BMRB Entry 18459

Title:
N0 domain of Neisseria meningitidis Pilus assembly protein PilQ
Deposition date:
2012-05-11
Original release date:
2013-01-03
Authors:
Phelan, Marie; Berry, J.; Derrick, J.; Lian, L.
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:
TYPE_IV_PILUS_BIOGENESIS_AND_COMPETENCE_PROTEIN_P, polymer, 128 residues, 14465.3886 Da.

Natural source:

Natural source:   Common Name: b-proteobacteria   Taxonomy ID: 487   Superkingdom: Bacteria   Kingdom: Neisseria   Genus/species: Neisseria meningitidis

Experimental source:

Experimental source:   Production method: recombinant technology   Host organism: Escherichia coli   Vector: pETM11

Entity Sequences (FASTA):

Data sets:
Data typeCount
13C chemical shifts518
15N chemical shifts133
1H chemical shifts869

Additional metadata:

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

Assembly:

Entity Assembly IDEntity NameEntity ID
1TYPE IV PILUS BIOGENESIS AND COMPETENCE PROTEIN P1

Entities:

Entity 1, TYPE IV PILUS BIOGENESIS AND COMPETENCE PROTEIN P 128 residues - 14465.3886 Da.

1   METLYSHISHISHISHISHISHISPROMET
2   SERASPTYRASPILEPROTHRTHRGLUASN
3   LEUTYRPHEGLUGLYALAMETGLYPHETHR
4   GLYARGLYSILESERLEUASPPHEGLNASP
5   VALGLUILEARGTHRILELEUGLNILELEU
6   ALALYSGLUSERGLYMETASNILEVALALA
7   SERASPSERVALASNGLYLYSMETTHRLEU
8   SERLEULYSASPVALPROTRPASPGLNALA
9   LEUASPLEUVALMETGLNALAARGASNLEU
10   ASPMETARGGLNGLNGLYASNILEVALASN
11   ILEALAPROARGASPGLULEULEUALALYS
12   ASPLYSALAPHELEUGLNALAGLULYSASP
13   ILEALAASPLEUGLYALALEUTYR

Samples:

sample_1: TYPE IV PILUS BIOGENESIS AND COMPETENCE PROTEIN P, [U-13C; U-15N], 0.5 mM; H2O 10%; D2O 90%

sample_conditions_1: ionic strength: 100.000 mM; pH: 6.800; pressure: 1.000 atm; temperature: 298.000 K

Experiments:

NameSampleSample stateSample conditions
3D CBCA(CO)NHsample_1solutionsample_conditions_1
3D HNCACBsample_1solutionsample_conditions_1
3D HN(CA)CO 3D HNCOsample_1solutionsample_conditions_1
2D 1H-15N HSQCsample_1solutionsample_conditions_1
3D HBHA(CO)NHsample_1solutionsample_conditions_1
3D HBHANHsample_1solutionsample_conditions_1
2D hbCBcgcdHDsample_1solutionsample_conditions_1
2D ali 1H-13C HSQCsample_1solutionsample_conditions_1
2D aro 1H-13C HSQCsample_1solutionsample_conditions_1
3D ali HC-NOESYsample_1solutionsample_conditions_1
3D aro HC-NOESYsample_1solutionsample_conditions_1
3D HN-NOESYsample_1solutionsample_conditions_1
3D ali HCcH-TOCSYsample_1solutionsample_conditions_1
3D aro HCcH-TOCSYsample_1solutionsample_conditions_1
3D HNCACBsample_1solutionsample_conditions_1

Software:

AutoDep v4.3, PDBe - collection

CCPN_analysis vany, CCPN - chemical shift assignment

CNS1.2 vany, Brunger, Adams, Clore, Gros, Nilges and Read - chemical shift assignment

CYANA2.1 vany, Guntert, Mumenthaler and Wuthrich - chemical shift assignment

TALOSPLUS vany, Cornilescu, Delaglio and Bax - chemical shift assignment

Topspin2.1 vany, Bruker Biospin - chemical shift assignment

NMR spectrometers:

  • Bruker Avance 800 MHz
  • Bruker Avance 600 MHz
  • Bruker AVANCE 600 MHz

Related Database Links:

UNP PILQ_NEIMB
BMRB 18428
PDB
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