BMRB Entry 19231

Title:
Structural Basis of DNA Recognition by the Effector Domain of Klebsiella pneumoniae PmrA
Deposition date:
2013-05-07
Original release date:
2014-01-21
Authors:
Wang, Iren; Lou, Yuan-Chao; Chen, Chinpan
Citation:

Citation: Lou, Yuan-Chao; Wang, Iren; Rajasekaran, M.; Kao, Yi-Fen; Ho, Meng-Ru; Hsu, Shang-Te Danny; Chou, Shan-Ho; Wu, Shih-Hsiung; Chen, Chinpan. "Solution structure and tandem DNA recognition of the C-terminal effector domain of PmrA from Klebsiella pneumoniae."  Nucleic Acids Res. 42, 4080-4093 (2014).
PubMed: 24371275

Assembly members:

Assembly members:
entity, polymer, 103 residues, 11854.557 Da.

Natural source:

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

Experimental source:

Experimental source:   Production method: recombinant technology   Host organism: Escherichia coli   Vector: pET29(+)

Data sets:
Data typeCount
13C chemical shifts460
15N chemical shifts110
1H chemical shifts737

Additional metadata:

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

Assembly:

Entity Assembly IDEntity NameEntity ID
1PmrA1

Entities:

Entity 1, PmrA 103 residues - 11854.557 Da.

1   ASNGLNGLYASPASNGLUILESERVALGLY
2   ASNLEUARGLEUASNVALTHRARGARGLEU
3   VALTRPLEUGLYGLUTHRALALEUASPLEU
4   THRPROLYSGLUTYRALALEULEUSERARG
5   LEUMETMETLYSALAGLYSERPROVALHIS
6   ARGGLUILELEUTYRASNASPILETYRSER
7   TRPASPASNGLUPROALATHRASNTHRLEU
8   GLUVALHISILEHISASNLEUARGGLULYS
9   ILEGLYLYSSERARGILEARGTHRVALARG
10   GLYPHEGLYTYRMETLEUALAASNASNILE
11   ASPTHRGLU

Samples:

sample_1: PmrAc, [U-99% 13C; U-99% 15N], 0.3 mM; H2O 90%; D2O 10%

sample_2: PmrAc, [U-99% 13C; U-99% 15N], 0.3 mM; D2O 100%

sample_conditions_1: ionic strength: 0.03 M; pH: 6.0; pressure: ambient atm; temperature: 298 K

Experiments:

NameSampleSample stateSample conditions
2D 1H-15N HSQCsample_1isotropicsample_conditions_1
3D HNCACBsample_1isotropicsample_conditions_1
3D CBCA(CO)NHsample_1isotropicsample_conditions_1
3D HNCOsample_1isotropicsample_conditions_1
3D HBHA(CO)NHsample_1isotropicsample_conditions_1
2D 1H-13C HSQC aliphaticsample_2isotropicsample_conditions_1
3D HCCH-TOCSYsample_2isotropicsample_conditions_1
3D 1H-15N NOESYsample_1isotropicsample_conditions_1
3D 1H-13C NOESY aliphaticsample_2isotropicsample_conditions_1
3D 1H-13C NOESY aromaticsample_2isotropicsample_conditions_1

Software:

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

NMRView, Johnson, One Moon Scientific - chemical shift assignment, data analysis, peak picking

X-PLOR_NIH, Schwieters, Kuszewski, Tjandra and Clore - refinement, structure solution

TOPSPIN, Bruker Biospin - collection, processing

ProcheckNMR, Laskowski and MacArthur - data analysis

NMR spectrometers:

  • Bruker Avance 600 MHz
  • Bruker Avance 800 MHz

Related Database Links:

BMRB 26532 26535
PDB
DBJ BAH62495
EMBL CCI78009 CCM81779 CCM90377 CCM95353 CCN28862
GB ABR76243 ACI11257 ADC59454 AEJ97287 AEW60332
REF WP_002895659 WP_004142095 WP_008805743 WP_016947497 WP_023279685

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