BMRB

Biological Magnetic Resonance Data Bank


A Repository for Data from NMR Spectroscopy on Proteins, Peptides, Nucleic Acids, and other Biomolecules
Member of WWPDB

BMRB Entry 17640

Title: EL222(14-222)   PubMed: 21606338

Deposition date: 2011-05-12 Original release date: 2012-06-04

Authors: Nash, Abigail; McNulty, Reginald; Shillito, Mary; Swartz, Trevor; Bogomolni, Roberto; Luecke, Hartmut; Gardner, Kevin

Citation: Nash, Abigail; McNulty, Reginald; Shillito, Mary Elizabeth; Swartz, Trevor; Bogomolni, Roberto; Luecke, Hartmut; Gardner, Kevin. "Structural basis of photosensitivity in a bacterial light-oxygen-voltage/helix-turn-helix (LOV-HTH) DNA-binding protein."  Proc. Natl. Acad. Sci. U.S.A. 108, 9449-9454 (2011).

Assembly members:
EL222(14-222), polymer, 212 residues, Formula weight is not available
FMN, non-polymer, 456.344 Da.

Natural source:   Common Name: Erythrobacter litoralis   Taxonomy ID: 314225   Superkingdom: Bacteria   Kingdom: not available   Genus/species: Erythrobacter litoralis

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

Entity Sequences (FASTA):
EL222(14-222): GEFGADDTRVEVQPPAQWVL DLIEASPIASVVSDPRLADN PLIAINQAFTDLTGYSEEEC VGRNCRFLAGSGTEPWLTDK IRQGVREHKPVLVEILNYKK DGTPFRNAVLVAPIYDDDDE LLYFLGSQVEVDDDQPNMGM ARRERAAEMLKTLSPRQLEV TTLVASGLRNKEVAARLGLS EKTVKMHRGLVMEKLNLKTS ADLVRIAVEAGI

Data sets:
Data typeCount
13C chemical shifts437
15N chemical shifts167
1H chemical shifts655

Additional metadata:

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

Assembly:

Entity Assembly IDEntity NameEntity ID
1EL222(14-222) protein1
2FMN2

Entities:

Entity 1, EL222(14-222) protein 212 residues - Formula weight is not available

EL222 = Erythrobactor litoralis HTCC2594 protein, 222aa total. GB incorrectly annotated to function and start Met aa. first three residues (GEF) are vector-derived; remainder of sequence are residues 14-222 of protein

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(14-222), [U-100% 13C; U-100% 15N], 0.1-1 mM; H20 90%; D20 10%

sample_2: EL222(14-222), [U-100% 13C; U-100% 15N], 0.1-1 mM; H20 90%; D20 10%

sample_conditions_1: ionic strength: 0.15 M; pH: 6; pressure: 1 atm; temperature: 298 K

Experiments:

NameSampleSample stateSample conditions
2D 1H-15N HSQCsample_1isotropicsample_conditions_1
3D 1H-15N NOESYsample_1isotropicsample_conditions_1
3D 1H-13C NOESY aliphaticsample_1isotropicsample_conditions_1
3D 1H-13C NOESY aromaticsample_1isotropicsample_conditions_1
2D 1H-13C HSQCsample_1isotropicsample_conditions_1
3D H(CCO)NHsample_1isotropicsample_conditions_1
3D HNCOsample_2isotropicsample_conditions_1
3D HNCAsample_2isotropicsample_conditions_1
3D HN(CO)CAsample_2isotropicsample_conditions_1
3D HNCACBsample_2isotropicsample_conditions_1
3D HN(COCA)CBsample_2isotropicsample_conditions_1

Software:

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

NMRView, Johnson, One Moon Scientific - chemical shift assignment, peak picking

NMR spectrometers:

  • Varian INOVA 800 MHz
  • Varian INOVA 600 MHz

Related Database Links:

PDB
GB ABC63043
REF WP_041685679

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