BMRB Entry 30303

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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/BMR30303
MolProbity Validation Chart

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Title:
Solution Structure of ETS Transcription Factor PU.1
Deposition date:
2017-06-07
Original release date:
2018-06-07
Authors:
Lau, D.; Okon, M.; McIntosh, L.
Citation:

Citation: Perez-Borrajero, Cecilia; Lin, Chang Sheng-Huei; Okon, Mark; Scheu, Karlton; Graves, Barbara; Murphy, Michael; McIntosh, Lawrence. "The Biophysical Basis for Phosphorylation-Enhanced DNA-Binding Autoinhibition of the ETS1 Transcription Factor."  J. Mol. Biol. 431, 593-614 (2019).
PubMed: 30597162

Assembly members:

Assembly members:
Transcription factor PU.1, polymer, 110 residues, 12932.241 Da.

Natural source:

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

Experimental source:

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

Entity Sequences (FASTA):

Entity Sequences (FASTA):
Transcription factor PU.1: HIHMGSKKKIRLYQFLLDLL RSGDMKDSIWWVDKDKGTFQ FSSKHKEALAHRWGIQKGNR KKMTYQKMARALRNYGKTGE VKKVKKKLTYQFSGEVLGRG GLAERRLPPH

Data typeCount
13C chemical shifts464
15N chemical shifts113
1H chemical shifts665

Additional metadata:

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

Entity Assembly IDEntity NameEntity ID
1entity_11

Entities:

Entity 1, entity_1 110 residues - 12932.241 Da.

1   HISILEHISMETGLYSERLYSLYSLYSILE
2   ARGLEUTYRGLNPHELEULEUASPLEULEU
3   ARGSERGLYASPMETLYSASPSERILETRP
4   TRPVALASPLYSASPLYSGLYTHRPHEGLN
5   PHESERSERLYSHISLYSGLUALALEUALA
6   HISARGTRPGLYILEGLNLYSGLYASNARG
7   LYSLYSMETTHRTYRGLNLYSMETALAARG
8   ALALEUARGASNTYRGLYLYSTHRGLYGLU
9   VALLYSLYSVALLYSLYSLYSLEUTHRTYR
10   GLNPHESERGLYGLUVALLEUGLYARGGLY
11   GLYLEUALAGLUARGARGLEUPROPROHIS

Samples:

sample_1: DNA binding protein, [U-99% 13C; U-99% 15N], 0.3 mM; potassium chloride 150 mM

sample_conditions_1: ionic strength: 150 mM; pH: 5.5; pressure: 1 atm; temperature: 298 K

Experiments:

NameSampleSample stateSample conditions
2D 1H-15N HSQCsample_1isotropicsample_conditions_1
2D 1H-13C HSQCsample_1isotropicsample_conditions_1
2D 1H-13C HSQC aliphaticsample_1isotropicsample_conditions_1
2D 1H-13C HSQC aromaticsample_1isotropicsample_conditions_1
3D 1H-15N NOESYsample_1isotropicsample_conditions_1
3D 1H-13C NOESYsample_1isotropicsample_conditions_1
3D 1H-13C NOESY aliphaticsample_1isotropicsample_conditions_1
3D 1H-13C NOESY aromaticsample_1isotropicsample_conditions_1

Software:

CYANA, Guntert P. - refinement, structure calculation

NMRe, Ryu H, Lim G, Sung BH, Lee J. - refinement

SPARKY, Goddard - chemical shift assignment, peak picking

NMR spectrometers:

  • Bruker AvanceIII 850 MHz

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