BMRB Entry 17485

Title:
Solution structure of Pf1 SID1-mSin3A PAH2 Complex
Deposition date:
2011-02-23
Original release date:
2011-03-30
Authors:
Senthil Kumar, Ganesan; Xie, Tao; Zhang, Yongbo; Radhakrishnan, Ishwar
Citation:

Citation: Kumar, Ganesan Senthil; Xie, Tao; Zhang, Yongbo; Radhakrishnan, Ishwar. "Solution Structure of the mSin3A PAH2-Pf1 SID1 Complex: A Mad1/Mxd1-Like Interaction Disrupted by MRG15 in the Rpd3S/Sin3S Complex."  J. Mol. Biol. 408, 987-1000 (2011).
PubMed: 21440557

Assembly members:

Assembly members:
entity_1, polymer, 45 residues, 4993.651 Da.
entity_2, polymer, 94 residues, 10816.996 Da.

Natural source:

Natural source:   Common Name: Human   Taxonomy ID: 9606   Superkingdom: Eukaryota   Kingdom: Metazoa   Genus/species: Homo sapiens

Experimental source:

Experimental source:   Production method: recombinant technology   Host organism: Escherichia coli   Vector: pMCSG7

Data sets:
Data typeCount
13C chemical shifts545
15N chemical shifts136
1H chemical shifts866

Additional metadata:

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

Assembly:

Entity Assembly IDEntity NameEntity ID
1entity_11
2entity_22

Entities:

Entity 1, entity_1 45 residues - 4993.651 Da.

1   SERASNALAASPTYRVALGLNPROGLNLEU
2   ARGARGPROPHEGLULEULEUILEALAALA
3   ALAMETGLUARGASNPROTHRGLNPHEGLN
4   LEUPROASNGLULEUTHRCYSTHRTHRALA
5   LEUPROGLYSERSER

Entity 2, entity_2 94 residues - 10816.996 Da.

1   SERASNALASERLEUGLNASNASNGLNPRO
2   VALGLUPHEASNHISALAILEASNTYRVAL
3   ASNLYSILELYSASNARGPHEGLNGLYGLN
4   PROASPILETYRLYSALAPHELEUGLUILE
5   LEUHISTHRTYRGLNLYSGLUGLNARGASN
6   ALALYSGLUALAGLYGLYASNTYRTHRPRO
7   ALALEUTHRGLUGLNGLUVALTYRALAGLN
8   VALALAARGLEUPHELYSASNGLNGLUASP
9   LEULEUSERGLUPHEGLYGLNPHELEUPRO
10   ASPALAASNSER

Samples:

sample_1: entity_1, [U-100% 13C; U-100% 15N], 0.75 – 1.7 mM; entity_2, [U-100% 13C; U-100% 15N], 0.75 – 1.7 mM; H2O, [U-100% 13C; U-100% 15N], 90%; D2O, [U-100% 13C; U-100% 15N], 10%

sample_conditions_1: ionic strength: 0 M; pH: 6.00; pressure: 1 atm; temperature: 298 K

Experiments:

NameSampleSample stateSample conditions
3D 1H-13C NOESY aliphaticsample_1isotropicsample_conditions_1
3D 1H-15N NOESYsample_1isotropicsample_conditions_1
3D HCCH-COSYsample_1isotropicsample_conditions_1

Software:

ARIA v1.2, Brunger, Adams, Clore, Gros, Nilges and Read, Linge, O'Donoghue and Nilges - refinement, structure solution

NMR spectrometers:

  • Varian Inova 600 MHz

Download HSQC peak lists in one of the following formats:
CSV: Backbone or all simulated peaks
SPARKY: Backbone or all simulated peaks