BMRB Entry 51254
Chem Shift validation: AVS_full
BMRB Entry DOI: doi:10.13018/BMR51254
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Title: Solution NMR backbone chemical shift assignment for the extended xRRM2 domain of human La-related protein 7 PubMed: 35320752
Deposition date: 2021-12-22 Original release date: 2022-03-28
Authors: Yang, Yuan; Eichhorn, Catherine; Hadjian, Tanya; Feigon, Juli
Citation: Yang, Yuan; Liu, Shiheng; Egloff, Sylvain; Eichhorn, Catherine; Hadjian, Tanya; Zhen, James; Kiss, Tamas; Zhou, Z. Hong; Feigon, Juli. "Structural basis of RNA conformational switching in the transcriptional regulator 7SK RNP" Mol. Cell 82, 1724-1736 (2022).
Assembly members:
entity_1, polymer, 213 residues, 24357 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 Vector: pETDuet-1
Entity Sequences (FASTA):
entity_1: GEEVIPLRVLSKSEWMDLKK
EYLALQKASMASLKKTISQI
KSESEMETDSGVPQNTGMKN
EKTANREECRTQEKVNATGP
QFVSGVIVKIISTEPLPGRK
QVRDTLAAISEVLYVDLLEG
DTECHARFKTPEDAQAVINA
YTEINKKHCWKLEILSGDHE
QRYWQKILVDRQAKLNQPRE
KKRGTEKLITKAEKIRLAKT
QQASKHIRFSEYD
- assigned_chemical_shifts
| Data type | Count |
| 13C chemical shifts | 528 |
| 15N chemical shifts | 198 |
| 1H chemical shifts | 198 |
Additional metadata:
Assembly:
| Entity Assembly ID | Entity Name | Entity ID |
|---|---|---|
| 1 | Larp7 extended xRRM2 domain | 1 |
Entities:
Entity 1, Larp7 extended xRRM2 domain 213 residues - 24357 Da.
| 1 | GLY | GLU | GLU | VAL | ILE | PRO | LEU | ARG | VAL | LEU | ||||
| 2 | SER | LYS | SER | GLU | TRP | MET | ASP | LEU | LYS | LYS | ||||
| 3 | GLU | TYR | LEU | ALA | LEU | GLN | LYS | ALA | SER | MET | ||||
| 4 | ALA | SER | LEU | LYS | LYS | THR | ILE | SER | GLN | ILE | ||||
| 5 | LYS | SER | GLU | SER | GLU | MET | GLU | THR | ASP | SER | ||||
| 6 | GLY | VAL | PRO | GLN | ASN | THR | GLY | MET | LYS | ASN | ||||
| 7 | GLU | LYS | THR | ALA | ASN | ARG | GLU | GLU | CYS | ARG | ||||
| 8 | THR | GLN | GLU | LYS | VAL | ASN | ALA | THR | GLY | PRO | ||||
| 9 | GLN | PHE | VAL | SER | GLY | VAL | ILE | VAL | LYS | ILE | ||||
| 10 | ILE | SER | THR | GLU | PRO | LEU | PRO | GLY | ARG | LYS | ||||
| 11 | GLN | VAL | ARG | ASP | THR | LEU | ALA | ALA | ILE | SER | ||||
| 12 | GLU | VAL | LEU | TYR | VAL | ASP | LEU | LEU | GLU | GLY | ||||
| 13 | ASP | THR | GLU | CYS | HIS | ALA | ARG | PHE | LYS | THR | ||||
| 14 | PRO | GLU | ASP | ALA | GLN | ALA | VAL | ILE | ASN | ALA | ||||
| 15 | TYR | THR | GLU | ILE | ASN | LYS | LYS | HIS | CYS | TRP | ||||
| 16 | LYS | LEU | GLU | ILE | LEU | SER | GLY | ASP | HIS | GLU | ||||
| 17 | GLN | ARG | TYR | TRP | GLN | LYS | ILE | LEU | VAL | ASP | ||||
| 18 | ARG | GLN | ALA | LYS | LEU | ASN | GLN | PRO | ARG | GLU | ||||
| 19 | LYS | LYS | ARG | GLY | THR | GLU | LYS | LEU | ILE | THR | ||||
| 20 | LYS | ALA | GLU | LYS | ILE | ARG | LEU | ALA | LYS | THR | ||||
| 21 | GLN | GLN | ALA | SER | LYS | HIS | ILE | ARG | PHE | SER | ||||
| 22 | GLU | TYR | ASP |
Samples:
sample_1: Larp7 extended xRRM2 domain, [U-13C; U-15N], 0.2 mM; sodium phosphate 20 mM; potassium chloride 50 mM; TCEP 1 mM; D2O 5%
sample_conditions_1: ionic strength: 0.07 M; pH: 6.13; pressure: 1 atm; temperature: 298.15 K
Experiments:
| Name | Sample | Sample state | Sample conditions |
|---|---|---|---|
| 2D 1H-15N HSQC | sample_1 | isotropic | sample_conditions_1 |
| 2D 1H-15N TROSY | sample_1 | isotropic | sample_conditions_1 |
| 3D HNCACB | sample_1 | isotropic | sample_conditions_1 |
| 3D CBCA(CO)NH | sample_1 | isotropic | sample_conditions_1 |
| 3D HNCA | sample_1 | isotropic | sample_conditions_1 |
| 3D CCONH | sample_1 | isotropic | sample_conditions_1 |
Software:
TOPSPIN vv4.0.7 - collection
TOPSPIN vv3.5pl7 - collection
NMRPipe vv2016.273.11.31 - processing
NMRFAM-SPARKY vv1.470 - chemical shift assignment
NMR spectrometers:
- Bruker AVANCE NEO 800 MHz
- Bruker AVANCE III HD 600 MHz
Download HSQC peak lists in one of the following formats:
CSV: Backbone
or all simulated shifts
SPARKY: Backbone
or all simulated shifts