BMRB Entry 34050

Title:
Structure of a Spumaretrovirus Gag central domain reveals an ancient retroviral capsid
Deposition date:
2016-10-07
Original release date:
2016-10-24
Authors:
Taylor, I.; Nicastro, G.; Ball, N.
Citation:

Citation: Goldstone, D.; Flower, T.; Ball, N.; Sanz-Ramos, M.; Yap, M.; Ogrodowicz, R.; Stanke, N.; Reh, J.; Lindemann, D.; Stoye, J.; Taylor, I.. "A unique spumavirus Gag N-terminal domain with functional properties of orthoretroviral matrix and capsid."  PLoS Pathog. 9, e1003376-e1003376 (2013).
PubMed: 23675305

Assembly members:

Assembly members:
entity_1, polymer, 180 residues, 19604.459 Da.

Natural source:

Natural source:   Common Name: SFVcpz(hu)   Taxonomy ID: 11963   Superkingdom: Viruses   Kingdom: not available   Genus/species: Human spumaretrovirus

Experimental source:

Experimental source:   Production method: recombinant technology   Host organism: Escherichia coli BL21(DE3)   Vector: PET47B

Data sets:
Data typeCount
15N chemical shifts183
1H chemical shifts1143

Additional metadata:

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

Assembly:

Entity Assembly IDEntity NameEntity ID
1entity_11

Entities:

Entity 1, entity_1 180 residues - 19604.459 Da.

1   PROILEGLYTHRVALILEPROILEGLNHIS
2   ILEARGSERVALTHRGLYGLUPROPROARG
3   ASNPROARGGLUILEPROILETRPLEUGLY
4   ARGASNALAPROALAILEASPGLYVALPHE
5   PROVALTHRTHRPROASPLEUARGCYSARG
6   ILEILEASNALAILELEUGLYGLYASNILE
7   GLYLEUSERLEUTHRPROGLYASPCYSLEU
8   THRTRPASPSERALAVALALATHRLEUPHE
9   ILEARGTHRHISGLYTHRPHEPROMETHIS
10   GLNLEUGLYASNVALILELYSGLYILEVAL
11   ASPGLNGLUGLYVALALATHRALATYRTHR
12   LEUGLYMETMETLEUSERGLYGLNASNTYR
13   GLNLEUVALSERGLYILEILEARGGLYTYR
14   LEUPROGLYGLNALAVALVALTHRALALEU
15   GLNGLNARGLEUASPGLNGLUILEASPASP
16   GLNTHRARGALAGLUTHRPHEILEGLNHIS
17   LEUASNALAVALTYRGLUILELEUGLYLEU
18   ASNALAARGGLYGLNSERILEARGLEUGLU

Samples:

sample_1: entity_1, [U-13C; U-15N], 0.3 mM; NaCl 20 mM; Tris 20 mM

sample_conditions_1: ionic strength: 40 mM; pH: 7.0; pressure: 1 Pa; temperature: 298 K

Experiments:

NameSampleSample stateSample conditions
3D 1H-13C NOESYsample_1isotropicsample_conditions_1
3D 1H-15N NOESYsample_1isotropicsample_conditions_1
3D 1H-13C NOESY aromaticsample_1isotropicsample_conditions_1

Software:

ARIA, Linge, O'Donoghue and Nilges - structure calculation

CARA, Keller and Wuthrich - chemical shift assignment

NMR spectrometers:

  • Bruker Avance 950 MHz
  • Bruker Avance 800 MHz
  • Bruker Avance 700 MHz
  • Bruker Avance 6 MHz

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