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Biological Magnetic Resonance Data Bank


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BMRB Entry 17741

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PDB ID:
Entry in NMR Restraints Grid
Validation report in NRG-CING
Chem Shift validation: AVS_full, LACS, SPARTA
BMRB Entry DOI: doi:10.13018/BMR17741
MolProbity Validation Chart

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Title: Q436   PubMed: 22584210

Deposition date: 2011-06-28 Original release date: 2012-05-21

Authors: Coyne, Harold; Green, Sean; Graves, Barbara; McIntosh, Lawrence

Citation: Coyne, H. Jerome; De, Soumya; Okon, Mark; Green, Sean; Bhachech, Niraja; Graves, Barbara; McIntosh, Lawrence. "Autoinhibition of ETV6 (TEL) DNA Binding: Appended Helices Sterically Block the ETS Domain."  J. Mol. Biol. 421, 67-84 (2012).

Assembly members:
entity, polymer, 106 residues, 13061.089 Da.

Natural source:   Common Name: 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):
entity: GSHMRLLWDYVYQLLSDSRY ENFIRWEDKESKIFRIVDPN GLARLWGNHKNRTNMTYEKM SRALRHYYKLNIIRKEPGQR LLFRFMKTPDEIMSGRTDRL EHLESQ

Data sets:
Data typeCount
13C chemical shifts497
15N chemical shifts112
1H chemical shifts778

Additional metadata:

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

Assembly:

Entity Assembly IDEntity NameEntity ID
1ETV6 Q4361

Entities:

Entity 1, ETV6 Q436 106 residues - 13061.089 Da.

GSHM appended to the N-terminus of Q436

1   GLYSERHISMETARGLEULEUTRPASPTYR
2   VALTYRGLNLEULEUSERASPSERARGTYR
3   GLUASNPHEILEARGTRPGLUASPLYSGLU
4   SERLYSILEPHEARGILEVALASPPROASN
5   GLYLEUALAARGLEUTRPGLYASNHISLYS
6   ASNARGTHRASNMETTHRTYRGLULYSMET
7   SERARGALALEUARGHISTYRTYRLYSLEU
8   ASNILEILEARGLYSGLUPROGLYGLNARG
9   LEULEUPHEARGPHEMETLYSTHRPROASP
10   GLUILEMETSERGLYARGTHRASPARGLEU
11   GLUHISLEUGLUSERGLN

Samples:

sample_1: sodium phosphate 50 mM; sodium chloride 200 mM; ETV6_Q436, [U-99% 13C; U-99% 15N], 0.6 mM; H2O 90%; D2O 10%

sample_conditions_1: ionic strength: 0.250 M; pH: 5.8; pressure: 1 atm; temperature: 303 K

Experiments:

NameSampleSample stateSample conditions
2D 1H-15N HSQCsample_1isotropicsample_conditions_1
3D 1H-13C NOESYsample_1isotropicsample_conditions_1
2D 1H-13C HSQC aromaticsample_1isotropicsample_conditions_1
3D CBCA(CO)NHsample_1isotropicsample_conditions_1
3D HNCACBsample_1isotropicsample_conditions_1
3D HCCH-TOCSYsample_1isotropicsample_conditions_1
3D HN(CO)CAsample_1isotropicsample_conditions_1
3D HNCOsample_1isotropicsample_conditions_1
3D HBHA(CO)NHsample_1isotropicsample_conditions_1
3D 1H-13C NOESYsample_1isotropicsample_conditions_1
dipsi3dnsample_1isotropicsample_conditions_1
Cmethyl NOESYsample_1isotropicsample_conditions_1
Nmethyl NOESYsample_1isotropicsample_conditions_1
ccctocsynnhsample_1isotropicsample_conditions_1
2D 1H-15N HSQCsample_1isotropicsample_conditions_1
2D 1H-13C HSQC aliphaticsample_1isotropicsample_conditions_1

Software:

ARIA v2.3, Linge, O, . - structure solution

TALOS+, Cornilescu, Delaglio and Bax - geometry optimization

SPARKY, Goddard - data analysis

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

NMR spectrometers:

  • Varian INOVA 600 MHz
  • Varian Unity 500 MHz

Related Database Links:

BMRB 17742
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