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 27882

Title: Backbone 1H, 13C, 15N chemical shift assignments for the ShkA kinase Rec2 domain from Caulobacter crescentus

Deposition date: 2019-04-23 Original release date: 2019-12-12

Authors: Boehm, Raphael; Hiller, Sebastian

Citation: Boehm, Raphael; Hiller, Sebastian; Dubey, Badri; Agustoni, Elia; Mangia, Francesca; Mazur, Adam; Kaczmarczyk, Andreas; Jenal, Urs; Plaza-Menacho, Ivan; Schirmer, Tilman. "Hybrid Histidine kinase activation by cyclic-di-GMP induced domain liberation"  .

Assembly members:
ShkA-Rec2, polymer, 169 residues, 17700 Da.

Natural source:   Common Name: Caulobacter crescentus   Taxonomy ID: 155892   Superkingdom: Bacteria   Kingdom: not available   Genus/species: Caulobacter crescentus

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

Entity Sequences (FASTA):
ShkA-Rec2: MGSSHHHHHHSSGLVPRGSH PAHDDRIAGAVASGARVLLA EDNPINALLARTLLEREGCI VDRVADGEQAIAAASAGVYD LILMDLRMPGLTGIEAARAL RAKGVATPIAALTADAFDED RRTCLAAGMDDFLVKPLTQE ALRDALKRWTTGGVSGGWTK PATRAKVAG

Data sets:
Data typeCount
13C chemical shifts183
15N chemical shifts99
1H chemical shifts99

Additional metadata:

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

Assembly:

Entity Assembly IDEntity NameEntity ID
1Rec21

Entities:

Entity 1, Rec2 169 residues - 17700 Da.

1   METGLYSERSERHISHISHISHISHISHIS
2   SERSERGLYLEUVALPROARGGLYSERHIS
3   PROALAHISASPASPARGILEALAGLYALA
4   VALALASERGLYALAARGVALLEULEUALA
5   GLUASPASNPROILEASNALALEULEUALA
6   ARGTHRLEULEUGLUARGGLUGLYCYSILE
7   VALASPARGVALALAASPGLYGLUGLNALA
8   ILEALAALAALASERALAGLYVALTYRASP
9   LEUILELEUMETASPLEUARGMETPROGLY
10   LEUTHRGLYILEGLUALAALAARGALALEU
11   ARGALALYSGLYVALALATHRPROILEALA
12   ALALEUTHRALAASPALAPHEASPGLUASP
13   ARGARGTHRCYSLEUALAALAGLYMETASP
14   ASPPHELEUVALLYSPROLEUTHRGLNGLU
15   ALALEUARGASPALALEULYSARGTRPTHR
16   THRGLYGLYVALSERGLYGLYTRPTHRLYS
17   PROALATHRARGALALYSVALALAGLY

Samples:

sample_1: ShkA-Rec2, [U-99% 13C; U-99% 15N], 375 uM

sample_conditions_1: ionic strength: 0.195 M; pH: 7.2; pressure: 1 atm; temperature: 298.15 K

Experiments:

NameSampleSample stateSample conditions
2D 1H-15N HSQCsample_1isotropicsample_conditions_1
3D HNCAsample_1isotropicsample_conditions_1
3D HNCACBsample_1isotropicsample_conditions_1
3D CBCA(CO)NHsample_1isotropicsample_conditions_1

Software:

TOPSPIN v3.0, Bruker Biospin - collection

CARA, Keller and Wuthrich - chemical shift assignment

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

NMR spectrometers:

  • Bruker Avance 700 MHz

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