BMRB Entry 15570

Title:
SOLUTION STRUCTURE OF THE MSIN3A PAH1-SAP25 SID COMPLEX
Deposition date:
2007-11-27
Original release date:
2008-06-27
Authors:
Sahu, S.; Swanson, K.; Kang, R.; Huang, K.; Brubaker, K.; Ratcliff, K.; Radhakrishnan, I.
Citation:

Citation: Sahu, S.; Swanson, K.; Kang, R.; Huang, K.; Brubaker, K.; Ratcliff, K.; Radhakrishnan, I.. "Conserved themes in target recognition by the PAH1 and PAH2 domains of the Sin3 transcriptional corepressor."  J. Mol. Biol. 375, 1444-1456 (2008).
PubMed: 18089292

Assembly members:

Assembly members:
PAIRED_AMPHIPATHIC_HELIX_PROTEIN_SIN3A, polymer, 71 residues, 8087.342 Da.
Sap25, polymer, 61 residues, Formula weight is not available

Natural source:

Natural source:   Common Name: MOUSE   Taxonomy ID: 10090   Superkingdom: Eukaryota   Kingdom: Metazoa   Genus/species: Mus Musculus

Experimental source:

Experimental source:   Production method: recombinant technology   Host organism: ESCHERICHIA COLI   Vector: PET30

Entity Sequences (FASTA):

Data sets:
Data typeCount
13C chemical shifts548
15N chemical shifts127
1H chemical shifts791

Additional metadata:

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

Assembly:

Entity Assembly IDEntity NameEntity ID
1PAH11
2Sap252

Entities:

Entity 1, PAH1 71 residues - 8087.342 Da.

119-189:PAH1 127-186:Sap25

1   GLNARGLEULYSVALGLUASPALALEUSER
2   TYRLEUASPGLNVALLYSLEUGLNPHEGLY
3   SERGLNPROGLNVALTYRASNASPPHELEU
4   ASPILEMETLYSGLUPHELYSSERGLNSER
5   ILEASPTHRPROGLYVALILESERARGVAL
6   SERGLNLEUPHELYSGLYHISPROASPLEU
7   ILEMETGLYPHEASNTHRPHELEUPROPRO
8   GLY

Entity 2, Sap25 61 residues - Formula weight is not available

In the chemical shift table it starts after PAH1 residues 119-189

1   SERSERTHRTRPLEUSERGLUALAGLUMET
2   ILEALALEUALAGLYLEULEUGLNMETSER
3   GLNGLYGLUGLNTHRPROASNCYSVALALA
4   SERSERLEUPROSERTHRSERCYSPROASP
5   PROVALSERVALSERGLUASPPROGLYPRO
6   SERGLYASPGLNSERCYSSERGLYTHRASP
7   THR

Samples:

sample_1: Sap25, [U-100% 15N], 1 mM; PAH1, [U-100% 13C; U-100% 15N], 1 mM; SODIUM PHOSPHATE 20 mM; SODIUM AZIDE 0.2%; DTT 2 mM; D2O, [U-100% 2H], 10%; H2O 90%

sample_conditions_1: ionic strength: 0.02 M; pH: 6; pressure: 1 atm; temperature: 303 K

Experiments:

NameSampleSample stateSample conditions
3D 1H-15N NOESYsample_1isotropicsample_conditions_1
3D 1H-13C NOESYsample_1isotropicsample_conditions_1

Software:

CNS v1.2, BRUNGER, ADAMS, CLORE, GROS, NILGES, READ - refinement

FELIX v98.0, Accelrys Software Inc. - data analysis

ARIA v1.2, Linge, O'Donoghue and Nilges - structure solution

VNMR, Varian - collection

NMR spectrometers:

  • VARIAN INOVA 600 MHz

Related Database Links:

BMRB 15569
PDB
EMBL CDQ82228 CAK36853
GB AAH81027 ETE65880 AAI52783 AAI56602
REF NP_001129640 XP_012362542 XP_013921538 NP_001075431
SP Q1EHW4
AlphaFold Q1EHW4

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