sample_conditions_1 |
3D HCC-TOCSY-NNH | sample_1 | isotropic | sample_conditions_1 |
3D CCC-TOCSY_NNH | sample_1 | isotropic | sample_conditions_1 |
2D 1H-15N HSQC | sample_2 | isotropic | sample_conditions_2 |
2D CLEANEX-PM | sample_3 | isotropic | sample_conditions_1 |
2D 1H-15N HSQC | sample_4 | isotropic | sample_conditions_1 |
2D nz cross-correlation | sample_4 | isotropic | sample_conditions_1 |
2D nxy cross-correlation | sample_4 | isotropic | sample_conditions_1 |
Software:
NMRDraw v1995, Delaglio, Grzesiek, Vuister, Zhu, Pfeifer and Bax - processing
NMRPipe v1995, Delaglio, Grzesiek, Vuister, Zhu, Pfeifer and Bax - processing
NMRView v5.2.2, Johnson, One Moon Scientific - chemical shift assignment, peak picking
CurveFit v1998, Palmer III - data analysis
NMR spectrometers:
- Varian INOVA 600 MHz
Related Database Links:
PDB |
Download simulated HSQC data in one of the following formats:
CSV: Backbone
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SPARKY: Backbone
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