BMRB Entry 15942
Chem Shift validation: AVS_full, LACS
BMRB Entry DOI: doi:10.13018/BMR15942
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NMR-STAR v3 text file.
XML gzip file.
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All files associated with the entry
Citation: Barsukov, Igor; Parnham, Stuart; Norman, Jim. "Solution structure of RRM2 domain of PABP1" .
Assembly members:
PABP1, polymer, 95 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: petM-11
Entity Sequences (FASTA):
PABP1: GADPSLRKSGVGNIFIKNLD
KSIDNKALYDTFSAFGNILS
CKVVCDENGSKGYGFVHFET
QEAAERAIEKMNGMLLNDRK
VFVGRFKSRKEREAE
- assigned_chemical_shifts
| Data type | Count |
| 13C chemical shifts | 325 |
| 15N chemical shifts | 100 |
| 1H chemical shifts | 660 |
Additional metadata:
Assembly:
| Entity Assembly ID | Entity Name | Entity ID |
|---|---|---|
| 1 | RRM2 | 1 |
Entities:
Entity 1, RRM2 95 residues - Formula weight is not available
residues 1 and 2 are from TEV cleavage site
| 1 | GLY | ALA | ASP | PRO | SER | LEU | ARG | LYS | SER | GLY | ||||
| 2 | VAL | GLY | ASN | ILE | PHE | ILE | LYS | ASN | LEU | ASP | ||||
| 3 | LYS | SER | ILE | ASP | ASN | LYS | ALA | LEU | TYR | ASP | ||||
| 4 | THR | PHE | SER | ALA | PHE | GLY | ASN | ILE | LEU | SER | ||||
| 5 | CYS | LYS | VAL | VAL | CYS | ASP | GLU | ASN | GLY | SER | ||||
| 6 | LYS | GLY | TYR | GLY | PHE | VAL | HIS | PHE | GLU | THR | ||||
| 7 | GLN | GLU | ALA | ALA | GLU | ARG | ALA | ILE | GLU | LYS | ||||
| 8 | MET | ASN | GLY | MET | LEU | LEU | ASN | ASP | ARG | LYS | ||||
| 9 | VAL | PHE | VAL | GLY | ARG | PHE | LYS | SER | ARG | LYS | ||||
| 10 | GLU | ARG | GLU | ALA | GLU |
Samples:
sample_1: PABP1, [U-98% 13C; U-98% 15N], 1 mM; sodium chloride 20 mM; sodium phosphate 20 mM; DTT 1 mM
sample_conditions_1: ionic strength: 0.04 M; pH: 6.1; pressure: 1 atm; temperature: 303 K
Experiments:
| Name | Sample | Sample state | Sample conditions |
|---|---|---|---|
| 2D 1H-15N HSQC | sample_1 | isotropic | sample_conditions_1 |
| 2D 1H-13C HSQC | sample_1 | isotropic | sample_conditions_1 |
| 3D CBCA(CO)NH | sample_1 | isotropic | sample_conditions_1 |
| 3D HNCACB | sample_1 | isotropic | sample_conditions_1 |
| 3D HNCO | sample_1 | isotropic | sample_conditions_1 |
| 3D HCCH-TOCSY | sample_1 | isotropic | sample_conditions_1 |
| 3D 1H-15N NOESY | sample_1 | isotropic | sample_conditions_1 |
| 3D 1H-13C NOESY | sample_1 | isotropic | sample_conditions_1 |
| 3D 1H-15N TOCSY | sample_1 | isotropic | sample_conditions_1 |
Software:
TOPSPIN v2.1, Bruker Biospin - collection
NMR spectrometers:
- Bruker Avance 800 MHz
Download HSQC peak lists in one of the following formats:
CSV: Backbone
or all simulated peaks
SPARKY: Backbone
or all simulated peaks