BMRB Entry 26061

Name: NMR solution structure of MAL/TIRAP TIR domain
Published: 2017-05-30

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PDB ID: 2ndh
Entry in NMR Restraints Grid
Validation report in NRG-CING
Chem Shift validation: AVS_full, LACS, SPARTA
BMRB Entry DOI: doi:10.13018/BMR26061
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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:

NMR solution structure of MAL/TIRAP TIR domain

Deposition date:

2016-05-27

Original release date:

2017-05-30

Authors:

Lavrencic, Peter; Mobli, Mehdi

Citation:

Citation: Hughes, Mark; Lavrencic, Peter; Coll, Rebecca; Ve, Thomas; Ryan, Dylan; Williams, Niamh; Menon, Deepthi; Mansell, Ashley; Board, Philip; Mobli, Mehdi; Kobe, Bostjan; O'Neill, Luke. "Solution structure of the TLR adaptor MAL/TIRAP reveals an intact BB loop and supports MAL Cys91 glutathionylation for signaling" Proc. Natl. Acad. Sci. U.S.A. 114, E6480-E6489 (2017).
PubMed: 28739909

Assembly members:

Assembly members:
entity, polymer, 143 residues, 15726.982 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: pMCSG7

Entity Sequences (FASTA):

Entity Sequences (FASTA):
entity: SSRWSKDYDVCVCHSEEDLV AAQDLVSYLEGSTASLRAFL QLRDATPGGAIVSELCQALS SSHCRVLLITPGFLQDPWCK YQMLQALTEAPGAEGCTIPL LSGLSRAAYPPELRFMYYVD GRGPDGGFRQVKEAVMRYLQ TLS

Data sets:

assigned_chemical_shifts
- assigned_chem_shift_list_1

Data type	Count
13C chemical shifts	419
15N chemical shifts	104
1H chemical shifts	662

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 143 residues - 15726.982 Da.

1

SER

ARG

TRP

SER

LYS

ASP

TYR

ASP

VAL

2

CYS

VAL

CYS

HIS

SER

GLU

ASP

LEU

VAL

3

ALA

GLN

ASP

LEU

VAL

SER

TYR

LEU

GLU

4

GLY

SER

THR

ALA

SER

LEU

ARG

ALA

PHE

LEU

5

GLN

LEU

ARG

ASP

ALA

THR

PRO

GLY

ALA

6

ILE

VAL

SER

GLU

LEU

CYS

GLN

ALA

LEU

SER

7

SER

HIS

CYS

ARG

VAL

LEU

ILE

THR

8

PRO

GLY

PHE

LEU

GLN

ASP

PRO

TRP

CYS

LYS

9

TYR

GLN

MET

LEU

GLN

ALA

LEU

THR

GLU

ALA

10

PRO

GLY

ALA

GLU

GLY

CYS

THR

ILE

PRO

LEU

11

LEU

SER

GLY

LEU

SER

ARG

ALA

TYR

PRO

12

PRO

GLU

LEU

ARG

PHE

MET

TYR

VAL

ASP

13

GLY

ARG

GLY

PRO

ASP

GLY

PHE

ARG

GLN

14

VAL

LYS

GLU

ALA

VAL

MET

ARG

TYR

LEU

GLN

15

THR

LEU

SER

Samples:

sample_1: entity, [U-99% 13C; U-99% 15N], 300 uM; TRIS 20 mM; D2O 5%; sodium chloride 200 mM; H2O 95%

sample_conditions_1: ionic strength: 0.2 M; pH: 8.6; pressure: 1 atm; temperature: 291 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 HCCH-TOCSY	sample_1	isotropic	sample_conditions_1
2D 1H-13C HSQC aliphatic	sample_1	isotropic	sample_conditions_1
2D 1H-13C HSQC aromatic	sample_1	isotropic	sample_conditions_1
3D 1H-15N NOESY	sample_1	isotropic	sample_conditions_1
3D HBHA(CO)NH	sample_1	isotropic	sample_conditions_1
3D HN(CO)CA	sample_1	isotropic	sample_conditions_1

Software:

TALOS vTALOS+, Cornilescu, Delaglio and Bax - chemical shift calculation

CCPNMR v2.4, CCPN - chemical shift assignment, data analysis, peak picking

TOPSPIN, Bruker Biospin - processing

Rowland_NMR_toolkit v3, JC Hoch et al. - processing

CYANA v2.1, Guntert, Mumenthaler and Wuthrich - structure solution

NMR spectrometers:

Bruker Avance 900 MHz

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