BMRB Entry 50380

Chem Shift validation: AVS_full
BMRB Entry DOI: doi:10.13018/BMR50380

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Title:
Hepatits C virus NS5A protein AHD1 domain
Deposition date:
2020-07-07
Original release date:
2021-03-11
Authors:
Jirasko, Vlastimil; Lends, Alons; Lakomek, Nils-Alexander; Fogeron, Marie-Laure; Weber, Marco; Malar, Alexander; Smith-Penzel, Susanne; Bartenschlager, Ralf; Meier, Beat; Bockmann, Anja
Citation:

Citation: Jirasko, Vlastimil; Lends, Alons; Lakomek, Nils-Alexander; Fogeron, Marie-Laure; Weber, Marco; Malar, Alexander; Smith-Penzel, Susanne; Bartenschlager, Ralf; Meier, Beat; Bockmann, Anja. "Dimer Organization of Membrane-Associated NS5A of Hepatitis C Virus as Determined by Highly Sensitive 1 H-Detected Solid-State NMR"  Angew. Chem. Int. Ed. Engl. 60, 5339-5347 (2021).
PubMed: 33205864

Assembly members:

Assembly members:
entity_1, polymer, 224 residues, Formula weight is not available

Natural source:

Natural source:   Common Name: Hepacivirus C   Taxonomy ID: 11103   Superkingdom: Viruses   Kingdom: not available   Genus/species: Hepacivirus Hepacivirus C

Experimental source:

Experimental source:   Production method: cell free synthesis   Host organism: wheat germ - cell free   Vector: pEU-01

Entity Sequences (FASTA):

Entity Sequences (FASTA):
entity_1: MSGSWLRDVWDWVCTILTDF KNWLTSKLFPKLPGLPFISC QKGYKGVWAGTGIMTTRCPC GANISGNVRLGSMRITGPKT CMNTWQGTFPINCYTEGQCA PKPPTNYKTAIWRVAASEYA EVTQHGSYSYVTGLTTDNLK IPCQLPSPEFFSWVDGVQIH RFAPTPKPFFRDEVSFCVGL NSYAVGSQLPCEPEPDADVL RSMLTDPPHITAETGSAWSH PQFEK

Data sets:
Data typeCount
13C chemical shifts264
15N chemical shifts97
1H chemical shifts97

Additional metadata:

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

Entity Assembly IDEntity NameEntity ID
1NS5A AHD1 domain1

Entities:

Entity 1, NS5A AHD1 domain 224 residues - Formula weight is not available

1   SERGLYSERTRPLEUARGASPVALTRPASP
2   TRPVALCYSTHRILELEUTHRASPPHELYS
3   ASNTRPLEUTHRSERLYSLEUPHEPROLYS
4   LEUPROGLYLEUPROPHEILESERCYSGLN
5   LYSGLYTYRLYSGLYVALTRPALAGLYTHR
6   GLYILEMETTHRTHRARGCYSPROCYSGLY
7   ALAASNILESERGLYASNVALARGLEUGLY
8   SERMETARGILETHRGLYPROLYSTHRCYS
9   METASNTHRTRPGLNGLYTHRPHEPROILE
10   ASNCYSTYRTHRGLUGLYGLNCYSALAPRO
11   LYSPROPROTHRASNTYRLYSTHRALAILE
12   TRPARGVALALAALASERGLUTYRALAGLU
13   VALTHRGLNHISGLYSERTYRSERTYRVAL
14   THRGLYLEUTHRTHRASPASNLEULYSILE
15   PROCYSGLNLEUPROSERPROGLUPHEPHE
16   SERTRPVALASPGLYVALGLNILEHISARG
17   PHEALAPROTHRPROLYSPROPHEPHEARG
18   ASPGLUVALSERPHECYSVALGLYLEUASN
19   SERTYRALAVALGLYSERGLNLEUPROCYS
20   GLUPROGLUPROASPALAASPVALLEUARG
21   SERMETLEUTHRASPPROPROHISILETHR
22   ALAGLUTHRGLYSERALATRPSERHISPRO
23   GLNPHEGLULYS

Samples:

sample_1: NS5A AHD1 domain, [U-13C; U-15N; U-2H], 200 ± 100 ug

sample_conditions_1: ionic strength: 0.15 M; pH: 8; pressure: 1 atm; temperature: 296 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

Software:

CcpNmr Analysis - chemical shift assignment

NMR spectrometers:

  • Bruker AVANCE III 850 MHz

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