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Biological Magnetic Resonance Data Bank


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BMRB Entry 18817

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PDB ID:
Entry in NMR Restraints Grid
Validation report in NRG-CING
Chem Shift validation: AVS_full, LACS, SPARTA
BMRB Entry DOI: doi:10.13018/BMR18817
MolProbity Validation Chart

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Title: Solution NMR analysis of intact KCNE2 in detergent micelles demonstrate a straight transmembrane helix   PubMed: 24827085

Deposition date: 2012-11-01 Original release date: 2014-04-28

Authors: Lai, Chaohua; Li, Pan; Chen, Liu; Zhang, Longhua; Wu, Fangming; Tian, Changlin

Citation: Li, Pan; Liu, Haowen; Lai, Chaohua; Sun, Peibei; Zeng, Wenping; Wu, Fangming; Zhang, Longhua; Wang, Sheng; Tian, Changlin; Ding, Jiuping. "Differential modulations of KCNQ1 by auxiliary proteins KCNE1 and KCNE2."  Sci. Rep. 4, 4973-4973 (2014).

Assembly members:
KCNE2, polymer, 123 residues, 14486.612 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):
KCNE2: MSTLSNFTQTLEDVFRRIFI TYMDNWRQNTTAEQEALQAK VDAENFYYVILYLMVMIGMF SFIIVAILVSTVKSKRREHS NDPYHQYIVEDWQEKYKSQI LNLEESKATIHENIGAAGFK MSP

Data sets:
Data typeCount
13C chemical shifts340
15N chemical shifts104
1H chemical shifts133

Additional metadata:

  • Assembly
  • Samples and Experiments
  • Software
  • Spectrometers
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Assembly:

Entity Assembly IDEntity NameEntity ID
1KCNE21

Entities:

Entity 1, KCNE2 123 residues - 14486.612 Da.

1   METSERTHRLEUSERASNPHETHRGLNTHR
2   LEUGLUASPVALPHEARGARGILEPHEILE
3   THRTYRMETASPASNTRPARGGLNASNTHR
4   THRALAGLUGLNGLUALALEUGLNALALYS
5   VALASPALAGLUASNPHETYRTYRVALILE
6   LEUTYRLEUMETVALMETILEGLYMETPHE
7   SERPHEILEILEVALALAILELEUVALSER
8   THRVALLYSSERLYSARGARGGLUHISSER
9   ASNASPPROTYRHISGLNTYRILEVALGLU
10   ASPTRPGLNGLULYSTYRLYSSERGLNILE
11   LEUASNLEUGLUGLUSERLYSALATHRILE
12   HISGLUASNILEGLYALAALAGLYPHELYS
13   METSERPRO

Samples:

15N-labeled: KCNE2, [U-15N], 1.0 mM; H2O 90%; D2O, [U-2H], 10%

15N-13C-labeled: KCNE2, [U-13C; U-15N], 1.0 mM; H2O 90%; D2O, [U-2H], 10%

15N-13C-2H-labeled: KCNE2, [U-13C; U-15N; U-2H], 1.0 mM; H2O 90%; D2O, [U-2H], 10%

sample_conditions_1: ionic strength: 50 mM; pH: 6.0; pressure: 1 atm; temperature: 308 K

Experiments:

NameSampleSample stateSample conditions
2D 1H-15N HSQC15N-labeledisotropicsample_conditions_1
2D 1H-15N HSQC15N-13C-labeledisotropicsample_conditions_1
2D 1H-15N HSQC15N-13C-2H-labeledisotropicsample_conditions_1
3D HNCO15N-13C-2H-labeledisotropicsample_conditions_1
3D HNCA15N-13C-2H-labeledisotropicsample_conditions_1
3D HN(CO)CA15N-13C-2H-labeledisotropicsample_conditions_1
3D HNCACB15N-13C-2H-labeledisotropicsample_conditions_1
3D HN(CO)CACB15N-13C-2H-labeledisotropicsample_conditions_1
3D HBHA(CO)NH15N-13C-labeledisotropicsample_conditions_1
3D 1H-15N NOESY15N-labeledisotropicsample_conditions_1

Software:

NMRPipe, Delaglio, Grzesiek, Vuister, Zhu, Pfeifer and Bax - data analysis

NMRView, Johnson, One Moon Scientific - chemical shift assignment

X-PLOR NIH, Schwieters, Kuszewski, Tjandra and Clore - structure solution

NMR spectrometers:

  • Bruker DMX 600 MHz
  • Bruker DMX 800 MHz

Related Database Links:

PDB
DBJ BAI47314
GB AAD28086 AAG13416 AAH93892 AAI12088 AAP72955
REF NP_751951 XP_001167300 XP_002830704 XP_003263935 XP_003824018
SP Q9Y6J6

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CSV: Backbone or all simulated shifts
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