BMRB Entry 25307

Title:
solution structure of SATB1 homeodomain
Deposition date:
2014-10-31
Original release date:
2015-11-02
Authors:
Yamasaki, Kazuhiko; Yamasaki, Tomoko
Citation:

Citation: Yamasaki, Kazuhiko; Yamasaki, Tomoko. "The combination of sequence-specific and nonspecific DNA-binding modes of transcription factor SATB1"  Biochem. J. 473, 3321-3339 (2016).
PubMed: 27462121

Assembly members:

Assembly members:
SATB1, polymer, 71 residues, 7903.208 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: pET15b

Entity Sequences (FASTA):

Data sets:
Data typeCount
15N chemical shifts73
1H chemical shifts82

Additional metadata:

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

Assembly:

Entity Assembly IDEntity NameEntity ID
1SATB1 homeodomain1

Entities:

Entity 1, SATB1 homeodomain 71 residues - 7903.208 Da.

1   GLYSERHISMETASNARGGLNLYSTHRARG
2   PROARGTHRLYSILESERVALGLUALALEU
3   GLYILELEUGLNSERPHEILEGLNASPVAL
4   GLYLEUTYRPROASPGLUGLUALAILEGLN
5   THRLEUSERALAGLNLEUASPLEUPROLYS
6   TYRTHRILEILELYSPHEPHEGLNASNGLN
7   ARGTYRTYRLEULYSHISHISGLYLYSLEU
8   LYS

Samples:

sample_1: SATB1 homeodomain, [U-15N], 0.3 mM; sodium phosphate 50 mM; sodium chloride 50 mM; DSS 0.5 mM; H2O 95%; D2O 5%

sample_2: SATB1 homeodomain, [U-15N], 0.7 – 1.2 mM; sodium phosphate 50 mM; sodium chloride 200 mM; DSS 0.5 mM; H2O 90%; D2O 5%

sample_3: SATB1 homeodomain, [U-15N], 0.7 – 1.2 mM; sodium phosphate 50 mM; sodium chloride 200 mM; DSS 0.5 mM; H2O 95%; D2O 5%

sample_conditions_1: ionic strength: 0.1 M; pH: 5.5; pressure: 1 atm; temperature: 298 K

sample_conditions_2: ionic strength: 0.25 M; pH: 5.5; pressure: 1 atm; temperature: 298 K

Experiments:

NameSampleSample stateSample conditions
2D 1H-15N HSQCsample_1isotropicsample_conditions_1
2D 1H-15N HSQCsample_2isotropicsample_conditions_2
3D 1H-15N NOESYsample_2isotropicsample_conditions_2
3D 1H-15N TOCSYsample_2isotropicsample_conditions_2
2D 1H-1H NOESYsample_3isotropicsample_conditions_2
2D DQF-COSYsample_3isotropicsample_conditions_2
2D 1H-1H TOCSYsample_3isotropicsample_conditions_2

Software:

CNS, Brunger, Adams, Clore, Gros, Nilges and Read - structure solution

Felix, Accelrys Software Inc. - data analysis

NMR spectrometers:

  • Bruker Avance 500 MHz
  • Bruker DMX 750 MHz
  • Bruker DMX 500 MHz

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