BMRB Entry 34286

Name: Solution structure of lipase binding domain LID1 of foldase from Pseudomonas aeruginosa
Published: 2018-12-17

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PDB ID: 6gsf
Entry in NMR Restraints Grid
Validation report in NRG-CING
Chem Shift validation: AVS_full, LACS
BMRB Entry DOI: doi:10.13018/BMR34286
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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:

Solution structure of lipase binding domain LID1 of foldase from Pseudomonas aeruginosa

Deposition date:

2018-06-14

Original release date:

2018-12-17

Authors:

Viegas, A.; Jaeger, K.; Etzkorn, M.; Gohlke, H.; Verma, N.; Dollinger, P.; Kovacic, F.

Citation:

Citation: Viegas, Aldino; Dollinger, Peter; Verma, Neha; Kubiak, Jakub; Viennet, Thibault; Seidel, Claus; Gohlke, Holger; Etzkorn, Manuel; Kovacic, Filip; Jaeger, Karl-Erich. "Structural and dynamic insights revealing how lipase binding domain MD1 of Pseudomonas aeruginosa foldase affects lipase activation" Sci. Rep. 10, 3578-3578 (2020).
PubMed: 32107397

Assembly members:

Assembly members:
Lipase chaperone, polymer, 89 residues, 10016.225 Da.

Natural source:

Natural source: Common Name: Pseudomonas aeruginosa PAO1 Taxonomy ID: 208964 Superkingdom: Bacteria Kingdom: not available Genus/species: Pseudomonas aeruginosa

Experimental source:

Experimental source: Production method: recombinant technology Host organism: Escherichia coli BL21(DE3) Vector: pEHTHis19

Entity Sequences (FASTA):

Entity Sequences (FASTA):
Lipase chaperone: MGHHHHHHLPTSFRGTSVDG SFSVDASGNLLITRDIRNLF DAFLSAVGEEPLQQSLDRLR AYIAAELQEPARGQALALMQ QYIDYKKEL

Data sets:

assigned_chemical_shifts
- assigned_chemical_shifts_1
spectral_peak_list
- spectral_peak_list_1
- spectral_peak_list_2

Data type	Count
13C chemical shifts	326
15N chemical shifts	71
1H chemical shifts	568

Additional metadata:

Assembly
Samples and Experiments
Software
Spectrometers
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Assembly:

Entity Assembly ID	Entity Name	Entity ID
1	entity_1	1

Entities:

Entity 1, entity_1 89 residues - 10016.225 Da.

1

MET

GLY

HIS

LEU

PRO

2

THR

SER

PHE

ARG

GLY

THR

SER

VAL

ASP

GLY

3

SER

PHE

SER

VAL

ASP

ALA

SER

GLY

ASN

LEU

4

LEU

ILE

THR

ARG

ASP

ILE

ARG

ASN

LEU

PHE

5

ASP

ALA

PHE

LEU

SER

ALA

VAL

GLY

GLU

6

PRO

LEU

GLN

SER

LEU

ASP

ARG

LEU

ARG

7

ALA

TYR

ILE

ALA

GLU

LEU

GLN

GLU

PRO

8

ALA

ARG

GLY

GLN

ALA

LEU

ALA

LEU

MET

GLN

9

GLN

TYR

ILE

ASP

TYR

LYS

GLU

LEU

Samples:

sample_1: Lipase-interaction domain 1, [U-13C; U-15N], 530 uM; Na3PO4 20 mM

sample_conditions_1: ionic strength: 20 mM; pH: 7.4; pressure: 1 atm; temperature: 303 K

Experiments:

Name	Sample	Sample state	Sample conditions
2D 1H-15N HSQC	sample_1	isotropic	sample_conditions_1
2D 1H-13C HSQC	sample_1	isotropic	sample_conditions_1
3D HN(CA)CO	sample_1	isotropic	sample_conditions_1
3D HNCACB	sample_1	isotropic	sample_conditions_1
3D HCCH-TOCSY	sample_1	isotropic	sample_conditions_1
3D 1H-15N NOESY	sample_1	isotropic	sample_conditions_1
3D 1H-13C NOESY	sample_1	isotropic	sample_conditions_1

Software:

TOPSPIN, Bruker Biospin - collection, data analysis, processing

CARA, Keller and Wuthrich - chemical shift assignment, peak picking

CYANA, Guntert, Mumenthaler and Wuthrich - structure calculation

AMBER, Case, Darden, Cheatham III, Simmerling, Wang, Duke, Luo, ... and Kollman - geometry optimization, refinement

NMR spectrometers:

Bruker AvanceIII 600 MHz

Download HSQC peak lists in one of the following formats:
CSV: Backbone or all simulated peaks
SPARKY: Backbone or all simulated peaks