BMRB Entry 50781

Name: Backbone 1H, 13C, and 15N chemical shift assignments for ClpX residues 1-55
Published: 2022-04-15

Chem Shift validation: AVS_full
BMRB Entry DOI: doi:10.13018/BMR50781

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 1H, 13C, and 15N chemical shift assignments for ClpX residues 1-55

Deposition date:

2021-02-19

Original release date:

2022-04-15

Authors:

Vos, Margaret; Peti, Wolfgang; Page, Rebecca

Citation:

Citation: Vos, Margaret; Piraino, Benjamin; LaBreck, Christopher; Rahmani, Negar; Trebino, Catherine; Schoenle, Marta; Peti, Wolfgang; Camberg, Jodi; Page, Rebecca. "Degradation of the E. coli antitoxin MqsA by the proteolytic complex ClpXP is regulated by zinc occupancy and oxidation" J. Biol. Chem. 298, 101557-101557 (2022).
PubMed: 34974059

Assembly members:

Assembly members:
entity_1, polymer, 57 residues, Formula weight is not available
entity_ZN, non-polymer, 65.409 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: RP1B

Entity Sequences (FASTA):

Entity Sequences (FASTA):
entity_1: GHMTDKRKDGSGKLLYCSFC GKSQHEVRKLIAGPSVYICD ECVDLCNDIIREEIKEV

Data sets:

assigned_chemical_shifts
- assigned_chemical_shifts_1

Data type	Count
13C chemical shifts	111
15N chemical shifts	53
1H chemical shifts	53

Additional metadata:

Assembly
Samples and Experiments
Software
Spectrometers
Hide all

Assembly:

Entity Assembly ID	Entity Name	Entity ID
1	ClpX Residues 1-55 Dimer, Chain 1	1
2	ClpX Residues 1-55 Dimer, Chain 2	1
3	Zinc Ion, 1	2
4	Zinc Ion, 2	2

Entities:

Entity 1, ClpX Residues 1-55 Dimer, Chain 1 57 residues - Formula weight is not available

GH are a cloning artifacts; ClpX sequence starts with MTD

1

GLY

HIS

MET

THR

ASP

LYS

ARG

LYS

ASP

GLY

2

SER

GLY

LYS

LEU

TYR

CYS

SER

PHE

CYS

3

GLY

LYS

SER

GLN

HIS

GLU

VAL

ARG

LYS

LEU

4

ILE

ALA

GLY

PRO

SER

VAL

TYR

ILE

CYS

ASP

5

GLU

CYS

VAL

ASP

LEU

CYS

ASN

ASP

ILE

6

ARG

GLU

ILE

LYS

GLU

VAL

Entity 2, Zinc Ion, 1 - Zn - 65.409 Da.

1

ZN

Samples:

sample_1: ClpX Residues 1-55, [U-99% 13C; U-99% 15N], 800 uM; TCEP 0.5 mM; sodium chloride 50 mM; sodium phosphate 20 mM; ZnSO4 500 uM

sample_2: ClpX Residues 1-55, [U-99% 15N], 200 uM; TCEP 0.5 mM; sodium chloride 50 mM; sodium phosphate 20 mM; ZnSO4 500 uM

sample_conditions_1: pH: 6.5; pressure: 1 atm; temperature: 298 K

Experiments:

Name	Sample	Sample state	Sample conditions
2D 1H-15N HSQC	sample_2	isotropic	sample_conditions_1
3D HNCA	sample_1	isotropic	sample_conditions_1
3D HNCACB	sample_1	isotropic	sample_conditions_1
3D HN(CO)CA	sample_1	isotropic	sample_conditions_1
3D CBCACONH	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 HCCCONH	sample_1	isotropic	sample_conditions_1

Software:

TOPSPIN v4.1.1 - collection, data analysis

CARA v1.9 - chemical shift assignment

NMR spectrometers:

Bruker AVANCE NEO 600 MHz