BMRB Entry 15256
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PDB ID:
Entry in NMR Restraints Grid
Validation report in NRG-CING
Chem Shift validation: AVS_full, LACS
BMRB Entry DOI: doi:10.13018/BMR15256
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Title: Antheraea polyphemus pheromone-binding protein 1: structure and assignments at pH 4.5. PubMed: 17884092
Deposition date: 2007-05-20 Original release date: 2007-10-29
Authors: Damberger, Fred; Wuthrich, Kurt; Leal, Walter; Ishida, Yuko
Citation: Damberger, Fred; Ishida, Yuko; Leal, Walter; Wuthrich, Kurt. "Structural basis of ligand binding and release in insect pheromone-binding proteins: NMR structure of Antheraea polyphemus PBP1 at pH 4.5" J. Mol. Biol. 373, 811-819 (2007).
Assembly members:
ApolPBP singlechain, polymer, 142 residues, 15797.063 Da.
Natural source: Common Name: not available Taxonomy ID: 7120 Superkingdom: Eukaryota Kingdom: Metazoa Genus/species: Antheraea polyphemus
Experimental source: Production method: recombinant technology Host organism: Escherichia coli
Entity Sequences (FASTA):
ApolPBP singlechain: SPEIMKNLSNNFGKAMDQCK
DELSLPDSVVADLYNFWKDD
YVMTDRLAGCAINCLATKLD
VVDPDGNLHHGNAKDFAMKH
GADETMAQQLVDIIHGCEKS
APPNDDKCMKTIDVAMCFKK
EIHKLNWVPNMDLVIGEVLA
EV
- assigned_chemical_shifts
| Data type | Count |
| 13C chemical shifts | 620 |
| 15N chemical shifts | 150 |
| 1H chemical shifts | 997 |
Additional metadata:
Assembly:
| Entity Assembly ID | Entity Name | Entity ID |
|---|---|---|
| 1 | singlechain | 1 |
Entities:
Entity 1, singlechain 142 residues - 15797.063 Da.
| 1 | SER | PRO | GLU | ILE | MET | LYS | ASN | LEU | SER | ASN | ||||
| 2 | ASN | PHE | GLY | LYS | ALA | MET | ASP | GLN | CYS | LYS | ||||
| 3 | ASP | GLU | LEU | SER | LEU | PRO | ASP | SER | VAL | VAL | ||||
| 4 | ALA | ASP | LEU | TYR | ASN | PHE | TRP | LYS | ASP | ASP | ||||
| 5 | TYR | VAL | MET | THR | ASP | ARG | LEU | ALA | GLY | CYS | ||||
| 6 | ALA | ILE | ASN | CYS | LEU | ALA | THR | LYS | LEU | ASP | ||||
| 7 | VAL | VAL | ASP | PRO | ASP | GLY | ASN | LEU | HIS | HIS | ||||
| 8 | GLY | ASN | ALA | LYS | ASP | PHE | ALA | MET | LYS | HIS | ||||
| 9 | GLY | ALA | ASP | GLU | THR | MET | ALA | GLN | GLN | LEU | ||||
| 10 | VAL | ASP | ILE | ILE | HIS | GLY | CYS | GLU | LYS | SER | ||||
| 11 | ALA | PRO | PRO | ASN | ASP | ASP | LYS | CYS | MET | LYS | ||||
| 12 | THR | ILE | ASP | VAL | ALA | MET | CYS | PHE | LYS | LYS | ||||
| 13 | GLU | ILE | HIS | LYS | LEU | ASN | TRP | VAL | PRO | ASN | ||||
| 14 | MET | ASP | LEU | VAL | ILE | GLY | GLU | VAL | LEU | ALA | ||||
| 15 | GLU | VAL |
Samples:
sample_1: entity, [U-99% 13C; U-99% 15N], 0.9 mM; H2O 93%; D2O 7%; potassium phosphate 50 mM; sodium azide 2 mM
sample_conditions_1: ionic strength: 0.05 M; pH: 4.50; pressure: 1 atm; temperature: 293 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 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 HNCA | 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 HCCH-TOCSY | sample_1 | isotropic | sample_conditions_1 |
| 3D 1H-15N NOESY | sample_1 | isotropic | sample_conditions_1 |
| 3D 1H-15N TOCSY | sample_1 | isotropic | sample_conditions_1 |
| 3D 1H-13C NOESY | sample_1 | isotropic | sample_conditions_1 |
| 3D 1H-13C NOESY | sample_1 | isotropic | sample_conditions_1 |
| 3D HCCH-COSY | sample_1 | isotropic | sample_conditions_1 |
| 3D HN(CA)CO | sample_1 | isotropic | sample_conditions_1 |
Software:
CARA v1.8, Keller and Wuthrich - chemical shift assignment
ATHNOS-CANDID, Herrmann, Guntert and Wuthrich - constraint collection, constraint combination, NOE assignment, peak picking
DYANA, Guntert, Braun and Wuthrich - structure calculation
Molmol v2.2K, Koradi, Billeter and Wuthrich - data analysis
OPALp v1.2, Luginbuhl, Guntert, Billeter and Wuthrich - refinement
NMR spectrometers:
- Bruker Avance 900 MHz
- Bruker DRX 750 MHz
- Bruker DRX 500 MHz
Download simulated HSQC data in one of the following formats:
CSV: Backbone
or all simulated shifts
SPARKY: Backbone
or all simulated shifts