BMRB Entry 25380
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PDB ID:
Entry in NMR Restraints Grid
Validation report in NRG-CING
Chem Shift validation: AVS_full, LACS, SPARTA
BMRB Entry DOI: doi:10.13018/BMR25380
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Title: Solution structure of HP0268 from Helicobacter pylori PubMed: 25916841
Deposition date: 2014-12-05 Original release date: 2015-12-07
Authors: Lee, Ki-Young
Citation: Lee, Ki-Young; Lee, Kyu-Yeon; Kim, Ji-Hun; Lee, In-Gyun; Lee, Sung-Hee; Sim, Dae-Won; Won, Hyung-Sik; Lee, Bong-Jin. "Structure-based functional identification of Helicobacter pylori HP0268 as a nuclease with both DNA nicking and RNase activities" Nucleic Acids Res. 43, 5194-5207 (2015).
Assembly members:
HP0268, polymer, 82 residues, 9700.074 Da.
Natural source: Common Name: e-proteobacteria Taxonomy ID: 210 Superkingdom: Bacteria Kingdom: not available Genus/species: Helicobacter pylori
Experimental source: Production method: recombinant technology Host organism: Helicobacter pylori
Entity Sequences (FASTA):
HP0268: SHMKLVLAKNTRKSDAKSVE
LEDLYHEFSEDKRSIFYFAP
TNAHKDMLKAVDFFKEKGHT
AYLDEVRVSTDEKDFLYELH
II
- assigned_chemical_shifts
| Data type | Count |
| 13C chemical shifts | 328 |
| 15N chemical shifts | 80 |
| 1H chemical shifts | 459 |
Additional metadata:
Assembly:
| Entity Assembly ID | Entity Name | Entity ID |
|---|---|---|
| 1 | entity | 1 |
Entities:
Entity 1, entity 82 residues - 9700.074 Da.
| 1 | SER | HIS | MET | LYS | LEU | VAL | LEU | ALA | LYS | ASN | ||||
| 2 | THR | ARG | LYS | SER | ASP | ALA | LYS | SER | VAL | GLU | ||||
| 3 | LEU | GLU | ASP | LEU | TYR | HIS | GLU | PHE | SER | GLU | ||||
| 4 | ASP | LYS | ARG | SER | ILE | PHE | TYR | PHE | ALA | PRO | ||||
| 5 | THR | ASN | ALA | HIS | LYS | ASP | MET | LEU | LYS | ALA | ||||
| 6 | VAL | ASP | PHE | PHE | LYS | GLU | LYS | GLY | HIS | THR | ||||
| 7 | ALA | TYR | LEU | ASP | GLU | VAL | ARG | VAL | SER | THR | ||||
| 8 | ASP | GLU | LYS | ASP | PHE | LEU | TYR | GLU | LEU | HIS | ||||
| 9 | ILE | ILE |
Samples:
sample_1: sodium phosphate, [U-99% 13C; U-99% 15N], 0.8-1 mM; sodium chloride 50 mM; H2O 90%; D2O 10%
sample_conditions_1: ionic strength: 50 mM; pH: 6.0; pressure: 1 atm; temperature: 298 K
Experiments:
| Name | Sample | Sample state | Sample conditions |
|---|---|---|---|
| 2D 1H-15N HSQC | sample_1 | isotropic | sample_conditions_1 |
| 3D HNCO | sample_1 | isotropic | sample_conditions_1 |
| 3D HNCACB | sample_1 | isotropic | sample_conditions_1 |
| 3D HBHA(CO)NH | sample_1 | isotropic | sample_conditions_1 |
| 3D CBCA(CO)NH | sample_1 | isotropic | sample_conditions_1 |
| 3D C(CO)NH | sample_1 | isotropic | sample_conditions_1 |
| 3D HCCH-TOCSY | sample_1 | isotropic | sample_conditions_1 |
| 2D 1H-1H NOESY | 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 |
| 3D HN(CA)CO | sample_1 | isotropic | sample_conditions_1 |
Software:
CYANA, Guntert, Mumenthaler and Wuthrich - structure solution
NMR spectrometers:
- Bruker DRX 600 MHz
Download simulated HSQC data in one of the following formats:
CSV: Backbone
or all simulated shifts
SPARKY: Backbone
or all simulated shifts