BMRB Entry 51508

Name: Backbone 1H, 13C, and 15N Chemical Shift Assignments for ASCb
Published: 2022-07-04

Chem Shift validation: AVS_full
BMRB Entry DOI: doi:10.13018/BMR51508

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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 1H, 13C, and 15N Chemical Shift Assignments for ASCb

Deposition date:

2022-06-29

Original release date:

2022-07-04

Authors:

Diaz-parga, Pedro; de Alba babastarrechea, Eva

Citation:

Citation: Diaz-parga, Pedro; de Alba babastarrechea, Eva. "Inflammasome regulation by adaptor isoforms, ASC and ASCb, via differential self-assembly" J. Biol. Chem. 298, 101566-101566 (2022).
PubMed: 35007535

Assembly members:

Assembly members:
entity_1, polymer, 196 residues, 22132.2344 Da.

Natural source:

Natural source: Common Name: Human Taxonomy ID: 9606 Superkingdom: Eukaryota Kingdom: Metazoa Genus/species: Homo sapiens

Experimental source:

Experimental source: Production method: recombinant technology Host organism: Escherichia coli Vector: PET-15b

Entity Sequences (FASTA):

Entity Sequences (FASTA):
entity_1: MGSSHHHHHHSSGLVPRGSH MGRARDAILDALENLTAEEL KKFKLKLLSVPLREGYGRIP RGALLSMDALDLTDKLVSFY LETYGAELTANVLRDMGLQE MAGQLQAATHQGLHFIDQHR AALIARVTNVEWLLDALYGK VLTDEQYQAVRAEPTNPSKM RKLFSFTPAWNWTCKDLLLQ ALRESQSYLVEDLERS

Data sets:

assigned_chemical_shifts
- assigned_chemical_shifts_1

Data type	Count
13C chemical shifts	321
15N chemical shifts	171
1H chemical shifts	171

Additional metadata:

Assembly
Samples and Experiments
Software
Spectrometers
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Assembly:

Entity Assembly ID	Entity Name	Entity ID
1	ASCb protein	1

Entities:

Entity 1, ASCb protein 196 residues - 22132.2344 Da.

Residues 1-20 contain a His-tag and a thrombin cleavage site. Sequence of ASCb begins at residue 21 (M) and is labeled as M1 in the NMR file.

1

MET

GLY

SER

HIS

2

SER

GLY

LEU

VAL

PRO

ARG

GLY

SER

HIS

3

MET

GLY

ARG

ALA

ARG

ASP

ALA

ILE

LEU

ASP

4

ALA

LEU

GLU

ASN

LEU

THR

ALA

GLU

LEU

5

LYS

PHE

LYS

LEU

LYS

LEU

SER

VAL

6

PRO

LEU

ARG

GLU

GLY

TYR

GLY

ARG

ILE

PRO

7

ARG

GLY

ALA

LEU

SER

MET

ASP

ALA

LEU

8

ASP

LEU

THR

ASP

LYS

LEU

VAL

SER

PHE

TYR

9

LEU

GLU

THR

TYR

GLY

ALA

GLU

LEU

THR

ALA

10

ASN

VAL

LEU

ARG

ASP

MET

GLY

LEU

GLN

GLU

11

MET

ALA

GLY

GLN

LEU

GLN

ALA

THR

HIS

12

GLN

GLY

LEU

HIS

PHE

ILE

ASP

GLN

HIS

ARG

13

ALA

LEU

ILE

ALA

ARG

VAL

THR

ASN

VAL

14

GLU

TRP

LEU

ASP

ALA

LEU

TYR

GLY

LYS

15

VAL

LEU

THR

ASP

GLU

GLN

TYR

GLN

ALA

VAL

16

ARG

ALA

GLU

PRO

THR

ASN

PRO

SER

LYS

MET

17

ARG

LYS

LEU

PHE

SER

PHE

THR

PRO

ALA

TRP

18

ASN

TRP

THR

CYS

LYS

ASP

LEU

GLN

19

ALA

LEU

ARG

GLU

SER

GLN

SER

TYR

LEU

VAL

20

GLU

ASP

LEU

GLU

ARG

SER

Samples:

sample_1: glycine 20 mM; TCEP 1 mM; ASCb, [U-99% 13C; U-99% 15N], 0.2 mM

sample_conditions_1: ionic strength: 0 M; pH: 3.8; pressure: 1 atm; temperature: 298 K

Experiments:

Name	Sample	Sample state	Sample conditions
2D 1H-15N HSQC	sample_1	isotropic	sample_conditions_1
3D CBCA(CO)NH	sample_1	isotropic	sample_conditions_1
3D HNCACB	sample_1	isotropic	sample_conditions_1

Software:

TOPSPIN - collection

NMR spectrometers:

Bruker AVANCE III HD 800 MHz

UNP	Q9ULZ3-2
AlphaFold	Q9ULZ3-2