BMRB Entry 52450

Chem Shift validation: AVS_full
BMRB Entry DOI: doi:10.13018/BMR52450

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Title:
Assignment of the Lassa virus glycoprotein 2 transmembrane domain in the postfusion state
Deposition date:
2024-05-10
Original release date:
2024-07-19
Authors:
Keating, Patrick; Lee, Jinwoo
Citation:

Citation: Keating, Patrick; Lee, Jinwoo. "Assignment of the Lassa virus transmembrane domain in the prefusion and postfusion states in detergent micelles"  Biomol. NMR Assign. 18, 165-169 (2024).
PubMed: 38916786

Assembly members:

Assembly members:
entity_1, polymer, 40 residues, Formula weight is not available

Natural source:

Natural source:   Common Name: Mammarenavirus lassaense   Taxonomy ID: 3052310   Superkingdom: Viruses   Kingdom: not available   Genus/species: Mammarenavirus lassaense

Experimental source:

Experimental source:   Production method: recombinant technology   Host organism: Escherichia coli   Vector: pET24a

Entity Sequences (FASTA):

Entity Sequences (FASTA):
entity_1: GSGKTPLGLVDLFVFSTSFY LISIFLHLVKIPTHRHIVGK

Data sets:
Data typeCount
13C chemical shifts109
15N chemical shifts36
1H chemical shifts36

Additional metadata:

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

Assembly:

Entity Assembly IDEntity NameEntity ID
1Lassa virus transmembrane domain1

Entities:

Entity 1, Lassa virus transmembrane domain 40 residues - Formula weight is not available

1   GLYSERGLYLYSTHRPROLEUGLYLEUVAL
2   ASPLEUPHEVALPHESERTHRSERPHETYR
3   LEUILESERILEPHELEUHISLEUVALLYS
4   ILEPROTHRHISARGHISILEVALGLYLYS

Samples:

sample_1: Lassa virus transmembrane domain, [U-13C; U-15N; U-2H], 400 uM; sodium chloride 100 mM; sodium phosphate 25 mM; LMPG 100 mM

sample_conditions_1: pH: 4.0; temperature: 310 K

Experiments:

NameSampleSample stateSample conditions
2D 1H-15N HSQCsample_1isotropicsample_conditions_1
3D HNCOsample_1isotropicsample_conditions_1
3D HNCAsample_1isotropicsample_conditions_1
3D HNCACBsample_1isotropicsample_conditions_1
3D HN(CA)COsample_1isotropicsample_conditions_1
3D HN(CO)CAsample_1isotropicsample_conditions_1

Software:

NMRPipe - processing

NMRbox - data analysis

TOPSPIN - collection

NMRFAM-SPARKY - chemical shift assignment

NMR spectrometers:

  • Bruker AVANCE III 800 MHz

Related Database Links:

UNP P08669

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