BMRB Entry 15034

Chem Shift validation: AVS_full, LACS
BMRB Entry DOI: doi:10.13018/BMR15034

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Title:
1H,13C and 15N NMR Assignments of the Yellow Fever Envelope Protein Domain III
Deposition date:
2006-11-16
Original release date:
2007-06-27
Authors:
Volk, David; Gandham, Sai; May, Fiona; Barrett, Alan; Gorenstein, David
Citation:

Citation: Volk, David; Gandham, Sai; May, Fiona; Anderson, Anjenique; Barrett, Alan; Gorenstein, David. "NMR assignments of the yellow fever virus envelope protein domain III"  Biomol. NMR Assignments 1, 49-50 (2007).
PubMed: 19636823

Assembly members:

Assembly members:
YFED3, polymer, 112 residues, Formula weight is not available

Natural source:

Natural source:   Common Name: Yellow fever virus   Taxonomy ID: 11089   Superkingdom: Viruses   Kingdom: not available   Genus/species: Flavivirus Yellow fever virus

Experimental source:

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

Entity Sequences (FASTA):

Entity Sequences (FASTA):
YFED3: MSALTLKGTSYKMCTDKMSF VKNPTDTGHGTVVMQVKVPK GAPCKIPVIVADDLTAAINK GILVTVNPIASTNDDEVLIE VNPPFGDSYIIVGTGDSRLT YQWHKEGSSIGK

Data sets:
Data typeCount
13C chemical shifts462
15N chemical shifts111
1H chemical shifts768

Additional metadata:

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

Assembly:

Entity Assembly IDEntity NameEntity ID
1YFED3 monomer1

Entities:

Entity 1, YFED3 monomer 112 residues - Formula weight is not available

All residues (1-112) represent natural amino acids in the YF-ED3

1   METSERALALEUTHRLEULYSGLYTHRSER
2   TYRLYSMETCYSTHRASPLYSMETSERPHE
3   VALLYSASNPROTHRASPTHRGLYHISGLY
4   THRVALVALMETGLNVALLYSVALPROLYS
5   GLYALAPROCYSLYSILEPROVALILEVAL
6   ALAASPASPLEUTHRALAALAILEASNLYS
7   GLYILELEUVALTHRVALASNPROILEALA
8   SERTHRASNASPASPGLUVALLEUILEGLU
9   VALASNPROPROPHEGLYASPSERTYRILE
10   ILEVALGLYTHRGLYASPSERARGLEUTHR
11   TYRGLNTRPHISLYSGLUGLYSERSERILE
12   GLYLYS

Samples:

sample_1: YFED3, [U-98% 13C; U-98% 15N], 0.1 – 0.3 mM

sample_conditions_1: ionic strength: 0.05 M; pH: 5.8; pressure: 1 atm; temperature: 298 K

Experiments:

NameSampleSample stateSample conditions
2D 1H-15N HSQCsample_1isotropicsample_conditions_1
2D 1H-13C HSQCsample_1isotropicsample_conditions_1
3D HNCOsample_1isotropicsample_conditions_1
3D CBCA(CO)NHsample_1isotropicsample_conditions_1
3D H(CCO)NHsample_1isotropicsample_conditions_1
3D C(CO)NHsample_1isotropicsample_conditions_1
3D HCCH-TOCSYsample_1isotropicsample_conditions_1
3D 1H-15N NOESYsample_1isotropicsample_conditions_1
3D HNCAsample_1isotropicsample_conditions_1
3D HNCACBsample_1isotropicsample_conditions_1

Software:

VNMRJ, Varian - collection, data analysis

NMR spectrometers:

  • Varian INOVA 600 MHz
  • Varian INOVA 750 MHz

Related Database Links:

PDB
GB AAA92693 AAA92694 AAA92695 AAA92698 AAA92699
SP Q074N0 Q1X880 Q1X881 Q6DV88 Q6J3P1
AlphaFold Q074N0 Q1X880 Q6J3P1 Q1X881 Q6DV88

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