BMRB Entry 27427

Chem Shift validation: AVS_full
BMRB Entry DOI: doi:10.13018/BMR27427

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Title:
Methyl assignment of human eukaryotic translation initiation factor 4E (eIF4E) in its apo form
Deposition date:
2018-03-18
Original release date:
2022-05-10
Authors:
Volpon, Laurent; Osborne, Michael; Borden, Katherine
Citation:

Citation: Osborne, Michael; Volpon, Laurent; Memarpoor-Yazdi, Mina; Pillay, Shubhadra; Thambipillai, Aksharh; Czarnota, Sylwia; Culjkovic-Kraljacic, Biljana; Trahan, Christian; Oeffinger, Marlene; Cowling, Victoria; Borden, Katherine. "Identification and Characterization of the Interaction Between the Methyl-7-Guanosine Cap Maturation Enzyme RNMT and the Cap-Binding Protein eIF4E"  J. Mol. Biol. 434, 167451-167451 (2022).
PubMed: 35026230

Assembly members:

Assembly members:
eIF4E, polymer, 217 residues, 25097.25 Da.

Natural source:

Natural source:   Common Name: Human   Taxonomy ID: 9606   Superkingdom: Eukaryota   Kingdom: Metazoa   Genus/species: Homo sapiens

Experimental source:

Experimental source:   Production method: recombinant technology   Host organism: Escherichia coli   Vector: pET28a

Entity Sequences (FASTA):

Entity Sequences (FASTA):
eIF4E: MATVEPETTPTPNPPTTEEE KTESNQEVANPEHYIKHPLQ NRWALWFFKNDKSKTWQANL RLISKFDTVEDFWALYNHIQ LSSNLMPGCDYSLFKDGIEP MWEDEKNKRGGRWLITLNKQ QRRSDLDRFWLETLLCLIGE SFDDYSDDVCGAVVNVRAKG DKIAIWTTECENREAVTHIG RVYKERLGLPPKIVIGYQSH ADTATKSGSTTKNRFVV

Data sets:
Data typeCount
13C chemical shifts171
15N chemical shifts207
1H chemical shifts411

Additional metadata:

  • Assembly
  • Samples and Experiments
  • Software
  • Spectrometers
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Assembly:

Entity Assembly IDEntity NameEntity ID
1monomer eIF4E1

Entities:

Entity 1, monomer eIF4E 217 residues - 25097.25 Da.

1   METALATHRVALGLUPROGLUTHRTHRPRO
2   THRPROASNPROPROTHRTHRGLUGLUGLU
3   LYSTHRGLUSERASNGLNGLUVALALAASN
4   PROGLUHISTYRILELYSHISPROLEUGLN
5   ASNARGTRPALALEUTRPPHEPHELYSASN
6   ASPLYSSERLYSTHRTRPGLNALAASNLEU
7   ARGLEUILESERLYSPHEASPTHRVALGLU
8   ASPPHETRPALALEUTYRASNHISILEGLN
9   LEUSERSERASNLEUMETPROGLYCYSASP
10   TYRSERLEUPHELYSASPGLYILEGLUPRO
11   METTRPGLUASPGLULYSASNLYSARGGLY
12   GLYARGTRPLEUILETHRLEUASNLYSGLN
13   GLNARGARGSERASPLEUASPARGPHETRP
14   LEUGLUTHRLEULEUCYSLEUILEGLYGLU
15   SERPHEASPASPTYRSERASPASPVALCYS
16   GLYALAVALVALASNVALARGALALYSGLY
17   ASPLYSILEALAILETRPTHRTHRGLUCYS
18   GLUASNARGGLUALAVALTHRHISILEGLY
19   ARGVALTYRLYSGLUARGLEUGLYLEUPRO
20   PROLYSILEVALILEGLYTYRGLNSERHIS
21   ALAASPTHRALATHRLYSSERGLYSERTHR
22   THRLYSASNARGPHEVALVAL

Samples:

sample_1: eIF4E, [U-13C; U-15N; U-2H with 1H for Ile, Leu and Val Methyls], 220 uM; sodium phosphate 50 mM; sodium chloride 100 mM; DTT 1 mM; sodium azide 0.02%

sample_2: eIF4E, [U-13C; U-15N; U-2H with 1H for Ile, Leu and Val Methyls], 220 uM; sodium phosphate 50 mM; sodium chloride 100 mM; DTT 1 mM; sodium azide 0.02%

sample_conditions_1: pH: 7.2; pressure: 1 atm; temperature: 273 K

Experiments:

NameSampleSample stateSample conditions
2D 1H-15N HSQCsample_1isotropicsample_conditions_1
2D 1H-13C HSQC aliphaticsample_2isotropicsample_conditions_1
(H)C-TOCSY-S-TOCSY-(C)Hsample_2isotropicsample_conditions_1

Software:

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

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

TOPSPIN, Bruker Biospin - collection

SPARKY, Goddard - data analysis

NMR spectrometers:

  • Bruker Avance 600 MHz

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