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 34517

Title: Structure of eIF4G1 (37-49) - PUB1 RRM3 chimera in solution

Deposition date: 2020-05-15 Original release date: 2021-05-21

Authors: Chaves-Arquero, B.; Martinez-Lumbreras, S.; Perez-Canadillas, J.

Citation: Chaves-Arquero, B.; Martinez-Lumbreras, S.; Sibille, N.; Camero, S.; Bernardo, P.; Jimenez, M.; Zorrilla, S.; Perez-Canadillas, J.. "Multivalent interactions between eIF4G1 IDR, Pub1 and Pab1 guide the formation of protein condensates"  .

Assembly members:
entity_1, polymer, 116 residues, 13031.693 Da.

Natural source:   Common Name: budding yeasts   Taxonomy ID: 559292   Superkingdom: Eukaryota   Kingdom: Fungi   Genus/species: Saccharomyces cerevisiae

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

Entity Sequences (FASTA):
entity_1: GSGYTNYNNGSNYTQKKQTI GLPPQVNPQAVDHIIRSAPP RVTTAYIGNIPHFATEADLI PLFQNFGFILDFKHYPEKGC CFIKYDTHEQAAVCIVALAN FPFQGRNLRTGWGKER

Data sets:
Data typeCount
13C chemical shifts351
15N chemical shifts127
1H chemical shifts754

Additional metadata:

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

Entity Assembly IDEntity NameEntity ID
1unit_11

Entities:

Entity 1, unit_1 116 residues - 13031.693 Da.

1   GLYSERGLYTYRTHRASNTYRASNASNGLY
2   SERASNTYRTHRGLNLYSLYSGLNTHRILE
3   GLYLEUPROPROGLNVALASNPROGLNALA
4   VALASPHISILEILEARGSERALAPROPRO
5   ARGVALTHRTHRALATYRILEGLYASNILE
6   PROHISPHEALATHRGLUALAASPLEUILE
7   PROLEUPHEGLNASNPHEGLYPHEILELEU
8   ASPPHELYSHISTYRPROGLULYSGLYCYS
9   CYSPHEILELYSTYRASPTHRHISGLUGLN
10   ALAALAVALCYSILEVALALALEUALAASN
11   PHEPROPHEGLNGLYARGASNLEUARGTHR
12   GLYTRPGLYLYSGLUARG

Samples:

sample_1: eIF4G1(37-49)/PUB1(RRM3) Chimera 250 uM; potassium phosphate 25 mM; sodium chloride 25 mM; DTT 0.1 mM

sample_2: eIF4G1(37-49)/PUB1(RRM3) Chimera 250 uM; potassium phosphate 25 mM; sodium chloride 25 mM; DTT 0.1 mM

sample_3: eIF4G1(37-49)/PUB1(RRM3) Chimera, [U-13C; U-15N], 148 uM; potassium phosphate 25 mM; sodium chloride 25 mM; DTT 0.1 mM

sample_conditions_1: ionic strength: 0.050 M; pH: 5.0; pressure: 1 atm; temperature: 301.2 K

sample_conditions_2: ionic strength: 0.050 M; pH: 5.0; pressure: 1 atm; temperature: 301.2 K

sample_conditions_3: ionic strength: 0.050 M; pH: 5.0; pressure: 1 atm; temperature: 301.2 K

Experiments:

NameSampleSample stateSample conditions
2D 1H-15N HSQCsample_3isotropicsample_conditions_3
2D 1H-13C HSQC aliphaticsample_3isotropicsample_conditions_3
3D HNCOsample_3isotropicsample_conditions_3
3D HNCAsample_3isotropicsample_conditions_3
3D CBCA(CO)NHsample_3isotropicsample_conditions_3
2D 1H-1H NOESYsample_1isotropicsample_conditions_1
2D 1H-1H NOESYsample_2isotropicsample_conditions_2
2D 1H-1H TOCSYsample_1isotropicsample_conditions_1
2D 1H-1H TOCSYsample_2isotropicsample_conditions_2

Software:

TopSpin, Bruker Biospin - collection, processing

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

CcpNmr Analysis, CCPN - chemical shift assignment

CYANA, Guntert, Mumenthaler and Wuthrich - structure calculation

Amber, Case, Darden, Cheatham III, Simmerling, Wang, Duke, Luo, ... and Kollman - refinement

NMR spectrometers:

  • Bruker AVANCE II 800 MHz

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