BMRB Entry 51937
Chem Shift validation: AVS_full
BMRB Entry DOI: doi:10.13018/BMR51937
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Title: 1H, 13C, and 15N resonance assignment and secondary structure of the pheromone binding protein 3 of Ostrinia nubilalis (OnubPBP3), an agricultural pest. PubMed: 37498448
Deposition date: 2023-04-24 Original release date: 2023-08-30
Authors: Al-Danoon, Omar; Mohanty, Smita
Citation: Al-Danoon, Omar; Mohanty, Smita. "Backbone and side chain NMR assignments and secondary structure calculation of the pheromone binding protein3 of Ostrinia nubilalis, an agricultural pest" Biomol. NMR Assignments 17, 223-227 (2023).
Assembly members:
entity_1, polymer, 144 residues, 16299.60 Da.
Natural source: Common Name: European corn borer Taxonomy ID: 29057 Superkingdom: Eukaryota Kingdom: Metazoa Genus/species: Ostrinia nubilalis
Experimental source: Production method: recombinant technology Host organism: Escherichia coli Vector: pET21a
Entity Sequences (FASTA):
entity_1: SQTVMREMTRNFIKAYEVCA
KEYNLPEATGSELINFWKEG
HELTTREAGCAILCMSTKLN
LLDVQGSVHRGNTVEFAKHH
GSDDAMAHQVVDILHACEKA
TPNEDKCMLALSIAMCFKAE
IHKLDWAPNHELMFEELVSD
MWNS
- assigned_chemical_shifts
| Data type | Count |
| 13C chemical shifts | 552 |
| 15N chemical shifts | 139 |
| 1H chemical shifts | 852 |
Additional metadata:
Assembly:
| Entity Assembly ID | Entity Name | Entity ID |
|---|---|---|
| 1 | OnubPBP3 | 1 |
Entities:
Entity 1, OnubPBP3 144 residues - 16299.60 Da.
| 1 | SER | GLN | THR | VAL | MET | ARG | GLU | MET | THR | ARG | ||||
| 2 | ASN | PHE | ILE | LYS | ALA | TYR | GLU | VAL | CYS | ALA | ||||
| 3 | LYS | GLU | TYR | ASN | LEU | PRO | GLU | ALA | THR | GLY | ||||
| 4 | SER | GLU | LEU | ILE | ASN | PHE | TRP | LYS | GLU | GLY | ||||
| 5 | HIS | GLU | LEU | THR | THR | ARG | GLU | ALA | GLY | CYS | ||||
| 6 | ALA | ILE | LEU | CYS | MET | SER | THR | LYS | LEU | ASN | ||||
| 7 | LEU | LEU | ASP | VAL | GLN | GLY | SER | VAL | HIS | ARG | ||||
| 8 | GLY | ASN | THR | VAL | GLU | PHE | ALA | LYS | HIS | HIS | ||||
| 9 | GLY | SER | ASP | ASP | ALA | MET | ALA | HIS | GLN | VAL | ||||
| 10 | VAL | ASP | ILE | LEU | HIS | ALA | CYS | GLU | LYS | ALA | ||||
| 11 | THR | PRO | ASN | GLU | ASP | LYS | CYS | MET | LEU | ALA | ||||
| 12 | LEU | SER | ILE | ALA | MET | CYS | PHE | LYS | ALA | GLU | ||||
| 13 | ILE | HIS | LYS | LEU | ASP | TRP | ALA | PRO | ASN | HIS | ||||
| 14 | GLU | LEU | MET | PHE | GLU | GLU | LEU | VAL | SER | ASP | ||||
| 15 | MET | TRP | ASN | SER |
Samples:
sample_1: Ostrinia nubilalis Pheromone Binding Protein 3, [U-100% 13C; U-100% 15N], 460 uM; EDTA 1 mM; sodium azide 0.01%
sample_conditions_1: ionic strength: 50 mM; pH: 6.5; pressure: 1 atm; temperature: 308 K
Experiments:
| Name | Sample | Sample state | Sample conditions |
|---|---|---|---|
| 2D 1H-15N HSQC | sample_1 | isotropic | sample_conditions_1 |
| 3D HNCA | sample_1 | isotropic | sample_conditions_1 |
| 3D HNCACB | sample_1 | isotropic | sample_conditions_1 |
| 3D CBCA(CO)NH | sample_1 | isotropic | sample_conditions_1 |
| 3D HNCO | sample_1 | isotropic | sample_conditions_1 |
| 3D HN(CA)CO | sample_1 | isotropic | sample_conditions_1 |
| 3D CC(CO)NH | sample_1 | isotropic | sample_conditions_1 |
| 3D H(CCO)NH | sample_1 | isotropic | sample_conditions_1 |
| 3D 15N-separated NOESY | sample_1 | isotropic | sample_conditions_1 |
| 3D 13C-separated NOESY | sample_1 | isotropic | sample_conditions_1 |
| 3D 15N-TOCSY-HSQC | sample_1 | isotropic | sample_conditions_1 |
Software:
TOPSPIN v3.98 - chemical shift assignment
NMRPipe v11.0 - processing
SPARKY v3.115 - chemical shift assignment
NMR spectrometers:
- Bruker AVANCE NEO 600 MHz
- Bruker AVANCE III 800 MHz
Download HSQC peak lists in one of the following formats:
CSV: Backbone
or all simulated shifts
SPARKY: Backbone
or all simulated shifts