BMRB

Biological Magnetic Resonance Data Bank


A Repository for Data from NMR Spectroscopy on Proteins, Peptides, Nucleic Acids, and other Biomolecules
Member of WWPDB

BMRB Entry 18419

Title: B2 domain of Neisseria meningitidis Pilus assembly protein PilQ   PubMed: 23028322

Deposition date: 2012-04-24 Original release date: 2013-01-03

Authors: Phelan, Marie; Berry, J.; Derrick, J.; Lian, L.

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).

Assembly members:
NmPilQ_B2, polymer, 138 residues, 15181.3338 Da.

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

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

Entity Sequences (FASTA):
NmPilQ_B2: MGSSHHHHHHGLVPRGSHMA SMTGGQQMGRGSKQTNIDFR KDGKNAGIIELAALGFAGQP DISQQHDHIIVTLKNHTLPT TLQRSLDVADFKTPVQKVTL KRLNNDTQLIITTAGNWELV NKSAAPGYFTFQVLPKKQ

Data sets:
Data typeCount
1H chemical shifts831
13C chemical shifts529
15N chemical shifts124

Additional metadata:

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

Assembly:

Entity Assembly IDEntity NameEntity ID
1NmPilQ_B21

Entities:

Entity 1, NmPilQ_B2 138 residues - 15181.3338 Da.

1   METGLYSERSERHISHISHISHISHISHIS
2   GLYLEUVALPROARGGLYSERHISMETALA
3   SERMETTHRGLYGLYGLNGLNMETGLYARG
4   GLYSERLYSGLNTHRASNILEASPPHEARG
5   LYSASPGLYLYSASNALAGLYILEILEGLU
6   LEUALAALALEUGLYPHEALAGLYGLNPRO
7   ASPILESERGLNGLNHISASPHISILEILE
8   VALTHRLEULYSASNHISTHRLEUPROTHR
9   THRLEUGLNARGSERLEUASPVALALAASP
10   PHELYSTHRPROVALGLNLYSVALTHRLEU
11   LYSARGLEUASNASNASPTHRGLNLEUILE
12   ILETHRTHRALAGLYASNTRPGLULEUVAL
13   ASNLYSSERALAALAPROGLYTYRPHETHR
14   PHEGLNVALLEUPROLYSLYSGLN

Samples:

sample_1: NmPilQ_B2, [U-13C; U-15N], 0.5 mM; potassium phosphate 50 mM; sodium chloride 50 mM; sodium azide 0.2%

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
nmrExptsample_1solutionsample_conditions_1

Software:

AutoDep v4.3, AutoDep - collection

CCPN_analysis v2.1.3, CCPN - chemical shift assignment, data analysis

CNS1.2 v1.2, Brunger, Adams, Clore, Gros, Nilges and Read - structure water refinement

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

TALOSPLUS vany, Cornilescu, Delaglio and Bax - dihedral angle calculation

Topspin2.1 vany, Bruker Biospin - spectra acquisition and processing

NMR spectrometers:

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

Related Database Links:

UNP PILQ_NEIMB
PDB
EMBL CAD91899 CAX50762 CBA04080 CBA04815 CBA09077
GB AAC43603 AAC96097 AAW88855 AAY52170 ACF28835
PRF 2210365A
REF NP_274809 WP_002214524 WP_002221480 WP_002224059 WP_002225652
SP P35819 Q5FAD2 Q70M91 Q9ZHF3

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