BMRB Entry 4635
Chem Shift validation: AVS_full
BMRB Entry DOI: doi:10.13018/BMR4635
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Title: Solution structure of the interacting domains of the Mad-Sin3 complex: implications for recruitment of a chromatin-modifying complex PubMed: 11106735
Deposition date: 2000-10-11 Original release date: 2001-05-07
Authors: Brubaker, K.; Cowley, S.; Huang, K.; Eisenman, R.; Radhakrishnan, I.
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).
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
Entity Sequences (FASTA):
MAD1 SID domain: RMNIQMLLEAADYLER
mSin3A PAH2 Domain: SLQNNQPVEFNHAINYVNKI
KNRFQGQPDIYKAFLEILHT
YQKEQRNAKEAGGNYTPALT
EQEVYAQVARLFKNQEDLLS
EFGQFLPDA
- assigned_chemical_shifts
- 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
Related Database Links:
PDB | |
DBJ | BAG35605 BAG73371 BAH13406 |
EMBL | CAG38734 CAG46493 |
GB | AAA36194 AAH69377 AAH69433 AAH98396 AAI13532 |
REF | NP_001179309 NP_001189442 NP_001189443 NP_001247787 NP_002348 |
SP | Q05195 |
TPG | DAA24557 |
GenBank | AAK95854 |