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 19136

Title: ERG Ets Domain Backbone Chemical Shifts   PubMed: 23898196

Deposition date: 2013-04-02 Original release date: 2013-08-15

Authors: Regan, Michael

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).

Assembly members:
ERGu, polymer, 94 residues, Formula weight is not available

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

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

Entity Sequences (FASTA):
ERGu: GAMGPGSGQIQLWQFLLELL SDSSNSSCITWEGTNGEFKM TDPDEVARRWGERKSKPNMN YDKLSRALRYYYDKNIMTKV HGKRYAYKFDFHGI

Data sets:
Data typeCount
13C chemical shifts250
15N chemical shifts84
1H chemical shifts164

Additional metadata:

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

Assembly:

Entity Assembly IDEntity NameEntity ID
1ERGu1

Entities:

Entity 1, ERGu 94 residues - Formula weight is not available

1   GLYALAMETGLYPROGLYSERGLYGLNILE
2   GLNLEUTRPGLNPHELEULEUGLULEULEU
3   SERASPSERSERASNSERSERCYSILETHR
4   TRPGLUGLYTHRASNGLYGLUPHELYSMET
5   THRASPPROASPGLUVALALAARGARGTRP
6   GLYGLUARGLYSSERLYSPROASNMETASN
7   TYRASPLYSLEUSERARGALALEUARGTYR
8   TYRTYRASPLYSASNILEMETTHRLYSVAL
9   HISGLYLYSARGTYRALATYRLYSPHEASP
10   PHEHISGLYILE

Samples:

sample_1: ERGu, [U-98% 13C; U-98% 15N], 0.5 mM; H2O 95%; D2O 5%; MgSO4 0.2 M; KPI 0.02 M; DTT 0.005 M; NaN3 0.1%

sample_conditions_1: ionic strength: 0.2 M; pH: 6.0; 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 19137 19138
PDB
DBJ BAB62744 BAB69948 BAB69949 BAB69950 BAC29518
EMBL CAA42055 CAA47389 CAA47399 CAA54404 CAA75077
GB AAA35811 AAA35812 AAA52398 AAB28525 AAB31417
REF NP_001008616 NP_001017381 NP_001026079 NP_001039763 NP_001079309
SP P11308 P26323 P41157 P81270 Q01543
TPG DAA13871 DAA32951

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