BMRB Entry 27397

Name: 1H, 13C, 15N Chemical shift assignment for the TolAIII-TolB-peptide complex.
Published: 2020-03-16

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PDB ID: 6s3w
Entry in NMR Restraints Grid
Validation report in NRG-CING
Chem Shift validation: AVS_full
BMRB Entry DOI: doi:10.13018/BMR27397
MolProbity Validation Chart

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Nicholas Rego and David Koes
3Dmol.js: molecular visualization with WebGL
Bioinformatics (2015) 31 (8): 1322-1324 doi:10.1093/bioinformatics/btu829

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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:

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" .

Assembly members:

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

Natural source:

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

Experimental source:

Experimental source: Production method: recombinant technology Host organism: Escherichia coli Vector: pREN28 pQE2/Im9

Entity Sequences (FASTA):

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

Data sets:

assigned_chemical_shifts
- assigned_chem_shift_list_1
- assignedchem_shift_list_2

Data type	Count
13C chemical shifts	523
15N chemical shifts	140
1H chemical shifts	891

Additional metadata:

Assembly
Samples and Experiments
Software
Spectrometers
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Assembly:

Entity Assembly ID	Entity Name	Entity ID
1	TolAIII	1
2	TolBp	2

Entities:

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

This is the 3rd domain of TolA

1

HIS

MET

ARG

ALA

LEU

ALA

GLU

LEU

SER

2

ASP

THR

GLU

ARG

GLN

ALA

LEU

ALA

3

ASP

GLU

VAL

GLY

SER

GLU

VAL

THR

GLY

SER

4

LEU

ASP

LEU

ILE

VAL

ASN

LEU

VAL

SER

5

GLN

TRP

ARG

PRO

SER

ALA

ARG

6

ASN

GLY

MET

SER

VAL

GLU

VAL

LEU

ILE

GLU

7

MET

LEU

PRO

ASP

GLY

THR

ILE

THR

ASN

ALA

8

SER

VAL

SER

ARG

SER

GLY

ASP

LYS

PRO

9

PHE

ASP

SER

ALA

VAL

ALA

VAL

ARG

10

ASN

VAL

GLY

ARG

ILE

PRO

GLU

MET

GLN

11

LEU

PRO

ARG

ALA

THR

PHE

ASP

SER

LEU

TYR

12

ARG

GLN

ARG

ILE

PHE

LYS

PRO

GLU

13

ASP

LEU

SER

LEU

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

1

ALA

ASP

PRO

LEU

VAL

ILE

SER

GLY

ASN

2

ASP

ARG

ALA

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:

Name	Sample	Sample state	Sample conditions
3D HNCO	sample_2	isotropic	sample_conditions_1
3D HNCA	sample_2	isotropic	sample_conditions_1
3D CBCANH	sample_2	isotropic	sample_conditions_1
3D CBCA(CO)NH	sample_2	isotropic	sample_conditions_1
3D H(CCO)NH	sample_2	isotropic	sample_conditions_1
3D C(CO)NH	sample_2	isotropic	sample_conditions_1
3D HBHA(CO)NH	sample_2	isotropic	sample_conditions_1
2D 1H-15N HSQC	sample_2	isotropic	sample_conditions_1
3D 1H-15N NOESY	sample_1	isotropic	sample_conditions_1
3D 1H-15N TOCSY	sample_1	isotropic	sample_conditions_1
2D 1H-15N HSQC	sample_1	isotropic	sample_conditions_1
2D 1H-13C HSQC	sample_2	isotropic	sample_conditions_1
3D 1H-13C NOESY aliphatic	sample_2	isotropic	sample_conditions_1
3D 1H-13C NOESY aliphatic	sample_4	isotropic	sample_conditions_1
2D HNCO	sample_3	isotropic	sample_conditions_1
2D HBHA(CO)NH	sample_3	isotropic	sample_conditions_1
2D HNCA	sample_3	isotropic	sample_conditions_1
2D CBCA(CO)NH	sample_3	isotropic	sample_conditions_1
2D 1H-15N HSQC	sample_3	isotropic	sample_conditions_1
2D 1H-13C HSQC	sample_3	isotropic	sample_conditions_1
2D HN(CA)CO	sample_3	isotropic	sample_conditions_1
2D 1H-13C NOESY	sample_3	isotropic	sample_conditions_1
2D 1H-15N NOESY	sample_3	isotropic	sample_conditions_1
3D HCCH-TOCSY	sample_2	isotropic	sample_conditions_1
2D 1H-13C HSQC	sample_2	isotropic	sample_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 HSQC peak lists in one of the following formats:
CSV: Backbone or all simulated peaks
SPARKY: Backbone or all simulated peaks