BMRB Entry 16231
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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/BMR16231
MolProbity Validation Chart
NMR-STAR file interactive viewer.
NMR-STAR v3 text file.
XML gzip file.
RDF gzip file.
All files associated with the entry
Citation: Dai, Huaien; Hiromasa, Yasuaki; An, Chunju; Fabrick, Jeffrey; VanderVelde, David; Kanost, Michael; Krishnamoorthi, Ramaswamy. "Solution Structure of a Pathogen Recognition Domain from a Lepidopteran Insect, Plodia interpunctella" .
Assembly members:
Pathogen Recognition Domain, polymer, 113 residues, Formula weight is not available
Natural source: Common Name: Indianmeal moth Taxonomy ID: 58824 Superkingdom: Eukaryota Kingdom: Metazoa Genus/species: Plodia interpunctella
Experimental source: Production method: recombinant technology Host organism: Escherichia coli Vector: pPROEX-HTb
Entity Sequences (FASTA):
Pathogen Recognition Domain: QYVVPSAKLEAIYPRGLRVS
IPDDGFSLFAFHGKLNEEMD
GLEAGHWARDITKPKEGRWT
FRDRNAKLKLGDKIYFWTYV
IKDGLGYRQDNGEWTVTEFV
NEDGTPADTSLEP
- assigned_chemical_shifts
| Data type | Count |
| 13C chemical shifts | 415 |
| 15N chemical shifts | 110 |
| 1H chemical shifts | 700 |
Additional metadata:
Assembly:
| Entity Assembly ID | Entity Name | Entity ID |
|---|---|---|
| 1 | Pathogen Recognition Domain | 1 |
Entities:
Entity 1, Pathogen Recognition Domain 113 residues - Formula weight is not available
| 1 | GLN | TYR | VAL | VAL | PRO | SER | ALA | LYS | LEU | GLU | ||||
| 2 | ALA | ILE | TYR | PRO | ARG | GLY | LEU | ARG | VAL | SER | ||||
| 3 | ILE | PRO | ASP | ASP | GLY | PHE | SER | LEU | PHE | ALA | ||||
| 4 | PHE | HIS | GLY | LYS | LEU | ASN | GLU | GLU | MET | ASP | ||||
| 5 | GLY | LEU | GLU | ALA | GLY | HIS | TRP | ALA | ARG | ASP | ||||
| 6 | ILE | THR | LYS | PRO | LYS | GLU | GLY | ARG | TRP | THR | ||||
| 7 | PHE | ARG | ASP | ARG | ASN | ALA | LYS | LEU | LYS | LEU | ||||
| 8 | GLY | ASP | LYS | ILE | TYR | PHE | TRP | THR | TYR | VAL | ||||
| 9 | ILE | LYS | ASP | GLY | LEU | GLY | TYR | ARG | GLN | ASP | ||||
| 10 | ASN | GLY | GLU | TRP | THR | VAL | THR | GLU | PHE | VAL | ||||
| 11 | ASN | GLU | ASP | GLY | THR | PRO | ALA | ASP | THR | SER | ||||
| 12 | LEU | GLU | PRO |
Samples:
sample_1: entity_2, [U-100% 13C; U-100% 15N], 1.5-2.0 mM; sodium phosphate buffer 20 mM
sample_conditions_1: ionic strength: 0.1 M; pH: 6.5; 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 HNCACB | sample_1 | isotropic | sample_conditions_1 |
| 3D H(CCO)NH | sample_1 | isotropic | sample_conditions_1 |
| 3D HN(CO)CA | sample_1 | isotropic | sample_conditions_1 |
| 3D HNCO | sample_1 | isotropic | sample_conditions_1 |
| 3D 1H-15N NOESY | sample_1 | isotropic | sample_conditions_1 |
| 3D 1H-13C NOESY | sample_1 | isotropic | sample_conditions_1 |
| 3D HCCH-TOCSY | sample_1 | isotropic | sample_conditions_1 |
Software:
CNS, Brunger A. T. et.al. - refinement
NMR spectrometers:
- Bruker Avance 800 MHz
Download HSQC peak lists in one of the following formats:
CSV: Backbone
or all simulated peaks
SPARKY: Backbone
or all simulated peaks