BMRB Entry 15101
Chem Shift validation: AVS_full, LACS
BMRB Entry DOI: doi:10.13018/BMR15101
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Title: Backbone 1H, 15N, and 13C Resonance Assignment and Secondary Structure Prediction of HP0495 from Helicobacter pylori PubMed: 17373705
Deposition date: 2007-01-18 Original release date: 2007-05-21
Authors: Seo, Min-Duk
Citation: Seo, Min-Duk; Park, Sung Jean; Kim, Hyun-Jung; Lee, Bong-Jin. "Solution structure of hypothetical protein, HP0495 (Y495_HELPY) from Helicobacter pylori" Proteins 67, 1189-1192 (2007).
Assembly members:
HP0495, polymer, 86 residues, Formula weight is not available
Natural source: Common Name: E. coli Taxonomy ID: 562 Superkingdom: Bacteria Kingdom: not available Genus/species: Escherichia coli
Experimental source: Production method: recombinant technology Host organism: Escherichia coli
Entity Sequences (FASTA):
HP0495: MPSDSKKPTIIYPCLWDYRV
IMTTKDTSTLKELLETYQRP
FKLEFKNTSKNAKFYSFNVS
MEVSNESERNEIFQKISQLD
KVVQTL
- assigned_chemical_shifts
Data type | Count |
13C chemical shifts | 246 |
15N chemical shifts | 80 |
1H chemical shifts | 159 |
Additional metadata:
Assembly:
Entity Assembly ID | Entity Name | Entity ID |
---|---|---|
1 | HP0495 | 1 |
Entities:
Entity 1, HP0495 86 residues - Formula weight is not available
1 | MET | PRO | SER | ASP | SER | LYS | LYS | PRO | THR | ILE | ||||
2 | ILE | TYR | PRO | CYS | LEU | TRP | ASP | TYR | ARG | VAL | ||||
3 | ILE | MET | THR | THR | LYS | ASP | THR | SER | THR | LEU | ||||
4 | LYS | GLU | LEU | LEU | GLU | THR | TYR | GLN | ARG | PRO | ||||
5 | PHE | LYS | LEU | GLU | PHE | LYS | ASN | THR | SER | LYS | ||||
6 | ASN | ALA | LYS | PHE | TYR | SER | PHE | ASN | VAL | SER | ||||
7 | MET | GLU | VAL | SER | ASN | GLU | SER | GLU | ARG | ASN | ||||
8 | GLU | ILE | PHE | GLN | LYS | ILE | SER | GLN | LEU | ASP | ||||
9 | LYS | VAL | VAL | GLN | THR | LEU |
Samples:
sample_1: HP0495, [U-99% 13C; U-99% 15N], 1.2 mM
sample_conditions_1: ionic strength: 0.15 M; pH: 6; pressure: 1 atm; temperature: 308 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 HNCA | 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 HCCH-TOCSY | sample_1 | isotropic | sample_conditions_1 |
3D 1H-15N NOESY | sample_1 | isotropic | sample_conditions_1 |
3D 1H-15N TOCSY | sample_1 | isotropic | sample_conditions_1 |
3D 1H-13C NOESY | sample_1 | isotropic | sample_conditions_1 |
Software:
NMRView, Johnson, One Moon Scientific - chemical shift assignment
NMR spectrometers:
- Bruker Avance 600 MHz
Related Database Links:
BMRB | 15190 |
PDB | |
GB | AAD07569 ADU82921 AFV41714 AFV43308 AFV44901 |
REF | NP_207292 WP_001138777 WP_001138778 |
SP | O25237 |
Download simulated HSQC data in one of the following formats:
CSV: Backbone
or all simulated shifts
SPARKY: Backbone
or all simulated shifts