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 18966

Title: Global folded of the type IV pilin ComP from Neisseria meningitidis   PubMed: 23386723

Deposition date: 2013-01-21 Original release date: 2013-02-11

Authors: Simpson, Peter

Citation: Cehovin, Ana; Simpson, Peter; McDowell, Melanie; Brown, Daniel; Noschese, Rossella; Pallett, Mitchell; Brady, Jacob; Baldwin, Geoffrey; Lea, Susan; Matthews, Stephen; Pelicic, Vladimir. "Specific DNA recognition mediated by a type IV pilin."  Proc. Natl. Acad. Sci. U.S.A. 110, 3065-3070 (2013).

Assembly members:
ComP, polymer, 119 residues, 13512.874 Da.

Natural source:   Common Name: b-proteobacteria   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):
ComP: ISEFEKAKINAVRAALLENA HFMEKFYLQNGRFKQTSTKW PSLPIKEAEGFCIRLNGIAR GALDSKFMLKAVAIDKDKNP FIIKMNENLVTFICKKSASS CSDGLDYFKGNDKDCKLFK

Data sets:
Data typeCount
13C chemical shifts466
15N chemical shifts93
1H chemical shifts709

Additional metadata:

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

Assembly:

Entity Assembly IDEntity NameEntity ID
1ComP1

Entities:

Entity 1, ComP 119 residues - 13512.874 Da.

1   ILESERGLUPHEGLULYSALALYSILEASN
2   ALAVALARGALAALALEULEUGLUASNALA
3   HISPHEMETGLULYSPHETYRLEUGLNASN
4   GLYARGPHELYSGLNTHRSERTHRLYSTRP
5   PROSERLEUPROILELYSGLUALAGLUGLY
6   PHECYSILEARGLEUASNGLYILEALAARG
7   GLYALALEUASPSERLYSPHEMETLEULYS
8   ALAVALALAILEASPLYSASPLYSASNPRO
9   PHEILEILELYSMETASNGLUASNLEUVAL
10   THRPHEILECYSLYSLYSSERALASERSER
11   CYSSERASPGLYLEUASPTYRPHELYSGLY
12   ASNASPLYSASPCYSLYSLEUPHELYS

Samples:

sample_1: ComP, [U-100% 13C; U-100% 15N], 0.1 – 0.5 mM; H2O 90%; D2O 10%

sample_conditions_1: ionic strength: 0.05 M; pH: 6.7; pressure: 1 atm; temperature: 310 K

Experiments:

NameSampleSample stateSample conditions
3D 1H-13C NOESYsample_1isotropicsample_conditions_1
2D 1H-15N HSQCsample_1isotropicsample_conditions_1
3D HCCH-TOCSYsample_1isotropicsample_conditions_1
3D HNCACBsample_1isotropicsample_conditions_1

Software:

ARIA, Linge, O, . - structure solution

NMR spectrometers:

  • Bruker DRX 800 MHz
  • Bruker DRX 600 MHz

Related Database Links:

PDB
EMBL CAM07712 CAM11151 CAX50978 CBA03591 CBN88156
GB AAF62338 AAW89839 ABX72399 ADO32435 ADY94460
REF NP_275008 WP_002214937 WP_002218144 WP_002221685 WP_002233205

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