BMRB Entry 18428

Title:
N0N1 domains of Neisseria meningitidis Pilus assembly protein PilQ
Deposition date:
2012-04-27
Original release date:
2013-01-03
Authors:
Phelan, Marie; Berry, Jamie-Lee; Derrick, jeremy; Lian, Lu-Yun
Citation:

Citation: Berry, Jamie-Lee; Phelan, Marie; Collins, Richard; Adomavicius, Tomas; Tnjum, Tone; Frye, Stefan; Bird, Louise; Owens, Ray; Ford, Robert; Lian, Lu-Yun; Derrick, Jeremy. "Structure and assembly of a trans-periplasmic channel for type IV pili in Neisseria meningitidis."  PLoS Pathog. 8, .-. (2012).
PubMed: 23028322

Assembly members:

Assembly members:
PilQ_N0N1, polymer, 237 residues, 26149.8016 Da.

Natural source:

Natural source:   Common Name: Neisseria meningitidis   Taxonomy ID: 487   Superkingdom: Bacteria   Kingdom: not available   Genus/species: Neisseria meningitidis

Experimental source:

Experimental source:   Production method: recombinant technology   Host organism: Escherichia coli   Vector: pET28a

Data sets:
Data typeCount
13C chemical shifts721
15N chemical shifts209
1H chemical shifts965

Additional metadata:

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

Assembly:

Entity Assembly IDEntity NameEntity ID
1PilQ_N0N11

Entities:

Entity 1, PilQ_N0N1 237 residues - 26149.8016 Da.

M309-S342 = non-native purification tag F343-L545 PilQ N0N1 domains

1   METGLYSERSERHISHISHISHISHISHIS
2   SERSERGLYLEUVALPROARGGLYSERHIS
3   METALASERMETTHRGLYGLYGLNGLNMET
4   GLYARGGLYSERPHETHRGLYARGLYSILE
5   SERLEUASPPHEGLNASPVALGLUILEARG
6   THRILELEUGLNILELEUALALYSGLUSER
7   GLYMETASNILEVALALASERASPSERVAL
8   ASNGLYLYSMETTHRLEUSERLEULYSASP
9   VALPROTRPASPGLNALALEUASPLEUVAL
10   METGLNALAARGASNLEUASPMETARGGLN
11   GLNGLYASNILEVALASNILEALAPROARG
12   ASPGLULEULEUALALYSASPLYSALAPHE
13   LEUGLNALAGLULYSASPILEALAASPLEU
14   GLYALALEUTYRSERGLNASNPHEGLNLEU
15   LYSTYRLYSASNVALGLUGLUPHEARGSER
16   ILELEUARGLEUASPASNALAASPTHRTHR
17   GLYASNARGASNTHRLEUVALSERGLYARG
18   GLYSERVALLEUILEASPPROALATHRASN
19   THRLEUILEVALTHRASPTHRARGSERVAL
20   ILEGLULYSPHEARGLYSLEUILEASPGLU
21   LEUASPVALPROALAGLNGLNVALMETILE
22   GLUALAARGILEVALGLUALAALAASPGLY
23   PHESERARGASPLEUGLYVALLYSPHEGLY
24   ALATHRGLYLYSLYSLYSLEU

Samples:

sample_1: PilQ_N0N1, [U-98% 13C; U-98% 15N], 600 ± 100 uM; sodium chloride 50 ± 1 mM; potassium phosphate 50 ± 1 mM; sodium azide 0.2 ± 0.02 %; H2O 90%; D2O 10%

sample_conditions_1: ionic strength: 100 mM; pH: 6.8; pressure: 1 atm; temperature: 298 K

Experiments:

NameSampleSample stateSample conditions
CBCACONH (H[N[co[{CA|ca[C]}]]])sample_1isotropicsample_conditions_1
3D HNCACBsample_1isotropicsample_conditions_1
HNCACO (H[N[ca[CO]]])sample_1isotropicsample_conditions_1
3D HNCOsample_1isotropicsample_conditions_1
2D 1H-15N HSQC/HMQCsample_1isotropicsample_conditions_1
2D 1H-13C HSQC/HMQCsample_1isotropicsample_conditions_1
2D 1H-13C HSQC/HMQCsample_1isotropicsample_conditions_1
3D HNCAsample_1isotropicsample_conditions_1
hbhaconh (H[N[co[{ca[H]|ca[c[H]]}]]])sample_1isotropicsample_conditions_1
hbhanh (H[N[{ca[H]|ca[c[H]}]])sample_1isotropicsample_conditions_1
3D HCCH-TOCSYsample_1isotropicsample_conditions_1
2D 1H-13C HSQC/HMQCsample_1isotropicsample_conditions_1
Cb_Hd (hbCBcgcdHD)sample_1isotropicsample_conditions_1
2D 1H-15N HSQCsample_1isotropicsample_conditions_1
2D 1H-13C HSQC aliphaticsample_1isotropicsample_conditions_1
2D 1H-13C HSQC aromaticsample_1isotropicsample_conditions_1

Software:

ANALYSIS v2.1, CCPN - chemical shift assignment, data analysis, peak picking

TOPSPIN v2.1, Bruker - Processing and acquisition

NMR spectrometers:

  • Bruker Avance 600 MHz
  • Bruker Avance 800 MHz

Related Database Links:

UniProt Q70M91
EMBL CAM09716 CKK77493
AlphaFold Q4W562

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