BMRB Entry 16637

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

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).
PubMed: 20042604

Assembly members:

Assembly members:
PDZ2-270, polymer, 128 residues, 14101.081 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: pET151/D-TOPO

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

Additional metadata:

  • Assembly
  • Samples and Experiments
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  • Spectrometers
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Assembly:

Entity Assembly IDEntity NameEntity ID
1PDZ2-2701

Entities:

Entity 1, PDZ2-270 128 residues - 14101.081 Da.

Residues 1-7 represent a non-native affinity tag

1   GLYILEASPPROPHETHRMETLEUARGPRO
2   ARGLEUCYSTHRMETLYSLYSGLYPROSER
3   GLYTYRGLYPHEASNLEUHISSERASPLYS
4   SERLYSPROGLYGLNPHEILEARGSERVAL
5   ASPPROASPSERPROALAGLUALASERGLY
6   LEUARGALAGLNASPARGILEVALGLUVAL
7   ASNGLYVALCYSMETGLUGLYLYSGLNHIS
8   GLYASPVALVALSERALAILEARGALAGLY
9   GLYASPGLUTHRLYSLEULEUVALVALASP
10   ARGGLUTHRASPGLUPHEPHELYSLYSCYS
11   ARGVALILEPROSERGLNGLUHISLEUASN
12   GLYPROLEUPROVALPROPHETHRASNGLY
13   GLUILEGLNLYSGLUASNSERARG

Related Database Links:

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

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