BMRB Entry 25561

Name: Structure and assembly of the mouse ASC filament by combined NMR spectroscopy and cryo-electron microscopy
Published: 2016-06-30

Chem Shift validation: AVS_full, LACS
BMRB Entry DOI: doi:10.13018/BMR25561

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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:

Structure and assembly of the mouse ASC filament by combined NMR spectroscopy and cryo-electron microscopy

Deposition date:

2015-04-01

Original release date:

2016-06-30

Authors:

Sborgi, Lorenzo

Citation:

Citation: Sborgi, Lorenzo; Ravotti, Francesco; Dandey, Venkata; Dick, Mathias; Mazur, Adam; Reckel, Sina; Chami, Mohamed; Scherer, Sebastian; Huber, Matthias; Bockmann, Anja; Egelman, Edward; Stahlberg, Henning; Broz, Petr; Meier, Beat; Hiller, Sebastian. "Structure and assembly of the mouse ASC inflammasome by combined NMR spectroscopy and cryo-electron microscopy" Proc. Natl. Acad. Sci. U. S. A. 112, 13237-13242 (2015).
PubMed: 26464513

Assembly members:

Assembly members:
ASC_PYD, polymer, 103 residues, Formula weight is not available

Natural source:

Natural source: Common Name: Mouse Taxonomy ID: 10090 Superkingdom: Eukaryota Kingdom: Metazoa Genus/species: Mus musculus

Experimental source:

Experimental source: Production method: recombinant technology Host organism: Escherichia coli Vector: pET28a

Entity Sequences (FASTA):

Entity Sequences (FASTA):
ASC_PYD: MGRARDAILDALENLSGDEL KKFKMKLLTVQLREGYGRIP RGALLQMDAIDLTDKLVSYY LESYGLELTMTVLRDMGLQE LAEQLQTTKEEGSGSLEHHH HHH

Data sets:

assigned_chemical_shifts
- assigned_chem_shift_list_1

Data type	Count
13C chemical shifts	192
15N chemical shifts	100
1H chemical shifts	100

Additional metadata:

Assembly
Samples and Experiments
Software
Spectrometers
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Assembly:

Entity Assembly ID	Entity Name	Entity ID
1	ASC Pyrin domain	1

Entities:

Entity 1, ASC Pyrin domain 103 residues - Formula weight is not available

1

MET

GLY

ARG

ALA

ARG

ASP

ALA

ILE

LEU

ASP

2

ALA

LEU

GLU

ASN

LEU

SER

GLY

ASP

GLU

LEU

3

LYS

PHE

LYS

MET

LYS

LEU

THR

VAL

4

GLN

LEU

ARG

GLU

GLY

TYR

GLY

ARG

ILE

PRO

5

ARG

GLY

ALA

LEU

GLN

MET

ASP

ALA

ILE

6

ASP

LEU

THR

ASP

LYS

LEU

VAL

SER

TYR

7

LEU

GLU

SER

TYR

GLY

LEU

GLU

LEU

THR

MET

8

THR

VAL

LEU

ARG

ASP

MET

GLY

LEU

GLN

GLU

9

LEU

ALA

GLU

GLN

LEU

GLN

THR

LYS

GLU

10

GLU

GLY

SER

GLY

SER

LEU

GLU

HIS

11

HIS

Samples:

sample_1: ASC PYD, [U-100% 13C; U-100% 15N], 0.3 mM

sample_conditions_1: ionic strength: 150 mM; pH: 3.7; pressure: 1 atm; temperature: 298 K

Experiments:

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

Software:

CARA, Keller and Wuthrich - chemical shift assignment

NMR spectrometers:

Bruker Ascend II 700 MHz

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