BMRB Entry 19390

Title:
Solution structure of the EBNA-2 N-terminal Dimerization (END) domain from the Epstein-Barr virus
Deposition date:
2013-07-26
Original release date:
2015-06-08
Authors:
Friberg, Anders; Sattler, Michael
Citation:

Citation: Friberg, Anders; Thumann, Sybille; Hennig, Janosch; Zou, Peijian; Ling, Paul; Sattler, Michael; Kempkes, Bettina. "The EBNA-2 N-Terminal Transactivation Domain Folds into a Dimeric Structure Required for Target Gene Activation"  Plos Pathog. 11, e1004910-e1004910 (2015).
PubMed: 26024477

Assembly members:

Assembly members:
END_domain, polymer, 62 residues, 6663.513 Da.

Natural source:

Natural source:   Common Name: Epstein-Barr virus   Taxonomy ID: 10377   Superkingdom: Viruses   Kingdom: not available   Genus/species: Lymphocryptovirus Human herpesvirus 4

Experimental source:

Experimental source:   Production method: recombinant technology   Host organism: Escherichia coli   Vector: pET-24d

Entity Sequences (FASTA):

Data sets:
Data typeCount
13C chemical shifts211
15N chemical shifts54
1H chemical shifts421

Additional metadata:

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

Entity Assembly IDEntity NameEntity ID
1END domain, chain 11
2END domain, chain 21

Entities:

Entity 1, END domain, chain 1 62 residues - 6663.513 Da.

Amino acids 1-4 represent residual non-native residues present after removal of the affinity and solubility tag.

1   GLYALAMETGLUMETPROTHRPHETYRLEU
2   ALALEUHISGLYGLYGLNTHRTYRHISLEU
3   ILEVALASPTHRASPSERLEUGLYASNPRO
4   SERLEUSERVALILEPROSERASNPROTYR
5   GLNGLUGLNLEUSERASPTHRPROLEUILE
6   PROLEUTHRILEPHEVALGLYGLUASNTHR
7   GLYVAL

Related Database Links:

UNP P12978
PDB 2N2J
DBJ BAP94392 BAQ20285
EMBL CAA24877 CAD53395 CEP79167 CEQ32332 CEQ32414
GB AAA45903 AAY41099 AFY97831 AFY97916 AGL80643
REF YP_401644
SP P12978 Q3KSV2
AlphaFold Q777H1 P12978 Q3KSV2

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