BMRB Entry 19249
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PDB ID:
Entry in NMR Restraints Grid
Validation report in NRG-CING
Chem Shift validation: AVS_full, SPARTA
BMRB Entry DOI: doi:10.13018/BMR19249
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Title: NMR structure of the PAI subdomain of Sleeping Beauty transposase PubMed: 24243759
Deposition date: 2013-05-17 Original release date: 2013-12-16
Authors: Eubanks, Claire; Schreifels, Jeff; Aronovich, Elena; Carlson, Daniel; Hacjkett, Perry; Nesmelova, Irina
Citation: Carpentier, Claire; Schreifels, Jeffrey; Aronovich, Elena; Carlson, Daniel; Hackett, Perry; Nesmelova, Irina. "NMR structural analysis of Sleeping Beauty transposase binding to DNA." Protein Sci. 23, 23-33 (2014).
Assembly members:
entity, polymer, 57 residues, 6394.522 Da.
Natural source: Common Name: not available Taxonomy ID: not available Superkingdom: not available Kingdom: not available Genus/species: not available not available
Experimental source: Production method: recombinant technology Host organism: Escherichia coli
Entity Sequences (FASTA):
entity: ASMGKSKEISQDLRKKIVDL
HKSGSSLGAISKRLKVPRSS
VQTIVRKYKHHGTTQHH
- assigned_chemical_shifts
| Data type | Count |
| 15N chemical shifts | 54 |
| 1H chemical shifts | 322 |
Additional metadata:
Assembly:
| Entity Assembly ID | Entity Name | Entity ID |
|---|---|---|
| 1 | PAI subdomain of Sleeping Beauty transposase | 1 |
Entities:
Entity 1, PAI subdomain of Sleeping Beauty transposase 57 residues - 6394.522 Da.
| 1 | ALA | SER | MET | GLY | LYS | SER | LYS | GLU | ILE | SER | ||||
| 2 | GLN | ASP | LEU | ARG | LYS | LYS | ILE | VAL | ASP | LEU | ||||
| 3 | HIS | LYS | SER | GLY | SER | SER | LEU | GLY | ALA | ILE | ||||
| 4 | SER | LYS | ARG | LEU | LYS | VAL | PRO | ARG | SER | SER | ||||
| 5 | VAL | GLN | THR | ILE | VAL | ARG | LYS | TYR | LYS | HIS | ||||
| 6 | HIS | GLY | THR | THR | GLN | HIS | HIS |
Samples:
sample_1: entity, [U-100% 15N], 0.15 mM; sodium phosphate 20 mM; H2O 90%; D2O 10%
sample_2: entity, [U-100% 15N], 0.15 mM; sodium phosphate 20 mM; H2O 90%; D2O 10%
sample_conditions_1: ionic strength: 20 mM; pH: 7; pressure: 1 atm; temperature: 273 K
Experiments:
| Name | Sample | Sample state | Sample conditions |
|---|---|---|---|
| 2D 1H-15N HSQC | sample_1 | isotropic | sample_conditions_1 |
| 2D 1H-1H TOCSY | sample_2 | isotropic | sample_conditions_1 |
| 2D 1H-1H NOESY | sample_2 | isotropic | sample_conditions_1 |
| 3D 1H-15N NOESY | sample_1 | isotropic | sample_conditions_1 |
| 3D 1H-15N TOCSY | sample_1 | isotropic | sample_conditions_1 |
Software:
X-PLOR NIH, Schwieters, Kuszewski, Tjandra and Clore - structure solution
NMR spectrometers:
- Bruker Avance 950 MHz
Download simulated HSQC data in one of the following formats:
CSV: Backbone
or all simulated shifts
SPARKY: Backbone
or all simulated shifts