BMRB Entry 4635

Title:
Solution structure of the interacting domains of the Mad-Sin3 complex: implications for recruitment of a chromatin-modifying complex
Deposition date:
2000-10-11
Original release date:
2001-05-07
Authors:
Brubaker, K.; Cowley, S.; Huang, K.; Eisenman, R.; Radhakrishnan, I.
Citation:

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:

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:

Natural source:   Common Name: not available   Taxonomy ID: not available   Superkingdom: not available   Kingdom: not available   Genus/species: not available not available

Experimental source:

Experimental source:   Production method: recombinant technology   Host organism: Escherichia coli   Vector: pET-24a(+)

Entity Sequences (FASTA):

Data sets:
  • coupling_constants
Data typeCount
coupling constants72

Additional metadata:

  • Assembly
  • Samples and Experiments
  • Software
  • Spectrometers
  • Hide all

Assembly:

Entity Assembly IDEntity NameEntity ID
1MAD1 SID domain1
2mSin3A PAH2 Domain2

Entities:

Entity 1, MAD1 SID domain 16 residues - Formula weight is not available

1   ARGMETASNILEGLNMETLEULEUGLUALA
2   ALAASPTYRLEUGLUARG

Entity 2, mSin3A PAH2 Domain 89 residues - Formula weight is not available

1   SERLEUGLNASNASNGLNPROVALGLUPHE
2   ASNHISALAILEASNTYRVALASNLYSILE
3   LYSASNARGPHEGLNGLYGLNPROASPILE
4   TYRLYSALAPHELEUGLUILELEUHISTHR
5   TYRGLNLYSGLUGLNARGASNALALYSGLU
6   ALAGLYGLYASNTYRTHRPROALALEUTHR
7   GLUGLNGLUVALTYRALAGLNVALALAARG
8   LEUPHELYSASNGLNGLUASPLEULEUSER
9   GLUPHEGLYGLNPHELEUPROASPALA

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:

NameSampleSample stateSample conditions
3D 15N-separated NOESYnot availablenot availablesample_cond_1
HNHAnot availablenot availablesample_cond_1
2D 13C,15N-double-half-filtered NOESYnot availablenot availablesample_cond_1
2D 13C-double-half-filtered NOESYnot availablenot availablesample_cond_1
3D 13C-separated_NOESYnot availablenot availablesample_cond_1
3D HACAHBnot availablenot availablesample_cond_1
3D HNHBnot availablenot availablesample_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
AlphaFold Q05195 Q05195 Q05195