BMRB Entry 19716

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PDB ID:
Entry in NMR Restraints Grid
Validation report in NRG-CING
Chem Shift validation: AVS_anomalous, AVS_full, SPARTA
BMRB Entry DOI: doi:10.13018/BMR19716
MolProbity Validation Chart

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Title:
Zn-binding domain of eukaryotic translation initiation factor 3, subunit G
Deposition date:
2014-01-03
Original release date:
2015-01-05
Authors:
Al-Abdul-Wahid, Mohamed Sameer; Menade, Marie; Xie, Jingwei; Kozlov, Guennadi; Gehring, Kalle
Citation:

Citation: Al-Abdul-Wahid, Mohamed Sameer; Menade, Marie; Xie, Jingwei; Kozlov, Guennadi; Gehring, Kalle. "Solution NMR structure of the Zn-binding domain of eukaryotic translation initiation factor 3, subunit G"  Proteins: Struct. Funct. Genet. ., .-..

Assembly members:

Assembly members:
eif3G_Zn, polymer, 24 residues, 2787.301 Da.
ZINC ION, non-polymer, 65.409 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: pGEX-6p1

Entity Sequences (FASTA):

Entity Sequences (FASTA):
eif3G_Zn: KIVSCRICKGDHWTTRCPYK DTLG

Data sets:
Data typeCount
13C chemical shifts78
15N chemical shifts24
1H chemical shifts152

Additional metadata:

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

Entity Assembly IDEntity NameEntity ID
1entity_11
2ZINC ION2

Entities:

Entity 1, entity_1 24 residues - 2787.301 Da.

1   LYSILEVALSERCYSARGILECYSLYSGLY
2   ASPHISTRPTHRTHRARGCYSPROTYRLYS
3   ASPTHRLEUGLY

Entity 2, ZINC ION - Zn - 65.409 Da.

1   ZN

Samples:

sample_1: eif3G_Zn 10 mM; HEPES 10 mM; sodium chloride 50 mM; zinc chloride 1 mM; H2O 90%; D2O 10%

sample_conditions_1: ionic strength: 0 mM; pH: 6.3; pressure: 1 atm; temperature: 298 K

Experiments:

NameSampleSample stateSample conditions
3D CBCA(CO)NHsample_1isotropicsample_conditions_1
3D HNCACBsample_1isotropicsample_conditions_1
3D 1H-13C NOESYsample_1isotropicsample_conditions_1
3D HCCH-TOCSYsample_1isotropicsample_conditions_1
3D HNHBsample_1isotropicsample_conditions_1
3D HNHAsample_1isotropicsample_conditions_1
3D 1H-15N NOESYsample_1isotropicsample_conditions_1
3D 1H-15N TOCSYsample_1isotropicsample_conditions_1

Software:

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

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

XPLOR-NIH, Schwieters, Kuszewski, Tjandra and Clore - structure solution

NMR spectrometers:

  • Bruker Avance 600 MHz
  • Varian INOVA 500 MHz

Related Database Links:

PDB
DBJ BAC29952 BAE40297 BAE87500 BAF84009 BAH11496
EMBL CAG12187 CAG33415 CAJ83120 CDQ73632 CDQ81098
GB AAB71866 AAC78728 AAD00176 AAF14221 AAG15396
REF NP_001013113 NP_001016749 NP_001073091 NP_001086477 NP_001087888
SP O75821 Q28CY2 Q3ZC12 Q5RK09 Q641B2
TPG DAA27948
AlphaFold O75821 Q28CY2 Q3ZC12 Q5RK09 Q641B2

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