BMRB Entry 17950
Chem Shift validation: AVS_full, LACS, SPARTA
BMRB Entry DOI: doi:10.13018/BMR17950
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Title: Solution structure of DNA binding domain of AtTRB2 PubMed: 22859734
Deposition date: 2011-09-20 Original release date: 2012-09-20
Authors: Yun, Ji-Hye; Lee, Weontae
Citation: Lee, Won Kyung; Yun, Ji-Hye; Lee, Weontae; Cho, Myeon Haeng. "DNA-binding domain of AtTRB2 reveals unique features of a single Myb histone protein family that binds to both Arabidopsis- and human-type telomeric DNA sequences." Mol. Plant 5, 1406-1408 (2012).
Assembly members:
AtTRB2, polymer, 64 residues, 7194.347 Da.
Natural source: Common Name: Thale cress Taxonomy ID: 3702 Superkingdom: Eukaryota Kingdom: Viridiplantae Genus/species: Arabidopsis thaliana
Experimental source: Production method: recombinant technology Host organism: Escherichia coli
Entity Sequences (FASTA):
AtTRB2: MGAPKQKWTPEEEAALKAGV
LKHGTGKWRTILSDTEFSLI
LKSRSNVDLKDKWRNISVTA
LWGS
- assigned_chemical_shifts
| Data type | Count |
| 13C chemical shifts | 260 |
| 15N chemical shifts | 66 |
| 1H chemical shifts | 420 |
Additional metadata:
Assembly:
| Entity Assembly ID | Entity Name | Entity ID |
|---|---|---|
| 1 | AtTRB2 | 1 |
Entities:
Entity 1, AtTRB2 64 residues - 7194.347 Da.
| 1 | MET | GLY | ALA | PRO | LYS | GLN | LYS | TRP | THR | PRO | ||||
| 2 | GLU | GLU | GLU | ALA | ALA | LEU | LYS | ALA | GLY | VAL | ||||
| 3 | LEU | LYS | HIS | GLY | THR | GLY | LYS | TRP | ARG | THR | ||||
| 4 | ILE | LEU | SER | ASP | THR | GLU | PHE | SER | LEU | ILE | ||||
| 5 | LEU | LYS | SER | ARG | SER | ASN | VAL | ASP | LEU | LYS | ||||
| 6 | ASP | LYS | TRP | ARG | ASN | ILE | SER | VAL | THR | ALA | ||||
| 7 | LEU | TRP | GLY | SER |
Samples:
DNA_binding_domain_of_AtTRB2: AtTRB2, [U-13C; U-15N], 1 mM; HEPES 10 mM; sodium chloride 100 mM; sodium azide 1.5 mM; H2O 90%; D2O 10%
sample_conditions_1: ionic strength: 100 mM; pH: 7.0; pressure: 1 atm; temperature: 298 K
Experiments:
| Name | Sample | Sample state | Sample conditions |
|---|---|---|---|
| 2D 1H-15N HSQC | DNA_binding_domain_of_AtTRB2 | isotropic | sample_conditions_1 |
| 3D CBCA(CO)NH | DNA_binding_domain_of_AtTRB2 | isotropic | sample_conditions_1 |
| 3D HNCACB | DNA_binding_domain_of_AtTRB2 | isotropic | sample_conditions_1 |
| 3D HNCA | DNA_binding_domain_of_AtTRB2 | isotropic | sample_conditions_1 |
| 3D HNCO | DNA_binding_domain_of_AtTRB2 | isotropic | sample_conditions_1 |
| 3D HBHA(CO)NH | DNA_binding_domain_of_AtTRB2 | isotropic | sample_conditions_1 |
| 3D HCCH-TOCSY | DNA_binding_domain_of_AtTRB2 | isotropic | sample_conditions_1 |
| 3D 1H-15N NOESY | DNA_binding_domain_of_AtTRB2 | isotropic | sample_conditions_1 |
| 3D 1H-13C NOESY | DNA_binding_domain_of_AtTRB2 | isotropic | sample_conditions_1 |
Software:
CYANA v2.1, Cornilescu, Delaglio and Bax, Delaglio, Grzesiek, Vuister, Zhu, Pfeifer and Bax, Delaglio, Grzesiek, Vuister, Zhu, Pfeifer and Bax, Goddard, Guntert, Mumenthaler and Wuthrich, Guntert, Mumenthaler and Wuthrich, Koradi, Billeter and Wuthrich, Zimmerman, Moseley, Kulikowski and Montelione - chemical shift assignment, data analysis, data analysis, data analysis, peak picking, processing, refinement, structure solution
NMR spectrometers:
- Bruker DRX 500 MHz
Related Database Links:
| DBJ | BAB08466 |
| GB | AAK63987 AAL73441 AAL73442 AAL76146 AAS10015 |
| REF | NP_201559 NP_851286 XP_002864993 |
| SP | Q9FJW5 |
Download simulated HSQC data in one of the following formats:
CSV: Backbone
or all simulated shifts
SPARKY: Backbone
or all simulated shifts