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 6029

Title: 1H, 13C and 15N resonance assignment of the nucleotide binding domain of KdpB from Escherichia coli   PubMed: 15213457

Deposition date: 2003-12-03 Original release date: 2004-07-06

Authors: Haupt, Melina; Coles, Murray; Truffault, Vincent; Bramkamp, Marc; Kessler, Horst; Altendorf, Karlheinz

Citation: Haupt, Melina; Coles, Murray; Truffault, Vincent; Bramkamp, Marc; Altendorf, Karlheinz; Kessler, Horst. "Letter to the Editor: 1H, 13C and 15N resonance assignment of the nucleotide binding domain of KdpB from Escherichia coli"  J. Biomol. NMR 29, 437-438 (2004).

Assembly members:
potassium transporting ATPase, polymer, 156 residues, 17000 Da.

Natural source:   Common Name: E. coli   Taxonomy ID: 562   Superkingdom: Eubacteria   Kingdom: not available   Genus/species: Escherichia coli

Experimental source:   Production method: recombinant technology   Host organism: Escherichia coli   Vector: pET16b

Entity Sequences (FASTA):
potassium transporting ATPase: MGHHHHHHHHHHSSGHGGRH NRQASEFIPAQGVDEKTLAD AAQLASLADETPEGRSIVIL AKQRFNLRERDVQSLHATFV PFTAQSRMSGINIDNRMIRK GSVDAIRRHVEANGGHFPTD VDQKVDQVARQGATPLVVVE GSRVLGVIALKDIVKG

Data sets:
Data typeCount
13C chemical shifts554
15N chemical shifts147
1H chemical shifts955

Additional metadata:

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

Assembly:

Entity Assembly IDEntity NameEntity ID
1KdpBN1

Entities:

Entity 1, KdpBN 156 residues - 17000 Da.

1   METGLYHISHISHISHISHISHISHISHIS
2   HISHISSERSERGLYHISGLYGLYARGHIS
3   ASNARGGLNALASERGLUPHEILEPROALA
4   GLNGLYVALASPGLULYSTHRLEUALAASP
5   ALAALAGLNLEUALASERLEUALAASPGLU
6   THRPROGLUGLYARGSERILEVALILELEU
7   ALALYSGLNARGPHEASNLEUARGGLUARG
8   ASPVALGLNSERLEUHISALATHRPHEVAL
9   PROPHETHRALAGLNSERARGMETSERGLY
10   ILEASNILEASPASNARGMETILEARGLYS
11   GLYSERVALASPALAILEARGARGHISVAL
12   GLUALAASNGLYGLYHISPHEPROTHRASP
13   VALASPGLNLYSVALASPGLNVALALAARG
14   GLNGLYALATHRPROLEUVALVALVALGLU
15   GLYSERARGVALLEUGLYVALILEALALEU
16   LYSASPILEVALLYSGLY

Samples:

KdpBN_sample: Type IA potassium translocating ATPase B chain, [U-13C; U-15N], 1.2 mM

KdpBN_cond: pH: 6.0 na; temperature: 300 K

Experiments:

NameSampleSample stateSample conditions
CBCA(CO)NHnot availablenot availablenot available
HNCAnot availablenot availablenot available
HNCACBnot availablenot availablenot available
HBHA(CO)NHnot availablenot availablenot available
HACACOnot availablenot availablenot available
HN(CA)HAnot availablenot availablenot available
HNHAnot availablenot availablenot available
HNHBnot availablenot availablenot available
HNCOnot availablenot availablenot available
(H)CCH-COSYnot availablenot availablenot available

Software:

No software information available

NMR spectrometers:

  • Bruker DMX 600 MHz
  • Bruker DMX 750 MHz
  • Bruker DMX 900 MHz

Related Database Links:

BMRB 6030
PDB
DBJ BAA35354 BAB34148 BAG76281 BAI24086 BAI29554
EMBL CAP75183 CAQ31162 CAQ89912 CAQ97541 CAR02071
GB AAB96336 AAC73791 AAG55018 AAN79255 AAZ87406
REF NP_286410 NP_308752 NP_415225 NP_752712 WP_000087925
SP A1A8W1 A7ZJ80 A7ZXV8 B1IY32 B1LLE1
AlphaFold A1A8W1 A1A8W1 A1A8W1 A7ZJ80 A7ZJ80 A7ZJ80 A7ZXV8 A7ZXV8 A7ZXV8 B1IY32 B1IY32 B1IY32 B1LLE1 B1LLE1 B1LLE1

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