BMRB Entry 18982
Click here to enlarge.
PDB ID:
Entry in NMR Restraints Grid
Validation report in NRG-CING
Chem Shift validation: AVS_anomalous, AVS_full
BMRB Entry DOI: doi:10.13018/BMR18982
MolProbity Validation Chart
NMR-STAR file interactive viewer.
NMR-STAR v3 text file.
NMR-STAR v2.1 text file (deprecated)
XML gzip file.
RDF gzip file.
All files associated with the entry
Title: Transcriptional regulatory protein PubMed: 24155902
Deposition date: 2013-01-28 Original release date: 2013-12-09
Authors: de Chiara, Cesira; Kelly, Geoff; Pastore, Annalisa
Citation: de Chiara, Cesira; Menon, Rajesh; Kelly, Geoff; Pastore, Annalisa. "Protein-Protein Interactions as a Strategy towards Protein-Specific Drug Design: The Example of Ataxin-1" PLoS One 8, e76456-e76456 (2013).
Assembly members:
CIC_polypeptide, polymer, 15 residues, 1726.026 Da.
Ataxin-1_AXH, polymer, 126 residues, 13517.461 Da.
Natural source: Common Name: Humans Taxonomy ID: 9606 Superkingdom: Eukaryota Kingdom: Metazoa Genus/species: Homo sapiens
Experimental source: Production method: chemical synthesis Host organism: Escherichia coli
Entity Sequences (FASTA):
CIC_polypeptide: VFPWHSLVPFLAPSQ
Ataxin-1_AXH: GAMAPPTLPPYFMKGSIIQL
ANGELKKVEDLKTEDFIQSA
EISNDLKIDSSTVERIEDSH
SPGVAVIQFAVGEHRAQVSV
EVLVEYPFFVFGQGWSSCCP
ERTSQLFDLPCSKLSVGDVC
ISLTLK
- assigned_chemical_shifts
| Data type | Count |
| 13C chemical shifts | 390 |
| 15N chemical shifts | 124 |
| 1H chemical shifts | 906 |
Additional metadata:
Assembly:
| Entity Assembly ID | Entity Name | Entity ID |
|---|---|---|
| 1 | CIC_polypeptide | 1 |
| 2 | Ataxin-1_AXH | 2 |
Entities:
Entity 1, CIC_polypeptide 15 residues - 1726.026 Da.
| 1 | VAL | PHE | PRO | TRP | HIS | SER | LEU | VAL | PRO | PHE | ||||
| 2 | LEU | ALA | PRO | SER | GLN |
Entity 2, Ataxin-1_AXH 126 residues - 13517.461 Da.
| 1 | GLY | ALA | MET | ALA | PRO | PRO | THR | LEU | PRO | PRO | ||||
| 2 | TYR | PHE | MET | LYS | GLY | SER | ILE | ILE | GLN | LEU | ||||
| 3 | ALA | ASN | GLY | GLU | LEU | LYS | LYS | VAL | GLU | ASP | ||||
| 4 | LEU | LYS | THR | GLU | ASP | PHE | ILE | GLN | SER | ALA | ||||
| 5 | GLU | ILE | SER | ASN | ASP | LEU | LYS | ILE | ASP | SER | ||||
| 6 | SER | THR | VAL | GLU | ARG | ILE | GLU | ASP | SER | HIS | ||||
| 7 | SER | PRO | GLY | VAL | ALA | VAL | ILE | GLN | PHE | ALA | ||||
| 8 | VAL | GLY | GLU | HIS | ARG | ALA | GLN | VAL | SER | VAL | ||||
| 9 | GLU | VAL | LEU | VAL | GLU | TYR | PRO | PHE | PHE | VAL | ||||
| 10 | PHE | GLY | GLN | GLY | TRP | SER | SER | CYS | CYS | PRO | ||||
| 11 | GLU | ARG | THR | SER | GLN | LEU | PHE | ASP | LEU | PRO | ||||
| 12 | CYS | SER | LYS | LEU | SER | VAL | GLY | ASP | VAL | CYS | ||||
| 13 | ILE | SER | LEU | THR | LEU | LYS |
Samples:
sample_1: Ataxin-1 AXH domain, [U-100% 13C; U-100% 15N], 0.5 mM; CIC polypeptide 0.6 mM; H2O 90 mM; D2O 10 mM
sample_2: Ataxin-1 AXH domain, [U-100% 15N], 0.5 mM; CIC polypeptide 0.6 mM; H2O 90 mM; D2O 10 mM
sample_conditions_1: ionic strength: 20 mM; pH: 6.8; pressure: 1 atm; temperature: 310 K
Experiments:
| Name | Sample | Sample state | Sample conditions |
|---|---|---|---|
| 3D 1H-15N NOESY | sample_2 | isotropic | sample_conditions_1 |
| 3D 1H-15N TOCSY | sample_2 | isotropic | sample_conditions_1 |
| 3D 1H-13C NOESY | sample_1 | isotropic | sample_conditions_1 |
| 3D HCCH-TOCSY | 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 HNCO | sample_1 | isotropic | sample_conditions_1 |
| 3D 15N-13C-filtered, 15N-13C-edited NOESY | sample_1 | isotropic | sample_conditions_1 |
| 2D 15N-13C-rejected NOESY | sample_1 | isotropic | sample_conditions_1 |
| 3D C(CO)NH | sample_1 | isotropic | sample_conditions_1 |
| 3D HNCACB | sample_1 | isotropic | sample_conditions_1 |
Software:
ARIA v2.3, Linge, O, . - automated NOEs assignment, refinement, structure solution
XEASY, Bartels et al. - data analysis, peak picking
NMRPipe, Delaglio, Grzesiek, Vuister, Zhu, Pfeifer and Bax - processing
NMRDraw, Delaglio, Grzesiek, Vuister, Zhu, Pfeifer and Bax - processing
NMR spectrometers:
- Varian INOVA 800 MHz
- Bruker Avance 700 MHz
- Bruker Avance 600 MHz
- Varian INOVA 600 MHz
Related Database Links:
| UNP | Q96RK0 P54253 |
| PDB | |
| DBJ | BAE27813 BAE27978 BAI45609 BAP18650 BAC33290 |
| GB | AAI40444 AAI52805 AAK73515 AAK73516 ABD61704 AAH58178 AAI17126 ADR83271 AIC49678 EAW55372 |
| REF | NP_001289740 NP_001291744 NP_055940 NP_082158 XP_001153776 NP_000323 NP_001121636 NP_001186233 NP_033150 NP_036858 |
| SP | Q924A2 Q96RK0 P54253 P54254 Q63540 |
| EMBL | CAA55793 CAA58533 CAA62822 |
| PRF | 2210312A |
Download simulated HSQC data in one of the following formats:
CSV: Backbone
or all simulated shifts
SPARKY: Backbone
or all simulated shifts