BMRB Entry 17939
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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/BMR17939
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Title: a protein from Haloferax volcanii
Deposition date: 2011-09-14 Original release date: 2012-10-09
Authors: Zhang, Wen; Liao, Shanhui; Fan, Kai
Citation: Liao, Shanhui; Zhang, Wen; Fan, Kai; Tu, Xiaoming. "structure of a protein from Haloferax volcanii" Not known ., .-..
Assembly members:
a protein from Haloferax volcanii, polymer, 132 residues, 14231.962 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):
a protein from Haloferax volcanii: MNVTVEVVGEETSEVAVDDD
GTYADLVRAVDLSPHEVTVL
VDGRPVPEDQSVEVDRVKVL
RLIKGGMNVTVEVVGEETSE
VAVDDDGTYADLVRAVDLSP
HEVTVLVDGRPVPEDQSVEV
DRVKVLRLIKGG
- assigned_chemical_shifts
| Data type | Count |
| 13C chemical shifts | 98 |
| 15N chemical shifts | 55 |
| 1H chemical shifts | 339 |
Additional metadata:
Assembly:
| Entity Assembly ID | Entity Name | Entity ID |
|---|---|---|
| 1 | a protein from Haloferax volcanii | 1 |
Entities:
Entity 1, a protein from Haloferax volcanii 132 residues - 14231.962 Da.
| 1 | MET | ASN | VAL | THR | VAL | GLU | VAL | VAL | GLY | GLU | ||||
| 2 | GLU | THR | SER | GLU | VAL | ALA | VAL | ASP | ASP | ASP | ||||
| 3 | GLY | THR | TYR | ALA | ASP | LEU | VAL | ARG | ALA | VAL | ||||
| 4 | ASP | LEU | SER | PRO | HIS | GLU | VAL | THR | VAL | LEU | ||||
| 5 | VAL | ASP | GLY | ARG | PRO | VAL | PRO | GLU | ASP | GLN | ||||
| 6 | SER | VAL | GLU | VAL | ASP | ARG | VAL | LYS | VAL | LEU | ||||
| 7 | ARG | LEU | ILE | LYS | GLY | GLY | MET | ASN | VAL | THR | ||||
| 8 | VAL | GLU | VAL | VAL | GLY | GLU | GLU | THR | SER | GLU | ||||
| 9 | VAL | ALA | VAL | ASP | ASP | ASP | GLY | THR | TYR | ALA | ||||
| 10 | ASP | LEU | VAL | ARG | ALA | VAL | ASP | LEU | SER | PRO | ||||
| 11 | HIS | GLU | VAL | THR | VAL | LEU | VAL | ASP | GLY | ARG | ||||
| 12 | PRO | VAL | PRO | GLU | ASP | GLN | SER | VAL | GLU | VAL | ||||
| 13 | ASP | ARG | VAL | LYS | VAL | LEU | ARG | LEU | ILE | LYS | ||||
| 14 | GLY | GLY |
Samples:
sample_1: a protein from Haloferax volcanii, [15N;13C], 0.6 mM; sodium phosphate 20 mM; sodium chloride 100 mM; H2O 90%; D2O 10%
sample_2: a protein from Haloferax volcanii, [15N;13C], 0.6 mM; sodium phosphate 20 mM; sodium chloride 100 mM; D2O 100%
sample_conditions_1: ionic strength: 0.12 M; pH: 6.5; pressure: 1 atm; temperature: 293 K
Experiments:
| Name | Sample | Sample state | Sample conditions |
|---|---|---|---|
| 3D 1H-13C NOESY | sample_2 | isotropic | sample_conditions_1 |
| 3D CBCA(CO)NH | sample_1 | isotropic | sample_conditions_1 |
| 3D HNCACB | sample_1 | isotropic | sample_conditions_1 |
| 3D H(CCO)NH | sample_1 | isotropic | sample_conditions_1 |
| 3D HBHA(CO)NH | sample_1 | isotropic | sample_conditions_1 |
| 3D 1H-15N NOESY | sample_1 | isotropic | sample_conditions_1 |
| 3D HCCH-TOCSY | sample_2 | isotropic | sample_conditions_1 |
| 2D 1H-15N HSQC | sample_1 | isotropic | sample_conditions_1 |
Software:
NMRDraw, Delaglio, Grzesiek, Vuister, Zhu, Pfeifer and Bax - data analysis
SPARKY, Goddard - data analysis
CNS, Brunger, Adams, Clore, Gros, Nilges and Read - chemical shift calculation
NMR spectrometers:
- Bruker DMX 500 MHz
Related Database Links:
| BMRB | 17204 |
| PDB | |
| GB | ADE03392 AKU06380 ELK50451 ELY23894 ELZ70132 |
| REF | WP_004045316 WP_004065555 WP_008609462 |
| SP | D4GZE7 |
Download simulated HSQC data in one of the following formats:
CSV: Backbone
or all simulated shifts
SPARKY: Backbone
or all simulated shifts