BMRB Entry 18850
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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/BMR18850
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Title: Solution structure of the Haloferax volcanii HVO_2177 protein PubMed: 23821306
Deposition date: 2012-11-21 Original release date: 2013-08-05
Authors: Li, Yunfeng; Maciejewski, Mark; Martin, Jonathan; Jin, Kai; Zhang, Yuhang; Lu, Min; Maupin-Furlow, Julie; Hao, Bing
Citation: Li, Yunfeng; Maciejewski, Mark; Martin, Jonathan; Jin, Kai; Zhang, Yuhang; Maupin-Furlow, Julie; Hao, Bing. "Crystal structure of the ubiquitin-like small archaeal modifier protein 2 from Haloferax volcanii." Protein Sci. 22, 1206-1217 (2013).
Assembly members:
Ubl_protein_HVO_2177, polymer, 106 residues, 11540.825 Da.
Natural source: Common Name: Haloferax volcanii Taxonomy ID: 2246 Superkingdom: Archaea Kingdom: not available Genus/species: Haloferax volcanii
Experimental source: Production method: recombinant technology Host organism: Escherichia coli
Entity Sequences (FASTA):
Ubl_protein_HVO_2177: GGGRDYKDDDDKGTMELELR
FFATFREVVGQKSIYWRVDD
DATVGDVLRSLEAEYDGLAG
RLIEDGEVKPHVNVLKNGRE
VVHLDGMATALDDGDAVSVF
PPVAGG
- assigned_chemical_shifts
| Data type | Count |
| 13C chemical shifts | 441 |
| 15N chemical shifts | 98 |
| 1H chemical shifts | 678 |
Additional metadata:
Assembly:
| Entity Assembly ID | Entity Name | Entity ID |
|---|---|---|
| 1 | Haloferax volcanii HVO_2177 protein | 1 |
Entities:
Entity 1, Haloferax volcanii HVO_2177 protein 106 residues - 11540.825 Da.
residues 1-14 represent a non-native affinity tag
| 1 | GLY | GLY | GLY | ARG | ASP | TYR | LYS | ASP | ASP | ASP | ||||
| 2 | ASP | LYS | GLY | THR | MET | GLU | LEU | GLU | LEU | ARG | ||||
| 3 | PHE | PHE | ALA | THR | PHE | ARG | GLU | VAL | VAL | GLY | ||||
| 4 | GLN | LYS | SER | ILE | TYR | TRP | ARG | VAL | ASP | ASP | ||||
| 5 | ASP | ALA | THR | VAL | GLY | ASP | VAL | LEU | ARG | SER | ||||
| 6 | LEU | GLU | ALA | GLU | TYR | ASP | GLY | LEU | ALA | GLY | ||||
| 7 | ARG | LEU | ILE | GLU | ASP | GLY | GLU | VAL | LYS | PRO | ||||
| 8 | HIS | VAL | ASN | VAL | LEU | LYS | ASN | GLY | ARG | GLU | ||||
| 9 | VAL | VAL | HIS | LEU | ASP | GLY | MET | ALA | THR | ALA | ||||
| 10 | LEU | ASP | ASP | GLY | ASP | ALA | VAL | SER | VAL | PHE | ||||
| 11 | PRO | PRO | VAL | ALA | GLY | GLY |
Samples:
sample_1: Ubl protein HVO_2177, [U-99% 13C; U-99% 15N], 1 mM; NaCl 500 mM; Na-K phosphate 25 mM; EDTA 0.2 mM; NaN3 0.02%
sample_2: Ubl protein HVO_2177, [U-99% 13C; U-99% 15N], 1 mM; NaCl 500 mM; Na-K phosphate 25 mM; EDTA 0.2 mM; NaN3 0.02%
sample_conditions_1: ionic strength: 0.5 M; pH: 7.2; 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_2 | isotropic | sample_conditions_1 |
| 3D HNCACB | sample_1 | isotropic | sample_conditions_1 |
| 3D HNCO | sample_1 | isotropic | sample_conditions_1 |
| 3D HCACO | sample_1 | isotropic | sample_conditions_1 |
| 3D HBHA(CO)NH | sample_1 | isotropic | sample_conditions_1 |
| 3D C(CO)NH | sample_1 | isotropic | sample_conditions_1 |
| 3D H(CCO)NH | sample_1 | isotropic | sample_conditions_1 |
| 3D HCCH-TOCSY | sample_2 | isotropic | sample_conditions_1 |
| 2D 1H-13C HSQC aromatic | 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-13C NOESY aliphatic | sample_2 | isotropic | sample_conditions_1 |
| 3D 1H-13C NOESY aromatic | sample_2 | isotropic | sample_conditions_1 |
Software:
XEASY v1.2, Bartels et al. - chemical shift assignment, peak picking
CYANA v3.0, Guntert, Mumenthaler and Wuthrich - structure solution
VNMRJ v3.1, Varian - collection
Rowland NMR Toolkit v3.0, Hoch, Jeffrey C. & Stern, Alan S. - processing
CNS v1.3, Brunger, Adams, Clore, Gros, Nilges and Read - refinement
TALOS+, Cornilescu, Delaglio and Bax, Shen, Delaglio, Cornilescu, and Bax - torsion angle restraints
NMR spectrometers:
- Varian VNMRS 600 MHz
- Varian VNMRS 800 MHz
Related Database Links:
| GB | 8923994 ADE02783 ELK45920 ELY33406 ELZ55725 ELZ67244 |
| PDB | |
| EMBL | CQR48598 |
| REF | WP_004042069 WP_006601267 |
| SP | D4GVB0 |
Download simulated HSQC data in one of the following formats:
CSV: Backbone
or all simulated shifts
SPARKY: Backbone
or all simulated shifts