BMRB Entry 18967

Title:
Solution structure of the C-terminal zinc-binding domain of HPV51 oncoprotein E6   PubMed: 23638119
Deposition date:
2013-01-21
Original release date:
2013-05-13
Authors:
Mischo, Andre; Ohlenschlager, Oliver; Gorlach, Matthias
Citation:

Citation: Mischo, Andre; Ohlenschlager, Oliver; Hortschansky, Peter; Ramachandran, Ramadurai; Gorlach, Matthias. "Structural insights into a wildtype domain of the oncoprotein E6 and its interaction with a PDZ domain"  PLOS One 8, e62584-e62584 (2013).

Assembly members:

Assembly members:
E6, polymer, 76 residues, 8951.278 Da.
ZINC ION, non-polymer, 65.409 Da.

Natural source:

Natural source:   Common Name: Human papillomavirus HPV   Taxonomy ID: 10566   Superkingdom: Viruses   Kingdom: not available   Genus/species: Human papillomavirus

Experimental source:   Production method: recombinant technology   Host organism: Escherichia coli   Vector: pET15B

Experimental source:

Natural source:   Common Name: Human papillomavirus HPV   Taxonomy ID: 10566   Superkingdom: Viruses   Kingdom: not available   Genus/species: Human papillomavirus

Experimental source:   Production method: recombinant technology   Host organism: Escherichia coli   Vector: pET15B

Entity Sequences (FASTA):

Data sets:
Data typeCount
13C chemical shifts337
15N chemical shifts80
1H chemical shifts527

Additional metadata:

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

Assembly:

Entity Assembly IDEntity NameEntity ID
1E61
2ZINC ION2

Entities:

Entity 1, E6 76 residues - 8951.278 Da.

Residues 1-4 represent a non-native sequence originating from protease cleavage

1   GLYSERHISMETSERARGSERVALTYRGLY
2   THRTHRLEUGLUALAILETHRLYSLYSSER
3   LEUTYRASPLEUSERILEARGCYSHISARG
4   CYSGLNARGPROLEUGLYPROGLUGLULYS
5   GLNLYSLEUVALASPGLULYSLYSARGPHE
6   HISGLUILEALAGLYARGTRPTHRGLYGLN
7   CYSALAASNCYSTRPGLNARGTHRARGGLN
8   ARGASNGLUTHRGLNVAL

Entity 2, ZINC ION - Zn - 65.409 Da.

1   ZN

Samples:

sample_1: E6, [U-100% 13C; U-100% 15N], 1.13 mM; sodium chloride 90 mM; L-arginine 45 mM; L-glutamate 45 mM; DTT 9 mM; sodium azide 0.05 w/v; H2O 90%; D2O 10%

sample_2: E6, [U-100% 13C; U-100% 15N], 0.9 mM; sodium chloride 90 mM; L-arginine 45 mM; L-glutamate 45 mM; DTT 9 mM; sodium azide 0.05 w/v; D2O 100%

sample_conditions_1: ionic strength: 180 mM; pH: 7.4; pressure: 1 atm; temperature: 283 K

Experiments:

NameSampleSample stateSample conditions
2D 1H-15N HSQCsample_1isotropicsample_conditions_1
2D 1H-13C HSQC aliphaticsample_1isotropicsample_conditions_1
2D 1H-13C HSQC aromaticsample_2isotropicsample_conditions_1
3D HNCACBsample_1isotropicsample_conditions_1
3D HNHAsample_1isotropicsample_conditions_1
3D 1H-15N NOESYsample_1isotropicsample_conditions_1
2D 1H-13C HSQC aliphaticsample_2isotropicsample_conditions_1
2D 1H-13C HSQC aromaticsample_2isotropicsample_conditions_1
3D HCCH-COSYsample_2isotropicsample_conditions_1
3D HNCOsample_1isotropicsample_conditions_1

Software:

CYANA v3, Guntert, Mumenthaler and Wuthrich - structure solution

CNS, Brunger, Adams, Clore, Gros, Nilges and Read - refinement

CARA, Keller and Wuthrich - data analysis

TOPSPIN, Bruker Biospin - collection & processing

NMR spectrometers:

  • Bruker AvanceIII 750 MHz
  • Bruker AvanceIII 600 MHz

Related Database Links:

UniProtKB P26554
PDB
EMBL CRH69907
GB ALJ32861 ALJ32868 ALJ32875 ALJ32882 ALJ32889
SP P26554

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