BMRB Entry 30004

Title:
Solution Structure of TAZ2-p53TAD
Deposition date:
2016-01-20
Original release date:
2016-03-14
Authors:
Krois, A.; Ferreon, J.; Martinez-Yamout, M.; Dyson, H.; Wright, P.
Citation:

Citation: Krois, A.; Ferreon, J.; Martinez-Yamout, M.; Dyson, H.; Wright, P.. "Recognition of the disordered p53 transactivation domain by the transcriptional adapter zinc finger domains of CREB-binding protein"  Proc. Natl. Acad. Sci. U. S. A. 113, E1853-E1862 (2016).
PubMed: 26976603

Assembly members:

Assembly members:
CREB-binding protein,Cellular tumor antigen p53 fusion protein, polymer, 158 residues, 17711.236 Da.
ZINC ION, 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

Entity Sequences (FASTA):

Data sets:
Data typeCount
13C chemical shifts509
15N chemical shifts153
1H chemical shifts1073

Additional metadata:

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

Assembly:

Entity Assembly IDEntity NameEntity ID
1entity_11
2entity ZN, 12
3entity ZN, 22
4entity ZN, 32

Entities:

Entity 1, entity_1 158 residues - 17711.236 Da.

1   SERPROGLNGLUSERARGARGLEUSERILE
2   GLNARGCYSILEGLNSERLEUVALHISALA
3   CYSGLNCYSARGASNALAASNCYSSERLEU
4   PROSERCYSGLNLYSMETLYSARGVALVAL
5   GLNHISTHRLYSGLYCYSLYSARGLYSTHR
6   ASNGLYGLYCYSPROVALCYSLYSGLNLEU
7   ILEALALEUCYSCYSTYRHISALALYSHIS
8   CYSGLNGLUASNLYSCYSPROVALPROPHE
9   CYSLEUASNILELYSHISLYSLEUARGGLN
10   GLNGLNGLYSERGLYSERGLYSERGLUGLU
11   PROGLNSERASPPROSERVALGLUPROPRO
12   LEUSERGLNGLUTHRPHESERASPLEUTRP
13   LYSLEULEUPROGLUASNASNVALLEUSER
14   PROLEUPROSERGLNALAMETASPASPLEU
15   METLEUSERPROASPASPILEGLUGLNTRP
16   PHETHRGLUASPPROGLYPROASP

Entity 2, entity ZN, 1 - Zn - 65.409 Da.

1   ZN

Samples:

sample_1: D2O, [U-2H], 10%; DTT 1 mM; TAZ2-p53TAD, [U-13C; U-15N], 1.75 ± 0.25 mM; TRIS 20 mM; sodium chloride 50 mM; H2O, [U-2H], 90%

sample_2: D2O, [U-2H], 99%; DTT, [U-2H], 1 mM; TAZ2-p53TAD, [U-13C; U-15N], 1.75 ± 0.25 mM; TRIS, [U-2H], 20 mM; sodium chloride 50 mM; H2O, [U-2H], 1%

sample_3: D2O, [U-2H], 99%; DTT, [U-2H], 2 mM; TAZ2, [U-13C], 1 mM; TRIS, [U-2H], 20 mM; p53(13-37 1 mM; p53(38-61) 1 mM; sodium chloride 50 mM; H2O, [U-2H], 1%

sample_4: D2O, [U-2H], 99%; DTT, [U-2H], 2 mM; TAZ2 1 mM; TRIS, [U-2H], 20 mM; p53(13-37), [U-13C], 1 mM; p53(38-61), [U-13C], 1 mM; sodium chloride 50 mM; H2O, [U-2H], 1%

sample_5: D2O, [U-2H], 10%; DTT 2 mM; TAZ2 1 mM; TRIS 20 mM; p53(13-61), [U-15N], 1 mM; sodium chloride 50 mM; H2O, [U-2H], 90%

sample_6: D2O, [U-2H], 10%; DTT 2 mM; TAZ2, [U-15N], 1 mM; TRIS 20 mM; p53(13-61) 1 mM; sodium chloride 50 mM; H2O, [U-2H], 90%

sample_7: D2O, [U-2H], 99%; DTT, [U-2H], 2 mM; TAZ2 1 mM; TRIS, [U-2H], 20 mM; p53(13-61), [U-13C], 1 mM; sodium chloride 50 mM; H2O, [U-2H], 1%

sample_8: D2O, [U-2H], 99%; DTT, [U-2H], 2 mM; TAZ2, [U-13C], 1 mM; TRIS, [U-2H], 20 mM; p53(13-61) 1 mM; sodium chloride 50 mM; H2O, [U-2H], 1%

sample_conditions_1: ionic strength: 50 mM; pH: 6.8; pressure: 1 atm; temperature: 305 K

sample_conditions_2: ionic strength: 50 mM; pH: 6.4 pD; pressure: 1 atm; temperature: 305 K

Experiments:

NameSampleSample stateSample conditions
3D 1H-15N NOESYsample_1isotropicsample_conditions_1
3D 1H-13C NOESYsample_2isotropicsample_conditions_2
3D HNCACBsample_1isotropicsample_conditions_1
3D 1H-15N TOCSYsample_5isotropicsample_conditions_1
3D 1H-13C NOESYsample_7isotropicsample_conditions_2
3D 1H-15N NOESYsample_5isotropicsample_conditions_1
3D 1H-13C NOESYsample_8isotropicsample_conditions_2
3D 1H-15N NOESYsample_6isotropicsample_conditions_1
3D HCCH-COSYsample_3isotropicsample_conditions_2
3D HCCH-COSYsample_4isotropicsample_conditions_2

Software:

AMBER v12, Case, Darden, Cheatham III, Simmerling, Wang, Duke, Luo, and Kollman - refinement

CYANA v2.1, Guntert, Mumenthaler and Wuthrich - structure calculation

NMRView v5.0.4, Johnson, One Moon Scientific - chemical shift assignment

PSVS v1.5, Bhattacharya and Montelione - data analysis

NMR spectrometers:

  • Bruker Avance 900 MHz
  • Bruker DRX 600 MHz

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