BMRB Entry 15782

Chem Shift validation: AVS_anomalous, AVS_full, LACS
BMRB Entry DOI: doi:10.13018/BMR15782

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Title:
1H, 13C and 15N chemical shifts of the sylvatic Dengue 1 Envelope Protein Domain III, strain P72-1244
Deposition date:
2008-05-27
Original release date:
2008-09-12
Authors:
Volk, David; Anderson, Kurtis; Gandham, Sai; May, Fiona; Beasley, David; Barrett, Alan; Gorenstein, David
Citation:

Citation: Volk, David; Anderson, Kurtis; Gandham, Sai; May, Fiona; Li, Li; Beasley, David; Barrett, Alan; Gorenstein, David. "NMR assignments of the sylvatic dengue 1 virus envelope protein domain III"  Biomol. NMR Assignments 2, 155-157 (2008).
PubMed: 19636893

Assembly members:

Assembly members:
DEN1ED3, polymer, 112 residues, Formula weight is not available

Natural source:

Natural source:   Common Name: Dengue virus   Taxonomy ID: 12637   Superkingdom: Viruses   Kingdom: not available   Genus/species: Flavivirus Dengue virus

Experimental source:

Experimental source:   Production method: recombinant technology   Host organism: Escherichia coli   Vector: pET-15

Entity Sequences (FASTA):

Entity Sequences (FASTA):
DEN1ED3: MDKLTLKGMSYVMCTGSFKL EKEVAETQHGTVLVQVKYEG TDAPCKIPFSTQDEKGITQN GRLITANPIVTDKEKPVSIE AKPPFGESYIVVGAGEKALK LSWFKKGSSIGK

Data sets:
Data typeCount
13C chemical shifts442
15N chemical shifts102
1H chemical shifts746

Additional metadata:

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

Assembly:

Entity Assembly IDEntity NameEntity ID
1subunit11

Entities:

Entity 1, subunit1 112 residues - Formula weight is not available

M289-K400 of the sylvatic Dengue 1 ED3, with mutations N366S,E370K

1   METASPLYSLEUTHRLEULYSGLYMETSER
2   TYRVALMETCYSTHRGLYSERPHELYSLEU
3   GLULYSGLUVALALAGLUTHRGLNHISGLY
4   THRVALLEUVALGLNVALLYSTYRGLUGLY
5   THRASPALAPROCYSLYSILEPROPHESER
6   THRGLNASPGLULYSGLYILETHRGLNASN
7   GLYARGLEUILETHRALAASNPROILEVAL
8   THRASPLYSGLULYSPROVALSERILEGLU
9   ALALYSPROPROPHEGLYGLUSERTYRILE
10   VALVALGLYALAGLYGLULYSALALEULYS
11   LEUSERTRPPHELYSLYSGLYSERSERILE
12   GLYLYS

Samples:

sample_1: DEN1ED3, [U-99% 13C; U-99% 15N], 0.25 ± 0.05 mM; sodium chloride 25 ± 1 mM; TRIS, [U-2H], 25 ± 1 mM

sample_conditions_1: ionic strength: 0.05 M; pH: 6.5; 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 CBCA(CO)NHsample_1isotropicsample_conditions_1
3D HNCACBsample_1isotropicsample_conditions_1
3D HNCOsample_1isotropicsample_conditions_1
3D HNCACOsample_1isotropicsample_conditions_1
3D C(CO)NHsample_1isotropicsample_conditions_1
3D H(CCO)NHsample_1isotropicsample_conditions_1
3D HCCH-TOCSYsample_1isotropicsample_conditions_1

Software:

FELIX v2000, Accelrys Software Inc. - chemical shift assignment, processing

NMR spectrometers:

  • Varian INOVA 800 MHz
  • Varian INOVA 600 MHz

Related Database Links:

DBJ BAJ72472
EMBL CBL95104
GB AAF59976 AAF59977 AAF61125 AAN32773 AAN32776

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