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 15425

Title: Partial chemical shift assignments of the N-terminal deletion mutant KChIP4a(Delta1-42) in its Ca2+- and Mg2+-loaded form   PubMed: 18458082

Deposition date: 2007-08-09 Original release date: 2007-10-03

Authors: Schwenk, Jochen; Kandias, Nikolaos; Neubauer, Isabel; Fakler, Bernd; Bentrop, Detlef

Citation: Schwenk, Jochen; Zolles, Gerd; Kandias, Nikolaos; Neubauer, Isabel; Kalbacher, Hubert; Covarrubias, Manuel; Fakler, Bernd; Bentrop, Detlef. "NMR Analysis of KChIP4a Reveals Structural Basis for Control of Surface Expression of Kv4 Channel Complexes"  J. Biol. Chem. 283, 18937-18946 (2008).

Assembly members:
KChIP4a(Delta1-42), polymer, 198 residues, Formula weight is not available
CA, non-polymer, 40.078 Da.
MG, non-polymer, 24.305 Da.

Natural source:   Common Name: Mouse   Taxonomy ID: 10090   Superkingdom: Eukaryota   Kingdom: Metazoa   Genus/species: Mus musculus

Experimental source:   Production method: recombinant technology   Host organism: Escherichia coli   Vector: pET30

Entity Sequences (FASTA):
KChIP4a(Delta1-42): GSTMGHHHHHHATVRHRPEA LELLEAQSKFTKKELQILYR GFKNECPSGVVNEETFKEIY SQFFPQGDSTTYAHFLFNAF DTDHNGAVSFEDFIKGLSIL LRGTVQEKLNWAFNLYDINK DGYITKEEMLDIMKAIYDMM GKCTYPVLKEDAPRQHVETF FQKMDKNKDGVVTIDEFIES CQKDENIMRSMQLFENVI

Data sets:
Data typeCount
13C chemical shifts393
15N chemical shifts135
1H chemical shifts135

Additional metadata:

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

Assembly:

Entity Assembly IDEntity NameEntity ID
1KChIP4a(Delta1-42)1
2ligand12
3ligand22
4ligand33

Entities:

Entity 1, KChIP4a(Delta1-42) 198 residues - Formula weight is not available

The first eleven residues represent a cloning artefact from a thrombin site and a non-native affinity tag. This is a N-terminal deletion mutant (Delta1-42) of KChIP4a.

1   GLYSERTHRMETGLYHISHISHISHISHIS
2   HISALATHRVALARGHISARGPROGLUALA
3   LEUGLULEULEUGLUALAGLNSERLYSPHE
4   THRLYSLYSGLULEUGLNILELEUTYRARG
5   GLYPHELYSASNGLUCYSPROSERGLYVAL
6   VALASNGLUGLUTHRPHELYSGLUILETYR
7   SERGLNPHEPHEPROGLNGLYASPSERTHR
8   THRTYRALAHISPHELEUPHEASNALAPHE
9   ASPTHRASPHISASNGLYALAVALSERPHE
10   GLUASPPHEILELYSGLYLEUSERILELEU
11   LEUARGGLYTHRVALGLNGLULYSLEUASN
12   TRPALAPHEASNLEUTYRASPILEASNLYS
13   ASPGLYTYRILETHRLYSGLUGLUMETLEU
14   ASPILEMETLYSALAILETYRASPMETMET
15   GLYLYSCYSTHRTYRPROVALLEULYSGLU
16   ASPALAPROARGGLNHISVALGLUTHRPHE
17   PHEGLNLYSMETASPLYSASNLYSASPGLY
18   VALVALTHRILEASPGLUPHEILEGLUSER
19   CYSGLNLYSASPGLUASNILEMETARGSER
20   METGLNLEUPHEGLUASNVALILE

Entity 2, ligand1 - Ca - 40.078 Da.

1   CA

Entity 3, ligand3 - Mg - 24.305 Da.

1   MG

Samples:

sample_1: KChIP4a(Delta1-42), [U-13C; U-15N; U-2H], 0.25 mM; MOPS 10 mM; DTT 4 mM; N-octylglucoside 5 mM; magnesium chloride 2 mM; H2O 90%; D2O 10%

sample_conditions_1: pH: 7.4; pressure: 1 atm; temperature: 300 K

Experiments:

NameSampleSample stateSample conditions
2D 1H-15N HSQCsample_1isotropicsample_conditions_1
3D HNCAsample_1isotropicsample_conditions_1
3D HN(CO)CAsample_1isotropicsample_conditions_1
3D HNCACBsample_1isotropicsample_conditions_1
3D HN(CO)CACBsample_1isotropicsample_conditions_1
3D HNCOsample_1isotropicsample_conditions_1
3D 1H-15N NOESYsample_1isotropicsample_conditions_1

Software:

TOPSPIN v1.3, Bruker Biospin - collection, processing

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

NMR spectrometers:

  • Bruker Avance 600 MHz

Related Database Links:

PDB
DBJ BAC30218 BAE21645 BAE28641 BAE38374 BAE90434
EMBL CAH90097
GB AAG36974 AAG36976 AAG36977 AAH32520 AAH51130
REF NP_001030175 NP_001030176 NP_001070403 NP_001127236 NP_001186171
SP Q2KI69 Q6PHZ8 Q6PIL6 Q8HYN7 Q99MG9
TPG DAA28811

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