BMRB Entry 51701
Chem Shift validation: AVS_full
BMRB Entry DOI: doi:10.13018/BMR51701
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Title: Backbone chemical shifts of human SAFB2 RRM domain at pH 5.0 PubMed: 36834708
Deposition date: 2022-11-21 Original release date: 2023-01-30
Authors: Schlundt, Andreas; Korn, Sophie
Citation: Korn, Sophie; Von Ehr, Julian; Dhamotharan, Karthikeyan; Tants, Jan-Niklas; Abele, Rupert; Schlundt, Andreas. "Insight into the Structural Basis for Dual Nucleic Acid-Recognition by the Scaffold Attachment Factor B2 Protein" Int. J. Mol. Sci. 24, 3286-3286 (2023).
Assembly members:
entity_1, polymer, 85 residues, 9131.46 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: pETTrx1a
Entity Sequences (FASTA):
entity_1: GAMGSGRNLWVSGLSSTTRA
TDLKNLFSKYGKVVGAKVVT
NARSPGARCYGFVTMSTSDE
ATKCISHLHRTELHGRMISV
EKAKN
- assigned_chemical_shifts
| Data type | Count |
| 13C chemical shifts | 246 |
| 15N chemical shifts | 84 |
| 1H chemical shifts | 87 |
Additional metadata:
Assembly:
| Entity Assembly ID | Entity Name | Entity ID |
|---|---|---|
| 1 | SAFB2 RRM domain | 1 |
Entities:
Entity 1, SAFB2 RRM domain 85 residues - 9131.46 Da.
Residues GAM (401-403) are artifacts from TEV cleavage, the natural sequence starts at Gly 404.
| 1 | GLY | ALA | MET | GLY | SER | GLY | ARG | ASN | LEU | TRP | ||||
| 2 | VAL | SER | GLY | LEU | SER | SER | THR | THR | ARG | ALA | ||||
| 3 | THR | ASP | LEU | LYS | ASN | LEU | PHE | SER | LYS | TYR | ||||
| 4 | GLY | LYS | VAL | VAL | GLY | ALA | LYS | VAL | VAL | THR | ||||
| 5 | ASN | ALA | ARG | SER | PRO | GLY | ALA | ARG | CYS | TYR | ||||
| 6 | GLY | PHE | VAL | THR | MET | SER | THR | SER | ASP | GLU | ||||
| 7 | ALA | THR | LYS | CYS | ILE | SER | HIS | LEU | HIS | ARG | ||||
| 8 | THR | GLU | LEU | HIS | GLY | ARG | MET | ILE | SER | VAL | ||||
| 9 | GLU | LYS | ALA | LYS | ASN |
Samples:
sample_1: SAFB2 RRM domain, [U-99% 15N], 620 ± 12.4 uM; NaCl 150 ± 1.5 mM; Bis-Tris 20 ± 0.2 mM; TCEP 2 ± 0.02 mM
sample_2: SAFB2 RRM domain, [U-98% 13C; U-98% 15N], 440 ± 8.8 uM; NaCl 150 ± 1.5 mM; Bis-Tris 20 ± 0.2 mM; TCEP 2 ± 0.02 mM
sample_conditions_1: ionic strength: 0.15 M; pH: 5.0; pressure: 1 atm; temperature: 298 K
Experiments:
| Name | Sample | Sample state | Sample conditions |
|---|---|---|---|
| 1D 1H | sample_1 | isotropic | sample_conditions_1 |
| 2D 1H-15N HSQC | sample_1 | isotropic | sample_conditions_1 |
| 2D 1H-13C HSQC | sample_2 | isotropic | sample_conditions_1 |
| 3D HNCO | sample_2 | isotropic | sample_conditions_1 |
| 3D HNCACB | sample_2 | isotropic | sample_conditions_1 |
| 3D HN(CA)CO | sample_2 | isotropic | sample_conditions_1 |
| 3D 1H-15N NOESY | sample_1 | isotropic | sample_conditions_1 |
Software:
TOPSPIN v4 - collection, processing
ANALYSIS v2.3 - chemical shift assignment
NMR spectrometers:
- Bruker AVANCE III 950 MHz
- Bruker AVANCE NEO 900 MHz
Download HSQC peak lists in one of the following formats:
CSV: Backbone
or all simulated shifts
SPARKY: Backbone
or all simulated shifts