BMRB Entry 4635
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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/BMR4635
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: Brubaker, K.; Cowley, S.; Huang, K.; Loo, L.; Yochum, G.; Ayer, D.; Eisenman, R.; Radhakrishnan, I.. "Solution structure of the interacting domains of the Mad-Sin3 complex:
implications for recruitment of a chromatin-modifying complex" Cell 103, 655-665 (2000).
PubMed: 11106735
Assembly members:
MAD1 SID domain, polymer, 16 residues, Formula weight is not available
mSin3A PAH2 Domain, polymer, 89 residues, Formula weight is not available
Natural source: Common Name: not available Taxonomy ID: not available Superkingdom: not available Kingdom: not available Genus/species: not available not available
Experimental source: Production method: recombinant technology Host organism: Escherichia coli Vector: pET-24a(+)
Entity Sequences (FASTA):
MAD1 SID domain: RMNIQMLLEAADYLER
mSin3A PAH2 Domain: SLQNNQPVEFNHAINYVNKI
KNRFQGQPDIYKAFLEILHT
YQKEQRNAKEAGGNYTPALT
EQEVYAQVARLFKNQEDLLS
EFGQFLPDA
- coupling_constants
| Data type | Count |
| coupling constants | 72 |
Additional metadata:
Assembly:
| Entity Assembly ID | Entity Name | Entity ID |
|---|---|---|
| 1 | MAD1 SID domain | 1 |
| 2 | mSin3A PAH2 Domain | 2 |
Entities:
Entity 1, MAD1 SID domain 16 residues - Formula weight is not available
| 1 | ARG | MET | ASN | ILE | GLN | MET | LEU | LEU | GLU | ALA | ||||
| 2 | ALA | ASP | TYR | LEU | GLU | ARG |
Entity 2, mSin3A PAH2 Domain 89 residues - Formula weight is not available
| 1 | SER | LEU | GLN | ASN | ASN | GLN | PRO | VAL | GLU | PHE | ||||
| 2 | ASN | HIS | ALA | ILE | ASN | TYR | VAL | ASN | LYS | ILE | ||||
| 3 | LYS | ASN | ARG | PHE | GLN | GLY | GLN | PRO | ASP | ILE | ||||
| 4 | TYR | LYS | ALA | PHE | LEU | GLU | ILE | LEU | HIS | THR | ||||
| 5 | TYR | GLN | LYS | GLU | GLN | ARG | ASN | ALA | LYS | GLU | ||||
| 6 | ALA | GLY | GLY | ASN | TYR | THR | PRO | ALA | LEU | THR | ||||
| 7 | GLU | GLN | GLU | VAL | TYR | ALA | GLN | VAL | ALA | ARG | ||||
| 8 | LEU | PHE | LYS | ASN | GLN | GLU | ASP | LEU | LEU | SER | ||||
| 9 | GLU | PHE | GLY | GLN | PHE | LEU | PRO | ASP | ALA |
Samples:
sample_1: MAD1 SID domain 1.0 mM; mSin3A PAH2 Domain, [U-15N], 1.0 mM; H2O 90%; D2O 10%
sample_2: MAD1 SID domain 1.6 mM; mSin3A PAH2 Domain, [U-15N; U-13C], 1.6 mM; H2O 90%; D2O 10%
sample_3: MAD1 SID domain 1.6 mM; mSin3A PAH2 Domain, [U-15N; U-13C], 1.6 mM; H2O 90%; D2O 10%; phosphate buffer 20 mM; NaN3 0.2%
sample_4: MAD1 SID domain 1.6 mM; mSin3A PAH2 Domain, [U-15N; U-13C], 1.6 mM; D2O 100%; phosphate buffer 20 mM; NaN3 0.2%
sample_cond_1: pH: 6.0; temperature: 300 K; ionic strength: 20 mM; pressure: 1 atm
Experiments:
| Name | Sample | Sample state | Sample conditions |
|---|---|---|---|
| 3D 15N-separated NOESY | not available | not available | sample_cond_1 |
| HNHA | not available | not available | sample_cond_1 |
| 2D 13C,15N-double-half-filtered NOESY | not available | not available | sample_cond_1 |
| 2D 13C-double-half-filtered NOESY | not available | not available | sample_cond_1 |
| 3D 13C-separated_NOESY | not available | not available | sample_cond_1 |
| 3D HACAHB | not available | not available | sample_cond_1 |
| 3D HNHB | not available | not available | sample_cond_1 |
Software:
FELIX v98 - processing, data analysis
DYANA v1.5 - structure solution
CNS v1.0 - refinement
NMR spectrometers:
- Varian INOVA 500 MHz