BMRB Entry 19845

Title:
Structure of a Conserved Golgi Complex-targeting Signal in Coronavirus Envelope Proteins
Deposition date:
2014-03-09
Original release date:
2014-03-31
Authors:
Li, Yan; Surya, Wahyu; Claudine, Stephanie; Torres, Jaume
Citation:

Citation: Li, Yan; Surya, Wahyu; Claudine, Stephanie; Torres, Jaume. "Structure of a Conserved Golgi Complex-targeting Signal in Coronavirus Envelope Proteins."  J. Biol. Chem. 289, 12535-12549 (2014).
PubMed: 24668816

Assembly members:

Assembly members:
entity, polymer, 58 residues, 6066.473 Da.

Natural source:

Natural source:   Common Name: Coronavirus   Taxonomy ID: not available   Superkingdom: viruses   Kingdom: not available   Genus/species: not available not available

Experimental source:

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

Entity Sequences (FASTA):

Data sets:
Data typeCount
13C chemical shifts260
15N chemical shifts63
1H chemical shifts461

Additional metadata:

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

Assembly:

Entity Assembly IDEntity NameEntity ID
1Coronavirus Envelope Proteins-11

Entities:

Entity 1, Coronavirus Envelope Proteins-1 58 residues - 6066.473 Da.

1   GLUTHRGLYTHRLEUILEVALASNSERVAL
2   LEULEUPHELEUALAPHEVALVALPHELEU
3   LEUVALTHRLEUALAILELEUTHRALALEU
4   ARGLEUALAALATYRALAALAASNILEVAL
5   ASNVALSERLEUVALLYSPROTHRVALTYR
6   VALTYRSERARGVALLYSASNLEU

Samples:

SARS_Etr: Coronavirus Envelope Proteins, [U-99% 13C; U-99% 15N], 0.8 mM; DSS 0.1 mM; D2O, [U-99% 2H], 5%; SDS 50 mM; sodium phosphate 20 mM; sodium chloride 50 mM

sample_conditions_1: ionic strength: 50 mM; pH: 5.5; pressure: 1 atm; temperature: 318 K

Experiments:

NameSampleSample stateSample conditions
2D 1H-15N HSQCSARS_Etrisotropicsample_conditions_1
3D HNCASARS_Etrisotropicsample_conditions_1
3D HN(CO)CASARS_Etrisotropicsample_conditions_1
3D HNCOSARS_Etrisotropicsample_conditions_1
3D HCCH-TOCSYSARS_Etrisotropicsample_conditions_1
3D 1H-13C NOESYSARS_Etrisotropicsample_conditions_1
3D 1H-13C NOESY aliphaticSARS_Etrisotropicsample_conditions_1
3D 1H-13C NOESY aromaticSARS_Etrisotropicsample_conditions_1

Software:

CARA, Keller and Wuthrich - chemical shift assignment

CYANA, Guntert, Mumenthaler and Wuthrich - refinement

TOPSPIN, Bruker Biospin - collection

NMR spectrometers:

  • Bruker Avance 700 MHz

Related Database Links:

PDB

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