BMRB Entry 27693

Name: Backbone and Sidechian 1H, 13C, and 15N Chemical Shift Assignments for Escherichia Coli Periplasmic Chaperone HdeA at pH 1.5
Published: 2018-12-19

Chem Shift validation: AVS_full, LACS
BMRB Entry DOI: doi:10.13018/BMR27693

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:

Backbone and Sidechian 1H, 13C, and 15N Chemical Shift Assignments for Escherichia Coli Periplasmic Chaperone HdeA at pH 1.5

Deposition date:

2018-11-19

Original release date:

2018-12-19

Authors:

Yu, Xing-Chi; Jin, Changwen; Hu, Yunfei

Citation:

Citation: Yu, Xing-Chi; Hu, Yunfei; Ding, Jienv; Li, Hongwei; Jin, Changwen. "Structural basis and mechanism of the unfolding-induced activation of HdeA, a bacterial acid response chaperone" J. Biol. Chem. 294, 3192-3206 (2019).
PubMed: 30573682

Assembly members:

Assembly members:
HdeA_F28W, polymer, 89 residues, 9779.95 Da.

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: pET-28a(+)

Entity Sequences (FASTA):

Entity Sequences (FASTA):
HdeA_F28W: ADAQKAADNKKPVNSWTCED FLAVDESWQPTAVGFAEALN NKDKPEDAVLDVQGIATVTP AIVQACTQDKQANFKDKVKG EWDKIKKDM

Data sets:

assigned_chemical_shifts
- assignments_HdeA

Data type	Count
13C chemical shifts	344
15N chemical shifts	84
1H chemical shifts	531

Additional metadata:

Assembly
Samples and Experiments
Software
Spectrometers
Hide all

Assembly:

Entity Assembly ID	Entity Name	Entity ID
1	HdeA monomer	1

Entities:

Entity 1, HdeA monomer 89 residues - 9779.95 Da.

The sequence is numbered according to the mature protein in which the signal peptide is cleaved.

1

ALA

ASP

ALA

GLN

LYS

ALA

ASP

ASN

LYS

2

LYS

PRO

VAL

ASN

SER

TRP

THR

CYS

GLU

ASP

3

PHE

LEU

ALA

VAL

ASP

GLU

SER

TRP

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

CYS

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_F28W, [U-100% 13C; U-100% 15N], 0.5 mM; H2O 90%; D2O, [U-100% 2H], 10%; sodium phosphate 50 mM; citric acid 45 mM; DSS 0.01 % w/v

sample_conditions_1: ionic strength: 0.15 M; pH: 1.5; pressure: 1 atm; temperature: 298 K

Experiments:

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

Software:

NMRPipe, Delaglio, Zhengrong and Bax - processing

NMRView vv5.0.4, Johnson, One Moon Scientific - chemical shift assignment, data analysis, peak picking

NMR spectrometers:

Bruker Avance 700 MHz

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