BMRB Entry 25865

Click here to enlarge.

PDB ID:
Entry in NMR Restraints Grid
Validation report in NRG-CING
Chem Shift validation: AVS_full, SPARTA
BMRB Entry DOI: doi:10.13018/BMR25865
MolProbity Validation Chart

NMR-STAR file interactive viewer.
NMR-STAR v3 text file.
XML gzip file.
RDF gzip file.
All files associated with the entry

Title:
Solution Structure of the rNedd4 WW2 Domain-Cx43CT Peptide Complex by NMR
Deposition date:
2015-10-27
Original release date:
2016-02-22
Authors:
Spagnol, Gaelle; Kieken, Fabien; Sorgen, Paul
Citation:

Citation: Spagnol, Gaelle; Kieken, Fabien; Kopanic, Jennifer; Li, Hanjun; Zach, Sydney; Stauch, Kelly; Grosely, Rosslyn; Sorgen, Paul. "Structural Studies of the Nedd4 WW Domains and their Selectivity for the Cx43 Carboxyl-terminus"  J. Biol. Chem. 291, 7637-7650 (2016).
PubMed: 26841867

Assembly members:

Assembly members:
rNedd4_WW2, polymer, 39 residues, 4436.736 Da.
Cx43CT_peptide, polymer, 14 residues, 1617.726 Da.

Natural source:

Natural source:   Common Name: Rat   Taxonomy ID: 10116   Superkingdom: Eukaryota   Kingdom: Metazoa   Genus/species: Rattus norvegicus

Experimental source:

Experimental source:   Production method: recombinant technology   Host organism: Escherichia coli   Vector: pGEX-KT

Entity Sequences (FASTA):

Entity Sequences (FASTA):
rNedd4_WW2: GSSSGLPPGWEEKQDDRGRS YYVDHNSKTTTWSKPTMQD
Cx43CT_peptide: APLXPMXPPGYKLV

Data sets:
Data typeCount
13C chemical shifts119
15N chemical shifts35
1H chemical shifts266

Additional metadata:

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

Assembly:

Entity Assembly IDEntity NameEntity ID
1rNedd4 WW2 Domain1
2Cx43CT Peptide2

Entities:

Entity 1, rNedd4 WW2 Domain 39 residues - 4436.736 Da.

1   GLYSERSERSERGLYLEUPROPROGLYTRP
2   GLUGLULYSGLNASPASPARGGLYARGSER
3   TYRTYRVALASPHISASNSERLYSTHRTHR
4   THRTRPSERLYSPROTHRMETGLNASP

Entity 2, Cx43CT Peptide 14 residues - 1617.726 Da.

1   ALAPROLEUSEPPROMETSEPPROPROGLY
2   TYRLYSLEUVAL

Samples:

sample_1: rNedd4 WW2, [U-98% 13C; U-98% 15N], 0.6 mM; Cx43CT peptide 13 mM; potassium phosphate 1.8 mM; DTT 1 mM; sodium chloride 137 mM; potassium chloride 2.7 mM; sodium phosphate 10 mM

sample_conditions_1: ionic strength: 156 mM; pH: 7.5; pressure: 1 atm; temperature: 298 K

Experiments:

NameSampleSample stateSample conditions
2D 1H-15N HSQCsample_1isotropicsample_conditions_1
2D 1H-13C HSQC aliphaticsample_1isotropicsample_conditions_1
3D HNHAsample_1isotropicsample_conditions_1
3D HNCACBsample_1isotropicsample_conditions_1
3D CBCA(CO)NHsample_1isotropicsample_conditions_1
3D 1H-15N NOESYsample_1isotropicsample_conditions_1
3D 1H-13C NOESY aliphaticsample_1isotropicsample_conditions_1
3D 1H-13C NOESY aromaticsample_1isotropicsample_conditions_1

Software:

ARIA v1.1, Dr. Michael Nilges, Institut Pasteur - geometry optimization, refinement, structure solution

NMRPipe, Delaglio, Grzesiek, Vuister, Zhu, Pfeifer and Bax - processing

NMRView, Johnson, One Moon Scientific - chemical shift assignment, data analysis, peak picking

NMRDraw, F. Delaglio, S. Grzesiek, G. W. Vuister, G. Zhu, J. Pfeifer and A. Bax - processing

NMR spectrometers:

  • Varian INOVA 600 MHz

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