BMRB Entry 52621

Chem Shift validation: AVS_full
BMRB Entry DOI: doi:10.13018/BMR52621

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Title:
Assignment of the transcription factor EL222 in the dark state
Deposition date:
2024-09-30
Original release date:
2026-02-03
Authors:
BRUTSCHER, Bernhard; FAVIER, Adrien
Citation:

Citation: Chaudhari, Aditya; FAVIER, Adrien; Aliakbartehrani, Zahra; Koval, Tomas; Andersson, Inger; Schneider, Bohdan; Dohnalek, Jan; Cerny, Jiri; Brutscher, Bernhard; Fuertes, Gustavo. "Light-dependent flavin redox and adduct states control the conformation and DNA-binding activity of the transcription factor EL222"  Nucleic Acids Res. 53, gkaf215-gkaf215 (2025).
PubMed: 40119733

Assembly members:

Assembly members:
entity_1, polymer, 212 residues, Formula weight is not available
entity_FMN, non-polymer, 456.344 Da.

Natural source:

Natural source:   Common Name: Erythrobacter litoralis   Taxonomy ID: 39960   Superkingdom: Bacteria   Kingdom: not available   Genus/species: Erythrobacter litoralis

Experimental source:

Experimental source:   Production method: recombinant technology   Host organism: Escherichia coli   Vector: BL21(DE3)

Entity Sequences (FASTA):

Entity Sequences (FASTA):
entity_1: GEFGADDTRVEVQPPAQWVL DLIEASPIASVVSDPRLADN PLIAINQAFTDLTGYSEEEC VGRNCRFLAGSGTEPWLTDK IRQGVREHKPVLVEILNYKK DGTPFRNAVLVAPIYDDDDE LLYFLGSQVEVDDDQPNMGM ARRERAAEMLKTLSPRQLEV TTLVASGLRNKEVAARLGLS EKTVKMHRGLVMEKLNLKTS ADLVRIAVEAGI

Data sets:
Data typeCount
13C chemical shifts354
15N chemical shifts174
1H chemical shifts174

Additional metadata:

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

Assembly:

Entity Assembly IDEntity NameEntity ID
1EL2221
2FMN2

Entities:

Entity 1, EL222 212 residues - Formula weight is not available

1   GLYGLUPHEGLYALAASPASPTHRARGVAL
2   GLUVALGLNPROPROALAGLNTRPVALLEU
3   ASPLEUILEGLUALASERPROILEALASER
4   VALVALSERASPPROARGLEUALAASPASN
5   PROLEUILEALAILEASNGLNALAPHETHR
6   ASPLEUTHRGLYTYRSERGLUGLUGLUCYS
7   VALGLYARGASNCYSARGPHELEUALAGLY
8   SERGLYTHRGLUPROTRPLEUTHRASPLYS
9   ILEARGGLNGLYVALARGGLUHISLYSPRO
10   VALLEUVALGLUILELEUASNTYRLYSLYS
11   ASPGLYTHRPROPHEARGASNALAVALLEU
12   VALALAPROILETYRASPASPASPASPGLU
13   LEULEUTYRPHELEUGLYSERGLNVALGLU
14   VALASPASPASPGLNPROASNMETGLYMET
15   ALAARGARGGLUARGALAALAGLUMETLEU
16   LYSTHRLEUSERPROARGGLNLEUGLUVAL
17   THRTHRLEUVALALASERGLYLEUARGASN
18   LYSGLUVALALAALAARGLEUGLYLEUSER
19   GLULYSTHRVALLYSMETHISARGGLYLEU
20   VALMETGLULYSLEUASNLEULYSTHRSER
21   ALAASPLEUVALARGILEALAVALGLUALA
22   GLYILE

Entity 2, FMN - C17 H21 N4 O9 P - 456.344 Da.

1   FMN

Samples:

sample_1: EL222, [U-100% 13C; U-100% 15N], 200 uM; FMN, [U-100% 13C; U-100% 15N], 200 uM; MES buffer 25 mM

sample_conditions_1: ionic strength: 50 mM; pH: 6.8; pressure: 1 atm; temperature: 298 K

Experiments:

NameSampleSample stateSample conditions
Best TROSYsample_1isotropicsample_conditions_1
DOSYsample_1isotropicsample_conditions_1
1D TRACTsample_1isotropicsample_conditions_1
BT HNCOsample_1isotropicsample_conditions_1
BT HNCAsample_1isotropicsample_conditions_1
BT HNCACBsample_1isotropicsample_conditions_1
BT HNCOCACBsample_1isotropicsample_conditions_1
BT HNCACOsample_1isotropicsample_conditions_1

Software:

TOPSPIN v3.5 - collection, processing

NMRlib v2.0 - collection

CcpNMR v2 - chemical shift assignment

NMR spectrometers:

  • Bruker AVANCE III 850 MHz

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