BMRB

Biological Magnetic Resonance Data Bank


A Repository for Data from NMR Spectroscopy on Proteins, Peptides, Nucleic Acids, and other Biomolecules
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BMRB Entry 15569

Title: SOLUTION STRUCTURE OF MSIN3A PAH1 DOMAIN   PubMed: 18089292

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: 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).

Assembly members:
PAIRED_AMPHIPATHIC_HELIX_PROTEIN_SIN3A, polymer, 71 residues, 8087.342 Da.

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

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

Entity Sequences (FASTA):
PAIRED_AMPHIPATHIC_HELIX_PROTEIN_SIN3A: QRLKVEDALSYLDQVKLQFG SQPQVYNDFLDIMKEFKSQS IDTPGVISRVSQLFKGHPDL IMGFNTFLPPG

Data sets:
Data typeCount
13C chemical shifts321
15N chemical shifts74
1H chemical shifts480

Additional metadata:

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

Assembly:

Entity Assembly IDEntity NameEntity ID
1PAH11

Entities:

Entity 1, PAH1 71 residues - 8087.342 Da.

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

Samples:

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

sample)_2: 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: 288 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 15570
PDB
EMBL CDQ82228
GB AAH81027 ETE65880
REF NP_001129640 XP_012362542 XP_013921538

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