BMRB Entry 34233

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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/BMR34233
MolProbity Validation Chart

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NMR-STAR v3 text file.
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Title:
Solution structure of p300Taz2-p73TA1
Deposition date:
2018-01-11
Original release date:
2018-05-24
Authors:
Gebel, J.; Kazemi, S.; Lohr, F.; Guntert, P.; Dotsch, V.
Citation:

Citation: Krauskopf, K.; Gebel, J.; Kazemi, S.; Tuppi, M.; Lohr, F.; Schafer, B.; Koch, J.; Guntert, P.; Dotsch, V.; Kehrloesser, S.. "Regulation of the Activity in the p53 Family Depends on the Organization of the Transactivation Domain"  Structure 26, 1091-1110 (2018).
PubMed: 30099987

Assembly members:

Assembly members:
entity_1, polymer, 130 residues, 13867.793 Da.
entity_ZN, 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 BL21(DE3)

Entity Sequences (FASTA):

Entity Sequences (FASTA):
entity_1: ATQSPGDSRRLSIQRAIQSL VHAAQCRNANCSLPSCQKMK RVVQHTKGCKRKTNGGCPIC KQLIALAAYHAKHCQENKCP VPFCLNIKQKGGSGGGTGGG SGTIEGRGDGGTTFEHLWSS LEPDSTYFDL

Data sets:
Data typeCount
13C chemical shifts402
15N chemical shifts129
1H chemical shifts749

Additional metadata:

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

Assembly:

Entity Assembly IDEntity NameEntity ID
1entity_11
2entity_2, 12
3entity_2, 22
4entity_2, 32

Entities:

Entity 1, entity_1 130 residues - 13867.793 Da.

1   ALATHRGLNSERPROGLYASPSERARGARG
2   LEUSERILEGLNARGALAILEGLNSERLEU
3   VALHISALAALAGLNCYSARGASNALAASN
4   CYSSERLEUPROSERCYSGLNLYSMETLYS
5   ARGVALVALGLNHISTHRLYSGLYCYSLYS
6   ARGLYSTHRASNGLYGLYCYSPROILECYS
7   LYSGLNLEUILEALALEUALAALATYRHIS
8   ALALYSHISCYSGLNGLUASNLYSCYSPRO
9   VALPROPHECYSLEUASNILELYSGLNLYS
10   GLYGLYSERGLYGLYGLYTHRGLYGLYGLY
11   SERGLYTHRILEGLUGLYARGGLYASPGLY
12   GLYTHRTHRPHEGLUHISLEUTRPSERSER
13   LEUGLUPROASPSERTHRTYRPHEASPLEU

Entity 2, entity_2, 1 - Zn - 65.409 Da.

1   ZN

Samples:

sample_1: Fusion construct of p300 Taz2 and the transactivation domain 1 of p73, [U-13C; U-15N], 700 uM; MES 25 mM; NaCl 50 mM; TCEP 0.5 mM

sample_conditions_1: ionic strength: 50 mM; pH: 6.3; pressure: 1 mbar; temperature: 303 K

Experiments:

NameSampleSample stateSample conditions
3D 1H-15N NOESYsample_1isotropicsample_conditions_1
3D 1H-13C NOESY aliphaticsample_1isotropicsample_conditions_1
3D 1H-13C NOESY aromaticsample_1isotropicsample_conditions_1
3D HNCACBsample_1isotropicsample_conditions_1
3D HN(COCA)CBsample_1isotropicsample_conditions_1
[13Cmethyl,1H]-SOFAST-HMQC-NOESY-[13Carom,1H]-HMQCsample_1isotropicsample_conditions_1
2D 1H-13C HSQC aromaticsample_1isotropicsample_conditions_1
2D 1H-13C HSQC aliphaticsample_1isotropicsample_conditions_1
2D 1H-15N HSQCsample_1isotropicsample_conditions_1
3D C(CO)NHsample_1isotropicsample_conditions_1
3D H(CCO)NHsample_1isotropicsample_conditions_1

Software:

SPARKY v3.114, T. D. Goddard and D. G. Kneller - chemical shift assignment

CYANA v3.9, Guntert, Mumenthaler and Wuthrich - structure calculation

OPAL, Luginbuhl, Guntert, Billeter and Wuthrich - refinement

NMR spectrometers:

  • Bruker AVNCE III 600 MHz
  • Bruker AVANCE III HD 700 MHz
  • Bruker AVANCE II 950 MHz
  • Bruker AVANCE III HD 800 MHz

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