BMRB Entry 17967
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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/BMR17967
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Title: Structure of the monomeric N-terminal domain of HPV16 E6 oncoprotein PubMed: 22483108
Deposition date: 2011-09-30 Original release date: 2012-04-04
Authors: Zanier, Katia; ould M, Abdellahi; 17967, .; 17967, .; 17967, .; 17967, .; 17967, .; 17967, .; 17967, .
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:
E6, polymer, 84 residues, 9898.498 Da.
ZN, non-polymer, 65.409 Da.
Natural source: Common Name: HPV 16 Taxonomy ID: 333760 Superkingdom: not available Kingdom: Alphapapillomavirus Genus/species: Human papillomavirus 16 not available
Experimental source: Production method: recombinant technology Host organism: Escherichia coli
Entity Sequences (FASTA):
E6: GAMFQDPQERPRKLPQLCTE
LQTTIHDIILECVYCKQQLL
RREVYDFARRDLCIVYRDGN
PYAVCDKCLKFYSKISEYRH
YSYS
- assigned_chemical_shifts
| Data type | Count |
| 13C chemical shifts | 264 |
| 15N chemical shifts | 83 |
| 1H chemical shifts | 554 |
Additional metadata:
Assembly:
| Entity Assembly ID | Entity Name | Entity ID |
|---|---|---|
| 1 | N-terminal domain of HPV16 E6 oncoprotein | 1 |
| 2 | ZINC ION | 2 |
Entities:
Entity 1, N-terminal domain of HPV16 E6 oncoprotein 84 residues - 9898.498 Da.
The natural E6 sequence starts at M1. Residues G-1 and A0 are introduced for colning purposes.
| 1 | GLY | ALA | MET | PHE | GLN | ASP | PRO | GLN | GLU | ARG | ||||
| 2 | PRO | ARG | LYS | LEU | PRO | GLN | LEU | CYS | THR | GLU | ||||
| 3 | LEU | GLN | THR | THR | ILE | HIS | ASP | ILE | ILE | LEU | ||||
| 4 | GLU | CYS | VAL | TYR | CYS | LYS | GLN | GLN | LEU | LEU | ||||
| 5 | ARG | ARG | GLU | VAL | TYR | ASP | PHE | ALA | ARG | ARG | ||||
| 6 | ASP | LEU | CYS | ILE | VAL | TYR | ARG | ASP | GLY | ASN | ||||
| 7 | PRO | TYR | ALA | VAL | CYS | ASP | LYS | CYS | LEU | LYS | ||||
| 8 | PHE | TYR | SER | LYS | ILE | SER | GLU | TYR | ARG | HIS | ||||
| 9 | TYR | SER | TYR | SER |
Entity 2, ZINC ION - Zn - 65.409 Da.
| 1 | ZN |
Samples:
E6_unl: E6 1 mM; H2O 90%; D2O 10%; sodium phosphate 20 mM; NaCl 50 mM; DTT 2 mM
E6_CN: E6, [U-100% 13C; U-100% 15N], 1 mM; H2O 90%; D2O 10%
E6_N: E6, [U-100% 15N], 1 mM; H2O 90%; D2O 10%
E6_conditions: ionic strength: 50 mM; pH: 6.8; pressure: 1 atm; temperature: 296 K
Experiments:
| Name | Sample | Sample state | Sample conditions |
|---|---|---|---|
| 2D 1H-15N HSQC | E6_N | isotropic | E6_conditions |
| 2D 1H-13C HSQC aliphatic | E6_CN | isotropic | E6_conditions |
| 2D 1H-13C HSQC aromatic | E6_CN | isotropic | E6_conditions |
| 3D HNCA | E6_CN | isotropic | E6_conditions |
| 3D HNCACB | E6_CN | isotropic | E6_conditions |
| 3D HN(CO)CA | E6_CN | isotropic | E6_conditions |
| 3D HBHA(CO)NH | E6_CN | isotropic | E6_conditions |
| 3D HCCH-TOCSY | E6_CN | isotropic | E6_conditions |
| 3D HCCH-COSY | E6_CN | isotropic | E6_conditions |
| 3D 1H-15N NOESY | E6_N | isotropic | E6_conditions |
| 3D 1H-13C NOESY aliphatic | E6_CN | isotropic | E6_conditions |
| 2D 1H-1H NOESY | E6_unl | isotropic | E6_conditions |
| 2D 1H-1H NOESY | E6_unl | isotropic | E6_conditions |
Software:
TOPSPIN v2.1, Bruker Biospin - collection
NMRPipe, Delaglio, Grzesiek, Vuister, Zhu, Pfeifer and Bax - processing
CARA v1.8.3, Keller and Wuthrich - data analysis
ATHNOS-CANDID, Herrmann, Guntert and Wuthrich - automatic noe assignment, peak picking
X-PLOR NIH, Schwieters, Kuszewski, Tjandra and Clore - structure solution
NMR spectrometers:
- Bruker DRX 600 MHz
- Bruker Avance 800 MHz
Related Database Links:
| BMRB | 17968 |
| PDB | |
| DBJ | BAN15903 BAN15905 BAN15906 BAN15907 BAN15908 |
| EMBL | CAB45104 CAB45106 CAB45112 CAB45114 CAB45124 |
| GB | AAA46939 AAA91658 AAA91668 AAA91670 AAA91673 |
| 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