BMRB Entry 34642
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PDB ID:
Entry in NMR Restraints Grid
Validation report in NRG-CING
Chem Shift validation: AVS_full
BMRB Entry DOI: doi:10.13018/BMR34642
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NMR-STAR v3 text file.
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Title: Solution structure of the N-terminal domain of human telomeric Repeat-binding factor 2-interacting protein 1 (hRap1): implication for Rap1-TRF2 interaction in Human.
Deposition date: 2021-06-25 Original release date: 2022-09-30
Authors: Miron, S.; LeDU, M.; Gaullier, G.; Zinn-justin, S.; Cuniasse, P.
Citation: Miron, S.; LeDU, M.; Gaullier, G.; Zinn-justin, S.; Cuniasse, P.. "Solution structure of the N-terminal domain of human telomeric Repeat-binding factor 2-interacting protein 1 (hRap1): implication for Rap1-TRF2 interaction in Human." .
Assembly members:
entity_1, polymer, 114 residues, 12138.556 Da.
Natural source: Common Name: Human Taxonomy ID: 9606 Superkingdom: Eukaryota Kingdom: Metazoa Genus/species: Homo sapiens
Experimental source: Production method: recombinant technology Host organism: Escherichia coli
Entity Sequences (FASTA):
entity_1: MAEAMDLGKDPNGPTHSSTL
FVRDDGSSMSFYVRPSPAKR
RLSTLILHGGGTVCRVQEPG
AVLLAQPGEALAEASGDFIS
TQYILDCVERNERLELEAYR
LGPASAADTGSEAK
- assigned_chemical_shifts
- spectral_peak_list
| Data type | Count |
| 13C chemical shifts | 442 |
| 15N chemical shifts | 107 |
| 1H chemical shifts | 660 |
Additional metadata:
Assembly:
| Entity Assembly ID | Entity Name | Entity ID |
|---|---|---|
| 1 | unit_1 | 1 |
Entities:
Entity 1, unit_1 114 residues - 12138.556 Da.
| 1 | MET | ALA | GLU | ALA | MET | ASP | LEU | GLY | LYS | ASP | ||||
| 2 | PRO | ASN | GLY | PRO | THR | HIS | SER | SER | THR | LEU | ||||
| 3 | PHE | VAL | ARG | ASP | ASP | GLY | SER | SER | MET | SER | ||||
| 4 | PHE | TYR | VAL | ARG | PRO | SER | PRO | ALA | LYS | ARG | ||||
| 5 | ARG | LEU | SER | THR | LEU | ILE | LEU | HIS | GLY | GLY | ||||
| 6 | GLY | THR | VAL | CYS | ARG | VAL | GLN | GLU | PRO | GLY | ||||
| 7 | ALA | VAL | LEU | LEU | ALA | GLN | PRO | GLY | GLU | ALA | ||||
| 8 | LEU | ALA | GLU | ALA | SER | GLY | ASP | PHE | ILE | SER | ||||
| 9 | THR | GLN | TYR | ILE | LEU | ASP | CYS | VAL | GLU | ARG | ||||
| 10 | ASN | GLU | ARG | LEU | GLU | LEU | GLU | ALA | TYR | ARG | ||||
| 11 | LEU | GLY | PRO | ALA | SER | ALA | ALA | ASP | THR | GLY | ||||
| 12 | SER | GLU | ALA | LYS |
Samples:
sample_1: human Telomeric Repeat-binding factor 2-interacting protein 1 (hRAP1), [U-100% 13C; U-100% 15N], 100 ± 10 uM; NaCl 150 mM
sample_conditions_1: ionic strength: 150 mM; pH: 6.5; pressure: 1 atm; temperature: 293 K
Experiments:
| Name | Sample | Sample state | Sample conditions |
|---|---|---|---|
| 2D 1H-15N HSQC | sample_1 | isotropic | sample_conditions_1 |
| 3D HNCACB | sample_1 | isotropic | sample_conditions_1 |
| 3D HNCO | sample_1 | isotropic | sample_conditions_1 |
| 3D HN(CA)CO | sample_1 | isotropic | sample_conditions_1 |
| 3D HCCH-TOSCY | sample_1 | isotropic | sample_conditions_1 |
| 3D 1H-15N TOCSY | sample_1 | isotropic | sample_conditions_1 |
| 3D 15N NOESY-HSQC | sample_1 | isotropic | sample_conditions_1 |
| 3D 13C (aromatic)NOESY-HSQC | sample_1 | isotropic | sample_conditions_1 |
| 3D 13C(aliphatic)NOESY-HSQC | sample_1 | isotropic | sample_conditions_1 |
| 3D 1H-15N NOESY | sample_1 | isotropic | sample_conditions_1 |
Software:
TopSpin v4.0.7, Bruker Biospin - processing
CcpNmr Analysis v2.4.2, CCPN - chemical shift assignment, peak picking
CYANA v3.98.5, Guntert, Mumenthaler and Wuthrich - structure calculation
X-PLOR NIH, Schwieters, Kuszewski, Tjandra and Clore - refinement
NMR spectrometers:
- Bruker AVANCE II 700 MHz
- Bruker AVANCE III 950 MHz
Download HSQC peak lists in one of the following formats:
CSV: Backbone
or all simulated shifts
SPARKY: Backbone
or all simulated shifts