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 15632

Title: Solution structure of C-terminal effector domain of putative two-component-system response regulator involved in copper resistance from Klebsiella pneumoniae

Deposition date: 2008-01-22 Original release date: 2014-03-05

Authors: Hung, Kuo-Wei; Fang, Pei-Ju; Chang, Chi-Fon; Tsai, Shih-Feng; Huang, Tai-Huang

Citation: Hung, Kuo-Wei; Fang, Pei-Ju; Lin, Yi-Chao; Chang, Chi-Fon; Tsai, Shih-Feng; Huang, Tai-Huang. "Solution structure of C-terminal effector domain of putative two-component-system response regulator involved in copper resistance from Klebsiella pneumoniae"  . ., .-..

Assembly members:
TCS_C-domain, polymer, 112 residues, 11860.905 Da.

Natural source:   Common Name: Klebsiella pneumoniae   Taxonomy ID: 573   Superkingdom: Bacteria   Kingdom: not available   Genus/species: Klebsiella pneumoniae

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

Entity Sequences (FASTA):
TCS_C-domain: MAATVCTIADMTVDMVRRTV IRSGKKIHLTGKEYVLLELL LQRTGEVLPRSLISSLVWNM NFDSDTNVIDVAVRRLRSKI DDDFEPKLIHTVRGAGYVLE IREELEHHHHHH

Data sets:
Data typeCount
13C chemical shifts407
15N chemical shifts97
1H chemical shifts655

Additional metadata:

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

Assembly:

Entity Assembly IDEntity NameEntity ID
1TCS C-domain1

Entities:

Entity 1, TCS C-domain 112 residues - 11860.905 Da.

1   METALAALATHRVALCYSTHRILEALAASP
2   METTHRVALASPMETVALARGARGTHRVAL
3   ILEARGSERGLYLYSLYSILEHISLEUTHR
4   GLYLYSGLUTYRVALLEULEUGLULEULEU
5   LEUGLNARGTHRGLYGLUVALLEUPROARG
6   SERLEUILESERSERLEUVALTRPASNMET
7   ASNPHEASPSERASPTHRASNVALILEASP
8   VALALAVALARGARGLEUARGSERLYSILE
9   ASPASPASPPHEGLUPROLYSLEUILEHIS
10   THRVALARGGLYALAGLYTYRVALLEUGLU
11   ILEARGGLUGLULEUGLUHISHISHISHIS
12   HISHIS

Samples:

sample_1: C-terminal domain of TCS response regulator, [U-13C; U-15N], 1 mM; Tris 20 mM; NaCl 150 mM; Glu 150 mM; Arg 150 mM

sample_conditions_1: ionic strength: 150 mM; pH: 7.5; pressure: 1 atm; temperature: 293 K

Experiments:

NameSampleSample stateSample conditions
3D HNCAsample_1isotropicsample_conditions_1
3D HN(CO)CAsample_1isotropicsample_conditions_1
3D CBCA(CO)NHsample_1isotropicsample_conditions_1
3D HNCACBsample_1isotropicsample_conditions_1
3D HBHA(CO)NHsample_1isotropicsample_conditions_1
3D 1H-15N NOESYsample_1isotropicsample_conditions_1
3D HNCOsample_1isotropicsample_conditions_1
3D HCACOsample_1isotropicsample_conditions_1
3D 1H-13C NOESYsample_1isotropicsample_conditions_1
3D HCCH-TOCSYsample_1isotropicsample_conditions_1

Software:

CYANA v2.1, Guntert, Mumenthaler and Wuthrich - refinement

NMR spectrometers:

  • Bruker Avance 500 MHz
  • Bruker DRX 600 MHz

Related Database Links:

PDB
DBJ BAH66041 BAN19330 BAS43820 GAB52600 GAL54239
EMBL CAA58529 CAE51683 CAV00324 CBA34756 CBI99735
GB AAR07822 ABF67806 ABR80316 ABU79433 ACA79029
REF NP_941227 NP_943472 WP_000936558 WP_001188929 WP_001188930
SP Q47456

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