BMRB Entry 16692
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PDB ID:
Entry in NMR Restraints Grid
Validation report in NRG-CING
Chem Shift validation: AVS_anomalous, AVS_full, LACS
BMRB Entry DOI: doi:10.13018/BMR16692
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Title: Solution NMR structure of a domain of protein A6KY75 from Bacteroides vulgatus, Northeast Structural Genomics target BvR106A
Deposition date: 2010-01-26 Original release date: 2010-03-02
Authors: Mills, Jeffrey; Sukumaran, Dinesh; Sathyamoorthy, Bharathwaj; Belote, Rachel; Ciccosanti, Colleen; Hamilton, Keith; Acton, T.; Xiao, R.; Swapna, GVT; Everett, J.; Montelione, G.; Szyperski, Thomas
Citation: Mills, Jeffrey; Sukumaran, Dinesh; Sathyamoorthy, Bharathwaj; Belote, Rachel; Ciccosanti, Colleen; Hamilton, Keith; Acton, T.; Xiao, R.; Swapna, GVT; Everett, J.; Montelione, G.; Szyperski, Thomas. "Solution NMR structure of a domain of protein A6KY75 from Bacteroides vulgatus, Northeast Structural Genomics target BvR106A." Not known ., .-..
Assembly members:
BvR106A, polymer, 74 residues, 9095.4 Da.
Natural source: Common Name: Bacteroides vulgatus Taxonomy ID: 821 Superkingdom: Bacteria Kingdom: not available Genus/species: Bacteroides vulgatus
Experimental source: Production method: recombinant technology Host organism: Escherichia coli
Entity Sequences (FASTA):
BvR106A: MNQNLQGEWMKNYEELKSFV
RKYRRFPKSTEGNLGGWCHT
QRKMRKQGKLPNDRRLLLDK
IGFVWSLEHHHHHH
- assigned_chemical_shifts
- spectral_peak_list
| Data type | Count |
| 13C chemical shifts | 247 |
| 15N chemical shifts | 77 |
| 1H chemical shifts | 518 |
Additional metadata:
Assembly:
| Entity Assembly ID | Entity Name | Entity ID |
|---|---|---|
| 1 | entity | 1 |
Entities:
Entity 1, entity 74 residues - 9095.4 Da.
| 1 | MET | ASN | GLN | ASN | LEU | GLN | GLY | GLU | TRP | MET | ||||
| 2 | LYS | ASN | TYR | GLU | GLU | LEU | LYS | SER | PHE | VAL | ||||
| 3 | ARG | LYS | TYR | ARG | ARG | PHE | PRO | LYS | SER | THR | ||||
| 4 | GLU | GLY | ASN | LEU | GLY | GLY | TRP | CYS | HIS | THR | ||||
| 5 | GLN | ARG | LYS | MET | ARG | LYS | GLN | GLY | LYS | LEU | ||||
| 6 | PRO | ASN | ASP | ARG | ARG | LEU | LEU | LEU | ASP | LYS | ||||
| 7 | ILE | GLY | PHE | VAL | TRP | SER | LEU | GLU | HIS | HIS | ||||
| 8 | HIS | HIS | HIS | HIS |
Samples:
NC: BvR106A, [U-99% 13C; U-99% 15N], 1.11 mM; D2O, [U-2H], 10%; H2O 90%; MES 20 mM; sodium chloride 100 mM; calcium chloride 5 mM; DTT 10 mM; DSS 50 uM; sodium azide 0.02%
sample_conditions_1: ionic strength: 235 mM; pH: 6.5; pressure: 1 atm; temperature: 298 K
Experiments:
| Name | Sample | Sample state | Sample conditions |
|---|---|---|---|
| 2D 1H-15N HSQC | NC | isotropic | sample_conditions_1 |
| 2D 1H-13C HSQC | NC | isotropic | sample_conditions_1 |
| (4,3)D GFT CABCA(CO)NH | NC | isotropic | sample_conditions_1 |
| (4,3)D GFT HNCABCA | NC | isotropic | sample_conditions_1 |
| (4,3)D GFT HABCAB(CO)NH | NC | isotropic | sample_conditions_1 |
| 3D HCCH-TOCSY | NC | isotropic | sample_conditions_1 |
| 3D simultaneous NOESY | NC | isotropic | sample_conditions_1 |
| 3D 1H-15N NOESY | NC | isotropic | sample_conditions_1 |
Software:
XEASY, Bartels et al. - chemical shift assignment, data analysis, peak picking
AutoAssign, Zimmerman, Moseley, Kulikowski and Montelione - chemical shift assignment
CSI, Wishart and Sykes - structure solution
TALOS, Cornilescu, Delaglio and Bax - structure solution
CYANA, Herrmann, Guntert and Wuthrich - structure solution
CNS, Brunger, Adams, Clore, Gros, Nilges and Read - refinement
Molmol, Koradi, Billeter and Wuthrich - data analysis, refinement
PSVS, Bhattacharya and Montelione - refinement
PROSA, Guntert - processing
VNMRJ, Varian - collection
NMR spectrometers:
- Varian UnityPlus 750 MHz
Related Database Links:
| PDB |
Download simulated HSQC data in one of the following formats:
CSV: Backbone
or all simulated shifts
SPARKY: Backbone
or all simulated shifts