BMRB Entry 30679
Chem Shift validation: AVS_full
BMRB Entry DOI: doi:10.13018/BMR30679
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Title: Gypsy Moth Pheromone-binding protein 1 (LdisPBP1) NMR Structure at pH 4.5 PubMed: 32877603
Deposition date: 2019-10-09 Original release date: 2020-09-18
Authors: Terrado, M.; Plettner, E.
Citation: Terrado, Mailyn; Okon, Mark; McIntosh, Lawrence; Plettner, Erika. "Ligand- and pH-Induced Structural Transition of Gypsy Moth Lymantria dispar Pheromone-Binding Protein 1 (LdisPBP1)" Biochemistry ., .-. (2020).
Assembly members:
entity_1, polymer, 143 residues, 16165.910 Da.
Natural source: Common Name: Gypsy moth Taxonomy ID: 13123 Superkingdom: Eukaryota Kingdom: Metazoa Genus/species: Lymantria dispar
Experimental source: Production method: recombinant technology Host organism: Escherichia coli
Entity Sequences (FASTA):
entity_1: SKEVMKQMTINFAKPMEACK
QELNVPDAVMQDFFNFWKEG
YQITNREAGCVILCLAKKLE
LLDQDMNLHHGKAMEFAMKH
GADEAMAKQLLDIKHSCEKV
ITIVADDPCQTMLNLAMCFK
AEIHKLDWAPTLDVAVGELL
ADT
- assigned_chemical_shifts
- spectral_peak_list
| Data type | Count |
| 13C chemical shifts | 610 |
| 15N chemical shifts | 156 |
| 1H chemical shifts | 980 |
Additional metadata:
Assembly:
| Entity Assembly ID | Entity Name | Entity ID |
|---|---|---|
| 1 | entity_1 | 1 |
Entities:
Entity 1, entity_1 143 residues - 16165.910 Da.
| 1 | SER | LYS | GLU | VAL | MET | LYS | GLN | MET | THR | ILE | ||||
| 2 | ASN | PHE | ALA | LYS | PRO | MET | GLU | ALA | CYS | LYS | ||||
| 3 | GLN | GLU | LEU | ASN | VAL | PRO | ASP | ALA | VAL | MET | ||||
| 4 | GLN | ASP | PHE | PHE | ASN | PHE | TRP | LYS | GLU | GLY | ||||
| 5 | TYR | GLN | ILE | THR | ASN | ARG | GLU | ALA | GLY | CYS | ||||
| 6 | VAL | ILE | LEU | CYS | LEU | ALA | LYS | LYS | LEU | GLU | ||||
| 7 | LEU | LEU | ASP | GLN | ASP | MET | ASN | LEU | HIS | HIS | ||||
| 8 | GLY | LYS | ALA | MET | GLU | PHE | ALA | MET | LYS | HIS | ||||
| 9 | GLY | ALA | ASP | GLU | ALA | MET | ALA | LYS | GLN | LEU | ||||
| 10 | LEU | ASP | ILE | LYS | HIS | SER | CYS | GLU | LYS | VAL | ||||
| 11 | ILE | THR | ILE | VAL | ALA | ASP | ASP | PRO | CYS | GLN | ||||
| 12 | THR | MET | LEU | ASN | LEU | ALA | MET | CYS | PHE | LYS | ||||
| 13 | ALA | GLU | ILE | HIS | LYS | LEU | ASP | TRP | ALA | PRO | ||||
| 14 | THR | LEU | ASP | VAL | ALA | VAL | GLY | GLU | LEU | LEU | ||||
| 15 | ALA | ASP | THR |
Samples:
sample_1: LdisPBP1, [U-99% 13C; U-99% 15N], 1.2 M; sodium acetate 50 mM; EDTA 1 mM; sodium azide 0.05 % w/v
sample_conditions_1: pH: 4.5; pressure: 1 atm; temperature: 308 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 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(CO)CA | sample_1 | isotropic | sample_conditions_1 |
| 3D C(CO)NH | sample_1 | isotropic | sample_conditions_1 |
| 3D HBHA(CO)NH | sample_1 | isotropic | sample_conditions_1 |
| 3D 1H-13C NOESY | sample_1 | isotropic | sample_conditions_1 |
| 3D 1H-15N NOESY | sample_1 | isotropic | sample_conditions_1 |
Software:
NMRe, Ryu H, Lim GT, Sung BH, Lee J - refinement
CYANA, Guntert, Mumenthaler and Wuthrich - structure calculation
Sparky, Goddard - chemical shift assignment, peak picking
NMR spectrometers:
- Bruker AVANCE III 600 MHz
- Bruker AVANCE III 850 MHz
Download simulated HSQC data in one of the following formats:
CSV: Backbone
or all simulated shifts
SPARKY: Backbone
or all simulated shifts