BMRB Entry 25417

Title:
NMR resonance assignments of CadC 1-159 from E.coli
Deposition date:
2015-01-07
Original release date:
2015-05-18
Authors:
Schlundt, Andreas; Sattler, Michael; Heydenreich, Thomas
Citation:

Citation: Schlundt, Andreas; Heydenreich, Thomas; Buchner, Sophie; Janowski, Robert; Niessing, Dierk; Sattler, Michael; Jung, Kirsten. "Structural and functional analysis of the signal transducing linker in the pH-responsive one component system CadC of Escherichia coli"  J. Mol. Biol. 427, 2548-2561 (2015).
PubMed: 25979249

Assembly members:

Assembly members:
CadC, polymer, 162 residues, 18160.6 Da.

Natural source:

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

Experimental source:

Experimental source:   Production method: recombinant technology   Host organism: Escherichia coli   Vector: pETTrx1a

Data sets:
Data typeCount
13C chemical shifts482
15N chemical shifts156
1H chemical shifts755

Additional metadata:

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

Assembly:

Entity Assembly IDEntity NameEntity ID
1CadC1-1591

Entities:

Entity 1, CadC1-159 162 residues - 18160.6 Da.

Sequence starts with -2. GAM is cloning remnant, an additional A is part of the restriction site. The original sequence number starts with Q2.

1   GLYALAMETALAGLNGLNPROVALVALARG
2   VALGLYGLUTRPLEUVALTHRPROSERILE
3   ASNGLNILESERARGASNGLYARGGLNLEU
4   THRLEUGLUPROARGLEUILEASPLEULEU
5   VALPHEPHEALAGLNHISSERGLYGLUVAL
6   LEUSERARGASPGLULEUILEASPASNVAL
7   TRPLYSARGSERILEVALTHRASNHISVAL
8   VALTHRGLNSERILESERGLULEUARGLYS
9   SERLEULYSASPASNASPGLUASPSERPRO
10   VALTYRILEALATHRVALPROLYSARGGLY
11   TYRLYSLEUMETVALPROVALILETRPTYR
12   SERGLUGLUGLUGLYGLUGLUILEMETLEU
13   SERSERPROPROPROILEPROGLUALAVAL
14   PROALATHRASPSERPROSERHISSERLEU
15   ASNILEGLNASNTHRALATHRPROPROGLU
16   GLNSERPROVALLYSSERLYSARGPHETHR
17   THRPHE

Samples:

sample_1: CadC, [U-100% 13C; U-100% 15N], 1 mM; H2O 90%; D2O 10%; BisTris"natural, abundance", 20 mM; NaCl 150 mM

sample_conditions_1: ionic strength: 0.15 M; pH: 6.5; pressure: 1 atm; temperature: 298 K

Experiments:

NameSampleSample stateSample conditions
2D 1H-15N HSQCsample_1isotropicsample_conditions_1
3D HNCACBsample_1isotropicsample_conditions_1
3D HCCH-TOCSYsample_1isotropicsample_conditions_1
3D HCACOsample_1isotropicsample_conditions_1
3D HBHA(CO)NHsample_1isotropicsample_conditions_1
3D CBCA(CO)NHsample_1isotropicsample_conditions_1
3D 1H-13C NOESY aliphaticsample_1isotropicsample_conditions_1
3D 1H-15N NOESYsample_1isotropicsample_conditions_1
3D 1H-13C NOESY aromaticsample_1isotropicsample_conditions_1
2D 1H-13C HSQC aliphaticsample_1isotropicsample_conditions_1
2D 1H-13C HSQC aromaticsample_1isotropicsample_conditions_1

Software:

CCPNMR_Analysis v2.3, CCPN - chemical shift assignment

NMR spectrometers:

  • Bruker Avance 600 MHz
  • Bruker Avance 800 MHz

Related Database Links:

UNP P23890
AlphaFold Q2M6H0

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