BMRB Entry 19390
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PDB ID:
Entry in NMR Restraints Grid
Validation report in NRG-CING
Chem Shift validation: AVS_full, LACS, SPARTA
BMRB Entry DOI: doi:10.13018/BMR19390
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Title: Solution structure of the EBNA-2 N-terminal Dimerization (END) domain from the Epstein-Barr virus PubMed: 26024477
Deposition date: 2013-07-26 Original release date: 2015-06-08
Authors: Friberg, Anders; Sattler, Michael
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).
Assembly members:
END_domain, polymer, 62 residues, 6663.513 Da.
Natural source: Common Name: Epstein-Barr virus Taxonomy ID: 10377 Superkingdom: Viruses Kingdom: not available Genus/species: Lymphocryptovirus Human herpesvirus 4
Experimental source: Production method: recombinant technology Host organism: Escherichia coli
Entity Sequences (FASTA):
END_domain: GAMEMPTFYLALHGGQTYHL
IVDTDSLGNPSLSVIPSNPY
QEQLSDTPLIPLTIFVGENT
GV
- assigned_chemical_shifts
| Data type | Count |
| 13C chemical shifts | 211 |
| 15N chemical shifts | 54 |
| 1H chemical shifts | 421 |
Additional metadata:
Assembly:
| Entity Assembly ID | Entity Name | Entity ID |
|---|---|---|
| 1 | END domain, chain 1 | 1 |
| 2 | END domain, chain 2 | 1 |
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 | GLY | ALA | MET | GLU | MET | PRO | THR | PHE | TYR | LEU | ||||
| 2 | ALA | LEU | HIS | GLY | GLY | GLN | THR | TYR | HIS | LEU | ||||
| 3 | ILE | VAL | ASP | THR | ASP | SER | LEU | GLY | ASN | PRO | ||||
| 4 | SER | LEU | SER | VAL | ILE | PRO | SER | ASN | PRO | TYR | ||||
| 5 | GLN | GLU | GLN | LEU | SER | ASP | THR | PRO | LEU | ILE | ||||
| 6 | PRO | LEU | THR | ILE | PHE | VAL | GLY | GLU | ASN | THR | ||||
| 7 | GLY | VAL |
Samples:
sample_1: END domain, [U-13C; U-15N], 1 mM; H2O 95%; D2O 5%; sodium phosphate 20 mM; sodium chloride 20 mM; NaN3 0.02%
sample_conditions_1: ionic strength: 20 mM; pH: 6.9; pressure: 1 atm; temperature: 323 K
Experiments:
| Name | Sample | Sample state | Sample conditions |
|---|---|---|---|
| 2D 1H-15N HSQC | sample_1 | isotropic | sample_conditions_1 |
| 2D 1H-13C HSQC | sample_1 | isotropic | sample_conditions_1 |
| 3D HNCA | sample_1 | isotropic | sample_conditions_1 |
| 3D HNCACB | sample_1 | isotropic | sample_conditions_1 |
| 3D CBCA(CO)NH | sample_1 | isotropic | sample_conditions_1 |
| 3D HCCH-TOCSY | sample_1 | isotropic | sample_conditions_1 |
| 3D 1H-15N NOESY | sample_1 | isotropic | sample_conditions_1 |
| 3D 1H-13C NOESY aliphatic | sample_1 | isotropic | sample_conditions_1 |
| 3D 1H-13C NOESY aromatic | sample_1 | isotropic | sample_conditions_1 |
Software:
CYANA v3.0, Guntert, Mumenthaler and Wuthrich - structure solution
NMRPipe, Delaglio, Grzesiek, Vuister, Zhu, Pfeifer and Bax - processing
TOPSPIN, Bruker Biospin - collection
NMRView, Johnson, One Moon Scientific - data analysis
SPARKY, Goddard - data analysis
ARIA v2.2, Linge, O'Donoghue and Nilges - structure solution
NMR spectrometers:
- Bruker Avance various MHz
Related Database Links:
| UNP | P12978 |
| PDB | |
| DBJ | BAP94392 BAQ20285 |
| EMBL | CAA24877 CAD53395 CEP79167 CEQ32332 CEQ32414 |
| GB | AAA45903 AAY41099 AFY97831 AFY97916 AGL80643 |
| REF | YP_401644 |
| SP | P12978 Q3KSV2 |
Download simulated HSQC data in one of the following formats:
CSV: Backbone
or all simulated shifts
SPARKY: Backbone
or all simulated shifts