BMRB Entry 25484

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PDB ID:
Entry in NMR Restraints Grid
Validation report in NRG-CING
Chem Shift validation: AVS_full, SPARTA
BMRB Entry DOI: doi:10.13018/BMR25484
MolProbity Validation Chart

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Title:
Characterization of the p300 Taz2-p53 TAD2 Complex and Comparison with the p300 Taz2-p53 TAD1 Complex
Deposition date:
2015-02-11
Original release date:
2015-03-23
Authors:
Miller Jenkins, Lisa; Feng, Hanqiao; Durell, Stewart; Tagad, Harichandra; Mazur, Sharlyn; Tropea, Joseph; Bai, Yawen; Appella, Ettore
Citation:

Citation: Miller Jenkins, Lisa; Feng, Hanqiao; Durell, Stewart; Tagad, Harichandra; Mazur, Sharlyn; Tropea, Joseph; Bai, Yawen; Appella, Ettore. "Characterization of the p300 Taz2-p53 TAD2 Complex and Comparison with the p300 Taz2-p53 TAD1 Complex"  Biochemistry 54, 2001-2010 (2015).
PubMed: 25753752

Assembly members:

Assembly members:
Taz2_domain_of_Histone_Acetyltransferase_p300, polymer, 90 residues, 9963.838 Da.
TAD2_sub-domain_of_Cellular_Tumor_Antigen_p53, polymer, 25 residues, 2851.098 Da.

Natural source:

Natural source:   Common Name: not available   Taxonomy ID: not available   Superkingdom: not available   Kingdom: not available   Genus/species: Homo sapiens

Experimental source:

Experimental source:   Production method: recombinant technology   Host organism: Escherichia coli   Vector: pJT57

Entity Sequences (FASTA):

Entity Sequences (FASTA):
Taz2_domain_of_Histone_Acetyltransferase_p300: ATQSPGDSRRLSIQRAIQSL VHAAQCRNANCSLPSCQKMK RVVQHTKGCKRKTNGGCPIC KQLIALAAYHAKHCQENKCP VPFCLNIKQK
TAD2_sub-domain_of_Cellular_Tumor_Antigen_p53: LPSQAMDDLMLSPDDIEQWF TEDPG

Data sets:
Data typeCount
13C chemical shifts442
15N chemical shifts99
1H chemical shifts729

Additional metadata:

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

Assembly:

Entity Assembly IDEntity NameEntity ID
1entity_11
2entity_22

Entities:

Entity 1, entity_1 90 residues - 9963.838 Da.

1   ALATHRGLNSERPROGLYASPSERARGARG
2   LEUSERILEGLNARGALAILEGLNSERLEU
3   VALHISALAALAGLNCYSARGASNALAASN
4   CYSSERLEUPROSERCYSGLNLYSMETLYS
5   ARGVALVALGLNHISTHRLYSGLYCYSLYS
6   ARGLYSTHRASNGLYGLYCYSPROILECYS
7   LYSGLNLEUILEALALEUALAALATYRHIS
8   ALALYSHISCYSGLNGLUASNLYSCYSPRO
9   VALPROPHECYSLEUASNILELYSGLNLYS

Entity 2, entity_2 25 residues - 2851.098 Da.

1   LEUPROSERGLNALAMETASPASPLEUMET
2   LEUSERPROASPASPILEGLUGLNTRPPHE
3   THRGLUASPPROGLY

Samples:

sample_1: Taz2 domain of Histone Acetyltransferase p300 1.1 mM; TAD2 sub-domain of Cellular Tumor Antigen p53, [U-100% 13C; U-100% 15N], 1.0 mM

sample_2: Taz2 domain of Histone Acetyltransferase p300, [U-100% 15N], 1.0 mM; TAD2 sub-domain of Cellular Tumor Antigen p53 1.1 mM

sample_3: Taz2 domain of Histone Acetyltransferase p300, [U-100% 13C; U-100% 15N], 1.0 mM; TAD2 sub-domain of Cellular Tumor Antigen p53 1.1 mM

sample_4: Taz2 domain of Histone Acetyltransferase p300 1.0 mM; TAD2 sub-domain of Cellular Tumor Antigen p53 1.1 mM

sample_conditions_1: ionic strength: 200 mM; pH: 6.3; pressure: 1 atm; temperature: 273 K

Experiments:

NameSampleSample stateSample conditions
2D 1H-15N HSQCsample_2isotropicsample_conditions_1
2D 1H-1H NOESYsample_4isotropicsample_conditions_1
3D CBCA(CO)NHsample_3isotropicsample_conditions_1
3D HNCACBsample_3isotropicsample_conditions_1
3D HNCOsample_3isotropicsample_conditions_1
3D HN(CA)COsample_3isotropicsample_conditions_1
3D HNCAsample_3isotropicsample_conditions_1
3D H(CCO)NHsample_3isotropicsample_conditions_1
3D HCCH-TOCSYsample_3isotropicsample_conditions_1
3D HNHAsample_2isotropicsample_conditions_1
3D 1H-15N NOESYsample_2isotropicsample_conditions_1
3D 1H-13C NOESYsample_3isotropicsample_conditions_1
2D 1H-15N HSQCsample_1isotropicsample_conditions_1
3D CBCA(CO)NHsample_1isotropicsample_conditions_1
3D HNCACBsample_1isotropicsample_conditions_1
3D HNCAsample_1isotropicsample_conditions_1
3D HNCOsample_1isotropicsample_conditions_1
3D HN(CA)COsample_1isotropicsample_conditions_1
3D H(CCO)NHsample_1isotropicsample_conditions_1
3D HCCH-TOCSYsample_1isotropicsample_conditions_1
3D 1H-15N NOESYsample_1isotropicsample_conditions_1
3D 1H-13C NOESYsample_1isotropicsample_conditions_1
3D HBHA(CO)NHsample_3isotropicsample_conditions_1
3D HBHA(CO)NHsample_1isotropicsample_conditions_1

Software:

NMRPipe, Delaglio, Grzesiek, Vuister, Zhu, Pfeifer and Bax - data analysis

NMRDraw, Delaglio, Grzesiek, Vuister, Zhu, Pfeifer and Bax - processing

NMRView, Johnson, One Moon Scientific - chemical shift assignment

TALOS, Cornilescu, Delaglio and Bax - structure solution

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

ProcheckNMR, Laskowski and MacArthur - refinement

NMR spectrometers:

  • Bruker Avance 500 MHz
  • Bruker DRX 700 MHz

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