BMRB Entry 19294
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PDB ID:
Entry in NMR Restraints Grid
Validation report in NRG-CING
Chem Shift validation: AVS_full, SPARTA
BMRB Entry DOI: doi:10.13018/BMR19294
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Title: DNA-binding domain of T. brucei telomeric protein tbTRF
Deposition date: 2013-06-09 Original release date: 2014-07-14
Authors: LI, Xiaohua; YE, Fei; ZHANG, Mingjie; ZHAO, Yanxiang
Citation: LI, Xiaohua; YE, Fei; ZHANG, Mingjie; ZHAO, Yanxiang. "DNA-binding domain of T. brucei telomeric protein tbTRF" Not known ., .-..
Assembly members:
entity, polymer, 106 residues, 12054.533 Da.
Natural source: Common Name: dog Taxonomy ID: 9615 Superkingdom: Eukaryota Kingdom: Metazoa Genus/species: Canis familiaris
Experimental source: Production method: recombinant technology Host organism: Escherichia coli
Entity Sequences (FASTA):
entity: GPGSLSNFANVGVGTSSGKQ
KRYKFSASEDEAIIKGLARF
TKGQQRFQQIYYAYRSVWHP
ARTVSQLYDHWRGTLRYKVI
QQQGYRGKNSVAARSPEKAS
NMENNE
- assigned_chemical_shifts
Data type | Count |
15N chemical shifts | 98 |
1H chemical shifts | 97 |
Additional metadata:
Assembly:
Entity Assembly ID | Entity Name | Entity ID |
---|---|---|
1 | DNA-binding domain of T. brucei telomeric protein tbTRF | 1 |
Entities:
Entity 1, DNA-binding domain of T. brucei telomeric protein tbTRF 106 residues - 12054.533 Da.
1 | GLY | PRO | GLY | SER | LEU | SER | ASN | PHE | ALA | ASN | ||||
2 | VAL | GLY | VAL | GLY | THR | SER | SER | GLY | LYS | GLN | ||||
3 | LYS | ARG | TYR | LYS | PHE | SER | ALA | SER | GLU | ASP | ||||
4 | GLU | ALA | ILE | ILE | LYS | GLY | LEU | ALA | ARG | PHE | ||||
5 | THR | LYS | GLY | GLN | GLN | ARG | PHE | GLN | GLN | ILE | ||||
6 | TYR | TYR | ALA | TYR | ARG | SER | VAL | TRP | HIS | PRO | ||||
7 | ALA | ARG | THR | VAL | SER | GLN | LEU | TYR | ASP | HIS | ||||
8 | TRP | ARG | GLY | THR | LEU | ARG | TYR | LYS | VAL | ILE | ||||
9 | GLN | GLN | GLN | GLY | TYR | ARG | GLY | LYS | ASN | SER | ||||
10 | VAL | ALA | ALA | ARG | SER | PRO | GLU | LYS | ALA | SER | ||||
11 | ASN | MET | GLU | ASN | ASN | GLU |
Samples:
sample_1: DNA-binding domain of T. brucei telomeric protein tbTRF mM; potassium phosphate 100 mM
sample_conditions_1: ionic strength: 0.1 M; pH: 5.6; pressure: 1 atm; temperature: 303 K
Experiments:
Name | Sample | Sample state | Sample conditions |
---|---|---|---|
2D 1H-15N HSQC | sample_1 | isotropic | sample_conditions_1 |
3D 1H-15N NOESY | sample_1 | isotropic | sample_conditions_1 |
2D 1H-1H NOESY | sample_1 | isotropic | sample_conditions_1 |
3D HNCACB | sample_1 | isotropic | sample_conditions_1 |
3D 1H-13C NOESY | sample_1 | isotropic | sample_conditions_1 |
3D CBCA(CO)NH | sample_1 | isotropic | sample_conditions_1 |
Software:
CNS, Brunger, Adams, Clore, Gros, Nilges and Read - structure solution
NMR spectrometers:
- Varian INOVA 500 MHz
Download simulated HSQC data in one of the following formats:
CSV: Backbone
or all simulated shifts
SPARKY: Backbone
or all simulated shifts