BMRB Entry 17577
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PDB ID:
Entry in NMR Restraints Grid
Validation report in NRG-CING
Chem Shift validation: AVS_full, LACS, SPARTA
BMRB Entry DOI: doi:10.13018/BMR17577
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: Coudevylle, Nicolas; Hoetzinger, Matthias; Geist, Leonhard; Kontaxis, Georg; Hartl, Markus; Bister, Klaus; Konrat, Robert. "Lipocalin Q83 reveals a dual ligand binding mode with potential implications for the functions of siderocalins." Biochemistry 50, 9192-9199 (2011).
PubMed: 21951132
Assembly members:
Q83, polymer, 157 residues, 18104.854 Da.
EB4, non-polymer, 669.554 Da.
GA, non-polymer, 69.723 Da.
ACD, non-polymer, 304.472 Da.
Natural source: Common Name: common quail Taxonomy ID: 9091 Superkingdom: Eukaryota Kingdom: Metazoa Genus/species: Coturnix coturnix
Experimental source: Production method: recombinant technology Host organism: Escherichia coli Vector: pET3d
- assigned_chemical_shifts
| Data type | Count |
| 13C chemical shifts | 613 |
| 15N chemical shifts | 151 |
| 1H chemical shifts | 718 |
Additional metadata:
Assembly:
| Entity Assembly ID | Entity Name | Entity ID |
|---|---|---|
| 1 | Siderocalin_Q83 | 1 |
| 2 | EB4 | 2 |
| 3 | Gallium (III) ion | 3 |
| 4 | ARACHIDONIC ACID | 4 |
Entities:
Entity 1, Siderocalin_Q83 157 residues - 18104.854 Da.
| 1 | MET | THR | VAL | PRO | ASP | ARG | SER | GLU | ILE | ALA | ||||
| 2 | GLY | LYS | TRP | TYR | VAL | VAL | ALA | LEU | ALA | SER | ||||
| 3 | ASN | THR | GLU | PHE | PHE | LEU | ARG | GLU | LYS | ASP | ||||
| 4 | LYS | MET | LYS | MET | ALA | MET | ALA | ARG | ILE | SER | ||||
| 5 | PHE | LEU | GLY | GLU | ASP | GLU | LEU | LYS | VAL | SER | ||||
| 6 | TYR | ALA | VAL | PRO | LYS | PRO | ASN | GLY | CYS | ARG | ||||
| 7 | LYS | TRP | GLU | THR | THR | PHE | LYS | LYS | THR | SER | ||||
| 8 | ASP | ASP | GLY | GLU | VAL | TYR | TYR | SER | GLU | GLU | ||||
| 9 | ALA | LYS | LYS | LYS | VAL | GLU | VAL | LEU | ASP | THR | ||||
| 10 | ASP | TYR | LYS | SER | TYR | ALA | VAL | ILE | TYR | ALA | ||||
| 11 | THR | ARG | VAL | LYS | ASP | GLY | ARG | THR | LEU | HIS | ||||
| 12 | MET | MET | ARG | LEU | TYR | SER | ARG | SER | PRO | GLU | ||||
| 13 | VAL | SER | PRO | ALA | ALA | THR | ALA | ILE | PHE | ARG | ||||
| 14 | LYS | LEU | ALA | GLY | GLU | ARG | ASN | TYR | THR | ASP | ||||
| 15 | GLU | MET | VAL | ALA | MET | LEU | PRO | ARG | GLN | GLU | ||||
| 16 | GLU | CYS | THR | VAL | ASP | GLU | VAL |
Entity 2, EB4 - C30 H27 N3 O15 - 669.554 Da.
| 1 | EB4 |
Entity 3, Gallium (III) ion - Ga - 69.723 Da.
| 1 | GA |
Entity 4, ARACHIDONIC ACID - C20 H32 O2 - 304.472 Da.
| 1 | ACD |
Samples:
sample_1: Q83, [U-100% 13C; U-100% 15N], 1 mM; EB4 1 mM; Gallium(III) 1 mM; ARACHIDONIC ACID 1 mM; NaCl 50 mM
sample_conditions_1: ionic strength: 50 mM; pH: 6.5; pressure: 1 atm; temperature: 273 K
Experiments:
| Name | Sample | Sample state | Sample conditions |
|---|---|---|---|
| 2D 1H-15N HSQC | sample_1 | isotropic | sample_conditions_1 |
| 3D HNCO | sample_1 | isotropic | sample_conditions_1 |
| 3D CBCA(CO)NH | sample_1 | isotropic | sample_conditions_1 |
| 3D HNCA | sample_1 | isotropic | sample_conditions_1 |
| 3D HNCACB | sample_1 | isotropic | sample_conditions_1 |
| 3D HN(CO)CA | sample_1 | isotropic | sample_conditions_1 |
| 3D HCCH-TOCSY | sample_1 | isotropic | sample_conditions_1 |
| 3D HNHA | sample_1 | isotropic | sample_conditions_1 |
| 3D 1H-15N NOESY | sample_1 | isotropic | sample_conditions_1 |
| 3D 1H-13C NOESY aliphatic | sample_1 | isotropic | sample_conditions_1 |
| 3D 1H-13C NOESY aromatic | sample_1 | isotropic | sample_conditions_1 |
| 2D 1H-15N HSQC | sample_1 | anisotropic | sample_conditions_1 |
Software:
NMRPipe, Delaglio, Grzesiek, Vuister, Zhu, Pfeifer and Bax - processing
NMR spectrometers:
- Varian INOVA 800 MHz
Download HSQC peak lists in one of the following formats:
CSV: Backbone
or all simulated peaks
SPARKY: Backbone
or all simulated peaks