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Biological Magnetic Resonance Data Bank


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BMRB Entry 34231

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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/BMR34231
MolProbity Validation Chart

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Title: Solution Structure of p300Taz2-p63TA

Deposition date: 2018-01-11 Original release date: 2018-05-24

Authors: Gebel, J.; Kazemi, S.; Lohr, F.; Guntert, P.; Dotsch, V.

Citation: Krauskopf, K.; Gebel, J.; Kazemi, S.; Tuppi, M.; Lohr, F.; Schafer, B.; Koch, J.; Guntert, P.; Dotsch, V.; Kehrloesser, S.. "The regulation of the transcriptional activity in the p53 protein family depends on the organization of the transactivation domain"  Structure ., .-. (2018).

Assembly members:
entity_1, polymer, 124 residues, 13834.022 Da.
entity_ZN, non-polymer, 65.409 Da.

Natural source:   Common Name: Human   Taxonomy ID: 9606   Superkingdom: Eukaryota   Kingdom: Metazoa   Genus/species: Homo sapiens

Experimental source:   Production method: recombinant technology   Host organism: Escherichia coli BL21(DE3)

Entity Sequences (FASTA):
entity_1: ATQSPGDSRRLSIQRAIQSL VHAAQCRNANCSLPSCQKMK RVVQHTKGCKRKTNGGCPIC KQLIALAAYHAKHCQENKCP VPFCLNIKQKGTIEGRGNEF LSPEVFQHIWDFLEQPISSV QPID

Data sets:
Data typeCount
13C chemical shifts528
15N chemical shifts126
1H chemical shifts817

Additional metadata:

  • Assembly
  • Samples and Experiments
  • Software
  • Spectrometers
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Assembly:

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

Entities:

Entity 1, entity_1 124 residues - 13834.022 Da.

1   ALATHRGLNSERPROGLYASPSERARGARG
2   LEUSERILEGLNARGALAILEGLNSERLEU
3   VALHISALAALAGLNCYSARGASNALAASN
4   CYSSERLEUPROSERCYSGLNLYSMETLYS
5   ARGVALVALGLNHISTHRLYSGLYCYSLYS
6   ARGLYSTHRASNGLYGLYCYSPROILECYS
7   LYSGLNLEUILEALALEUALAALATYRHIS
8   ALALYSHISCYSGLNGLUASNLYSCYSPRO
9   VALPROPHECYSLEUASNILELYSGLNLYS
10   GLYTHRILEGLUGLYARGGLYASNGLUPHE
11   LEUSERPROGLUVALPHEGLNHISILETRP
12   ASPPHELEUGLUGLNPROILESERSERVAL
13   GLNPROILEASP

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

1   ZN

Samples:

sample_1: Fusion construct of p300 Taz2 and the transactivation domain of p63, [U-13C; U-15N], 1200 uM; MES 25 mM; NaCl 200 mM; TCEP 0.5 mM

sample_conditions_1: ionic strength: 200 mM; pH: 6.3; pressure: 1 mbar; temperature: 303 K

Experiments:

NameSampleSample stateSample conditions
3D 1H-13C NOESY aliphaticsample_1isotropicsample_conditions_1
3D 1H-13C NOESY aromaticsample_1isotropicsample_conditions_1
3D 1H-15N NOESYsample_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 HNCACBsample_1isotropicsample_conditions_1
3D HN(COCA)CBsample_1isotropicsample_conditions_1
3D HNCOsample_1isotropicsample_conditions_1
3D H(CCO)NH TOCSYsample_1isotropicsample_conditions_1
3D C(CO)NH TOCSYsample_1isotropicsample_conditions_1

Software:

OPAL, Luginbuhl, Guntert, Billeter and Wuthrich - refinement

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

Sparky v3.13, T. D. Goddard and D. G. Kneller, SPARKY 3, University of California, San Francisco - chemical shift assignment

NMR spectrometers:

  • Bruker Avance III 600 MHz
  • Bruker Avance III HD 700 MHz
  • Bruker Avance III HD 800 MHz
  • Bruker Avance 900 MHz

Download simulated HSQC data in one of the following formats:
CSV: Backbone or all simulated shifts
SPARKY: Backbone or all simulated shifts