BMRB

Biological Magnetic Resonance Data Bank


A Repository for Data from NMR Spectroscopy on Proteins, Peptides, Nucleic Acids, and other Biomolecules
Member of WWPDB

BMRB Entry 16637

Title: Solution Structure of extended PDZ2 Domain from NHERF1 (150-270)   PubMed: 20042604

Deposition date: 2009-12-18 Original release date: 2010-02-01

Authors: Bhattacharya, Shibani; Dai, Zhongping; Li, Jianquan; Baxter, Sabine; Callaway, David; Cowburn, David; Bu, Zimei

Citation: Bhattacharya, Shibani; Dai, Zhongping; Li, Jianquan; Baxter, Sabine; Callaway, David; Cowburn, David; Bu, Zimei. "A conformational switch in the scaffolding protein NHERF1 controls autoinhibition and complex formation."  J. Biol. Chem. 285, 9981-9994 (2010).

Assembly members:
PDZ2-270, polymer, 128 residues, 14101.081 Da.

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

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

Entity Sequences (FASTA):
PDZ2-270: GIDPFTMLRPRLCTMKKGPS GYGFNLHSDKSKPGQFIRSV DPDSPAEASGLRAQDRIVEV NGVCMEGKQHGDVVSAIRAG GDETKLLVVDRETDEFFKKC RVIPSQEHLNGPLPVPFTNG EIQKENSR

Data sets:
Data typeCount
13C chemical shifts495
15N chemical shifts123
1H chemical shifts845

Additional metadata:

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

Related Database Links:

BMRB 15567 16638 18826
PDB 2JXO 2KJD 2KRG 2M0V 2OZF 4Q3H
DBJ BAG54683
GB EAW89189 EHH58322

Download simulated HSQC data in one of the following formats:
CSV: Backbone or all simulated shifts
SPARKY: Backbone or all simulated shifts