BMRB Entry 17653
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PDB ID:
Entry in NMR Restraints Grid
Validation report in NRG-CING
Chem Shift validation: AVS_anomalous, AVS_full, LACS
BMRB Entry DOI: doi:10.13018/BMR17653
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Title: solution structure of the mSin3A PAH3-SAP30 SID complex PubMed: 21676866
Deposition date: 2011-05-16 Original release date: 2011-10-26
Authors: Xie, Tao; He, Yuan; Korkeamaki, Hanna; Zhang, Yongbo; Imhoff, Rebecca; Lohi, Olli; Radhakrishnan, Ishwar
Citation: Xie, Tao; He, Yuan; Korkeamaki, Hanna; Zhang, Yongbo; Imhoff, Rebecca; Lohi, Olli; Radhakrishnan, Ishwar. "Structure of the 30-kDa Sin3-associated protein (SAP30) in complex with the mammalian Sin3A corepressor and its role in nucleic acid binding." J. Biol. Chem. 286, 27814-27824 (2011).
Assembly members:
SAP30, polymer, 94 residues, 10546.846 Da.
entity_2, polymer, 75 residues, 8674.021 Da.
Natural source: Common Name: 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):
SAP30: SNAGSDDDGGDSPVQDIDTP
EVDLYQLQVNTLRRYKRHFK
LPTRPGLNKAQLVEIVGCHF
KSIPVNEKDTLTCFIYSVRN
DKNKSDLKADSGVH
entity_2: SNASKHGVGTESLFFDKVRK
ALRSAEAYENFLRCLVIFNQ
EVISRAELVQLVSPFLGKFP
ELFNWFKNFLGYKES
- assigned_chemical_shifts
| Data type | Count |
| 13C chemical shifts | 699 |
| 15N chemical shifts | 174 |
| 1H chemical shifts | 1086 |
Additional metadata:
Assembly:
| Entity Assembly ID | Entity Name | Entity ID |
|---|---|---|
| 1 | SAP30 | 1 |
| 2 | PAH3 | 2 |
Entities:
Entity 1, SAP30 94 residues - 10546.846 Da.
Residues 1-3 are from non-native tag. This is the SID domain of SAP30 protein.
| 1 | SER | ASN | ALA | GLY | SER | ASP | ASP | ASP | GLY | GLY | ||||
| 2 | ASP | SER | PRO | VAL | GLN | ASP | ILE | ASP | THR | PRO | ||||
| 3 | GLU | VAL | ASP | LEU | TYR | GLN | LEU | GLN | VAL | ASN | ||||
| 4 | THR | LEU | ARG | ARG | TYR | LYS | ARG | HIS | PHE | LYS | ||||
| 5 | LEU | PRO | THR | ARG | PRO | GLY | LEU | ASN | LYS | ALA | ||||
| 6 | GLN | LEU | VAL | GLU | ILE | VAL | GLY | CYS | HIS | PHE | ||||
| 7 | LYS | SER | ILE | PRO | VAL | ASN | GLU | LYS | ASP | THR | ||||
| 8 | LEU | THR | CYS | PHE | ILE | TYR | SER | VAL | ARG | ASN | ||||
| 9 | ASP | LYS | ASN | LYS | SER | ASP | LEU | LYS | ALA | ASP | ||||
| 10 | SER | GLY | VAL | HIS |
Entity 2, PAH3 75 residues - 8674.021 Da.
Residues 1-3 are from non-native tag. This is the PAH3 domain of mSIN3A.
| 1 | SER | ASN | ALA | SER | LYS | HIS | GLY | VAL | GLY | THR | ||||
| 2 | GLU | SER | LEU | PHE | PHE | ASP | LYS | VAL | ARG | LYS | ||||
| 3 | ALA | LEU | ARG | SER | ALA | GLU | ALA | TYR | GLU | ASN | ||||
| 4 | PHE | LEU | ARG | CYS | LEU | VAL | ILE | PHE | ASN | GLN | ||||
| 5 | GLU | VAL | ILE | SER | ARG | ALA | GLU | LEU | VAL | GLN | ||||
| 6 | LEU | VAL | SER | PRO | PHE | LEU | GLY | LYS | PHE | PRO | ||||
| 7 | GLU | LEU | PHE | ASN | TRP | PHE | LYS | ASN | PHE | LEU | ||||
| 8 | GLY | TYR | LYS | GLU | SER |
Samples:
sample_1: entity_1, [U-100% 13C; U-100% 15N], 1 mM; entity_2 1 mM; H2O 90%; D2O 10%
sample_2: entity_1 1 mM; entity_2, [U-100% 13C; U-100% 15N], 1 mM; H2O 90%; D2O 10%
sample_3: entity_1, [U-100% 13C; U-100% 15N], 1 mM; entity_2 1 mM; D2O 100%
sample_4: entity_1 1 mM; entity_2, [U-100% 13C; U-100% 15N], 1 mM; D2O 100%
sample_conditions_1: pH: 6.5; temperature: 273 K
Experiments:
| Name | Sample | Sample state | Sample conditions |
|---|---|---|---|
| 3D 1H-15N NOESY | sample_1 | isotropic | sample_conditions_1 |
| 3D 1H-15N NOESY | sample_2 | isotropic | sample_conditions_1 |
| 3D 1H-13C NOESY aliphatic | sample_3 | isotropic | sample_conditions_1 |
| 3D 1H-13C NOESY aliphatic | sample_4 | isotropic | sample_conditions_1 |
| 2D 1H-15N HSQC | sample_1 | isotropic | sample_conditions_1 |
| 2D 1H-15N HSQC | sample_2 | isotropic | sample_conditions_1 |
| 3D CBCA(CO)NH | sample_1 | isotropic | sample_conditions_1 |
| 3D CBCA(CO)NH | sample_2 | isotropic | sample_conditions_1 |
| 3D HNCACB | sample_1 | isotropic | sample_conditions_1 |
| 3D HNCACB | sample_2 | isotropic | sample_conditions_1 |
| 3D HNCO | sample_1 | isotropic | sample_conditions_1 |
| 3D HNCO | sample_2 | isotropic | sample_conditions_1 |
| 3D HNCA | sample_1 | isotropic | sample_conditions_1 |
| 3D HNCA | sample_2 | isotropic | sample_conditions_1 |
| 3D HCCH-COSY | sample_3 | isotropic | sample_conditions_1 |
| 3D HCCH-COSY | sample_4 | isotropic | sample_conditions_1 |
| 3D HCCH-TOCSY | sample_3 | isotropic | sample_conditions_1 |
| 3D HCCH-TOCSY | sample_4 | isotropic | sample_conditions_1 |
| 2D 1H-13C HSQC aromatic | sample_3 | isotropic | sample_conditions_1 |
| 2D 1H-13C HSQC aromatic | sample_4 | isotropic | sample_conditions_1 |
Software:
ARIA v1.2, Linge, O, . - structure solution
SPARKY, Goddard - chemical shift assignment, data analysis, peak picking
FELIX v98, Accelrys Software Inc. - processing
VNMRJ, Varian - collection
CNS, Brunger, Adams, Clore, Gros, Nilges and Read - refinement, structure solution
NMR spectrometers:
- Varian INOVA 600 MHz
Related Database Links:
| PDB | |
| DBJ | BAB27273 BAC40543 BAD90217 |
| GB | AAC26007 AAI32082 AAI32088 EDL28616 EDL28617 AAA69772 AAA69773 AAA89119 AAB01610 AAH52716 |
| REF | NP_068560 XP_005607821 XP_006253148 XP_008512731 XP_008770398 NP_001102231 NP_001103820 NP_001103821 NP_035508 XP_001491398 |
| SP | O88574 Q60520 |
| TPG | DAA17551 |
Download simulated HSQC data in one of the following formats:
CSV: Backbone
or all simulated shifts
SPARKY: Backbone
or all simulated shifts