BMRB Entry 50449

Name: Backbone Chemical Shift Assignments, Chemical shift perturbation and PRE data for XcpH soluble domain from P. aeruginosa
Published: 2021-05-03

Chem Shift validation: AVS_full
BMRB Entry DOI: doi:10.13018/BMR50449

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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:

Backbone Chemical Shift Assignments, Chemical shift perturbation and PRE data for XcpH soluble domain from P. aeruginosa

Deposition date:

2020-08-31

Original release date:

2021-05-03

Authors:

Escobar, Cristian; Forest, Katrina

Citation:

Citation: Escobar, Cristian. "Backbone Chemical Shift Assignments, Chemical shift perturbation and PRE data for XcpH soluble domain from P. aeruginosa" Structure ., .-..

Assembly members:

Assembly members:
entity_1, polymer, 145 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: pETG-20A

Entity Sequences (FASTA):

Entity Sequences (FASTA):
entity_1: GSTGFASTSRELDSEAERLA GLIGVLTDEAVLDNREYGLR LERDAYQVLRYDEAKARWLP VARDSHRLPEWAELTFELDG QPLVLAGSKGEKEQKKGTDQ PQLLILSSGELSPFRLRLAE RGPEGRALSLSSDGFRLPRV EVARR

Data sets:

assigned_chemical_shifts
- assigned_chemical_shifts_1
chem_shift_perturbation
- chem_shift_perturbation_1

Data type	Count
13C chemical shifts	343
15N chemical shifts	110
1H chemical shifts	109
molecule interaction chemical shift values	71

Additional metadata:

Assembly
Samples and Experiments
Software
Spectrometers
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Assembly:

Entity Assembly ID	Entity Name	Entity ID
1	XcpH	1

Entities:

Entity 1, XcpH 145 residues - Formula weight is not available

First Glycine residue is left after TEV cleavage and is not present in native protein. Amino acid numbering corresponds to the mature protein where the N-terminal phenylalanine left after signal peptide cleavage correspond to Phe1.

1

GLY

SER

THR

GLY

PHE

ALA

SER

THR

SER

ARG

2

GLU

LEU

ASP

SER

GLU

ALA

GLU

ARG

LEU

ALA

3

GLY

LEU

ILE

GLY

VAL

LEU

THR

ASP

GLU

ALA

4

VAL

LEU

ASP

ASN

ARG

GLU

TYR

GLY

LEU

ARG

5

LEU

GLU

ARG

ASP

ALA

TYR

GLN

VAL

LEU

ARG

6

TYR

ASP

GLU

ALA

LYS

ALA

ARG

TRP

LEU

PRO

7

VAL

ALA

ARG

ASP

SER

HIS

ARG

LEU

PRO

GLU

8

TRP

ALA

GLU

LEU

THR

PHE

GLU

LEU

ASP

GLY

9

GLN

PRO

LEU

VAL

LEU

ALA

GLY

SER

LYS

GLY

10

GLU

LYS

GLU

GLN

LYS

GLY

THR

ASP

GLN

11

PRO

GLN

LEU

ILE

LEU

SER

GLY

GLU

12

LEU

SER

PRO

PHE

ARG

LEU

ARG

LEU

ALA

GLU

13

ARG

GLY

PRO

GLU

GLY

ARG

ALA

LEU

SER

LEU

14

SER

ASP

GLY

PHE

ARG

LEU

PRO

ARG

VAL

15

GLU

VAL

ALA

ARG

Samples:

sample_1: XcpH soluble domain monomer, [U-13C; U-15N], 500 uM; sodium phosphate pH 6.5 25 mM; sodium chloride 25 mM; DSS 50 uM; sodium azide 0.01%; D2O 8%

sample_2: XcpH soluble domain monomer, [U-15N], 100 uM; sodium phosphate pH 6.5 25 mM; sodium chloride 25 mM; DSS 50 uM; sodium azide 0.01%; D2O 8%; XcpJ soluble domain 80 uM

sample_3: XcpH soluble domain monomer, [U-15N], 100 uM; sodium phosphate pH 6.5 25 mM; sodium chloride 25 mM; DSS 50 uM; sodium azide 0.01%; D2O 8%; XcpJ soluble domain 50 uM

sample_4: XcpH soluble domain monomer, [U-15N], 100 uM; sodium phosphate pH 6.5 25 mM; sodium chloride 25 mM; DSS 50 uM; sodium azide 0.01%; D2O 8%; XcpJ soluble domain 20 uM

sample_5: XcpH soluble domain monomer, [U-15N], 80 uM; sodium phosphate pH 6.5 25 mM; sodium chloride 25 mM; DSS 50 uM; sodium azide 0.01%; D2O 8%; XcpJ-R46C-MTSL 24 uM

sample_6: XcpH soluble domain monomer, [U-15N], 80 uM; sodium phosphate pH 6.5 25 mM; sodium chloride 25 mM; DSS 50 uM; sodium azide 0.01%; D2O 8%; XcpJ-R46C-MTSL 24 uM; Sodium ascorbate 2 mM

sample_7: XcpH soluble domain monomer, [U-15N], 80 uM; sodium phosphate pH 6.5 25 mM; sodium chloride 25 mM; DSS 50 uM; sodium azide 0.01%; D2O 8%; XcpJ-R53C-MTSL 24 uM

sample_8: XcpH soluble domain monomer, [U-15N], 80 uM; sodium phosphate pH 6.5 25 mM; sodium chloride 25 mM; DSS 50 uM; sodium azide 0.01%; D2O 8%; XcpJ-R53C-MTSL 24 uM; Sodium ascorbate 2 mM

sample_9: XcpH soluble domain monomer, [U-15N], 80 uM; sodium phosphate pH 6.5 25 mM; sodium chloride 25 mM; DSS 50 uM; sodium azide 0.01%; D2O 8%; XcpJ-T178C-MTSL 24 uM

sample_10: XcpH soluble domain monomer, [U-15N], 80 uM; sodium phosphate pH 6.5 25 mM; sodium chloride 25 mM; DSS 50 uM; sodium azide 0.01%; D2O 8%; XcpJ-T178C-MTSL 24 uM; Sodium ascorbate 2 mM

sample_11: XcpH soluble domain monomer, [U-15N], 80 uM; sodium phosphate pH 6.5 25 mM; sodium chloride 25 mM; DSS 50 uM; sodium azide 0.01%; D2O 8%; XcpJ-E180C-MTSL 24 uM

sample_12: XcpH soluble domain monomer, [U-15N], 80 uM; sodium phosphate pH 6.5 25 mM; sodium chloride 25 mM; DSS 50 uM; sodium azide 0.01%; D2O 8%; XcpJ-E180C-MTSL 24 uM; Sodium ascorbate 2 mM

sample_conditions_1: ionic strength: 50 mM; pH: 6.5; pressure: 1 atm; temperature: 310 K

sample_conditions_2: ionic strength: 50 mM; pH: 6.5; pressure: 1 atm; temperature: 310 K

sample_conditions_3: ionic strength: 50 mM; pH: 6.5; pressure: 1 atm; temperature: 310 K

Experiments:

Name	Sample	Sample state	Sample conditions
2D 1H-15N HSQC	sample_1	isotropic	sample_conditions_1
3D HNCO	sample_1	isotropic	sample_conditions_1
3D HN(CA)CO	sample_1	isotropic	sample_conditions_1
3D CBCA(CO)NH	sample_1	isotropic	sample_conditions_1
3D HNCACB	sample_1	isotropic	sample_conditions_1
2D 1H-15N HSQC	sample_3	isotropic	sample_conditions_3
2D 1H-15N HSQC	sample_3	isotropic	sample_conditions_3
2D 1H-15N HSQC	sample_7	isotropic	sample_conditions_3
2D 1H-15N HSQC	sample_4	isotropic	sample_conditions_3
2D 1H-15N HSQC	sample_8	isotropic	sample_conditions_3
2D 1H-15N HSQC	sample_5	isotropic	sample_conditions_3
2D 1H-15N HSQC	sample_9	isotropic	sample_conditions_3
2D 1H-15N HSQC	sample_6	isotropic	sample_conditions_3
2D 1H-15N HSQC	sample_10	isotropic	sample_conditions_3
2D 1H-15N HSQC	sample_12	isotropic	sample_conditions_2
2D 1H-15N HSQC	sample_11	isotropic	sample_conditions_2
2D 1H-15N HSQC	sample_2	isotropic	sample_conditions_2

Software:

NMRFAM-SPARKY - chemical shift assignment

NMRPipe - processing

TOPSPIN - Signal Intensity measurement

NMR spectrometers:

Bruker AVANCE III 900 MHz

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