BMRB Entry 30002

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PDB ID:
Entry in NMR Restraints Grid
Validation report in NRG-CING
Chem Shift validation: AVS_full, LACS
BMRB Entry DOI: doi:10.13018/BMR30002
MolProbity Validation Chart

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NMR-STAR v3 text file.
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Title:
Solution Structure of p53TAD-TAZ1
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:
Cellular tumor antigen p53,CREB-binding protein fusion protein, polymer, 171 residues, 19112.639 Da.
ZINC ION, non-polymer, 65.409 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: pET21

Entity Sequences (FASTA):

Entity Sequences (FASTA):
Cellular tumor antigen p53,CREB-binding protein fusion protein: GSHMEEPQSDPSVEPPLSQE TFSDLWKLLPENNVLSPLPS QAMDDLMLSPDDIEQWFTED PGPDGSCFNGTATGPTADPE KRKLIQQQLVLLLHAHKCQR REQANGEVRACSLPHCRTMK NVLNHMTHCQAGKACQVAHC ASSRQIISHWKNCTRHDCPV CLPLKNASDKR

Data sets:
Data typeCount
13C chemical shifts531
15N chemical shifts162
1H chemical shifts1148

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_1 171 residues - 19112.639 Da.

1   GLYSERHISMETGLUGLUPROGLNSERASP
2   PROSERVALGLUPROPROLEUSERGLNGLU
3   THRPHESERASPLEUTRPLYSLEULEUPRO
4   GLUASNASNVALLEUSERPROLEUPROSER
5   GLNALAMETASPASPLEUMETLEUSERPRO
6   ASPASPILEGLUGLNTRPPHETHRGLUASP
7   PROGLYPROASPGLYSERCYSPHEASNGLY
8   THRALATHRGLYPROTHRALAASPPROGLU
9   LYSARGLYSLEUILEGLNGLNGLNLEUVAL
10   LEULEULEUHISALAHISLYSCYSGLNARG
11   ARGGLUGLNALAASNGLYGLUVALARGALA
12   CYSSERLEUPROHISCYSARGTHRMETLYS
13   ASNVALLEUASNHISMETTHRHISCYSGLN
14   ALAGLYLYSALACYSGLNVALALAHISCYS
15   ALASERSERARGGLNILEILESERHISTRP
16   LYSASNCYSTHRARGHISASPCYSPROVAL
17   CYSLEUPROLEULYSASNALASERASPLYS
18   ARG

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

1   ZN

Samples:

sample_1: D2O, [U-2H], 5%; DTT 2 mM; TRIS 20 mM; p53TAD-TAZ1 fusion protein, [U-15N] p53TAD - [NA] TAZ1, 1.0 mM; sodium chloride 50 mM; H2O, [U-2H], 95%

sample_2: D2O, [U-2H], 99%; DTT, [U-2H], 2 mM; TRIS, [U-2H], 20 mM; p53TAD-TAZ1 fusion protein, [U-15N][U-13C] p53TAD - [NA] TAZ1, 1.0 mM; sodium chloride 50 mM; H2O, [U-2H], 1%

sample_3: D2O, [U-2H], 5%; DTT 2 mM; TRIS 20 mM; p53TAD-TAZ1 fusion protein, [NA] p53TAD - [U-15N] TAZ1, 1.0 mM; sodium chloride 50 mM; H2O, [U-2H], 95%

sample_4: D2O, [U-2H], 99%; DTT, [U-2H], 2 mM; TRIS, [U-2H], 20 mM; p53TAD-TAZ1 fusion protein, [NA] p53TAD - [U-15N][U-13C] TAZ1, 1.0 mM; sodium chloride 50 mM; D2O, [U-2H], 1%

sample_5: D2O, [U-2H], 5%; DTT 2 mM; TRIS 20 mM; p53TAD-TAZ1 fusion protein, [U-15N][U-13C] p53TAD - [NA] TAZ1, 1.0 mM; sodium chloride 50 mM; H2O, [U-2H], 95%

sample_6: D2O, [U-2H], 5%; DTT 2 mM; TRIS 20 mM; p53TAD-TAZ1 fusion protein, [NA] p53TAD - [U-15N][U-13C] TAZ1, 1 mM; sodium chloride 50 mM; H2O, [U-2H], 95%

sample_conditions_1: ionic strength: 50 mM; pH: 6.8; pressure: 1 atm; temperature: 308 K

sample_conditions_2: ionic strength: 50 mM; pH: 6.4 pD; pressure: 1 atm; temperature: 308 K

Experiments:

NameSampleSample stateSample conditions
3D 1H-15N NOESYsample_1isotropicsample_conditions_1
3D 1H-13C NOESYsample_2isotropicsample_conditions_2
3D 1H-15N NOESYsample_3isotropicsample_conditions_1
3D 1H-13C NOESYsample_4isotropicsample_conditions_2
3D HNCACBsample_5isotropicsample_conditions_1
3D HN(CO)CAsample_5isotropicsample_conditions_1
3D HNCACBsample_6isotropicsample_conditions_1
3D HN(CO)CAsample_6isotropicsample_conditions_1
3D HCCH-TOCSYsample_5isotropicsample_conditions_2
3D HCCH-TOCSYsample_6isotropicsample_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 v5.0.04, Johnson, One Moon Scientific - chemical shift assignment

PSVS v1.5, Bhattacharya and Montelione - data analysis

NMR spectrometers:

  • Bruker DRX 800 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