BMRB Entry 25599
Click here to enlarge.
PDB ID:
Entry in NMR Restraints Grid
Validation report in NRG-CING
Chem Shift validation: AVS_full
BMRB Entry DOI: doi:10.13018/BMR25599
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: Solution structure of Sds3 in complex with Sin3A PubMed: 26124119
Deposition date: 2015-05-08 Original release date: 2015-07-13
Authors: Clark, Michael; Radhakrishnan, Ishwar
Citation: Clark, Michael; Marcum, Ryan; Graveline, Richard; Chan, Clarence; Xie, Tao; Chen, Zhonglei; Ding, Yujia; Zhang, Yongbo; Mondragon, Alfonso; David, Gregory; Radhakrishnan, Ishwar. "Structural Insights into the Assembly of the Histone Deacetylase-Associated Sin3L/Rpd3L Corepressor Complex" Proc. Natl. Acad. Sci. U.S.A. 112, E3669-E3678 (2015).
Assembly members:
Sds3SID, polymer, 27 residues, 3125.556 Da.
Sin3HID, polymer, 125 residues, 14698.959 Da.
Natural source: Common Name: house mouse Taxonomy ID: 10090 Superkingdom: Eukaryota Kingdom: Metazoa Genus/species: Mus musculus
Experimental source: Production method: recombinant technology Host organism: Escherichia coli
Entity Sequences (FASTA):
Sds3SID: SNAAQLNYLLTDEQIMEDLR
TLNKLKS
Sin3HID: SNAEHIYRCEDERFELDVVL
ETNLATIRVLEAIQKKLSRL
SAEEQAKFRLDNTLGGTSEV
IHRKALQRIYADKAADIIDG
LRKNPSIAVPIVLKRLKMKE
EEWREAQRGFNKVWREQNEK
YYLKS
- assigned_chemical_shifts
| Data type | Count |
| 13C chemical shifts | 631 |
| 15N chemical shifts | 154 |
| 1H chemical shifts | 1005 |
Additional metadata:
Assembly:
| Entity Assembly ID | Entity Name | Entity ID |
|---|---|---|
| 1 | Sds3SID | 1 |
| 2 | Sin3HID | 2 |
Entities:
Entity 1, Sds3SID 27 residues - 3125.556 Da.
| 1 | SER | ASN | ALA | ALA | GLN | LEU | ASN | TYR | LEU | LEU | ||||
| 2 | THR | ASP | GLU | GLN | ILE | MET | GLU | ASP | LEU | ARG | ||||
| 3 | THR | LEU | ASN | LYS | LEU | LYS | SER |
Entity 2, Sin3HID 125 residues - 14698.959 Da.
| 1 | SER | ASN | ALA | GLU | HIS | ILE | TYR | ARG | CYS | GLU | ||||
| 2 | ASP | GLU | ARG | PHE | GLU | LEU | ASP | VAL | VAL | LEU | ||||
| 3 | GLU | THR | ASN | LEU | ALA | THR | ILE | ARG | VAL | LEU | ||||
| 4 | GLU | ALA | ILE | GLN | LYS | LYS | LEU | SER | ARG | LEU | ||||
| 5 | SER | ALA | GLU | GLU | GLN | ALA | LYS | PHE | ARG | LEU | ||||
| 6 | ASP | ASN | THR | LEU | GLY | GLY | THR | SER | GLU | VAL | ||||
| 7 | ILE | HIS | ARG | LYS | ALA | LEU | GLN | ARG | ILE | TYR | ||||
| 8 | ALA | ASP | LYS | ALA | ALA | ASP | ILE | ILE | ASP | GLY | ||||
| 9 | LEU | ARG | LYS | ASN | PRO | SER | ILE | ALA | VAL | PRO | ||||
| 10 | ILE | VAL | LEU | LYS | ARG | LEU | LYS | MET | LYS | GLU | ||||
| 11 | GLU | GLU | TRP | ARG | GLU | ALA | GLN | ARG | GLY | PHE | ||||
| 12 | ASN | LYS | VAL | TRP | ARG | GLU | GLN | ASN | GLU | LYS | ||||
| 13 | TYR | TYR | LEU | LYS | SER |
Samples:
sample_1: Sin3HID, [U-100% 13C; U-100% 15N], 0.5 – 1 mM; Sds3SID0.5 – 1 mM; H2O 90%; D2O 10%
sample_2: Sds3SID, [U-100% 13C; U-100% 15N], 0.5 – 1 mM; Sin3HID0.5 – 1 mM; H2O 90%; D2O 10%
sample_conditions_1: ionic strength: 0.12 M; pH: 6.7; pressure: 1 atm; temperature: 303 K
Experiments:
| Name | Sample | Sample state | Sample conditions |
|---|---|---|---|
| 3D 1H-15N NOESY | sample_1 | isotropic | sample_conditions_1 |
| 3D 1H-13C NOESY | sample_1 | isotropic | sample_conditions_1 |
| 3D 1H-15N NOESY | sample_2 | isotropic | sample_conditions_1 |
| 3D 1H-13C NOESY | sample_2 | isotropic | sample_conditions_1 |
| 3D CBCA(CO)NH | sample_1 | isotropic | sample_conditions_1 |
| 3D HNCACB | sample_1 | isotropic | sample_conditions_1 |
| 3D CBCA(CO)NH | sample_2 | isotropic | sample_conditions_1 |
| 3D HNCACB | sample_2 | isotropic | sample_conditions_1 |
Software:
ARIA, Linge, O'Donoghue and Nilges - structure solution
NMR spectrometers:
- Agilent DD2 600 MHz
Download simulated HSQC data in one of the following formats:
CSV: Backbone
or all simulated shifts
SPARKY: Backbone
or all simulated shifts