BMRB

Biological Magnetic Resonance Data Bank


A Repository for Data from NMR Spectroscopy on Proteins, Peptides, Nucleic Acids, and other Biomolecules
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BMRB Entry 6046

Title: 1H, 13C and 15N resonance assignments for domain III of the West Nile Virus envelope protein   PubMed: 15213461

Deposition date: 2003-12-12 Original release date: 2004-07-06

Authors: Volk, David; Kallick, Deborah; Holbrook, Michael; Beasley, David; Barrett, Alan; Gorenstein, David

Citation: Volk, David; Kallick, Deborah; Holbrook, Michael; Beasley, David; Barrett, Alan; Gorenstein, David. "Letter to the Editor: 1H, 13C and 15N resonance assignments for domain III of the West Nile Virus envelope protein"  J. Biomol. NMR 29, 445-446 (2004).

Assembly members:
West Nile Virus envelope protein domain III, polymer, 115 residues, 12185 Da.

Natural source:   Common Name: West Nile Virus I strain 385-99   Taxonomy ID: 11082   Superkingdom: Viruses   Kingdom: not available   Genus/species: Flavivirus West Nile Virus I

Experimental source:   Production method: recombinant technology

Entity Sequences (FASTA):
West Nile Virus envelope protein domain III: ISEFQLKGTTYGVCSKAFKF LGTPADTGHGTVVLELQYTG TDGPCKVPISSVASLNDLTP VGRLVTVNPFVSVATANAKV LIELEPPFGDSYIVVGRGEQ QINHHWHKSGSSIGK

Data sets:
Data typeCount
13C chemical shifts444
15N chemical shifts110
1H chemical shifts743

Additional metadata:

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

Entity Assembly IDEntity NameEntity ID
1wnd3 subunit 11

Entities:

Entity 1, wnd3 subunit 1 115 residues - 12185 Da.

1   ILESERGLUPHEGLNLEULYSGLYTHRTHR
2   TYRGLYVALCYSSERLYSALAPHELYSPHE
3   LEUGLYTHRPROALAASPTHRGLYHISGLY
4   THRVALVALLEUGLULEUGLNTYRTHRGLY
5   THRASPGLYPROCYSLYSVALPROILESER
6   SERVALALASERLEUASNASPLEUTHRPRO
7   VALGLYARGLEUVALTHRVALASNPROPHE
8   VALSERVALALATHRALAASNALALYSVAL
9   LEUILEGLULEUGLUPROPROPHEGLYASP
10   SERTYRILEVALVALGLYARGGLYGLUGLN
11   GLNILEASNHISHISTRPHISLYSSERGLY
12   SERSERILEGLYLYS

Samples:

sample_1: West Nile Virus envelope protein domain III, [U-95% 13C; U-95% 15N], 0.7 mM; K2HPO4 50 mM; NaCl 100 mM; NaN3 10 mM; EDTA 0.1 mM

Ex-cond_1: ionic strength: 0.26 M; pH: 6.8; temperature: 298 K

Experiments:

NameSampleSample stateSample conditions
HNCAnot availablenot availablenot available
HNCOnot availablenot availablenot available
HNCACBnot availablenot availablenot available
H(CC)CONH-TOCSYnot availablenot availablenot available
(H)CC(CO)NH-TOCSYnot availablenot availablenot available
HCCH-TOCSYnot availablenot availablenot available
15N-edited NOESY-HSQCnot availablenot availablenot available
13C-edited NOESY-HSQCnot availablenot availablenot available

Software:

No software information available

NMR spectrometers:

  • Varian UnityPlus 750 MHz

Related Database Links:

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Download simulated HSQC data in one of the following formats:
CSV: Backbone or all simulated shifts
SPARKY: Backbone or all simulated shifts