BMRB Entry 15444
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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/BMR15444
MolProbity Validation Chart
NMR-STAR file interactive viewer.
NMR-STAR v3 text file.
XML gzip file.
RDF gzip file.
All files associated with the entry
Citation: Ko, Sunggeon; Jun, Sung-Hoon; Bae, Hansol; Byun, Jung-Sue; Han, Woong; Park, Heeyoung; Yang, Seong Wook; Park, Sam-Yong; Jeon, Young Ho; Cheong, Chaejoon; Kim, Woo Taek; Lee, Weontae; Cho, Hyun-Soo. "Structure of the DNA-binding domain of NgTRF1 reveals unique features
of plant telomere-binding proteins" Nucleic Acids Res. 36, 2739-2755 (2008).
PubMed: 18367475
Assembly members:
NgTRF1, polymer, 121 residues, 13917.033 Da.
Natural source: Common Name: Nicotiana tabacum Taxonomy ID: 4097 Superkingdom: Eukaryota Kingdom: Viridiplantae Genus/species: Nicotiana tabacum
Experimental source: Production method: recombinant technology Host organism: Escherichia coli Vector: pET15b
Entity Sequences (FASTA):
NgTRF1: PVNQKSKRSELSQRRIRRPF
SVAEVEALVEAVEHLGTGRW
RDVKMRAFDNADHRTYVDLK
DKWKTLVHTASIAPQQRRGE
PVPQDLLDRVLAAHAYWSQQ
QGKQHVEPLKILDAKAQKVG
A
- assigned_chemical_shifts
| Data type | Count |
| 13C chemical shifts | 423 |
| 15N chemical shifts | 114 |
| 1H chemical shifts | 550 |
Additional metadata:
Assembly:
| Entity Assembly ID | Entity Name | Entity ID |
|---|---|---|
| 1 | entity | 1 |
Entities:
Entity 1, entity 121 residues - 13917.033 Da.
| 1 | PRO | VAL | ASN | GLN | LYS | SER | LYS | ARG | SER | GLU | ||||
| 2 | LEU | SER | GLN | ARG | ARG | ILE | ARG | ARG | PRO | PHE | ||||
| 3 | SER | VAL | ALA | GLU | VAL | GLU | ALA | LEU | VAL | GLU | ||||
| 4 | ALA | VAL | GLU | HIS | LEU | GLY | THR | GLY | ARG | TRP | ||||
| 5 | ARG | ASP | VAL | LYS | MET | ARG | ALA | PHE | ASP | ASN | ||||
| 6 | ALA | ASP | HIS | ARG | THR | TYR | VAL | ASP | LEU | LYS | ||||
| 7 | ASP | LYS | TRP | LYS | THR | LEU | VAL | HIS | THR | ALA | ||||
| 8 | SER | ILE | ALA | PRO | GLN | GLN | ARG | ARG | GLY | GLU | ||||
| 9 | PRO | VAL | PRO | GLN | ASP | LEU | LEU | ASP | ARG | VAL | ||||
| 10 | LEU | ALA | ALA | HIS | ALA | TYR | TRP | SER | GLN | GLN | ||||
| 11 | GLN | GLY | LYS | GLN | HIS | VAL | GLU | PRO | LEU | LYS | ||||
| 12 | ILE | LEU | ASP | ALA | LYS | ALA | GLN | LYS | VAL | GLY | ||||
| 13 | ALA |
Samples:
sample_1: NgTRF1, [U-100% 15N], 1 mM; sodium phosphate 25 mM; NaCl 100 mM; H2O 90%; D2O 10%
sample_2: NgTRF1, [U-100% 13C; U-100% 15N], 1 mM; sodium phosphate 25 mM; NaCl 100 mM; H2O 90%; D2O 10%
sample_conditions_1: ionic strength: 100 mM; pH: 7; pressure: 1 atm; temperature: 298 K
Experiments:
| Name | Sample | Sample state | Sample conditions |
|---|---|---|---|
| 2D 1H-15N HSQC | sample_1 | isotropic | sample_conditions_1 |
| 3D CBCA(CO)NH | sample_1 | isotropic | sample_conditions_1 |
| 3D HNCO | 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 HNCA | sample_1 | isotropic | sample_conditions_1 |
| 3D 1H-15N NOESY | sample_1 | isotropic | sample_conditions_1 |
| 3D HBHA(CO)NH | sample_1 | isotropic | sample_conditions_1 |
| 3D 1H-13C NOESY | sample_1 | isotropic | sample_conditions_1 |
| 3D HCCH-TOCSY | sample_1 | isotropic | sample_conditions_1 |
Software:
CYANA v2.2.5, P.GUNTERT ET AL. - refinement, structure solution
CYANA v2.4, Delaglio, Grzesiek, Vuister, Zhu, Pfeifer and Bax - data analysis
CYANA v2.3, Delaglio, Grzesiek, Vuister, Zhu, Pfeifer and Bax - processing
CYANA v3.114, Goddard - peak picking
CYANA v3.1, Zimmerman, Moseley, Kulikowski and Montelione - chemical shift assignment
CYANA v1.0, Cornilescu, Delaglio and Bax - data analysis
CYANA v2.6, Koradi, Billeter and Wuthrich - data analysis
NMR spectrometers:
- Bruker DRX 500 MHz
- Bruker DRX 600 MHz
Download HSQC peak lists in one of the following formats:
CSV: Backbone
or all simulated peaks
SPARKY: Backbone
or all simulated peaks