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 15422

Title: Partial chemical shift assignments of KChIP4a in its Ca2+- and Mg2+-loaded form   PubMed: 18458082

Deposition date: 2007-08-08 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, polymer, 237 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

Entity Sequences (FASTA):
KChIP4a: MGHHHHHHMNLEGLEMIAVL IVIVLFVKLLEQFGLIEAGL EDSVEDELEMATVRHRPEAL ELLEAQSKFTKKELQILYRG FKNECPSGVVNEETFKEIYS QFFPQGDSTTYAHFLFNAFD TDHNGAVSFEDFIKGLSILL RGTVQEKLNWAFNLYDINKD GYITKEEMLDIMKAIYDMMG KCTYPVLKEDAPRQHVETFF QKMDKNKDGVVTIDEFIESC QKDENIMRSMQLFENVI

Data sets:
Data typeCount
13C chemical shifts477
15N chemical shifts161
1H chemical shifts161

Additional metadata:

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

Assembly:

Entity Assembly IDEntity NameEntity ID
1KChIP4a1
2ligand12
3ligand22
4ligand33

Entities:

Entity 1, KChIP4a 237 residues - Formula weight is not available

The first eight residues represent a non-native affinity tag.

1   METGLYHISHISHISHISHISHISMETASN
2   LEUGLUGLYLEUGLUMETILEALAVALLEU
3   ILEVALILEVALLEUPHEVALLYSLEULEU
4   GLUGLNPHEGLYLEUILEGLUALAGLYLEU
5   GLUASPSERVALGLUASPGLULEUGLUMET
6   ALATHRVALARGHISARGPROGLUALALEU
7   GLULEULEUGLUALAGLNSERLYSPHETHR
8   LYSLYSGLULEUGLNILELEUTYRARGGLY
9   PHELYSASNGLUCYSPROSERGLYVALVAL
10   ASNGLUGLUTHRPHELYSGLUILETYRSER
11   GLNPHEPHEPROGLNGLYASPSERTHRTHR
12   TYRALAHISPHELEUPHEASNALAPHEASP
13   THRASPHISASNGLYALAVALSERPHEGLU
14   ASPPHEILELYSGLYLEUSERILELEULEU
15   ARGGLYTHRVALGLNGLULYSLEUASNTRP
16   ALAPHEASNLEUTYRASPILEASNLYSASP
17   GLYTYRILETHRLYSGLUGLUMETLEUASP
18   ILEMETLYSALAILETYRASPMETMETGLY
19   LYSCYSTHRTYRPROVALLEULYSGLUASP
20   ALAPROARGGLNHISVALGLUTHRPHEPHE
21   GLNLYSMETASPLYSASNLYSASPGLYVAL
22   VALTHRILEASPGLUPHEILEGLUSERCYS
23   GLNLYSASPGLUASNILEMETARGSERMET
24   GLNLEUPHEGLUASNVALILE

Entity 2, ligand1 - Ca - 40.078 Da.

1   CA

Entity 3, ligand3 - Mg - 24.305 Da.

1   MG

Samples:

sample_1: KChIP4a, [U-13C; U-15N; U-2H], 0.1 – 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