BMRB Entry 19687
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PDB ID:
Entry in NMR Restraints Grid
Validation report in NRG-CING
Chem Shift validation: AVS_anomalous, AVS_full, LACS, SPARTA
BMRB Entry DOI: doi:10.13018/BMR19687
MolProbity Validation Chart
NMR-STAR file interactive viewer.
NMR-STAR v3 text file.
XML gzip file.
RDF gzip file.
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Citation: Berry, Richard; Headey, Stephen; Call, Matthew; McCluskey, James; Tregaskes, Clive; Kaufman, Jim; Koh, Ruide; Mohanty, Biswaranjan; Scanlon, Martin; Call, Melissa; Rossjohn, Jamie. "immune signalling subunit" .
Assembly members:
entity, polymer, 178 residues, 19569.904 Da.
Natural source: Common Name: chicken Taxonomy ID: 9031 Superkingdom: Eukaryota Kingdom: Metazoa Genus/species: Gallus gallus
Experimental source: Production method: recombinant technology Host organism: Escherichia coli Vector: pET28b
- assigned_chemical_shifts
| Data type | Count |
| 1H chemical shifts | 829 |
| 13C chemical shifts | 408 |
| 15N chemical shifts | 144 |
Additional metadata:
Assembly:
| Entity Assembly ID | Entity Name | Entity ID |
|---|---|---|
| 1 | immune signalling subunit | 1 |
Entities:
Entity 1, immune signalling subunit 178 residues - 19569.904 Da.
| 1 | GLY | SER | HIS | MET | GLY | GLN | GLU | GLU | PHE | ALA | ||||
| 2 | VAL | GLU | ILE | SER | GLY | THR | THR | VAL | THR | ILE | ||||
| 3 | THR | CYS | PRO | SER | SER | GLY | ASP | ASP | ILE | LYS | ||||
| 4 | TRP | LYS | PRO | ASP | PRO | ALA | LEU | GLY | ASP | ASN | ||||
| 5 | ASN | LYS | TYR | ILE | ILE | GLN | ASN | HIS | ASP | SER | ||||
| 6 | SER | PRO | LEU | THR | VAL | SER | CYS | THR | ALA | GLY | ||||
| 7 | ASP | GLN | GLU | HIS | THR | MET | TYR | LEU | ASN | ALA | ||||
| 8 | LYS | VAL | GLY | SER | ALA | ASP | ASP | ALA | LYS | LYS | ||||
| 9 | ASP | ALA | ALA | LYS | LYS | ASP | ASP | ALA | LYS | LYS | ||||
| 10 | ASP | ASP | ALA | LYS | LYS | ASP | GLY | SER | VAL | ALA | ||||
| 11 | LYS | LEU | GLY | VAL | HIS | GLY | LEU | SER | MET | SER | ||||
| 12 | VAL | LYS | GLU | VAL | SER | GLY | LYS | VAL | PHE | LEU | ||||
| 13 | GLN | CYS | GLN | GLU | SER | LYS | ASP | LEU | ASN | THR | ||||
| 14 | ASN | TYR | LEU | TRP | LYS | LYS | GLY | LYS | GLU | GLU | ||||
| 15 | LEU | GLY | ASN | MET | ARG | GLN | LEU | ASP | LEU | GLY | ||||
| 16 | ALA | ILE | TYR | ASP | ASP | PRO | ARG | GLY | THR | TYR | ||||
| 17 | THR | CYS | GLN | ARG | ASP | GLU | ASN | VAL | ASN | SER | ||||
| 18 | THR | LEU | HIS | VAL | HIS | TYR | ARG | MET |
Samples:
sample_1: protein, [U-98% 13C; U-98% 15N], 0.5 mM; HEPES 50 mM; arginine 125 mM; glutamate 125 mM; azide 0.01%; Roche protease inhibitor 0.01%; EDTA 0.5 mM
deuterated: protein, [U-100% 13C; U-100% 15N; U-80% 2H], 0.5 mM; HEPES 50 mM; arginine 125 mM; glutamate 125 mM; azide 0.01%; Roche protease inhibitor 0.01%; EDTA 0.5 mM
sample_conditions_1: temperature: 293 K; pH: 7.6; pressure: 1 atm; ionic strength: 0.3 M
Experiments:
| Name | Sample | Sample state | Sample conditions |
|---|---|---|---|
| 2D 1H-15N HSQC | sample_1 | isotropic | sample_conditions_1 |
| 3D HN(COCA)CB | deuterated | isotropic | sample_conditions_1 |
| 3D HNCACB | deuterated | isotropic | sample_conditions_1 |
| 3D H(CCO)NH | sample_1 | isotropic | sample_conditions_1 |
| 3D HNCA | sample_1 | isotropic | sample_conditions_1 |
| 3D HNCO | sample_1 | isotropic | sample_conditions_1 |
| 3D HN(CO)CA | deuterated | 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 |
| 3D 1H-15N NOESY | sample_1 | isotropic | sample_conditions_1 |
Software:
TOPSPIN, Bruker Biospin - collection, processing
XEASY, Bartels et al. - data analysis
CNS, Brunger, Adams, Clore, Gros, Nilges and Read - structure solution
NMR spectrometers:
- Bruker Avance 600 MHz
- Bruker Avance 800 MHz
Related Database Links:
| PDB |
Download HSQC peak lists in one of the following formats:
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