BMRB Entry 19426

Chem Shift validation: AVS_full, LACS
BMRB Entry DOI: doi:10.13018/BMR19426

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Title:
1H, 13C, and 15N Chemical Shift Assignments for a peptide encompassing the first 61 residues of the Kv1.4 channel
Deposition date:
2013-08-14
Original release date:
2014-02-12
Authors:
Ohlenschlager, Oliver; Heinemann, Stefan; Goradia, Nishit; Sahoo, Nirakar
Citation:

Citation: Sahoo, Nirakar; Goradia, Nishit; Ohlenschlager, Oliver; Schonherr, Roland; Friedrich, Manfred; Plass, Winfried; Kappl, Reinhard; Hoshi, Toshinori; Heinemann, Stefan. "Heme impairs the ball-and-chain inactivation of potassium channels."  Proc. Natl. Acad. Sci. U.S.A. 110, E4036-E4044 (2013).
PubMed: 24082096

Assembly members:

Assembly members:
kv14_pep61, polymer, 63 residues, 6076.6 Da.

Natural source:

Natural source:   Common Name: Rat   Taxonomy ID: 10116   Superkingdom: Eukaryota   Kingdom: Metazoa   Genus/species: Rattus norvegicus

Experimental source:

Experimental source:   Production method: recombinant technology   Host organism: Escherichia coli   Vector: pETM-41

Entity Sequences (FASTA):

Entity Sequences (FASTA):
kv14_pep61: GAMEVAMVSAESSGCNSHMP YGYAAQARARERERLAHSRA AAAAAVAAATAAVEGTGGSG GGP

Data sets:
Data typeCount
13C chemical shifts210
15N chemical shifts56
1H chemical shifts339

Additional metadata:

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

Assembly:

Entity Assembly IDEntity NameEntity ID
1kv14_pep611

Entities:

Entity 1, kv14_pep61 63 residues - 6076.6 Da.

1   GLYALAMETGLUVALALAMETVALSERALA
2   GLUSERSERGLYCYSASNSERHISMETPRO
3   TYRGLYTYRALAALAGLNALAARGALAARG
4   GLUARGGLUARGLEUALAHISSERARGALA
5   ALAALAALAALAALAVALALAALAALATHR
6   ALAALAVALGLUGLYTHRGLYGLYSERGLY
7   GLYGLYPRO

Samples:

sample_1: kv14_pep61, [U-100% 15N], 150 uM; H2O 90%; D2O 10%; sodium phosphate 25 mM; sodium chloride 150 mM

sample_2: kv14_pep61, [U-100% 13C; U-100% 15N], 150 uM; H2O 90%; D2O 10%; sodium phosphate 25 mM; sodium chloride 150 mM

sample_conditions_1: ionic strength: 175 mM; pH: 7.4; pressure: 1 atm; temperature: 283 K

Experiments:

NameSampleSample stateSample conditions
2D 1H-15N HSQCsample_1isotropicsample_conditions_1
2D 1H-13C HSQCsample_2isotropicsample_conditions_1
3D HNCACBsample_2isotropicsample_conditions_1
3D C(CO)NHsample_2isotropicsample_conditions_1
3D HNCOsample_2isotropicsample_conditions_1
3D HCCH-TOCSYsample_2isotropicsample_conditions_1
3D HCCH-COSYsample_2isotropicsample_conditions_1
3D 1H-15N NOESYsample_1isotropicsample_conditions_1
3D 1H-13C NOESY aliphaticsample_2isotropicsample_conditions_1

Software:

TOPSPIN, Bruker Biospin - collection

CcpNMR, CCPN - data analysis

CS-Rosetta, Shen, Vernon, Baker and Bax - chemical shift based modelling

NMR spectrometers:

  • Bruker Avance 600 MHz
  • Bruker Avance 750 MHz

Related Database Links:

UniProtKB P15385
PDB
DBJ BAC29309
EMBL CAA34133 CAA40349 CAH89891
GB AAA36140 AAA41469 AAA61275 AAB60261 AAB60668
REF NP_001124883 NP_001185937 NP_002224 NP_037103 NP_067250
SP P15385 P22459 Q05037 Q28527 Q61423
TPG DAA21850
AlphaFold P15385 P22459 Q05037 Q28527 Q61423

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