BMRB Entry 52398
Chem Shift validation: AVS_full
BMRB Entry DOI: doi:10.13018/BMR52398
NMR-STAR file interactive viewer.
NMR-STAR v3 text file.
XML gzip file.
RDF gzip file.
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Citation: Vu, Duc-Duy; Bonucci, Alessio; Breniere, Manon; Cisneros-Aguirre, Metztli; Pelupessy, Philippe; Wang, Ziqing; Carlier, Ludovic; Bouvignies, Guillaume; Cortes, Patricia; Aggarwal, Aneel; Blackledge, Martin; Gueroui, Zoher; Belle, Valerie; Stark, Jeremy; Modesti, Mauro; Ferrage, Fabien. "Multivalent interactions of the disordered regions of XLF and XRCC4 foster robust cellular NHEJ and drive the formation of ligation-boosting condensates in vitro" Nat. Struct. Mol. Biol. ., .-. (2024).
Assembly members:
entity_1, polymer, 136 residues, Formula weight is not available
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 Vector: pMAL-c5x
Entity Sequences (FASTA):
entity_1: AAQEREKDIKQEGETAICSE
MTADRDPVYDESTDEESENQ
TDLSGLASAAVSKDDSIISS
LDVTDIAPSRKRRQRMQRNL
GTEPKMAPQENQLQEKENSR
PDSSLPETSKKEHISAENMS
LETLRNSSPEDLFDEI
- assigned_chemical_shifts
| Data type | Count |
| 13C chemical shifts | 365 |
| 15N chemical shifts | 121 |
| 1H chemical shifts | 120 |
Additional metadata:
Assembly:
| Entity Assembly ID | Entity Name | Entity ID |
|---|---|---|
| 1 | C-terminal region of XRCC4 | 1 |
Entities:
Entity 1, C-terminal region of XRCC4 136 residues - Formula weight is not available
| 1 | ALA | ALA | GLN | GLU | ARG | GLU | LYS | ASP | ILE | LYS | ||||
| 2 | GLN | GLU | GLY | GLU | THR | ALA | ILE | CYS | SER | GLU | ||||
| 3 | MET | THR | ALA | ASP | ARG | ASP | PRO | VAL | TYR | ASP | ||||
| 4 | GLU | SER | THR | ASP | GLU | GLU | SER | GLU | ASN | GLN | ||||
| 5 | THR | ASP | LEU | SER | GLY | LEU | ALA | SER | ALA | ALA | ||||
| 6 | VAL | SER | LYS | ASP | ASP | SER | ILE | ILE | SER | SER | ||||
| 7 | LEU | ASP | VAL | THR | ASP | ILE | ALA | PRO | SER | ARG | ||||
| 8 | LYS | ARG | ARG | GLN | ARG | MET | GLN | ARG | ASN | LEU | ||||
| 9 | GLY | THR | GLU | PRO | LYS | MET | ALA | PRO | GLN | GLU | ||||
| 10 | ASN | GLN | LEU | GLN | GLU | LYS | GLU | ASN | SER | ARG | ||||
| 11 | PRO | ASP | SER | SER | LEU | PRO | GLU | THR | SER | LYS | ||||
| 12 | LYS | GLU | HIS | ILE | SER | ALA | GLU | ASN | MET | SER | ||||
| 13 | LEU | GLU | THR | LEU | ARG | ASN | SER | SER | PRO | GLU | ||||
| 14 | ASP | LEU | PHE | ASP | GLU | ILE |
Samples:
sample_1: C-terminal region of XRCC4, [U-100% 13C; U-100% 15N], 350 uM; Bistris 6.5 20 mM; potassium chloride 150 mM; EDTA 1 mM; DTT 1 mM
sample_conditions_1: ionic strength: 0.15 M; pH: 6.5; pressure: 1 atm; temperature: 298 K
Experiments:
| Name | Sample | Sample state | Sample conditions |
|---|---|---|---|
| 2D 1H-15N HSQC | sample_1 | isotropic | sample_conditions_1 |
| 3D HNCA | sample_1 | isotropic | sample_conditions_1 |
| 3D HNCACB | sample_1 | isotropic | sample_conditions_1 |
| 3D HNCACO | sample_1 | isotropic | sample_conditions_1 |
| 3D HNCO | sample_1 | isotropic | sample_conditions_1 |
Software:
SPARKY - chemical shift assignment
TOPSPIN - collection
NMR spectrometers:
- Bruker AVANCE NEO 800 MHz
Download HSQC peak lists in one of the following formats:
CSV: Backbone
or all simulated peaks
SPARKY: Backbone
or all simulated peaks