BMRB Entry 27925

Title:
NMR assignments of capsid protrusion domain of dragon grouper nervous necrosis virus
Deposition date:
2019-05-26
Original release date:
2020-02-11
Authors:
Sterbova, Petra; Wu, Danny; Lou, Yuan-Chao; Tzou, Der-Lii
Citation:

Citation: Sterbova, Petra; Wu, Danny; Lou, Yuan-Chao; Wang, Chun-Hsiung; Chang, Wei-Hau; Tzou, Der-Lii. "1H, 13C, and 15N resonance assignments of the capsid protrusion domain of dragon grouper nervous necrosis virus"  Biomol. NMR Assignments 14, 63-66 (2020).
PubMed: 31848940

Assembly members:

Assembly members:
Protrusion_domain, polymer, 125 residues, 13809.3 Da.

Natural source:

Natural source:   Common Name: Dragon grouper nervous necrosis virus   Taxonomy ID: 292633   Superkingdom: virus   Kingdom: not available   Genus/species: betanodavirus not available

Experimental source:

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

Data sets:
Data typeCount
13C chemical shifts552
15N chemical shifts127
1H chemical shifts843

Additional metadata:

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

Assembly:

Entity Assembly IDEntity NameEntity ID
1Protrusio domain monomer1

Entities:

Entity 1, Protrusio domain monomer 125 residues - 13809.3 Da.

This is the protrusion domain of Dragon grouper nervous necrosis virus coat protein

1   THRPROGLUGLUTHRTHRALAPROILEMET
2   THRGLNGLYSERLEUTYRASNASPSERLEU
3   SERTHRASNASPPHELYSSERILELEULEU
4   GLYSERTHRPROLEUASPILEALAPROASP
5   GLYALAVALPHEGLNLEUASPARGPROLEU
6   SERILEASPTYRSERLEUGLYTHRGLYASP
7   VALASPARGALAVALTYRTRPHISLEULYS
8   LYSPHEALAGLYASNALAGLYTHRPROALA
9   GLYTRPPHEARGTRPGLYILETRPASPASN
10   PHEASNLYSTHRPHETHRASPGLYVALALA
11   TYRTYRSERASPGLUGLNPROARGGLNILE
12   LEULEUPROVALGLYTHRVALCYSTHRARG
13   VALASPSERGLUASN

Samples:

sample_1: Protrusion Domain, [U15N; U13C], 1.2 mM; HEPES 20 mM; sodium chloride 100 mM; DTT 1 mM

sample_conditions_1: ionic strength: 0.12 M; pH: 7.0; 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 HNCOsample_1isotropicsample_conditions_1
3D HNCACBsample_1isotropicsample_conditions_1
3D HBHA(CO)NHsample_1isotropicsample_conditions_1
3D HCCH-TOCSYsample_1isotropicsample_conditions_1
3D 1H-15N NOESYsample_1isotropicsample_conditions_1

Software:

SPARKY, Goddard - chemical shift assignment

NMR spectrometers:

  • Bruker Avance 600 MHz
  • Bruker Avance 800 MHz

Related Database Links:

UNP Q9E6H7
AlphaFold Q9E6H7

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