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 16602

Title: 1H, 13C and 15N Chemical Shift Assignment Assignment of Human Membrane Protein KCNE3 in LMPC micelles   PubMed: 20044833

Deposition date: 2009-11-09 Original release date: 2010-02-11

Authors: Kang, Congbao; Vanoye, Carlos; Sakakura, Masayoshi; Welch, Richard; Sanders, Charles

Citation: Kang, Congbao; Vanoye, Carlos; Welch, Richard; Van Horn, Wade; Sanders, Charles. "Functional delivery of a membrane protein into oocyte membranes using bicelles."  Biochemistry 49, 653-655 (2010).

Assembly members:
KCNE3, polymer, 112 residues, Formula weight is not available

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):
KCNE3: MGHHHHHHGMETTNGTETWY ESLHAVLKALNATLHSNLLC RPGPGLGPDNQTEERRASLP GRDDNSYMYILFVMFLFAVT VGSLILGYTRSRKVDKRSDP YHVYIKNRVSMI

Data sets:
Data typeCount
13C chemical shifts264
15N chemical shifts91
1H chemical shifts108

Additional metadata:

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

Entity Assembly IDEntity NameEntity ID
1KCNE31

Entities:

Entity 1, KCNE3 112 residues - Formula weight is not available

The first nine residues are an affinity tag used in protein purification

1   METGLYHISHISHISHISHISHISGLYMET
2   GLUTHRTHRASNGLYTHRGLUTHRTRPTYR
3   GLUSERLEUHISALAVALLEULYSALALEU
4   ASNALATHRLEUHISSERASNLEULEUCYS
5   ARGPROGLYPROGLYLEUGLYPROASPASN
6   GLNTHRGLUGLUARGARGALASERLEUPRO
7   GLYARGASPASPASNSERTYRMETTYRILE
8   LEUPHEVALMETPHELEUPHEALAVALTHR
9   VALGLYSERLEUILELEUGLYTYRTHRARG
10   SERARGLYSVALASPLYSARGSERASPPRO
11   TYRHISVALTYRILELYSASNARGVALSER
12   METILE

Samples:

sample_KCNE3: D2O 10%; DTT 2 mM; EDTA 2 mM; imidazole 250 mM; LMPC 10%; KCNE3, [U-100% 13C; U-100% 15N; U-80% 2H], 0.8 mM

sample_conditions_1: ionic strength: 0.25 M; pH: 6.5; pressure: 1 atm; temperature: 313 K

Experiments:

NameSampleSample stateSample conditions
2D TROSY-1H-15N HSQCsample_KCNE3isotropicsample_conditions_1
3D TROSY-HNCAsample_KCNE3isotropicsample_conditions_1
3D TROSY-CBCA(CO)NHsample_KCNE3isotropicsample_conditions_1
3DTROSY- HN(CO)CAsample_KCNE3isotropicsample_conditions_1
3D TROSYHNCACBsample_KCNE3isotropicsample_conditions_1

Software:

NMRPipe, Delaglio, Grzesiek, Vuister, Zhu, Pfeifer and Bax - processing

NMRView, Johnson, One Moon Scientific - chemical shift assignment

NMR spectrometers:

  • Bruker Avance 800 MHz

Related Database Links:

BMRB 16621
DBJ BAG34817
EMBL CAG33490 CAI56768
GB AAD28089 AAG16255 AAI10613 AAI13744 ABB00304
REF NP_005463 XP_001115704 XP_001174917 XP_002822287 XP_003777893
SP Q9Y6H6

Download simulated HSQC data in one of the following formats:
CSV: Backbone or all simulated shifts
SPARKY: Backbone or all simulated shifts