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:

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

Assembly:

Entity Assembly IDEntity NameEntity ID
1NHERF1_(150-358)1

Entities:

Entity 1, NHERF1_(150-358) 216 residues - 23669.648 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   GLUILEGLNLYSGLUASNSERARGGLUALA
14   LEUALAGLUALAALALEUGLUSERPROARG
15   PROALALEUVALARGSERALASERSERASP
16   THRSERGLUGLULEUASNSERGLNASPSER
17   PROPROLYSGLNASPSERTHRALAPROSER
18   SERTHRSERSERSERASPPROILELEUASP
19   PHEASNILESERLEUALAMETALALYSGLU
20   ARGALAHISGLNLYSARGSERSERLYSARG
21   ALAPROGLNMETASPTRPSERLYSLYSASN
22   GLULEUPHESERASNLEU

Samples:

sample_1: NHERF1 (150-358), [U-100% 13C; U-100% 15N], 557 uM; HEPES 20 mM; sodium chloride 150 mM; DTT 0.5 mM; PMSF 0.1 mM; D2O 10%

sample_2: NHERF1 (150-358), [U-100% 13C; U-100% 15N; U-80% 2H], 389 uM; HEPES 20 mM; sodium chloride 150 mM; DTT 0.5 mM; PMSF 0.1 mM; D2O 10%

sample_3: NHERF1 (150-358), [U-100% 13C; U-100% 15N]-Leu,Val,Phe, 413 uM; HEPES 20 mM; sodium chloride 150 mM; DTT 0.5 mM; PMSF 0.1 mM; D2O 10%

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 CBCA(CO)NHsample_1isotropicsample_conditions_1
3D HNCAsample_1isotropicsample_conditions_1
3D HN(CO)CAsample_1isotropicsample_conditions_1
3D HNCOsample_1isotropicsample_conditions_1
3D HNCACBsample_2isotropicsample_conditions_1
3D HNCACBsample_3isotropicsample_conditions_1
3D 1H-15N NOESYsample_1isotropicsample_conditions_1
3D 1H-13C NOESYsample_1isotropicsample_conditions_1
3D 1H-15N NOESYsample_3isotropicsample_conditions_1
3D 1H-13C NOESYsample_3isotropicsample_conditions_1
3D H(CCO)NHsample_1isotropicsample_conditions_1
3D HCCH-TOCSYsample_1isotropicsample_conditions_1
3D HCCH-COSYsample_1isotropicsample_conditions_1

Software:

TOPSPIN v2.1.3, Bruker Biospin - collection, processing

CARA v1.5, Keller and Wuthrich - chemical shift assignment, data analysis

CYANA v2.1, Guntert, Mumenthaler and Wuthrich - structure solution

X-PLOR NIH v2.24, Schwieters, Kuszewski, Tjandra and Clore - refinement, structure solution

NMR spectrometers:

  • Bruker Avance 900 MHz
  • Bruker Avance 700 MHz

Related Database Links:

BMRB 16637 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