BMRB Entry 50437

Name: Mutation that removes disulfide in HdeA results in an unfolded protein that gains structure at low pH
Published: 2020-11-02

Chem Shift validation: AVS_full
BMRB Entry DOI: doi:10.13018/BMR50437

NMR-STAR file interactive viewer.
NMR-STAR v3 text file.
XML gzip file.
RDF gzip file.
All files associated with the entry

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

Select model:

I am color blind

Download raw data. Direct link to this display. Help

Title:

Mutation that removes disulfide in HdeA results in an unfolded protein that gains structure at low pH

Deposition date:

2020-08-14

Original release date:

2020-11-02

Authors:

Aguirre-Cardenas, M. Imex; Geddes-Buehre, Dane; Crowhurst, Karin

Citation:

Citation: Aguirre-Cardenas, M. Imex; Geddes-Buehre, Dane; Crowhurst, Karin. "Removal of disulfide from acid stress chaperone HdeA does not wholly eliminate structure or function at low pH" Biochem. Biophys. Rep. 27, 101064-101064 (2021).

Assembly members:

Assembly members:
entity_1, polymer, 89 residues, Formula weight is not available

Natural source:

Natural source: Common Name: E. coli Taxonomy ID: 562 Superkingdom: Bacteria Kingdom: not available Genus/species: Escherichia coli

Experimental source:

Experimental source: Production method: recombinant technology Host organism: Escherichia coli Vector: pET21a

Entity Sequences (FASTA):

Entity Sequences (FASTA):
entity_1: ADAQKAADNKKPVNSWTSED FLAVDESFQPTAVGFAEALN NKDKPEDAVLDVQGIATVTP AIVQASTQDKQANFKDKVKG EWDKIKKDM

Data sets:

assigned_chemical_shifts
- assigned_chemical_shifts_1
- assigned_chemical_shifts_2

Data type	Count
13C chemical shifts	433
15N chemical shifts	164
1H chemical shifts	164

Additional metadata:

Assembly
Samples and Experiments
Software
Spectrometers
Hide all

Assembly:

Entity Assembly ID	Entity Name	Entity ID
1	HdeA-C18S-C66S	1

Entities:

Entity 1, HdeA-C18S-C66S 89 residues - Formula weight is not available

1

ALA

ASP

ALA

GLN

LYS

ALA

ASP

ASN

LYS

2

LYS

PRO

VAL

ASN

SER

TRP

THR

SER

GLU

ASP

3

PHE

LEU

ALA

VAL

ASP

GLU

SER

PHE

GLN

PRO

4

THR

ALA

VAL

GLY

PHE

ALA

GLU

ALA

LEU

ASN

5

ASN

LYS

ASP

LYS

PRO

GLU

ASP

ALA

VAL

LEU

6

ASP

VAL

GLN

GLY

ILE

ALA

THR

VAL

THR

PRO

7

ALA

ILE

VAL

GLN

ALA

SER

THR

GLN

ASP

LYS

8

GLN

ALA

ASN

PHE

LYS

ASP

LYS

VAL

LYS

GLY

9

GLU

TRP

ASP

LYS

ILE

LYS

ASP

MET

Samples:

sample_1: HdeA-C18S-C66S, [U-100% 13C; U-100% 15N], 0.45 mM; sodium citrate 50 mM

sample_2: HdeA-C18S-C66S, [U-100% 13C; U-100% 15N], 0.45 mM; sodium citrate 50 mM

sample_conditions_1: ionic strength: 0.05 M; pH: 2.0; pressure: 1 atm; temperature: 298 K

sample_conditions_2: ionic strength: 0.05 M; pH: 6.0; pressure: 1 atm; temperature: 298 K

Experiments:

Name	Sample	Sample state	Sample conditions
2D 1H-15N HSQC	sample_1	isotropic	sample_conditions_1
2D 1H-15N HSQC	sample_2	isotropic	sample_conditions_2
3D CBCA(CO)NH	sample_1	isotropic	sample_conditions_1
3D CBCA(CO)NH	sample_2	isotropic	sample_conditions_2
3D HNCO	sample_1	isotropic	sample_conditions_1
3D HNCO	sample_2	isotropic	sample_conditions_2
3D HNCACB	sample_1	isotropic	sample_conditions_1
3D HNCACB	sample_2	isotropic	sample_conditions_2
3D HN(CA)CO	sample_1	isotropic	sample_conditions_1
3D HN(CA)CO	sample_2	isotropic	sample_conditions_2
3D HNN	sample_1	isotropic	sample_conditions_1
3D HNN	sample_2	isotropic	sample_conditions_2

Software:

VNMRj - collection

NMRPipe v4.0 - processing

NMRViewJ - chemical shift assignment, data analysis

NMR spectrometers:

Agilent DD2 600 MHz

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