BMRB Entry 52077
Chem Shift validation: AVS_full
BMRB Entry DOI: doi:10.13018/BMR52077
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Title: TRBP2_dsRBD2 chemical shift assignment and dynamics data.
Deposition date: 2023-08-12 Original release date: 2023-09-08
Authors: Parvez, Firdousi
Citation: Parvez, Firdousi. "Differential conformational dynamics in two type-A RNA-binding domains drive the double-stranded RNA recognition and binding" .
Assembly members:
entity_1, polymer, 84 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: pHMGWA
Entity Sequences (FASTA):
entity_1: SNAQQSECNPVGALQELVVQ
KGWRLPEYTVTQESGPAHRK
EFTMTCRVERFIEIGSGTSK
KLAKRNAAAKMLLRVHTVPL
DARD
- assigned_chemical_shifts
- heteronucl_NOEs
- heteronucl_T1_relaxation
- heteronucl_T1rho_relaxation
- heteronucl_T2_relaxation
| Data type | Count |
| 13C chemical shifts | 183 |
| 15N chemical shifts | 73 |
| 1H chemical shifts | 379 |
| T1 relaxation values | 100 |
| T2 relaxation values | 98 |
| heteronuclear NOE values | 95 |
Additional metadata:
Assembly:
| Entity Assembly ID | Entity Name | Entity ID |
|---|---|---|
| 1 | TRBP2-dsRBD2 | 1 |
Entities:
Entity 1, TRBP2-dsRBD2 84 residues - Formula weight is not available
| 1 | SER | ASN | ALA | GLN | GLN | SER | GLU | CYS | ASN | PRO | ||||
| 2 | VAL | GLY | ALA | LEU | GLN | GLU | LEU | VAL | VAL | GLN | ||||
| 3 | LYS | GLY | TRP | ARG | LEU | PRO | GLU | TYR | THR | VAL | ||||
| 4 | THR | GLN | GLU | SER | GLY | PRO | ALA | HIS | ARG | LYS | ||||
| 5 | GLU | PHE | THR | MET | THR | CYS | ARG | VAL | GLU | ARG | ||||
| 6 | PHE | ILE | GLU | ILE | GLY | SER | GLY | THR | SER | LYS | ||||
| 7 | LYS | LEU | ALA | LYS | ARG | ASN | ALA | ALA | ALA | LYS | ||||
| 8 | MET | LEU | LEU | ARG | VAL | HIS | THR | VAL | PRO | LEU | ||||
| 9 | ASP | ALA | ARG | ASP |
Samples:
sample_1: TRBP2-dsRBD2 (TAR RNA binding protein isoform 1, second dsRNA binding domain), [U-13C; U-15N], 1.25 mM; TRBP2-dsRBD2 (TAR RNA binding protein isoform 1, second dsRNA binding domain), [U-15N], 1.25 mM
sample_conditions_1: ionic strength: 0.1 M; pH: 6.4; pressure: 1 atm; temperature: 298 K
Experiments:
| Name | Sample | Sample state | Sample conditions |
|---|---|---|---|
| 3D 1H-15N NOESY | sample_1 | isotropic | sample_conditions_1 |
| 3D 1H-15N TOCSY | sample_1 | isotropic | sample_conditions_1 |
| 2D 1H-15N HSQC | sample_1 | isotropic | sample_conditions_1 |
| 2D 1H-13C HSQC | 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 HNCA | sample_1 | isotropic | sample_conditions_1 |
| 3D HN(CO)CA | sample_1 | isotropic | sample_conditions_1 |
| 3D HNCACB | sample_1 | isotropic | sample_conditions_1 |
| 3D CBCA(CO)NH | sample_1 | isotropic | sample_conditions_1 |
| 1H-15N heteronoe | sample_1 | isotropic | sample_conditions_1 |
| 1H-15N heteronoe | sample_1 | isotropic | sample_conditions_1 |
| T1/R1 relaxation | sample_1 | isotropic | sample_conditions_1 |
| T2/R2 relaxation | sample_1 | isotropic | sample_conditions_1 |
| T1rho/R1rho relaxation | sample_1 | isotropic | sample_conditions_1 |
| T2rho/R2rho relaxation | sample_1 | isotropic | sample_conditions_1 |
| T1/R1 relaxation | sample_1 | isotropic | sample_conditions_1 |
| T2/R2 relaxation | sample_1 | isotropic | sample_conditions_1 |
Software:
CARA - chemical shift assignment
SPARKY - peak picking
Mathematica - data analysis
NMRPipe - processing
NMR spectrometers:
- Bruker Avance 600 MHz
- Bruker Avance 800 MHz
Download HSQC peak lists in one of the following formats:
CSV: Backbone
or all simulated shifts
SPARKY: Backbone
or all simulated shifts