BMRB Entry 17840
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PDB ID:
Entry in NMR Restraints Grid
Validation report in NRG-CING
Chem Shift validation: AVS_full, LACS, SPARTA
BMRB Entry DOI: doi:10.13018/BMR17840
MolProbity Validation Chart
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Title: GB98 solution structure PubMed: 22325777
Deposition date: 2011-08-08 Original release date: 2012-02-28
Authors: He, Yanan; Chen, Yihong; Alexander, Patrick; Bryan, Philip; Orban, John
Citation: He, Yanan; Chen, Yihong; Alexander, Patrick; Bryan, Philip; Orban, John. "Mutational tipping points for switching protein folds and functions" Structure 20, 283-291 (2012).
Assembly members:
GB98, polymer, 56 residues, 6405.436 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):
GB98: TTYKLILNLKQAKEEAIKEL
VDAGTAEKYFKLIANAKTVE
GVWTYKDEIKTFTVTE
- assigned_chemical_shifts
| Data type | Count |
| 13C chemical shifts | 213 |
| 15N chemical shifts | 56 |
| 1H chemical shifts | 346 |
Additional metadata:
Assembly:
| Entity Assembly ID | Entity Name | Entity ID |
|---|---|---|
| 1 | GB98 | 1 |
Entities:
Entity 1, GB98 56 residues - 6405.436 Da.
| 1 | THR | THR | TYR | LYS | LEU | ILE | LEU | ASN | LEU | LYS | ||||
| 2 | GLN | ALA | LYS | GLU | GLU | ALA | ILE | LYS | GLU | LEU | ||||
| 3 | VAL | ASP | ALA | GLY | THR | ALA | GLU | LYS | TYR | PHE | ||||
| 4 | LYS | LEU | ILE | ALA | ASN | ALA | LYS | THR | VAL | GLU | ||||
| 5 | GLY | VAL | TRP | THR | TYR | LYS | ASP | GLU | ILE | LYS | ||||
| 6 | THR | PHE | THR | VAL | THR | GLU |
Samples:
sample_1: GB98, [U-100% 13C; U-100% 15N], 0.1 – 0.3 mM; potassium phosphate 100 mM; H2O 95%; D2O 5%
sample_conditions_1: ionic strength: 100 mM; pH: 7.0; pressure: 1 atm; temperature: 278 K
Experiments:
| Name | Sample | Sample state | Sample conditions |
|---|---|---|---|
| 2D 1H-15N HSQC | sample_1 | isotropic | sample_conditions_1 |
| 3D CBCA(CO)NH | sample_1 | isotropic | sample_conditions_1 |
| 3D HNCACB | sample_1 | isotropic | sample_conditions_1 |
| 3D C(CO)NH | sample_1 | isotropic | sample_conditions_1 |
| 3D HNCO | sample_1 | isotropic | sample_conditions_1 |
| 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 |
| 3D H(CCO)NH | sample_1 | isotropic | sample_conditions_1 |
| 3D HBHA(CO)NH | sample_1 | isotropic | sample_conditions_1 |
Software:
CNS, Brunger A. T. et.al. - structure determination
TOPSPIN, Bruker Biospin - collection
NMRPipe, Delaglio, Grzesiek, Vuister, Zhu, Pfeifer and Bax - data processing
NMRDraw, Delaglio, Grzesiek, Vuister, Zhu, Pfeifer and Bax - data processing display
SPARKY, Goddard - data analysis
Molmol, Koradi, Billeter and Wuthrich - structure display
CSI, Wishart, D.S. and B.D. Sykes. - secondary structure prediction
TALOS, Cornilescu, Delaglio and Bax - dihedral angle restraints determination
Procheck, Laskowski, MacArthur, Smith, Jones, Hutchinson, Morris, Moss and Tho - protein structure quality check
NOEID, Lisa Parsons - generate noe peak lists
NMR spectrometers:
- Bruker DMX 600 MHz
Download simulated HSQC data in one of the following formats:
CSV: Backbone
or all simulated shifts
SPARKY: Backbone
or all simulated shifts