BMRB Entry 15660

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PDB ID:
Entry in NMR Restraints Grid
Validation report in NRG-CING
Chem Shift validation: AVS_full, LACS
BMRB Entry DOI: doi:10.13018/BMR15660
MolProbity Validation Chart

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Title:
NMR assignment of the arenaviral protein Z from Lassa fever virus
Deposition date:
2008-02-15
Original release date:
2008-06-05
Authors:
Volpon, Laurent; Osborne, Michael; Borden, Katherine
Citation:

Citation: Volpon, Laurent; Osborne, Michael; Capul, Althea; de la Torre, Juan; Borden, Katherine. "Structural characterization of the Z RING-eIF4E complex reveals a distinct mode of control for eIF4E"  Proc. Natl. Acad. Sci. U. S. A. 107, 5441-5446 (2010).
PubMed: 20212144

Assembly members:

Assembly members:
LFV-Z, polymer, 99 residues, Formula weight is not available
ZN, non-polymer, 65.409 Da.

Natural source:

Natural source:   Common Name: Arenaviru Lassa virus   Taxonomy ID: 11620   Superkingdom: Viruses   Kingdom: not available   Genus/species: Arenavirus Lassa virus

Experimental source:

Experimental source:   Production method: recombinant technology   Host organism: Escherichia coli   Vector: pGEX-6p1

Entity Sequences (FASTA):

Entity Sequences (FASTA):
LFV-Z: MGNKQAKAPESKDSPRASLI PDATHLGPQFCKSCWFENKG LVECNNHYLCLNCLTLLLSV SNRCPICKMPLPTKLRPSAA PTAPPTGAADSIRPPPYSP

Data sets:
Data typeCount
13C chemical shifts351
15N chemical shifts84
1H chemical shifts516

Additional metadata:

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

Assembly:

Entity Assembly IDEntity NameEntity ID
1LFV-Z1
2ZN2

Entities:

Entity 1, LFV-Z 99 residues - Formula weight is not available

1   METGLYASNLYSGLNALALYSALAPROGLU
2   SERLYSASPSERPROARGALASERLEUILE
3   PROASPALATHRHISLEUGLYPROGLNPHE
4   CYSLYSSERCYSTRPPHEGLUASNLYSGLY
5   LEUVALGLUCYSASNASNHISTYRLEUCYS
6   LEUASNCYSLEUTHRLEULEULEUSERVAL
7   SERASNARGCYSPROILECYSLYSMETPRO
8   LEUPROTHRLYSLEUARGPROSERALAALA
9   PROTHRALAPROPROTHRGLYALAALAASP
10   SERILEARGPROPROPROTYRSERPRO

Entity 2, ZN - Zn - 65.409 Da.

1   ZN

Samples:

sample_1: LFV-Z, [U-100% 15N], 0.2 mM; potassium phosphate 20 mM; sodium chloride 200 mM; sodium azide 3 mM; zinc sulfate 0.05 mM; TCEP 0.05 mM; D2O 7%; H2O 93%

sample_2: LFV-Z, [U-100% 13C; U-100% 15N], 0.2 mM; potassium phosphate 20 mM; sodium chloride 200 mM; sodium azide 3 mM; zinc sulfate 0.05 mM; TCEP 0.05 mM; D2O 7%; H2O 93%

sample_3: LFV-Z, [U-100% 13C; U-100% 15N], 0.2 mM; potassium phosphate 20 mM; sodium chloride 200 mM; sodium azide 3 mM; zinc sulfate 0.05 mM; TCEP 0.05 mM; D2O 100%

sample_conditions_1: ionic strength: 0.25 M; pH: 7.2; pressure: 1 atm; temperature: 293 K

Experiments:

NameSampleSample stateSample conditions
2D 1H-15N HSQCsample_1isotropicsample_conditions_1
2D 1H-13C HSQCsample_3isotropicsample_conditions_1
3D 1H-15N TOCSYsample_1isotropicsample_conditions_1
3D 1H-15N NOESYsample_1isotropicsample_conditions_1
3D 1H-13C NOESYsample_3isotropicsample_conditions_1
3D HNCACBsample_2isotropicsample_conditions_1
3D CBCA(CO)NHsample_2isotropicsample_conditions_1
3D HCCH-TOCSYsample_3isotropicsample_conditions_1
3D HNCOsample_2isotropicsample_conditions_1
3D HBHA(CO)NHsample_2isotropicsample_conditions_1
2D (HB)CB(CGCD)HDsample_2isotropicsample_conditions_1
2D (HB)CB(CGCDCE)HEsample_2isotropicsample_conditions_1
3D C(CO)NH-TOCSYsample_2isotropicsample_conditions_1

Software:

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

SPARKY, Goddard - chemical shift assignment, data analysis, peak picking

NMR spectrometers:

  • Varian INOVA 600 MHz

Related Database Links:

PDB
GB AAC05816 AAC05818 AAT49001 ADY11072 ADY11074
REF NP_694871
SP O73557
AlphaFold O73557

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