BMRB Entry 16175
Chem Shift validation: AVS_anomalous, AVS_full, LACS
BMRB Entry DOI: doi:10.13018/BMR16175
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Title: Backbone assignments for odorant binding protein 1 PubMed: 19888689
Deposition date: 2009-02-13 Original release date: 2009-07-10
Authors: Ames, James
Citation: Xu, Xianzhong; Xu, Wei; Ishida, Yuko; Li, Yun; Leal, Walter; Ames, James. "(1)H, (15)N, and (13)C chemical shift assignments of the mosquito odorant binding protein-1 (CquiOBP1) bound to the mosquito oviposition pheromone." Biomol NMR Assign 3, 195-197 (2009).
Assembly members:
CquiOBP1, polymer, 125 residues, Formula weight is not available
Natural source: Common Name: southern house mosquito Taxonomy ID: 7176 Superkingdom: Eukaryota Kingdom: Metazoa Genus/species: Culex Culex pipiens quinquefasciatus
Experimental source: Production method: recombinant technology Host organism: Escherichia coli
Entity Sequences (FASTA):
CquiOBP1: DVTPRRDAEYPPPELLEALK
PLHDICAKKTGVTDEAIIEF
SDGKIHEDEKLKCYMNCLFH
EAKVVDDNGDVHLEKLRDSL
PNSMHDIAMHMGKRCLYPEG
ENLCEKAFWLHKCWKQADPK
HYFLV
- assigned_chemical_shifts
Data type | Count |
13C chemical shifts | 496 |
15N chemical shifts | 120 |
1H chemical shifts | 804 |
Additional metadata:
Assembly:
Entity Assembly ID | Entity Name | Entity ID |
---|---|---|
1 | subunit 1 | 1 |
Entities:
Entity 1, subunit 1 125 residues - Formula weight is not available
1 | ASP | VAL | THR | PRO | ARG | ARG | ASP | ALA | GLU | TYR | ||||
2 | PRO | PRO | PRO | GLU | LEU | LEU | GLU | ALA | LEU | LYS | ||||
3 | PRO | LEU | HIS | ASP | ILE | CYS | ALA | LYS | LYS | THR | ||||
4 | GLY | VAL | THR | ASP | GLU | ALA | ILE | ILE | GLU | PHE | ||||
5 | SER | ASP | GLY | LYS | ILE | HIS | GLU | ASP | GLU | LYS | ||||
6 | LEU | LYS | CYS | TYR | MET | ASN | CYS | LEU | PHE | HIS | ||||
7 | GLU | ALA | LYS | VAL | VAL | ASP | ASP | ASN | GLY | ASP | ||||
8 | VAL | HIS | LEU | GLU | LYS | LEU | ARG | ASP | SER | LEU | ||||
9 | PRO | ASN | SER | MET | HIS | ASP | ILE | ALA | MET | HIS | ||||
10 | MET | GLY | LYS | ARG | CYS | LEU | TYR | PRO | GLU | GLY | ||||
11 | GLU | ASN | LEU | CYS | GLU | LYS | ALA | PHE | TRP | LEU | ||||
12 | HIS | LYS | CYS | TRP | LYS | GLN | ALA | ASP | PRO | LYS | ||||
13 | HIS | TYR | PHE | LEU | VAL |
Samples:
sample_1: CquiOBP1, [U-98% 13C; U-98% 15N], 0.5 mM
sample_conditions_1: ionic strength: 20 mM; pH: 7.0; pressure: 1 atm; temperature: 298 K
Experiments:
Name | Sample | Sample state | Sample conditions |
---|---|---|---|
2D 1H-15N HSQC | sample_1 | isotropic | sample_conditions_1 |
3D CBCA(CO)NH | sample_1 | isotropic | sample_conditions_1 |
3D C(CO)NH | 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 H(CCO)NH | sample_1 | isotropic | sample_conditions_1 |
Software:
NMRPipe, Delaglio, Grzesiek, Vuister, Zhu, Pfeifer and Bax - processing
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