BMRB Entry 36034

Title:
NMR structure of eIF3 36-163
Deposition date:
2016-11-21
Original release date:
2017-05-30
Authors:
Nagata, T.; Obayashi, E.
Citation:

Citation: Obayashi, Eiji; Luna, Rafael; Nagata, Takashi; Martin-Marcos, Pilar; Hiraishi, Hiroyuki; Singh, Chingakham Ranjit; Erzberger, Jan Peter; Zhang, Fan; Arthanari, Haribabu; Morris, Jacob; Pellarin, Riccardo; Moore, Chelsea; Harmon, Ian; Papadopoulos, Evangelos; Yoshida, Hisashi; Nasr, Mahmoud; Unzai, Satoru; Thompson, Brytteny; Aube, Eric; Hustak, Samantha; Stengel, Florian; Dagraca, Eddie; Ananbandam, Asokan; Gao, Philip; Urano, Takeshi; Hinnebusch, Alan; Wagner, Gerhard; Asano, Katsura. "Molecular Landscape of the Ribosome Pre-initiation Complex during mRNA Scanning: Structural Role for eIF3c and Its Control by eIF5"  Cell Rep. 18, 2651-2663 (2017).
PubMed: 28297669

Assembly members:

Assembly members:
entity_1, polymer, 128 residues, 14598.317 Da.

Natural source:

Natural source:   Common Name: Baker's yeast   Taxonomy ID: 559292   Superkingdom: Eukaryota   Kingdom: Fungi   Genus/species: Saccharomyces Saccharomyces cerevisiae

Experimental source:

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

Data sets:
Data typeCount
13C chemical shifts429
15N chemical shifts103
1H chemical shifts601

Additional metadata:

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

Assembly:

Entity Assembly IDEntity NameEntity ID
1entity_11

Entities:

Entity 1, entity_1 128 residues - 14598.317 Da.

1   SERGLUSERGLULEUASPGLNGLUSERASP
2   ASPSERPHEPHEASNGLUSERGLUSERGLU
3   SERGLUALAASPVALASPSERASPASPSER
4   ASPALALYSPROTYRGLYPROASPTRPPHE
5   LYSLYSSERGLUPHEARGLYSGLNGLYGLY
6   GLYSERASNLYSPHELEULYSSERSERASN
7   TYRASPSERSERASPGLUGLUSERASPGLU
8   GLUASPGLYLYSLYSVALVALLYSSERALA
9   LYSGLULYSLEULEUASPGLUMETGLNASP
10   VALTYRASNLYSILESERGLNALAGLUASN
11   SERASPASPTRPLEUTHRILESERASNGLU
12   PHEASPLEUILESERARGLEULEUVALARG
13   ALAGLNGLNGLNASNTRPGLYTHR

Samples:

sample_1: eIF3c 36-163, [U-100% 13C; U-100% 15N], 0.4 mM; DTT 1 mM; sodium chloride 150 mM; sodium phosphate 20 mM; H2O 95%; D2O, [U-2H], 5%

sample_conditions_1: ionic strength: 170 mM; pH: 7; pressure: 1 atm; temperature: 298 K

Experiments:

NameSampleSample stateSample conditions
2D 1H-15N HSQCsample_1isotropicsample_conditions_1
3D HNCOsample_1isotropicsample_conditions_1
3D HN(CA)COsample_1isotropicsample_conditions_1
3D CBCA(CO)NHsample_1isotropicsample_conditions_1
3D HNCACBsample_1isotropicsample_conditions_1
3D C(CO)NHsample_1isotropicsample_conditions_1
3D HBHA(CO)NHsample_1isotropicsample_conditions_1
2D 1H-13C HSQCsample_1isotropicsample_conditions_1
3D HCCH-TOCSYsample_1isotropicsample_conditions_1
3D HCCH-COSYsample_1isotropicsample_conditions_1
3D 1H-15N NOESYsample_1isotropicsample_conditions_1
3D 1H-13C NOESYsample_1isotropicsample_conditions_1

Software:

AMBER v9, Case, Darden, Cheatham III, Simmerling, Wang, Duke, Luo, ... and Kollman - refinement

CYANA v2.1, Guntert, Mumenthaler and Wuthrich - structure calculation

Kujira v0.98, Naohiro Kobayashi - chemical shift assignment

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

NMRView, Johnson, One Moon Scientific - peak picking

NMR spectrometers:

  • Bruker Avance 800 MHz
  • 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