BMRB

Biological Magnetic Resonance Data Bank


A Repository for Data from NMR Spectroscopy on Proteins, Peptides, Nucleic Acids, and other Biomolecules
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BMRB Entry 19474

Title: Structure of uninhibited ETV6 ETS domain   PubMed: 24333486

Deposition date: 2013-08-29 Original release date: 2013-09-27

Authors: De, Soumya; McIntosh, Lawrence; Chan, Anson; Coyne, Harold; Okon, Mark; Graves, Barbara; Murphy, Michael

Citation: De, Soumya; Chan, Anson; Coyne, H. Jerome; Bhachech, Niraja; Hermsdorf, Ulrike; Okon, Mark; Murphy, Michael; Graves, Barbara; McIntosh, Lawrence. "Steric Mechanism of Auto-Inhibitory Regulation of Specific and Non-Specific DNA Binding by the ETS Transcriptional Repressor ETV6."  J. Mol. Biol. ., .-. (2013).

Assembly members:
u_ETV6_ETS, polymer, 102 residues, 12450.446 Da.

Natural source:   Common Name: house mouse   Taxonomy ID: 10090   Superkingdom: Eukaryota   Kingdom: Metazoa   Genus/species: Mus musculus

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

Entity Sequences (FASTA):
u_ETV6_ETS: GSHMGRIADSRLLWDYVYQL LSDSRYENFIRWEDKESKIF RIVDPNGLARLWGNHKNRTN MTYEKMSRALRHYYKLNIIR KEPGQRLLFRFMKTPDEIMS GR

Data sets:
Data typeCount
13C chemical shifts349
15N chemical shifts101
1H chemical shifts728

Additional metadata:

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

Assembly:

Entity Assembly IDEntity NameEntity ID
1uninhibited ETV6 ETS domain1

Entities:

Entity 1, uninhibited ETV6 ETS domain 102 residues - 12450.446 Da.

1   GLYSERHISMETGLYARGILEALAASPSER
2   ARGLEULEUTRPASPTYRVALTYRGLNLEU
3   LEUSERASPSERARGTYRGLUASNPHEILE
4   ARGTRPGLUASPLYSGLUSERLYSILEPHE
5   ARGILEVALASPPROASNGLYLEUALAARG
6   LEUTRPGLYASNHISLYSASNARGTHRASN
7   METTHRTYRGLULYSMETSERARGALALEU
8   ARGHISTYRTYRLYSLEUASNILEILEARG
9   LYSGLUPROGLYGLNARGLEULEUPHEARG
10   PHEMETLYSTHRPROASPGLUILEMETSER
11   GLYARG

Samples:

sample_1: uninhibited ETV6 ETS domain, [U-99% 13C; U-99% 15N], 0.6 mM; sodium phosphate 0.02 mM; sodium chloride 0.05 mM; H2O 93%; D2O 7%

sample_conditions_1: ionic strength: 0.11 M; pH: 6.5; pressure: 1 atm; temperature: 298 K

Experiments:

NameSampleSample stateSample conditions
2D 1H-15N HSQCsample_1isotropicsample_conditions_1
2D 1H-13C HSQC aliphaticsample_1isotropicsample_conditions_1
2D 1H-13C HSQC aromaticsample_1isotropicsample_conditions_1
3D H(CCO)NHsample_1isotropicsample_conditions_1
3D (H)CC(CO)NHsample_1isotropicsample_conditions_1
3D HCCH-TOCSYsample_1isotropicsample_conditions_1
3D HNCACBsample_1isotropicsample_conditions_1
3D 1H-15N NOESYsample_1isotropicsample_conditions_1
2D 1H-13C HSQC aliphaticsample_1isotropicsample_conditions_1
2D 1H-13C HSQC aromaticsample_1isotropicsample_conditions_1

Software:

TOPSPIN, Bruker Biospin - collection

SPARKY, Goddard - chemical shift assignment

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

CYANA, Guntert, Mumenthaler and Wuthrich - structure solution

CNS, Brunger, Adams, Clore, Gros, Nilges and Read - geometry optimization, refinement

NMR spectrometers:

  • Bruker Avance 850 MHz
  • Bruker Avance 600 MHz
  • Bruker Avance 500 MHz

Related Database Links:

PDB
DBJ BAC28991 BAC37386 BAE32681 BAE33079 BAE34018
EMBL CAA69220
GB AAA19786 AAB17135 AAC97200 AAH43399 AAH52163
REF NP_001015514 NP_001032430 NP_001186202 NP_001253009 NP_001290031
SP P41212 P97360 Q0VC65
TPG DAA29357

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