BMRB Entry 18608

Name: Backbone resonance assignment of ASC pyrin domain
Published: 2012-10-18

Chem Shift validation: AVS_full, LACS
BMRB Entry DOI: doi:10.13018/BMR18608

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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 resonance assignment of ASC pyrin domain

Deposition date:

2012-07-23

Original release date:

2012-10-18

Authors:

Vajjhala, Parimala; Mirams, Ruth; Hill, Justine

Citation:

Citation: Vajjhala, Parimala; Mirams, Ruth; Hill, Justine. "Multiple binding sites on the pyrin domain of ASC protein allow self-association and interaction with NLRP3 protein." J. Biol. Chem. 287, 41732-41743 (2012).
PubMed: 23066025

Assembly members:

Assembly members:
ASC_PYD, polymer, 108 residues, Formula weight is not available

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: pQE-30

Entity Sequences (FASTA):

Entity Sequences (FASTA):
ASC_PYD: MRGSHHHHHHGSMGRARDAI LDALENLTAEELKKFKLKLL SVPLREGYGRIPRGALLSMD SLDLTDKLVSFYLETYGAEL TANVLRDMGLQEMAGQLQAA THQGSGAA

Data sets:

assigned_chemical_shifts
- assigned_chem_shift_list_1

Data type	Count
13C chemical shifts	266
15N chemical shifts	89
1H chemical shifts	88

Additional metadata:

Assembly
Samples and Experiments
Software
Spectrometers
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Assembly:

Entity Assembly ID	Entity Name	Entity ID
1	ASC PYD	1

Entities:

Entity 1, ASC PYD 108 residues - Formula weight is not available

1

MET

ARG

GLY

SER

HIS

2

GLY

SER

MET

GLY

ARG

ALA

ARG

ASP

ALA

ILE

3

LEU

ASP

ALA

LEU

GLU

ASN

LEU

THR

ALA

GLU

4

GLU

LEU

LYS

PHE

LYS

LEU

LYS

LEU

5

SER

VAL

PRO

LEU

ARG

GLU

GLY

TYR

GLY

ARG

6

ILE

PRO

ARG

GLY

ALA

LEU

SER

MET

ASP

7

SER

LEU

ASP

LEU

THR

ASP

LYS

LEU

VAL

SER

8

PHE

TYR

LEU

GLU

THR

TYR

GLY

ALA

GLU

LEU

9

THR

ALA

ASN

VAL

LEU

ARG

ASP

MET

GLY

LEU

10

GLN

GLU

MET

ALA

GLY

GLN

LEU

GLN

ALA

11

THR

HIS

GLN

GLY

SER

GLY

ALA

Samples:

sample_1: ASC PYD, [U-99% 15N], 0.3 mM; sodium phosphate 50 mM; sodium chloride 150 mM; D2O, [U-99% 2H], 10%; H2O 90%

sample_2: ASC PYD, [U-99% 13C; U-99% 15N], 0.9 mM; sodium phosphate 50 mM; sodium chloride 150 mM; D2O, [U-99% 2H], 10%; H2O 90%

sample_conditions_1: ionic strength: 150 mM; pH: 4; pressure: 1 atm; temperature: 298 K

Experiments:

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

Software:

TOPSPIN, Bruker Biospin - collection

NMRPipe, Delaglio, Grzesiek, Vuister, Zhu, Pfeifer and Bax - processing

NMRDraw, Delaglio, Grzesiek, Vuister, Zhu, Pfeifer and Bax - processing

Analysis, CCPN - processing

HADDOCK, Alexandre Bonvin - structure solution

NMR spectrometers:

Bruker Avance 750 MHz

PDB	1UCP 3J63
DBJ	BAA87339 BAG37041 BAG73625
GB	AAF99665 AAG01187 AAG01188 AAG30286 AAH13569
REF	NP_037390 NP_660183 XP_001158625 XP_001158687 XP_003280507
SP	Q9ULZ3
AlphaFold	Q9ULZ3