BMRB

Biological Magnetic Resonance Data Bank


A Repository for Data from NMR Spectroscopy on Proteins, Peptides, Nucleic Acids, and other Biomolecules
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BMRB Entry 27397

Title: 1H, 13C, 15N Chemical shift assignment for the TolAIII-TolB-peptide complex.

Deposition date: 2018-02-07 Original release date: 2020-03-16

Authors: Redfield, Christina; Holmes, Peter; Rajasekar, Karthik; Kleanthous, Colin

Citation: Holmes, Peter; Rajasekar, Karthik; Rassam, Patrice; Cassels, Eoin; Redfield, Christina; Kleanthous, Colin. "Structure of the TolA-TolB complex suggests 'Pal-uncapping' is the primary role of the Tol-Pal system in bacteria"  Not known ., .-..

Assembly members:
TolAIII, polymer, 124 residues, Formula weight is not available
TolBp, polymer, 13 residues, Formula weight is not available

Natural source:   Common Name: Pseudomonas aeruginosa   Taxonomy ID: 287   Superkingdom: Bacteria   Kingdom: not available   Genus/species: Pseudomonas aeruginosa

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

Entity Sequences (FASTA):
TolAIII: HMRALAELLSDTTERQQALA DEVGSEVTGSLDDLIVNLVS QQWRRPPSARNGMSVEVLIE MLPDGTITNASVSRSSGDKP FDSSAVAAVRNVGRIPEMQQ LPRATFDSLYRQRRIIFKPE DLSL
TolBp: ADPLVISSGNDRA

Data sets:
Data typeCount
13C chemical shifts523
15N chemical shifts140
1H chemical shifts891

Additional metadata:

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

Assembly:

Entity Assembly IDEntity NameEntity ID
1TolAIII1
2TolBp2

Entities:

Entity 1, TolAIII 124 residues - Formula weight is not available

This is the 3rd domain of TolA

1   HISMETARGALALEUALAGLULEULEUSER
2   ASPTHRTHRGLUARGGLNGLNALALEUALA
3   ASPGLUVALGLYSERGLUVALTHRGLYSER
4   LEUASPASPLEUILEVALASNLEUVALSER
5   GLNGLNTRPARGARGPROPROSERALAARG
6   ASNGLYMETSERVALGLUVALLEUILEGLU
7   METLEUPROASPGLYTHRILETHRASNALA
8   SERVALSERARGSERSERGLYASPLYSPRO
9   PHEASPSERSERALAVALALAALAVALARG
10   ASNVALGLYARGILEPROGLUMETGLNGLN
11   LEUPROARGALATHRPHEASPSERLEUTYR
12   ARGGLNARGARGILEILEPHELYSPROGLU
13   ASPLEUSERLEU

Entity 2, TolBp 13 residues - Formula weight is not available

1   ALAASPPROLEUVALILESERSERGLYASN
2   ASPARGALA

Samples:

sample_1: TolAIII, [U-98% 15N], 0.6 ± 0.05 mM; TolBp 3 ± 0.1 mM; sodium phosphate 20 ± 0.5 mM; sodium chloride 60 ± 0.5 mM

sample_2: TolAIII, [U-98% 13C; U-98% 15N], 0.6 ± 0.05 mM; TolBp 3 ± 0.1 mM; sodium phosphate 20 ± 0.5 mM; sodium chloride 60 ± 0.5 mM

sample_3: TolAIII 1.1 ± 0.05 mM; TolBp, [U-98% 13C; U-98% 15N], 0.2 ± 0.02 mM; sodium phosphate 20 ± 0.5 mM; sodium chloride 60 ± 0.5 mM

sample_4: TolAIII, [U-98% 13C; U-98% 15N], 0.6 ± 0.05 mM; TolBp 3 ± 0.1 mM; sodium phosphate 20 ± 0.5 mM; sodium chloride 60 ± 0.5 mM

sample_conditions_1: ionic strength: 140 mM; pH: 7.0; pressure: 1 atm; temperature: 293 K

Experiments:

NameSampleSample stateSample conditions
3D HNCOsample_2isotropicsample_conditions_1
3D HNCAsample_2isotropicsample_conditions_1
3D CBCANHsample_2isotropicsample_conditions_1
3D CBCA(CO)NHsample_2isotropicsample_conditions_1
3D H(CCO)NHsample_2isotropicsample_conditions_1
3D C(CO)NHsample_2isotropicsample_conditions_1
3D HBHA(CO)NHsample_2isotropicsample_conditions_1
2D 1H-15N HSQCsample_2isotropicsample_conditions_1
3D 1H-15N NOESYsample_1isotropicsample_conditions_1
3D 1H-15N TOCSYsample_1isotropicsample_conditions_1
2D 1H-15N HSQCsample_1isotropicsample_conditions_1
2D 1H-13C HSQCsample_2isotropicsample_conditions_1
3D 1H-13C NOESY aliphaticsample_2isotropicsample_conditions_1
3D 1H-13C NOESY aliphaticsample_4isotropicsample_conditions_1
2D HNCOsample_3isotropicsample_conditions_1
2D HBHA(CO)NHsample_3isotropicsample_conditions_1
2D HNCAsample_3isotropicsample_conditions_1
2D CBCA(CO)NHsample_3isotropicsample_conditions_1
2D 1H-15N HSQCsample_3isotropicsample_conditions_1
2D 1H-13C HSQCsample_3isotropicsample_conditions_1
2D HN(CA)COsample_3isotropicsample_conditions_1
2D 1H-13C NOESYsample_3isotropicsample_conditions_1
2D 1H-15N NOESYsample_3isotropicsample_conditions_1
3D HCCH-TOCSYsample_2isotropicsample_conditions_1
2D 1H-13C HSQCsample_2isotropicsample_conditions_1

Software:

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

Analysis v2.3, CCPN - chemical shift assignment, peak picking

ARIA, Linge, O'Donoghue and Nilges - structure solution

NMR spectrometers:

  • Bruker Avance 500 MHz
  • Home-built OMEGA 750 MHz
  • Home-built OMEGA 950 MHz

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