BMRB Entry 30003

Click here to enlarge.

PDB ID:
Entry in NMR Restraints Grid
Validation report in NRG-CING
Chem Shift validation: AVS_full, LACS
BMRB Entry DOI: doi:10.13018/BMR30003
MolProbity Validation Chart

NMR-STAR file interactive viewer.
NMR-STAR v3 text file.
XML gzip file.
RDF gzip file.
All files associated with the entry

Title:
Solution Structure of TAZ2-p53AD2
Deposition date:
2016-01-19
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, 122 residues, 13707.868 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):

Entity Sequences (FASTA):
CREB-binding protein,Cellular tumor antigen p53 fusion protein: SPQESRRLSIQRCIQSLVHA CQCRNANCSLPSCQKMKRVV QHTKGCKRKTNGGCPVCKQL IALCCYHAKHCQENKCPVPF CLNIKHKLRQQQGSGSGSQA MDDLMLSPDDIEQWFTEDPG PD

Data sets:
Data typeCount
13C chemical shifts385
15N chemical shifts122
1H chemical shifts822

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_1 122 residues - 13707.868 Da.

1   SERPROGLNGLUSERARGARGLEUSERILE
2   GLNARGCYSILEGLNSERLEUVALHISALA
3   CYSGLNCYSARGASNALAASNCYSSERLEU
4   PROSERCYSGLNLYSMETLYSARGVALVAL
5   GLNHISTHRLYSGLYCYSLYSARGLYSTHR
6   ASNGLYGLYCYSPROVALCYSLYSGLNLEU
7   ILEALALEUCYSCYSTYRHISALALYSHIS
8   CYSGLNGLUASNLYSCYSPROVALPROPHE
9   CYSLEUASNILELYSHISLYSLEUARGGLN
10   GLNGLNGLYSERGLYSERGLYSERGLNALA
11   METASPASPLEUMETLEUSERPROASPASP
12   ILEGLUGLNTRPPHETHRGLUASPPROGLY
13   PROASP

Entity 2, entity_ZN, 1 - Zn - 65.409 Da.

1   ZN

Samples:

sample_1: D2O, [U-2H], 10%; DTT 2 mM; TAZ2-p53AD2, [U-13C; U-15N], 1 mM; TRIS 20 mM; sodium chloride 50 mM; H2O, [U-2H], 90%

sample_2: D2O, [U-2H], 99%; DTT, [U-2H], 2 mM; TAZ2-p53AD2, [U-13C; U-15N], 1 mM; TRIS, [U-2H], 20 mM; sodium chloride 50 mM; H2O, [U-2H], 1%

sample_3: D2O, [U-2H], 5%; DTT 2 mM; TAZ2-p53AD2, [U-13C; U-15N], 1 mM; TRIS 20 mM; sodium chloride 50 mM; H2O, [U-2H], 95%

sample_4: D2O, [U-2H], 5%; DTT, [U-2H], 2 mM; TAZ2, [U-13C], 1 mM; TRIS, [U-2H], 20 mM; p53AD2(38-61) 1 mM; sodium chloride 50 mM; H2O, [U-2H], 95%

sample_5: D2O, [U-2H], 99%; DTT, [U-2H], 2 mM; TAZ2 1 mM; TRIS, [U-2H], 20 mM; p53AD2, [U-13C], 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_3isotropicsample_conditions_1
3D HCCH-COSYsample_4isotropicsample_conditions_2
3D HCCH-COSYsample_5isotropicsample_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