BMRB Entry 25943

Name: 3D NMR solution structure of NLRP3 PYD
Published: 2016-07-25

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PDB ID: 2naq
Entry in NMR Restraints Grid
Validation report in NRG-CING
Chem Shift validation: AVS_full, LACS, SPARTA
BMRB Entry DOI: doi:10.13018/BMR25943
MolProbity Validation Chart

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Bioinformatics (2015) 31 (8): 1322-1324 doi:10.1093/bioinformatics/btu829

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Title: 3D NMR solution structure of NLRP3 PYD PubMed: 27432880

Deposition date: 2016-01-07 Original release date: 2016-07-25

Authors: de Alba, Eva; Oroz, Javier

Citation: Oroz, Javier; Barrera-Vilarmau, Susana; Alfonso, Carlos; Rivas, German; de Alba, Eva. "Asc pyrin domain self-associates and binds nlrp3 using Equivalent binding interfaces" J. Biol. Chem. 291, 19487-19501 (2016).

Assembly members:
entity, polymer, 91 residues, 10643.387 Da.

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

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

Entity Sequences (FASTA):
entity: MASTRCKLARYLEDLEDVDL KKFKMHLEDYPPQKGCIPLP RGQTEKADHVDLATLMIDFN GEEKAWAMAVWIFAAINRRD LYEKAKRDEPK

Data sets:

assigned_chemical_shifts
- assigned_chem_shift_list_1

Data type	Count
13C chemical shifts	289
15N chemical shifts	84
1H chemical shifts	614

Additional metadata:

Assembly
Samples and Experiments
Software
Spectrometers
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Assembly:

Entity Assembly ID	Entity Name	Entity ID
1	entity	1

Entities:

Entity 1, entity 91 residues - 10643.387 Da.

1

MET

ALA

SER

THR

ARG

CYS

LYS

LEU

ALA

ARG

2

TYR

LEU

GLU

ASP

LEU

GLU

ASP

VAL

ASP

LEU

3

LYS

PHE

LYS

MET

HIS

LEU

GLU

ASP

TYR

4

PRO

GLN

LYS

GLY

CYS

ILE

PRO

LEU

PRO

5

ARG

GLY

GLN

THR

GLU

LYS

ALA

ASP

HIS

VAL

6

ASP

LEU

ALA

THR

LEU

MET

ILE

ASP

PHE

ASN

7

GLY

GLU

LYS

ALA

TRP

ALA

MET

ALA

VAL

8

TRP

ILE

PHE

ALA

ILE

ASN

ARG

ASP

9

LEU

TYR

GLU

LYS

ALA

LYS

ARG

ASP

GLU

PRO

10

LYS

Samples:

sample_1: entity, [U-13C; U-15N], 100 – 200 uM; TCEP, [U-2H], 5 mM; sodium azide 100 uM; H2O 95%; D2O 5%

sample_conditions_1: ionic strength: 0.0051 M; pH: 3.6; pressure: 1 atm; temperature: 303 K

Experiments:

Name	Sample	Sample state	Sample conditions
2D 1H-15N HSQC	sample_1	isotropic	sample_conditions_1
3D HNCACB	sample_1	isotropic	sample_conditions_1
3D CBCA(CO)NH	sample_1	isotropic	sample_conditions_1
3D HBHA(CO)NH	sample_1	isotropic	sample_conditions_1
3D H(CCO)NH	sample_1	isotropic	sample_conditions_1
3D HCCH-TOCSY	sample_1	isotropic	sample_conditions_1
3D 1H-15N NOESY	sample_1	isotropic	sample_conditions_1
3D 1H-13C NOESY	sample_1	isotropic	sample_conditions_1
2D 1H-15N HSQC	sample_1	isotropic	sample_conditions_1

Software:

X-PLOR_NIH, Schwieters, Kuszewski, Tjandra and Clore - structure solution

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

NMRDraw, Delaglio, Grzesiek, Vuister, Zhu, Pfeifer and Bax - data analysis

PIPP, Garrett - chemical shift assignment

TOPSPIN, Bruker Biospin - collection

TALOS, Cornilescu, Delaglio and Bax - data analysis

Molmol, Koradi, Billeter and Wuthrich - data analysis

ProcheckNMR, Laskowski and MacArthur - geometry optimization

NMR spectrometers:

Bruker Avance 600 MHz
Bruker Avance 600 MHz

Download simulated HSQC data in one of the following formats:
CSV: Backbone or all simulated shifts
SPARKY: Backbone or all simulated shifts