BMRB Entry 30680
Click here to enlarge.
PDB ID:
Entry in NMR Restraints Grid
Validation report in NRG-CING
Chem Shift validation: AVS_full
BMRB Entry DOI: doi:10.13018/BMR30680
MolProbity Validation Chart
NMR-STAR file interactive viewer.
NMR-STAR v3 text file.
XML gzip file.
RDF gzip file.
All files associated with the entry
Title: Sleeping Beauty transposase PAI subdomain mutant - H19Y
Deposition date: 2019-10-24 Original release date: 2020-10-23
Authors: Nesmelova, I.; Leighton, G.; Yan, C.; Lustig, J.; Corona, R.; Guo, J.; Ivics, Z.
Citation: Nesmelova, I.; Leighton, G.; Yan, C.; Lustig, J.; Corona, R.; Guo, J.; Ivics, Z.. "H19Y mutation in the primary DNA-recognition subdomain of the Sleeping Beauty transposase improves structural stability, transposon DNA-binding and transposition" .
Assembly members:
entity_1, polymer, 57 residues, 6389.402 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: ASMGKSKEISQDLRKRIVDL
YKSGSSLGAISKRLAVPRSS
VQTIVRKYKHHGTTQHH
- assigned_chemical_shifts
| Data type | Count |
| 13C chemical shifts | 143 |
| 15N chemical shifts | 55 |
| 1H chemical shifts | 360 |
Additional metadata:
Assembly:
| Entity Assembly ID | Entity Name | Entity ID |
|---|---|---|
| 1 | entity_1 | 1 |
Entities:
Entity 1, entity_1 57 residues - 6389.402 Da.
| 1 | ALA | SER | MET | GLY | LYS | SER | LYS | GLU | ILE | SER | ||||
| 2 | GLN | ASP | LEU | ARG | LYS | ARG | ILE | VAL | ASP | LEU | ||||
| 3 | TYR | LYS | SER | GLY | SER | SER | LEU | GLY | ALA | ILE | ||||
| 4 | SER | LYS | ARG | LEU | ALA | 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: pai subdomain mutant, [U-13C; U-15N], 0.5 mM
sample_conditions_1: ionic strength: 25 mM; pH: 5; pressure: 1 atm; temperature: 278 K
sample_conditions_2: ionic strength: 25 mM; pH: 5; pressure: 1 atm; temperature: 308 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 1H-15N 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 |
| 2D 1H-15N HSQC | sample_1 | isotropic | sample_conditions_2 |
| 3D CBCA(CO)NH | sample_1 | isotropic | sample_conditions_2 |
| 3D HNCACB | sample_1 | isotropic | sample_conditions_2 |
Software:
CARA, Keller and Wuthrich - chemical shift assignment
X-PLOR NIH, Schwieters, Kuszewski, Tjandra and Clore - structure calculation
NMRView, Johnson, One Moon Scientific - data analysis
NMR spectrometers:
- Bruker AVANCE III 700 MHz
- Bruker AVANCE III 950 MHz
Download HSQC peak lists in one of the following formats:
CSV: Backbone
or all simulated shifts
SPARKY: Backbone
or all simulated shifts