BMRB Entry 18492
Click here to enlarge.
PDB ID:
Entry in NMR Restraints Grid
Validation report in NRG-CING
Chem Shift validation: AVS_full, SPARTA
BMRB Entry DOI: doi:10.13018/BMR18492
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 the SANT2 domain of the human nuclear receptor corepressor 2 (NCoR2), Northeast Structural Genomics Consortium (NESG) target ID HR4636E.
Deposition date: 2012-05-30 Original release date: 2012-06-18
Authors: Montecchio, Meri; Lemak, Alexander; Yee, Adelinda; Xu, Chao; Garcia, Maite; Houliston, Scott; Bellanda, Massimo; Min, Jinrong; Arrowsmith, Cheryl; Montelione, G.T.
Citation: Montecchio, Meri; Lemak, Alexander; Yee, Adelinda; Xu, Chao; Garcia, Maite; Houliston, Scott; Bellanda, Massimo; Min, Jinrong; Arrowsmith, Cheryl. "Solution structure of the SANT2 domain of the human nuclear receptor corepressor 2 (NCoR2)." Not known ., .-..
Assembly members:
entity_1, polymer, 89 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
Entity Sequences (FASTA):
entity_1: MHHHHHHSSGRENLYFQGWT
EEEMGTAKKGLLEHGRNWSA
IARMVGSKTVSQCKNFYFNY
KKRQNLDEILQQHKLKMEKE
RNARRKKKK
- assigned_chemical_shifts
- spectral_peak_list
| Data type | Count |
| 13C chemical shifts | 287 |
| 15N chemical shifts | 71 |
| 1H chemical shifts | 466 |
Additional metadata:
Assembly:
| Entity Assembly ID | Entity Name | Entity ID |
|---|---|---|
| 1 | SANT2 domain of NCoR2 | 1 |
Entities:
Entity 1, SANT2 domain of NCoR2 89 residues - Formula weight is not available
| 1 | MET | HIS | HIS | HIS | HIS | HIS | HIS | SER | SER | GLY | ||||
| 2 | ARG | GLU | ASN | LEU | TYR | PHE | GLN | GLY | TRP | THR | ||||
| 3 | GLU | GLU | GLU | MET | GLY | THR | ALA | LYS | LYS | GLY | ||||
| 4 | LEU | LEU | GLU | HIS | GLY | ARG | ASN | TRP | SER | ALA | ||||
| 5 | ILE | ALA | ARG | MET | VAL | GLY | SER | LYS | THR | VAL | ||||
| 6 | SER | GLN | CYS | LYS | ASN | PHE | TYR | PHE | ASN | TYR | ||||
| 7 | LYS | LYS | ARG | GLN | ASN | LEU | ASP | GLU | ILE | LEU | ||||
| 8 | GLN | GLN | HIS | LYS | LEU | LYS | MET | GLU | LYS | GLU | ||||
| 9 | ARG | ASN | ALA | ARG | ARG | LYS | LYS | LYS | LYS |
Samples:
sample_1: SANT2, [U-13C; U-15N], 1 mM; sodium phosphate 25 mM; NaCl 200 mM; ZnSO4 0.01 mM; DTT 10 mM; benzamidine 1 mM; NaN3 0.01%; H2O 95%; D2O 5%
sample_conditions_1: ionic strength: 200 mM; pH: 6.5; pressure: 1 atm; temperature: 298 K
Experiments:
| Name | Sample | Sample state | Sample conditions |
|---|---|---|---|
| 2D 1H-15N HSQC | sample_1 | isotropic | sample_conditions_1 |
| 3D CBCA(CO)NH | sample_1 | isotropic | sample_conditions_1 |
| 3D HNCO | sample_1 | isotropic | sample_conditions_1 |
| 3D HNCA | sample_1 | isotropic | sample_conditions_1 |
| 3D HBHA(CO)NH | sample_1 | isotropic | sample_conditions_1 |
| 3D 1H-15N NOESY | sample_1 | isotropic | sample_conditions_1 |
| 2D 1H-13C HSQC aliphatic | sample_1 | isotropic | sample_conditions_1 |
| 2D 1H-13C HSQC aromatic | 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 |
| 3D H(C)CH-TOCSY | sample_1 | isotropic | sample_conditions_1 |
| 3D (H)CCH-TOCSY | sample_1 | isotropic | sample_conditions_1 |
Software:
NMRPipe, Delaglio, Grzesiek, Vuister, Zhu, Pfeifer and Bax - processing
TALOS, Cornilescu, Delaglio and Bax - data analysis
SPARKY, Goddard - peak picking
MDDGUI, Gutmanas A., Orekhov V. - processing
FMCGUI, Lemak A., Steren C., Llinas M., Arrowsmith C. - chemical shift assignment
CYANA, Guntert, Mumenthaler and Wuthrich - structure solution
CNS, Brunger, Adams, Clore, Gros, Nilges and Read - refinement
PSVS, Bhattacharya and Montelione - structure validation
NMR spectrometers:
- Bruker Avance 600 MHz
- Bruker Avance 800 MHz
Related Database Links:
| PDB | |
| DBJ | BAE34400 |
| GB | EPY89720 KQK78591 KQL90039 KQL90040 KQL90041 |
| REF | XP_005193418 XP_005612752 XP_007539833 XP_007665136 XP_008111869 |
Download simulated HSQC data in one of the following formats:
CSV: Backbone
or all simulated shifts
SPARKY: Backbone
or all simulated shifts