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 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

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

Samples:

sample_1: PDZ2-270, [U-100% 13C; U-100% 15N], 550 uM; HEPES 20 mM; DTT 0.5 mM; PMSF 0.1 mM; sodium chloride 150 mM

sample_conditions_1: pH: 7.5; pressure: 1 atm; temperature: 303 K

Experiments:

NameSampleSample stateSample conditions
2D 1H-15N HSQCsample_1isotropicsample_conditions_1
2D 1H-13C HSQCsample_1isotropicsample_conditions_1
3D HNCACBsample_1isotropicsample_conditions_1
3D HCCH-TOCSYsample_1isotropicsample_conditions_1
3D H(CCO)NHsample_1isotropicsample_conditions_1
3D 1H-15N NOESYsample_1isotropicsample_conditions_1
3D 1H-13C NOESYsample_1isotropicsample_conditions_1

Software:

CYANA v1.3, Guntert, Mumenthaler and Wuthrich - structure solution

ARIA v2.2, Linge, O, . - refinement, structure solution

CARA v1.5, Keller and Wuthrich - data analysis

TOPSPIN v2.1, Bruker Biospin - collection, processing

TALOS, Cornilescu, Delaglio and Bax - Dihedral Angle Calculation

NMR spectrometers:

  • Bruker Avance 800 MHz
  • Bruker Avance 900 MHz

Related Database Links:

BMRB 15567 16638 18826
PDB
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