BMRB Entry 19138

Chem Shift validation: AVS_full, LACS
BMRB Entry DOI: doi:10.13018/BMR19138

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Title:
ERG DNA Complex
Deposition date:
2013-04-02
Original release date:
2013-08-15
Authors:
Regan, Michael
Citation:

Citation: Regan, Michael; Horanyi, Peter; Pryor, Edward; Sarver, Jessica; Cafiso, David; Bushweller, John. "Structural and dynamic studies of the transcription factor ERG reveal DNA binding is allosterically autoinhibited."  Proc. Natl. Acad. Sci. U.S.A. 110, 13374-13379 (2013).
PubMed: 23898196

Assembly members:

Assembly members:
EDComplex, polymer, 122 residues, Formula weight is not available
DNA_EDComplex_1, polymer, 16 residues, Formula weight is not available
DNA_EDComplex_2, polymer, 16 residues, Formula weight is not available

Natural source:

Natural source:   Common Name: not available   Taxonomy ID: not available   Superkingdom: not available   Kingdom: not available   Genus/species: not available not available

Experimental source:

Experimental source:   Production method: recombinant technology   Host organism: Escherichia coli   Vector: pHis-Parallel2

Entity Sequences (FASTA):

Entity Sequences (FASTA):
EDComplex: GAMAPQLDPYQILGPTSSRL ANPGSGQIQLWQFLLELLSD SSNSSCITWEGTNGEFKMTD PDEVARRWGERKSKPNMNYD KLSRALRYYYDKNIMTKVHG KRYAYKFDFHGIAQALQPHP PE
DNA_EDComplex_1: AGGACCGGAAGTAACT
DNA_EDComplex_2: AGTTACTTCCGGTCCT

Data sets:
Data typeCount
13C chemical shifts329
15N chemical shifts101
1H chemical shifts203

Additional metadata:

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

Assembly:

Entity Assembly IDEntity NameEntity ID
1EDComplex1
2DNA 5'- AGGACCGGAAGTAACT-32
3DNA 5'- AGTACTTCCGGTCCT-33

Entities:

Entity 1, EDComplex 122 residues - Formula weight is not available

1   GLYALAMETALAPROGLNLEUASPPROTYR
2   GLNILELEUGLYPROTHRSERSERARGLEU
3   ALAASNPROGLYSERGLYGLNILEGLNLEU
4   TRPGLNPHELEULEUGLULEULEUSERASP
5   SERSERASNSERSERCYSILETHRTRPGLU
6   GLYTHRASNGLYGLUPHELYSMETTHRASP
7   PROASPGLUVALALAARGARGTRPGLYGLU
8   ARGLYSSERLYSPROASNMETASNTYRASP
9   LYSLEUSERARGALALEUARGTYRTYRTYR
10   ASPLYSASNILEMETTHRLYSVALHISGLY
11   LYSARGTYRALATYRLYSPHEASPPHEHIS
12   GLYILEALAGLNALALEUGLNPROHISPRO
13   PROGLU

Entity 2, DNA 5'- AGGACCGGAAGTAACT-3 16 residues - Formula weight is not available

1   DADGDGDADCDCDGDGDADA
2   DGDTDADADCDT

Entity 3, DNA 5'- AGTACTTCCGGTCCT-3 16 residues - Formula weight is not available

1   DADGDTDTDADCDTDTDCDC
2   DGDGDTDCDCDT

Samples:

sample_1: EDComplex, [U-98% 13C; U-98% 15N], 0.5 mM; DNA_EDComplex_1; DNA_EDComplex_2; H2O 95%; D2O 5%; K3PO4 0.02 M; Dithithreitol 0.005 M; NaN3 0.01%

sample_conditions_1: ionic strength: 0.02 M; pH: 6.9; pressure: 1 atm; temperature: 303 K

Experiments:

NameSampleSample stateSample conditions
2D 1H-15N HSQCsample_1isotropicsample_conditions_1
2D 1H-13C HSQCsample_1isotropicsample_conditions_1
3D CBCA(CO)NHsample_1isotropicsample_conditions_1
3D HNCOsample_1isotropicsample_conditions_1
3D HNCACBsample_1isotropicsample_conditions_1
3D HNHAsample_1isotropicsample_conditions_1
3D HCACOsample_1isotropicsample_conditions_1

Software:

SPARKY, Goddard - chemical shift assignment

NMR spectrometers:

  • Bruker Avance 600 MHz

Related Database Links:

BMRB 19136 19137
PDB
DBJ BAB62744 BAB69948 BAB69949 BAB69950 BAC34461
EMBL CAA47389 CAA54404 CAA75077 CAA75078 CAB46566
GB AAA35811 AAA52398 AAB28525 AAB31417 AAB31419
REF NP_001008616 NP_001026079 NP_001079309 NP_001079310 NP_001084371
SP P11308 P41157 P81270 Q90837
TPG DAA32951
AlphaFold P11308 P41157 P81270 Q90837

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