BMRB Entry 17968
Click here to enlarge.
PDB ID: 2ljy
Entry in NMR Restraints Grid
Validation report in NRG-CING
Chem Shift validation: AVS_full, LACS, SPARTA
BMRB Entry DOI: doi:10.13018/BMR17968
MolProbity Validation Chart
NMR-STAR file interactive viewer.
NMR-STAR v3 text file.
NMR-STAR v2.1 text file (deprecated)
XML gzip file.
RDF gzip file.
All files associated with the entry
Title: Haddock model structure of the N-terminal domain dimer of HPV16 E6 PubMed: 22483108
Deposition date: 2011-09-30 Original release date: 2012-04-04
Authors: Zanier, Katia; ould M, Abdellahi; 17968, .; 17968, .; 17968, .; 17968, .; 17968, .; 17968, .; 17968, .
Citation: Zanier, Katia; Boulade-Ladame, Abdellahi; Rybin, Charlotte; Chappelle, Vladimir; Atkinson, Anne; Kieffer, Andrew; Trave, Bruno. "Solution structure analysis of the HPV16 E6 oncoprotein reveals a self-association mechanism required for E6-mediated degradation of p53." Structure 20, 604-617 (2012).
Assembly members:
HPV16_E6, polymer, 82 residues, 8505.967 Da.
ZN, non-polymer, 65.409 Da.
Natural source: Common Name: Human papillomavirus type 16 Taxonomy ID: 333760 Superkingdom: Viruses Kingdom: not available Genus/species: Alphapapillomavirus Human papillomavirus 16
Experimental source: Production method: recombinant technology Host organism: Escherichia coli
Entity Sequences (FASTA):
HPV16_E6: GAMFQDPQERPRKLPQLCTE
LQTTIHDIILECVYCKQQLL
RREVYDFAFRDLCIVYRDGN
PYAVCDKCLKFYSKISEYRH
YS
- assigned_chemical_shifts
Data type | Count |
13C chemical shifts | 259 |
15N chemical shifts | 83 |
1H chemical shifts | 549 |
Additional metadata:
Related Database Links:
BMRB | 17967 |
PDB | 2LJX 2LJY 4GIZ |
DBJ | BAN15903 BAN15904 BAN15905 BAN15906 BAN15907 |
EMBL | CAB45104 CAB45106 CAB45108 CAB45110 CAB45112 |
GB | AAA46939 AAA91654 AAA91655 AAA91656 AAA91657 |
REF | NP_041325 |
SP | P03126 |
Download simulated HSQC data in one of the following formats:
CSV: Backbone
or all simulated shifts
SPARKY: Backbone
or all simulated shifts