BMRB Entry 16015

Title:
Structure of protein complex
Deposition date:
2008-10-30
Original release date:
2009-02-16
Authors:
Wojciak, Jonathan; Martinez-Yamout, Maria; Dyson, Helen; Wright, Peter
Citation:

Citation: Wojciak, Jonathan; Martinez-Yamout, Maria; Dyson, Helen; Wright, Peter. "Structural basis for recruitment of CBP/p300 coactivators by STAT1 and STAT2 transactivation"  EMBO J. 28, 948-958 (2009).
PubMed: 19214187

Assembly members:

Assembly members:
TAZ2, polymer, 92 residues, Formula weight is not available
STAT1, polymer, 45 residues, Formula weight is not available
ZN, non-polymer, 65.409 Da.

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: pET

Data sets:
Data typeCount
13C chemical shifts434
15N chemical shifts142
1H chemical shifts933

Additional metadata:

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

Assembly:

Entity Assembly IDEntity NameEntity ID
1TAZ21
2STAT12
3ZINC ION_13
4ZINC ION_23
5ZINC ION_33

Entities:

Entity 1, TAZ2 92 residues - Formula weight is not available

1   SERPROGLNGLUSERARGARGLEUSERILE
2   GLNARGCYSILEGLNSERLEUVALHISALA
3   CYSGLNCYSARGASNALAASNCYSSERLEU
4   PROSERCYSGLNLYSMETLYSARGVALVAL
5   GLNHISTHRLYSGLYCYSLYSARGLYSTHR
6   ASNGLYGLYCYSPROVALCYSLYSGLNLEU
7   ILEALALEUCYSCYSTYRHISALALYSHIS
8   CYSGLNGLUASNLYSCYSPROVALPROPHE
9   CYSLEUASNILELYSHISLYSLEUARGGLN
10   GLNGLN

Entity 2, STAT1 45 residues - Formula weight is not available

1   GLYSERHISMETSERGLUVALHISPROSER
2   ARGLEUGLNTHRTHRASPASNLEULEUPRO
3   METSERPROGLUGLUPHEASPGLUVALSER
4   ARGILEVALGLYSERVALGLUPHEASPSER
5   METMETASNTHRVAL

Entity 3, ZINC ION_1 - Zn - 65.409 Da.

1   ZN

Samples:

sample_1: TAZ2, [U-100% 15N], 1 mM; STAT1; ZINC_ION; H2O 90%; D2O 10%

sample_conditions_1: ionic strength: 0.05 M; pH: 6.8; pressure: 1 atm; temperature: 290 K

Experiments:

NameSampleSample stateSample conditions
2D 1H-15N HSQCsample_1isotropicsample_conditions_1

Software:

AMBER, Case, Darden, Cheatham, III, Simmerling, Wang, Duke, Luo, ... and Kollm - refinement

NMR spectrometers:

  • Bruker DRX 600 MHz
  • Bruker Avance 900 MHz

Related Database Links:

BMRB 16318
PDB
DBJ BAE06125 BAI45616
EMBL CAF96470 CAG06082 CDQ92618
GB AAB28651 AAC17736 AAC51331 AAC51340 AAC51770
PRF 1923401A
REF NP_001020603 NP_001073315 NP_001088637 NP_001157494 NP_001192159
SP P45481 Q6JHU9 Q92793
TPG DAA15549
AlphaFold Q9UDL5 P45481 Q6JHU9 Q92793

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