BMRB Entry 28121

Chem Shift validation: AVS_full
BMRB Entry DOI: doi:10.13018/BMR28121

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Title:
Assignment of first 249 residues of yeast eIF4G1
Deposition date:
2020-05-15
Original release date:
2022-10-27
Authors:
Chaves-Arquero, Belen; Martinez-Lumbreras, Santiago; Perez-Canadillas, Jose Manuel
Citation:

Citation: Chaves-Arquero, Belen; Martinez-Lumbreras, Santiago; Sibille, Nathalie; Camero, Sergio; Bernado, Pau; Jimenez, Maria Angeles; Zorrilla, Silvia; Perez-Canadillas, Jose Manuel. "eIF4G1 N-terminal intrinsically disordered domain is a multi-docking station for RNA, Pab1, Pub1, and self-assembly"  Front. Mol. Biosci. 9, 986121-986121 (2022).
PubMed: 36213119

Assembly members:

Assembly members:
eIF4G1, polymer, 249 residues, Formula weight is not available

Natural source:

Natural source:   Common Name: baker's yeast   Taxonomy ID: 4932   Superkingdom: Eukaryota   Kingdom: Fungi   Genus/species: Saccharomyces cerevisiae

Experimental source:

Experimental source:   Production method: recombinant technology   Host organism: Escherichia coli   Vector: pET28

Entity Sequences (FASTA):

Entity Sequences (FASTA):
eIF4G1: MTDETAHPTQSASKQESAAL KQTGDDQQESQQQRGYTNYN NGSNYTQKKPYNSNRPHQQR GGKFGPNRYNNRGNYNGGGS FRGGHMGANSSNVPWTGYYN NYPVYYQPQQMAAAGSAPAN PIPVEEKSPVPTKIEITTKS GEHLDLKEQHKAKLQSQERS TVSPQPESKLKETSDSTSTS TPTPTPSTNDSKASSEENIS EAEKTRRNFIEQVKLRKAAL EKKRKEQLEGSSGNNNIPMK TTPENVEEK

Data sets:
Data typeCount
13C chemical shifts721
15N chemical shifts249
1H chemical shifts734

Additional metadata:

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

Assembly:

Entity Assembly IDEntity NameEntity ID
1eIF4G11

Entities:

Entity 1, eIF4G1 249 residues - Formula weight is not available

1   METTHRASPGLUTHRALAHISPROTHRGLN
2   SERALASERLYSGLNGLUSERALAALALEU
3   LYSGLNTHRGLYASPASPGLNGLNGLUSER
4   GLNGLNGLNARGGLYTYRTHRASNTYRASN
5   ASNGLYSERASNTYRTHRGLNLYSLYSPRO
6   TYRASNSERASNARGPROHISGLNGLNARG
7   GLYGLYLYSPHEGLYPROASNARGTYRASN
8   ASNARGGLYASNTYRASNGLYGLYGLYSER
9   PHEARGGLYGLYHISMETGLYALAASNSER
10   SERASNVALPROTRPTHRGLYTYRTYRASN
11   ASNTYRPROVALTYRTYRGLNPROGLNGLN
12   METALAALAALAGLYSERALAPROALAASN
13   PROILEPROVALGLUGLULYSSERPROVAL
14   PROTHRLYSILEGLUILETHRTHRLYSSER
15   GLYGLUHISLEUASPLEULYSGLUGLNHIS
16   LYSALALYSLEUGLNSERGLNGLUARGSER
17   THRVALSERPROGLNPROGLUSERLYSLEU
18   LYSGLUTHRSERASPSERTHRSERTHRSER
19   THRPROTHRPROTHRPROSERTHRASNASP
20   SERLYSALASERSERGLUGLUASNILESER
21   GLUALAGLULYSTHRARGARGASNPHEILE
22   GLUGLNVALLYSLEUARGLYSALAALALEU
23   GLULYSLYSARGLYSGLUGLNLEUGLUGLY
24   SERSERGLYASNASNASNILEPROMETLYS
25   THRTHRPROGLUASNVALGLUGLULYS

Samples:

sample_1: eIF4G1, [U-100% 13C; U-100% 15N], 200 uM; potassium phosphate 25 mM; sodium chloride 25 mM; DTT 0.1 mM

sample_conditions_1: ionic strength: 0.05 M; pH: 6.5; pressure: 1 atm; temperature: 301.2 K

Experiments:

NameSampleSample stateSample conditions
2D 1H-15N HSQCsample_1isotropicsample_conditions_1
2D 1H-13C HSQC aliphaticsample_1isotropicsample_conditions_1
3D HNCOsample_1isotropicsample_conditions_1
3D HNCAsample_1isotropicsample_conditions_1
3D HN(CO)CAsample_1isotropicsample_conditions_1
3D HNCACBsample_1isotropicsample_conditions_1
3D CBCA(CO)NHsample_1isotropicsample_conditions_1
3D HCCH-TOCSYsample_1isotropicsample_conditions_1

Software:

TOPSPIN, Bruker Biospin - collection, processing

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

CCPNanalysis, CCPN - chemical shift assignment

NMR spectrometers:

  • Bruker Avance 800 MHz

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