BMRB Entry 15902
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PDB ID:
Entry in NMR Restraints Grid
Validation report in NRG-CING
Chem Shift validation: AVS_anomalous, AVS_full, LACS, SPARTA
BMRB Entry DOI: doi:10.13018/BMR15902
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Title: Solution NMR structure of the OB domain of Ta0387 from Thermoplasma acidophilum. Northeast Structural Genomics Consortium target TaR80b.
Deposition date: 2008-08-01 Original release date: 2008-08-13
Authors: Ramelot, Theresa; Ding, Keyang; Lee, Dan; Jiang, Mei; Ciccosanti, Colleen; Xiao, Rong; Nair, Rajesh; Everett, John; Swapna, G.V.T; Acton, Thomas; Rost, Burkhard; Montelione, Gaetano; Kennedy, Michael
Citation: Ramelot, Theresa; Ding, Keyang; Lee, Dan; Jiang, Mei; Ciccosanti, Colleen; Xiao, Rong; Nair, Rajesh; Everett, John; Swapna, G.V.T; Acton, Thomas; Rost, Burkhard; Montelione, Gaetano; Kennedy, Michael. "Solution NMR structure of the OB domain of Ta0387 from Thermoplasma acidophilum." Not known ., .-..
Assembly members:
Ta0387, polymer, 106 residues, 11896.298 Da.
Natural source: Common Name: Thermoplasma acidophilum Taxonomy ID: 2303 Superkingdom: Archaea Kingdom: not available Genus/species: Thermoplasma acidophilum
Experimental source: Production method: recombinant technology Host organism: Escherichia coli
Entity Sequences (FASTA):
Ta0387: SDLVKIRDVSLSTPYVSVIG
KITGIHKKEYESDGTTKSVY
QGYIEDDTARIRISSFGKQL
QDSDVVRIDNARVAQFNGYL
SLSVGDSSRIESVNVNIPLE
HHHHHH
- assigned_chemical_shifts
- spectral_peak_list
| Data type | Count |
| 13C chemical shifts | 467 |
| 15N chemical shifts | 117 |
| 1H chemical shifts | 733 |
Additional metadata:
Assembly:
| Entity Assembly ID | Entity Name | Entity ID |
|---|---|---|
| 1 | Ta0387 | 1 |
Entities:
Entity 1, Ta0387 106 residues - 11896.298 Da.
residues 105-202 of Ta0387
| 1 | SER | ASP | LEU | VAL | LYS | ILE | ARG | ASP | VAL | SER | ||||
| 2 | LEU | SER | THR | PRO | TYR | VAL | SER | VAL | ILE | GLY | ||||
| 3 | LYS | ILE | THR | GLY | ILE | HIS | LYS | LYS | GLU | TYR | ||||
| 4 | GLU | SER | ASP | GLY | THR | THR | LYS | SER | VAL | TYR | ||||
| 5 | GLN | GLY | TYR | ILE | GLU | ASP | ASP | THR | ALA | ARG | ||||
| 6 | ILE | ARG | ILE | SER | SER | PHE | GLY | LYS | GLN | LEU | ||||
| 7 | GLN | ASP | SER | ASP | VAL | VAL | ARG | ILE | ASP | ASN | ||||
| 8 | ALA | ARG | VAL | ALA | GLN | PHE | ASN | GLY | TYR | LEU | ||||
| 9 | SER | LEU | SER | VAL | GLY | ASP | SER | SER | ARG | ILE | ||||
| 10 | GLU | SER | VAL | ASN | VAL | ASN | ILE | PRO | LEU | GLU | ||||
| 11 | HIS | HIS | HIS | HIS | HIS | HIS |
Samples:
NC_sample: ammonium acetate 20 ± 1 mM; sodium chloride 100 ± 5 mM; DTT 10 ± 0.5 mM; calcium chloride 5 ± 0.05 mM; sodium azide 0.02 ± 0.001 %; protein, [U-100% 13C; U-100% 15N], 1.0 ± 0.1 mM; D2O 5%; H2O 95%
NC5_sample: ammonium acetate 20 ± 1 mM; sodium chloride 100 ± 5 mM; DTT 10 ± 0.5 mM; calcium chloride 5 ± 0.05 mM; sodium azide 0.02 ± 0.001 %; protein, [U-5% 13C; U-100% 15N], 1.3 ± .1 mM; D2O 5%; H2O 95%
NC_sample_in_D2O: ammonium acetate 20 ± 1 mM; sodium chloride 100 ± 5 mM; DTT 10 ± 0.5 mM; calcium chloride 5 ± 0.05 mM; sodium azide 0.02 ± 0.001 %; protein, [U-100% 13C; U-100% 15N], 1.0 ± 0.1 mM; D2O 100%
sample_conditions_1: ionic strength: 100 mM; pH: 4.5; pressure: 1 atm; temperature: 293 K
Experiments:
| Name | Sample | Sample state | Sample conditions |
|---|---|---|---|
| 2D 1H-15N HSQC | NC_sample | isotropic | sample_conditions_1 |
| 2D 1H-13C HSQC | NC_sample | isotropic | sample_conditions_1 |
| 2D 1H-13C HSQC | NC5_sample | isotropic | sample_conditions_1 |
| 3D 1H-15N NOESY | NC_sample | isotropic | sample_conditions_1 |
| 3D 1H-13C NOESY | NC_sample | isotropic | sample_conditions_1 |
| 3D HNCO | NC_sample | isotropic | sample_conditions_1 |
| 3D HNCA | NC_sample | isotropic | sample_conditions_1 |
| 3D HNCACB | NC_sample | isotropic | sample_conditions_1 |
| 3D CBCA(CO)NH | NC_sample | isotropic | sample_conditions_1 |
| 3D HBHA(CO)NH | NC_sample | isotropic | sample_conditions_1 |
| 3D HCCH-TOCSY | NC_sample | isotropic | sample_conditions_1 |
| 3D HCCH-COSY | NC_sample | isotropic | sample_conditions_1 |
| 3D H(CCO)NH | NC_sample | isotropic | sample_conditions_1 |
| 3D C(CO)NH | NC_sample | isotropic | sample_conditions_1 |
| 2D 1H-15N HSQC (1 hr) | NC_sample_in_D2O | isotropic | sample_conditions_1 |
| 2D 1H-13C HSQC | NC_sample_in_D2O | isotropic | sample_conditions_1 |
| 3D 1H-13C NOESY | NC_sample_in_D2O | isotropic | sample_conditions_1 |
| 4D CC NOESY | NC_sample_in_D2O | isotropic | sample_conditions_1 |
| 3D 1H-13C NOESY | NC_sample | isotropic | sample_conditions_1 |
| 2D 1H-15N HSQC (1 day) | NC_sample_in_D2O | isotropic | sample_conditions_1 |
Software:
AutoAssign v2.3.0, Zimmerman, Moseley, Kulikowski and Montelione - chemical shift assignment
NMRPipe vlinux9, Delaglio, Grzesiek, Vuister, Zhu, Pfeifer and Bax - processing
VNMR v6.1C, Varian - collection
TOPSPIN v2.1, Bruker Biospin - collection
AutoStruct v2.2.1, Huang, Tejero, Powers and Montelione - data analysis
X-PLOR NIH v2.20.0, Schwieters, Kuszewski, Tjandra and Clore - refinement, structure solution
SPARKY v3.113, Goddard - data analysis
PSVS v1.3, Bhattacharya and Montelione - structure solution
NMR spectrometers:
- Varian INOVA 600 MHz
- Bruker AvanceIII 850 MHz
Download simulated HSQC data in one of the following formats:
CSV: Backbone
or all simulated shifts
SPARKY: Backbone
or all simulated shifts