BMRB

Biological Magnetic Resonance Data Bank


A Repository for Data from NMR Spectroscopy on Proteins, Peptides, Nucleic Acids, and other Biomolecules
Member of WWPDB

BMRB Entry 34049

Title: Structure of a Spumaretrovirus Gag central domain reveals an ancient retroviral capsid   PubMed: 23675305

Deposition date: 2016-10-07 Original release date: 2019-03-21

Authors: Nicastro, G.; Ball, N.; Taylor, I.

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).

Assembly members:
entity_1, polymer, 99 residues, 10949.391 Da.

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

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

Entity Sequences (FASTA):
entity_1: RTHGTFPMHQLGNVIKGIVD QEGVATAYTLGMMLSGQNYQ LVSGIIRGYLPGQAVVTALQ QRLDQEIDDQTRAETFIQHL NAVYEILGLNARGQSIRLE

Data typeCount
13C chemical shifts568
15N chemical shifts93
1H chemical shifts1851

Additional metadata:

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

Assembly:

Entity Assembly IDEntity NameEntity ID
1entity_1, 11
2entity_1, 21

Entities:

Entity 1, entity_1, 1 99 residues - 10949.391 Da.

1   ARGTHRHISGLYTHRPHEPROMETHISGLN
2   LEUGLYASNVALILELYSGLYILEVALASP
3   GLNGLUGLYVALALATHRALATYRTHRLEU
4   GLYMETMETLEUSERGLYGLNASNTYRGLN
5   LEUVALSERGLYILEILEARGGLYTYRLEU
6   PROGLYGLNALAVALVALTHRALALEUGLN
7   GLNARGLEUASPGLNGLUILEASPASPGLN
8   THRARGALAGLUTHRPHEILEGLNHISLEU
9   ASNALAVALTYRGLUILELEUGLYLEUASN
10   ALAARGGLYGLNSERILEARGLEUGLU

Samples:

sample_1: GAG protein, [U-13C; U-15N; U-2H], 0.5 mM; NaCl 20 mM; Tris 20 mM

sample_conditions_1: ionic strength: 40 mM; pH: 7; pressure: 1 Pa; temperature: 298 K

Experiments:

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

Software:

CARA, Keller and Wuthrich - chemical shift assignment

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

NMR spectrometers:

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