BMRB

Biological Magnetic Resonance Data Bank


A Repository for Data from NMR Spectroscopy on Proteins, Peptides, Nucleic Acids, and other Biomolecules
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BMRB Entry 16638

Title: Solution Structure of human sodium/ hydrogen exchange regulatory factor 1(150-358).   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:
NHERF1_(150-358), polymer, 216 residues, 23669.648 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):
NHERF1_(150-358): GIDPFTMLRPRLCTMKKGPS GYGFNLHSDKSKPGQFIRSV DPDSPAEASGLRAQDRIVEV NGVCMEGKQHGDVVSAIRAG GDETKLLVVDRETDEFFKKC RVIPSQEHLNGPLPVPFTNG EIQKENSREALAEAALESPR PALVRSASSDTSEELNSQDS PPKQDSTAPSSTSSSDPILD FNISLAMAKERAHQKRSSKR APQMDWSKKNELFSNL

Data sets:
Data typeCount
13C chemical shifts758
15N chemical shifts174
1H chemical shifts1241

Additional metadata:

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Related Database Links:

BMRB 16637 18826
PDB 2KJD 2KRG 2M0V
DBJ BAG54683
GB EAW89189 EHH58322

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