BMRB Entry 15190
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PDB ID:
Entry in NMR Restraints Grid
Validation report in NRG-CING
Chem Shift validation: AVS_anomalous, AVS_full, LACS, SPARTA
BMRB Entry DOI: doi:10.13018/BMR15190
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Title: Solution Structure of Protein HP0495 from H. pylori; Northeast structural genomics consortium target PT2; Ontario Centre for Structural Proteomics target HP0488
Deposition date: 2007-03-19 Original release date: 2009-06-15
Authors: Gutmanas, Aleksandras; Lemak, Alexander; Yee, Adelinda; Karra, Murthy; Srisailam, Sampath; Semesi, Anthony; Arrowsmith, Cheryl
Citation: Gutmanas, Aleksandras; Lemak, Alexander; Yee, Adelinda; Karra, Murthy; Srisailam, Sampath; Semesi, Anthony; Arrowsmith, Cheryl. "Solution Structure of Protein HP0495 from H. pylori" The BMRB entry is the only known published source for the data..
Assembly members:
HP0495, polymer, 91 residues, 10677.271 Da.
Natural source: Common Name: not available Taxonomy ID: 210 Superkingdom: Bacteria Kingdom: not available Genus/species: Helicobacter pylori
Experimental source: Production method: recombinant technology Host organism: Escherichia coli
Entity Sequences (FASTA):
HP0495: QGHMPSDSKKPTIIYPCLWD
YRVIMTTKDTSTLKELLETY
QRPFKLEFKNTSKNAKFYSF
NVSMEVSNESERNEIFQKIS
QLDKVVQTLGS
- assigned_chemical_shifts
- spectral_peak_list
| Data type | Count |
| 13C chemical shifts | 413 |
| 15N chemical shifts | 91 |
| 1H chemical shifts | 653 |
Additional metadata:
Assembly:
| Entity Assembly ID | Entity Name | Entity ID |
|---|---|---|
| 1 | HP0495 | 1 |
Entities:
Entity 1, HP0495 91 residues - 10677.271 Da.
Residues 1-3 are from a non-native N-terminal affinity tag; Residues 90-91 are from non-native C-terminal affinity tag
| 1 | GLN | GLY | HIS | MET | PRO | SER | ASP | SER | LYS | LYS | ||||
| 2 | PRO | THR | ILE | ILE | TYR | PRO | CYS | LEU | TRP | ASP | ||||
| 3 | TYR | ARG | VAL | ILE | MET | THR | THR | LYS | ASP | THR | ||||
| 4 | SER | THR | LEU | LYS | GLU | LEU | LEU | GLU | THR | TYR | ||||
| 5 | GLN | ARG | PRO | PHE | LYS | LEU | GLU | PHE | LYS | ASN | ||||
| 6 | THR | SER | LYS | ASN | ALA | LYS | PHE | TYR | SER | PHE | ||||
| 7 | ASN | VAL | SER | MET | GLU | VAL | SER | ASN | GLU | SER | ||||
| 8 | GLU | ARG | ASN | GLU | ILE | PHE | GLN | LYS | ILE | SER | ||||
| 9 | GLN | LEU | ASP | LYS | VAL | VAL | GLN | THR | LEU | GLY | ||||
| 10 | SER |
Samples:
sample_1: HP0495, [U-13C; U-15N], 0.5 mM; TRIS 10 mM; sodium chloride 300 mM; benzamidine 1 mM; DTT 10 mM; sodium azide 0.01%; H2O 95%; D2O 5%
sample_2: HP0495, [U-13C; U-15N], 0.5 mM; TRIS 10 mM; sodium chloride 300 mM; benzamidine 1 mM; DTT 10 mM; sodium azide 0.01%; D2O 100%
sample_conditions_1: ionic strength: 300 mM; pH: 7; pressure: 1 atm; temperature: 298 K
Experiments:
| Name | Sample | Sample state | Sample conditions |
|---|---|---|---|
| 2D 1H-15N HSQC | sample_1 | isotropic | sample_conditions_1 |
| 2D 1H-13C HSQC | sample_1 | isotropic | sample_conditions_1 |
| 3D CBCA(CO)NH | sample_1 | isotropic | sample_conditions_1 |
| 3D HNCO sparse | sample_1 | isotropic | sample_conditions_1 |
| 3D HNCA sparse | sample_1 | isotropic | sample_conditions_1 |
| 3D H(CCCO)NH-TOCSY sparse | sample_1 | isotropic | sample_conditions_1 |
| 3D (H)C(CCO)NH-TOCSY | sample_1 | isotropic | sample_conditions_1 |
| 4D HBHACBCA(CO)NH PR | sample_1 | isotropic | sample_conditions_1 |
| 4D HC(CCO)NH-TOCSY PR | sample_1 | isotropic | sample_conditions_1 |
| 3D 1H-15N NOESY sparse | sample_1 | isotropic | sample_conditions_1 |
| 3D 1H-13C NOESY aliphatic | sample_1 | isotropic | sample_conditions_1 |
| 3D H(C)CH-TOCSY sparse | sample_2 | isotropic | sample_conditions_1 |
| 3D (H)CCH-TOCSY sparse | sample_2 | isotropic | sample_conditions_1 |
| 3D 1H-13C NOESY aromatic | sample_1 | isotropic | sample_conditions_1 |
| 3D 1H-13C NOESY sparse | sample_2 | isotropic | sample_conditions_1 |
| 3D H(C)CH-TOCSY aromatic, sparse | sample_2 | isotropic | sample_conditions_1 |
| 3D (H)CCH-TOCSY aromatic | sample_2 | isotropic | sample_conditions_1 |
| 2D CT 1H-13C HSQC | sample_2 | isotropic | sample_conditions_1 |
| 2D CT 1H-13C HSQC aromatic | sample_2 | isotropic | sample_conditions_1 |
Software:
CNS v1.1, Brunger, Adams, Clore, Gros, Nilges and Read - refinement
CYANA v2.1, Guntert, Mumenthaler and Wuthrich - structure solution
SPARKY, Goddard - peak picking
TALOS, Cornilescu, Delaglio and Bax - dihedral angle constraints prediction
ABACUS, A. Lemak, A. Grishaev, M. Llinas, CH Arrowsmith - chemical shift and NOE assignment
MDD/MDDgui, A. Gutmanas, CH Arrowsmith, I Ibraghimov, V Yu Orekhov - processing of non-uniformly sampled data
NMRPipe, Delaglio, Grzesiek, Vuister, Zhu, Pfeifer and Bax - processing
PR, M Karra, CH Arrowsmith - processing of Projection-Reconstruction spectra
NMR spectrometers:
- Bruker Avance 500 MHz
- Bruker Avance 600 MHz
- Bruker Avance 800 MHz
- Varian INOVA 500 MHz
Related Database Links:
| BMRB | 15101 |
| 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