BMRB Entry 30239
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PDB ID:
Entry in NMR Restraints Grid
Validation report in NRG-CING
Chem Shift validation: AVS_full, LACS
BMRB Entry DOI: doi:10.13018/BMR30239
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Title: NMR structure of the RED subdomain of the Sleeping Beauty transposase PubMed: 28345263
Deposition date: 2017-01-31 Original release date: 2017-06-02
Authors: Konnova, T.; Singer, C.; Nesmelova, I.
Citation: Konnova, T.; Singer, C.; Nesmelova, I.. "NMR solution structure of the RED subdomain of the Sleeping Beauty transposase." Protein Sci. 26, 1171-1181 (2017).
Assembly members:
entity_1, polymer, 62 residues, 7122.414 Da.
Natural source: Common Name: Rainbow trout Taxonomy ID: 8022 Superkingdom: Eukaryota Kingdom: Metazoa Genus/species: Oncorhynchus mykiss
Experimental source: Production method: recombinant technology Host organism: Escherichia coli
Entity Sequences (FASTA):
entity_1: ASMVLSPRDERTLVRKVQIN
PRTTAKDLVKMLEETGTKVS
ISTVKRVLYRHNLKGRSARK
LE
- assigned_chemical_shifts
| Data type | Count |
| 13C chemical shifts | 164 |
| 15N chemical shifts | 62 |
| 1H chemical shifts | 404 |
Additional metadata:
Assembly:
| Entity Assembly ID | Entity Name | Entity ID |
|---|---|---|
| 1 | entity_1 | 1 |
Entities:
Entity 1, entity_1 62 residues - 7122.414 Da.
| 1 | ALA | SER | MET | VAL | LEU | SER | PRO | ARG | ASP | GLU | ||||
| 2 | ARG | THR | LEU | VAL | ARG | LYS | VAL | GLN | ILE | ASN | ||||
| 3 | PRO | ARG | THR | THR | ALA | LYS | ASP | LEU | VAL | LYS | ||||
| 4 | MET | LEU | GLU | GLU | THR | GLY | THR | LYS | VAL | SER | ||||
| 5 | ILE | SER | THR | VAL | LYS | ARG | VAL | LEU | TYR | ARG | ||||
| 6 | HIS | ASN | LEU | LYS | GLY | ARG | SER | ALA | ARG | LYS | ||||
| 7 | LEU | GLU |
Samples:
sample_1: MES 20 mM; RED subdomain of the Sleeping Beauty transposase, [U-13C; U-15N], 2 mg/mL; sodium sulfate 650 mM
sample_2: MES 20 mM; RED subdomain of the Sleeping Beauty transposase, [U-13C; U-15N], 2 mg/mL; sodium sulfate 650 mM
sample_conditions_1: ionic strength: 650 mM; pH: 5; pressure: 1 .; temperature: 293 K
Experiments:
| Name | Sample | Sample state | Sample conditions |
|---|---|---|---|
| 3D HNCACB | sample_1 | isotropic | sample_conditions_1 |
| 3D CBCA(CO)NH | sample_1 | isotropic | sample_conditions_1 |
| 3D HCCH-TOCSY | sample_2 | isotropic | sample_conditions_1 |
| 3D 1H-15N TOCSY | sample_1 | isotropic | sample_conditions_1 |
| 3D 1H-15N NOESY | sample_1 | isotropic | sample_conditions_1 |
| 3D 1H-13C NOESY | sample_2 | isotropic | sample_conditions_1 |
Software:
CARA, Keller and Wuthrich - chemical shift assignment
NMRPipe, Delaglio, Grzesiek, Vuister, Zhu, Pfeifer and Bax - processing
TALOS, Cornilescu, Delaglio and Bax - geometry optimization
TOPSPIN, Bruker Biospin - collection
xplor-nih, Schwieters, C. D., Kuszewski, J. J., Tjandra, N. and Clore, G. M. - structure calculation
NMR spectrometers:
- Bruker AvanceIII 950 MHz
Download simulated HSQC data in one of the following formats:
CSV: Backbone
or all simulated shifts
SPARKY: Backbone
or all simulated shifts