BMRB Entry 16368
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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/BMR16368
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Title: Solution NMR structure of the homodimeric winged helix-turn-helix DNA-binding domain (fragment 1-100) Mb0332 from Mycobacterium bovis, a possible ArsR-family transcriptional regulator. Northeast Structural Genomics Consortium Target MbR242E.
Deposition date: 2009-06-26 Original release date: 2009-08-06
Authors: Ramelot, Theresa; Ramelot, John; Wang, D.; Ciccosanti, Colleen; Jiang, Mei; Nair, R.; Rost, Burkhard; Swapna, G.V.T.; Acton, Thomas; Xiao, Rong; Everett, John; Montelione, Gaetano; Kennedy, Michael
Citation: Ramelot, Theresa; Cort, John; Wang, D.; Ciccosanti, Colleen; Jiang, Mei; Nair, R.; Rost, Burkhard; Swapna, G.V.T.; Acton, Thomas; Xiao, Rong; Everett, John; Montelione, Gaetano; Kennedy, Michael. "Solution NMR structure of the homodimeric winged helix-turn-helix DNA-binding domain (fragment 1-100) Mb0332 from Mycobacterium bovis, a possible ArsR-family transcriptional regulator. Northeast Structural Genomics Consortium Target MbR242E." Not known ., .-..
Assembly members:
Mb0332, polymer, 109 residues, 11700 Da.
Natural source: Common Name: Mycobacterium bovis Taxonomy ID: 1765 Superkingdom: Bacteria Kingdom: not available Genus/species: Mycobacterium bovis
Experimental source: Production method: recombinant technology Host organism: Escherichia coli
Entity Sequences (FASTA):
Mb0332: XMAGQSDRKAALLDQVARVG
KALANGRRLQILDLLAQGER
AVEAIATATGMNLTTASANL
QALKSGGLVEARREGTRQYY
RIAGEDVARLFALVQVVADE
HLEHHHHHH
- assigned_chemical_shifts
- spectral_peak_list
| Data type | Count |
| 13C chemical shifts | 431 |
| 15N chemical shifts | 116 |
| 1H chemical shifts | 720 |
Additional metadata:
Assembly:
| Entity Assembly ID | Entity Name | Entity ID |
|---|---|---|
| 1 | Mb0332, chain A | 1 |
| 2 | Mb0332, chain B | 1 |
Entities:
Entity 1, Mb0332, chain A 109 residues - 11700 Da.
8 non-native residues at C-terminus (LEHHHHHH)
| 1 | ACE | MET | ALA | GLY | GLN | SER | ASP | ARG | LYS | ALA | ||||
| 2 | ALA | LEU | LEU | ASP | GLN | VAL | ALA | ARG | VAL | GLY | ||||
| 3 | LYS | ALA | LEU | ALA | ASN | GLY | ARG | ARG | LEU | GLN | ||||
| 4 | ILE | LEU | ASP | LEU | LEU | ALA | GLN | GLY | GLU | ARG | ||||
| 5 | ALA | VAL | GLU | ALA | ILE | ALA | THR | ALA | THR | GLY | ||||
| 6 | MET | ASN | LEU | THR | THR | ALA | SER | ALA | ASN | LEU | ||||
| 7 | GLN | ALA | LEU | LYS | SER | GLY | GLY | LEU | VAL | GLU | ||||
| 8 | ALA | ARG | ARG | GLU | GLY | THR | ARG | GLN | TYR | TYR | ||||
| 9 | ARG | ILE | ALA | GLY | GLU | ASP | VAL | ALA | ARG | LEU | ||||
| 10 | PHE | ALA | LEU | VAL | GLN | VAL | VAL | ALA | ASP | GLU | ||||
| 11 | HIS | LEU | GLU | HIS | HIS | HIS | HIS | HIS | HIS |
Samples:
NC_sample: MES 20 ± 2.5 mM; sodium chloride 200 ± 10 mM; DTT 10 ± 0.5 mM; sodium azide 0.02 ± 0.001 %; protein, [U-100% 13C; U-100% 15N], 1.1 ± 0.05 mM; DSS 50 ± 2.5 uM; H2O 95%; D2O 5%
NC5_sample: MES 20 ± 2.5 mM; sodium chloride 200 ± 2.5 mM; DTT 10 ± 0.5 mM; sodium azide 0.02 ± 0.001 %; protein, [U-5% 13C; U-100% 15N], 0.8 ± 0.1 mM; DSS 50 ± 2.5 uM; H2O 95%; D2O 5%
NC50_sample: MES 20 ± 2.5 mM; sodium chloride 200 ± 2.5 mM; DTT 10 ± 0.5 mM; sodium azide 0.02 ± 0.001 %; protein, [U-100% 13C; U-100% 15N], 0.5 ± 0.05 mM; DSS 50 ± 2.5 uM; protein .5 ± 0.05 mM; H2O 95%; D2O 5%
sample_conditions_1: ionic strength: 200 mM; pH: 6.0; 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 |
| 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 CBCA(CO)NH | NC_sample | isotropic | sample_conditions_1 |
| 3D HNCACB | NC_sample | isotropic | sample_conditions_1 |
| 3D C(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 |
| 2D 1H-13C HSQC arom | NC5_sample | isotropic | sample_conditions_1 |
| 3D 1H-13C NOESY arom | NC_sample | isotropic | sample_conditions_1 |
| 3D CN filt 1H-13C NOESY | NC50_sample | isotropic | sample_conditions_1 |
| 2D 1H-13C HSQC | NC50_sample | isotropic | sample_conditions_1 |
| 3D HNCOCA | NC_sample | isotropic | sample_conditions_1 |
| 2D 1H-13C HSQC aliph | NC5_sample | isotropic | sample_conditions_1 |
| 2D 1H-15N HSQC | NC5_sample | isotropic | sample_conditions_1 |
Software:
NMRPipe v2008, Delaglio, Grzesiek, Vuister, Zhu, Pfeifer and Bax - processing
VNMR v6.1C, Varian - collection
TOPSPIN v2.1.3, Bruker Biospin - collection
AutoStruct v2.2.1, Huang, Tejero, Powers and Montelione - data analysis
X-PLOR NIH v2.20, Schwieters, Kuszewski, Tjandra and Clore - structure solution
SPARKY v3.113, Goddard - data analysis
PSVS v1.3, Bhattacharya and Montelione - structure validation
AutoAssign v2.3.0, Zimmerman, Moseley, Kulikowski and Montelione - chemical shift assignment
PDBStat v5.1, (PDBStat) R. Tejero, G.T. Montelione - data analysis
CNS v1.2, Brunger, Adams, Clore, Gros, Nilges and Read - refinement
NMR spectrometers:
- Varian INOVA 600 MHz
- Bruker AvanceIII 850 MHz
- Varian INOVA 750 MHz
Download simulated HSQC data in one of the following formats:
CSV: Backbone
or all simulated shifts
SPARKY: Backbone
or all simulated shifts