BMRB Entry 50793
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PDB ID:
Entry in NMR Restraints Grid
Validation report in NRG-CING
Chem Shift validation: AVS_full
BMRB Entry DOI: doi:10.13018/BMR50793
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: Rosa e Silva, Ivan; Bino, Lucia; Johnson, Christopher; Rutherford, Trevor; Neuhaus, David; Andreeva, Antonina; Cajanek, Lukas; van Breugel, Mark. "Molecular mechanisms underlying the role of the centriolar CEP164-TTBK2 complex in ciliopathies" Structure 30, 114-128 (2022).
PubMed: 34499853
Assembly members:
entity_1, polymer, 109 residues, Formula weight is not available
Natural source: Common Name: Human Taxonomy ID: 9606 Superkingdom: Eukaryota Kingdom: Metazoa Genus/species: Homo sapiens
Experimental source: Production method: recombinant technology Host organism: Escherichia coli Vector: pGEX6P1
Entity Sequences (FASTA):
entity_1: MAGRPLRIGDQLVLEEDYDE
TYIPSEQEILEFAREIGIDP
IKEPELMWLAREGIVAPLPG
EWKPCQDITGDIYYFNFANG
QSMWDHPCDEHYRSLVIQER
AKLSTSGAI
- assigned_chemical_shifts
| Data type | Count |
| 13C chemical shifts | 441 |
| 15N chemical shifts | 103 |
| 1H chemical shifts | 755 |
Additional metadata:
Assembly:
| Entity Assembly ID | Entity Name | Entity ID |
|---|---|---|
| 1 | CEP164 | 1 |
Entities:
Entity 1, CEP164 109 residues - Formula weight is not available
| 1 | MET | ALA | GLY | ARG | PRO | LEU | ARG | ILE | GLY | ASP | ||||
| 2 | GLN | LEU | VAL | LEU | GLU | GLU | ASP | TYR | ASP | GLU | ||||
| 3 | THR | TYR | ILE | PRO | SER | GLU | GLN | GLU | ILE | LEU | ||||
| 4 | GLU | PHE | ALA | ARG | GLU | ILE | GLY | ILE | ASP | PRO | ||||
| 5 | ILE | LYS | GLU | PRO | GLU | LEU | MET | TRP | LEU | ALA | ||||
| 6 | ARG | GLU | GLY | ILE | VAL | ALA | PRO | LEU | PRO | GLY | ||||
| 7 | GLU | TRP | LYS | PRO | CYS | GLN | ASP | ILE | THR | GLY | ||||
| 8 | ASP | ILE | TYR | TYR | PHE | ASN | PHE | ALA | ASN | GLY | ||||
| 9 | GLN | SER | MET | TRP | ASP | HIS | PRO | CYS | ASP | GLU | ||||
| 10 | HIS | TYR | ARG | SER | LEU | VAL | ILE | GLN | GLU | ARG | ||||
| 11 | ALA | LYS | LEU | SER | THR | SER | GLY | ALA | ILE |
Samples:
sample_1: CEP164 N-terminal domain, [U-100% 13C; U-100% 15N], 120 uM; sodium phosphate 25 mM; sodium chloride 125 mM; DTT 4 mM; complete protease inhibitor cocktail, EDTA free 0.4 tablet/100mL
sample_2: CEP164 N-terminal domain, [U-100% 15N], 500 uM; sodium phosphate 25 mM; sodium chloride 125 mM; DTT 4 mM; complete protease inhibitor cocktail, EDTA free 0.4 tablet/100mL
sample_conditions_1: ionic strength: 185 mM; pH: 7.4; pressure: 1 atm; temperature: 293 K
sample_conditions_2: ionic strength: 185 mM; pH: 7.4; pressure: 1 atm; temperature: 293 K
Experiments:
| Name | Sample | Sample state | Sample conditions |
|---|---|---|---|
| 2D 1H-15N TROSY | sample_1 | isotropic | sample_conditions_1 |
| 2D 1H-13C HSQC aliphatic | sample_1 | isotropic | sample_conditions_1 |
| 3D HN(CA)CO | sample_1 | isotropic | sample_conditions_1 |
| 3D HNCACB | sample_1 | isotropic | sample_conditions_1 |
| 2D 1H-1H NOESY | sample_1 | isotropic | sample_conditions_1 |
| 2D (HB)CB(CGCD)HD | sample_1 | isotropic | sample_conditions_1 |
Software:
TOPSPIN v3.2 - collection, processing
SPARKY v3.12 - chemical shift assignment
X-PLOR NIH v2.28 - structure solution
AMBER11 - structure solution
TALOS+ v3.80F1 Rev 2012.080.14.41 - structure solution
NMR spectrometers:
- Bruker AVANCE III 600 MHz
- Bruker AVANCE III 700 MHz
- Bruker AVANCE III 800 MHz
Download HSQC peak lists in one of the following formats:
CSV: Backbone
or all simulated peaks
SPARKY: Backbone
or all simulated peaks