BMRB Entry 51200

Title:
WWOX-WW1WW2-PY3
Deposition date:
2021-11-30
Original release date:
2022-10-12
Authors:
Adamsky-Keinan, Keren; Rotem-Bamberger, Shahar; Shalev, Deborah; Schueler-Furman, Ora; Chill, Jordan
Citation:

Citation: Rotem-Bamberger, Shahar; Fahoum, Jamal; Keinan-Adamsky, Keren; Tsaban, Tomer; Avraham, Orly; Shalev, Deborah; Chill, Jordan; Schueler-Furman, Ora. "Structural insights into the role of the WW2 domain on tandem WW-PPxY motif interactions of oxidoreductase WWOX"  J. Biol. Chem. 298, 102145-102145 (2022).
PubMed: 35716775

Assembly members:

Assembly members:
entity_1, polymer, 80 residues, 9379.28 Da.
entity_2, polymer, 13 residues, 1503.73 Da.

Natural source:

Natural source:   Common Name: Human   Taxonomy ID: 9606   Superkingdom: Eukaryota   Kingdom: Metazoa   Genus/species: Homo sapiens

Experimental source:

Experimental source:   Production method: recombinant technology   Host organism: Escherichia coli   Vector: pETM 30

Entity Sequences (FASTA):

Data sets:
Data typeCount
15N chemical shifts59
1H chemical shifts62

Additional metadata:

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

Assembly:

Entity Assembly IDEntity NameEntity ID
1WW1WW21
2PY32

Entities:

Entity 1, WW1WW2 80 residues - 9379.28 Da.

1   GLYALAMETGLYASPGLULEUPROPROGLY
2   TRPGLUGLUARGTHRTHRLYSASPGLYTRP
3   VALTYRTYRALAASNHISTHRGLUGLULYS
4   THRGLNTRPGLUHISPROLYSTHRGLYLYS
5   ARGLYSARGVALALAGLYASPLEUPROTYR
6   GLYTRPGLUGLNGLUTHRASPGLUASNGLY
7   GLNVALPHEPHEVALASPHISILEASNLYS
8   ARGTHRTHRTYRLEUASPPROARGLEUALA

Entity 2, PY3 13 residues - 1503.73 Da.

numbering is according to the ErbB4 sequence

1   GLYTHRVALLEUPROPROPROPROTYRARG
2   HISARGASN

Samples:

sample_1: H2O 93 ± 1 %; D2O, [U-99% 2H], 7 ± 1 %; sodium phosphate 20 ± 1 mM; sodium chloride 100 ± 1 mM; AEBSF protease inhibitor 0.1 ± 0.01 %; WW1WW2, [U-99% 13C; U-99% 15N], 0.2 ± 0.005 mM; PY3 0.4 ± 0.01 mM

sample_conditions_1: ionic strength: 0.032 M; pH: 6.8; pressure: 1 atm; temperature: 286 K

Experiments:

NameSampleSample stateSample conditions
2D 1H-15N HSQCsample_1isotropicsample_conditions_1
3D HN(CO)CACBsample_1isotropicsample_conditions_1
3D HNCACBsample_1isotropicsample_conditions_1
3D HNCAsample_1isotropicsample_conditions_1
3D 1H-15N NOESYsample_1isotropicsample_conditions_1

Software:

TOPSPIN v3.6 - chemical shift assignment, collection

NMR spectrometers:

  • Bruker DRX 700 MHz

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