BMRB Entry 51700
Chem Shift validation: AVS_full
BMRB Entry DOI: doi:10.13018/BMR51700
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Title: Backbone chemical shifts of human SAFB2 SAP domain PubMed: 36834708
Deposition date: 2022-11-21 Original release date: 2023-01-30
Authors: Korn, Sophie; Schlundt, Andreas
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, 53 residues, 5868.77 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: GAMGVAETGTRRLSELRVID
LRAELKKRNLDTGGNKSVLM
ERLKKAVKEEGQD
- assigned_chemical_shifts
| Data type | Count |
| 13C chemical shifts | 152 |
| 15N chemical shifts | 52 |
| 1H chemical shifts | 180 |
Additional metadata:
Assembly:
| Entity Assembly ID | Entity Name | Entity ID |
|---|---|---|
| 1 | SAP_A, chain 1 | 1 |
| 2 | SAP_A, chain 2 | 1 |
Entities:
Entity 1, SAP_A, chain 1 53 residues - 5868.77 Da.
Residues GAM (18-20) are artifacts from TEV cleavage, the natural sequence starts at Gly 21.
| 1 | GLY | ALA | MET | GLY | VAL | ALA | GLU | THR | GLY | THR | ||||
| 2 | ARG | ARG | LEU | SER | GLU | LEU | ARG | VAL | ILE | ASP | ||||
| 3 | LEU | ARG | ALA | GLU | LEU | LYS | LYS | ARG | ASN | LEU | ||||
| 4 | ASP | THR | GLY | GLY | ASN | LYS | SER | VAL | LEU | MET | ||||
| 5 | GLU | ARG | LEU | LYS | LYS | ALA | VAL | LYS | GLU | GLU | ||||
| 6 | GLY | GLN | ASP |
Samples:
sample_1: SAP dimer, [U-99% 15N], 0.25 ± 0.05 mM; NaCl 250 ± 2.5 mM; Bis-Tris 20 ± 0.2 mM
sample_2: SAP dimer, [U-98% 13C; U-98% 15N], 1 ± 0.2 mM; NaCl 250 ± 2.5 mM; Bis-Tris 20 ± 0.2 mM
sample_conditions_1: ionic strength: 0.25 M; pH: 6.5; 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 1H-15N NOESY | sample_1 | isotropic | sample_conditions_1 |
| 3D HNCACO | sample_2 | isotropic | sample_conditions_1 |
| 3D HNCACB | sample_2 | isotropic | sample_conditions_1 |
| 3D HNCO | sample_2 | isotropic | sample_conditions_1 |
| 3D HN(CO)CACB | sample_2 | isotropic | sample_conditions_1 |
| 3D HBHANH | sample_2 | isotropic | sample_conditions_1 |
| 3D HBHA(CO)NH | sample_2 | isotropic | sample_conditions_1 |
Software:
TOPSPIN v4 - collection, processing
ANALYSIS v2.4 - chemical shift assignment
NMR spectrometers:
- Bruker AVANCE III 950 MHz
- Bruker AVANCE NEO 600 MHz
Download HSQC peak lists in one of the following formats:
CSV: Backbone
or all simulated shifts
SPARKY: Backbone
or all simulated shifts