BMRB Entry 25510

Name: NMR Solution structure of AIM2 PYD from Mus musculus
Published: 2015-04-21

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PDB ID: 2n00
Entry in NMR Restraints Grid
Validation report in NRG-CING
Chem Shift validation: AVS_anomalous, AVS_full, SPARTA
BMRB Entry DOI: doi:10.13018/BMR25510
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Bioinformatics (2015) 31 (8): 1322-1324 doi:10.1093/bioinformatics/btu829

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Title: NMR Solution structure of AIM2 PYD from Mus musculus PubMed: 25888795

Deposition date: 2015-03-01 Original release date: 2015-04-21

Authors: Hou, Xianhui; Niu, Xiaogang

Citation: Hou, Xianhui; Niu, Xiaogang. "The NMR solution structure of AIM2 PYD domain from Mus musculus reveals a distinct 2-3 helix conformation from its human homologues" Biochem. Biophys. Res. Commun. 461, 396-400 (2015).

Assembly members:
entity, polymer, 95 residues, 10963.646 Da.

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

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

Entity Sequences (FASTA):
entity: MESEYREMLLLTGLDHITEE ELKRFKYFALTEFQIARSTL DVADRTELADHLIQSAGAAS AVTKAINIFQKLNYMHIANA LEEKKKEAERKLMTN

Data sets:

assigned_chemical_shifts
- assigned_chem_shift_list_1

Data type	Count
13C chemical shifts	378
15N chemical shifts	94
1H chemical shifts	589

Additional metadata:

Assembly
Samples and Experiments
Software
Spectrometers
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Assembly:

Entity Assembly ID	Entity Name	Entity ID
1	AIM2 PYD	1

Entities:

Entity 1, AIM2 PYD 95 residues - 10963.646 Da.

1

MET

GLU

SER

GLU

TYR

ARG

GLU

MET

LEU

2

LEU

THR

GLY

LEU

ASP

HIS

ILE

THR

GLU

3

GLU

LEU

LYS

ARG

PHE

LYS

TYR

PHE

ALA

LEU

4

THR

GLU

PHE

GLN

ILE

ALA

ARG

SER

THR

LEU

5

ASP

VAL

ALA

ASP

ARG

THR

GLU

LEU

ALA

ASP

6

HIS

LEU

ILE

GLN

SER

ALA

GLY

ALA

SER

7

ALA

VAL

THR

LYS

ALA

ILE

ASN

ILE

PHE

GLN

8

LYS

LEU

ASN

TYR

MET

HIS

ILE

ALA

ASN

ALA

9

LEU

GLU

LYS

GLU

ALA

GLU

ARG

10

LYS

LEU

MET

THR

ASN

Samples:

sample_1: entity, [U-100% 13C; U-100% 15N], 0.5 mM; NaAc/HAc 20 mM; H2O 90%; D2O 10%

sample_conditions_1: ionic strength: 0.02 M; pH: 4.0; 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
3D HNCO	sample_1	isotropic	sample_conditions_1
3D H(CCO)NH	sample_1	isotropic	sample_conditions_1
3D HCCH-COSY	sample_1	isotropic	sample_conditions_1
3D C(CO)NH	sample_1	isotropic	sample_conditions_1
3D 1H-15N NOESY	sample_1	isotropic	sample_conditions_1

Software:

CNS, Brunger, Adams, Clore, Gros, Nilges and Read - refinement

NMR spectrometers:

Bruker Avance 700 MHz

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