BMRB Entry 30237

Name: NMR structure of monomeric human IRAK-M Death Domain R56D, Y61E mutant
Published: 2018-01-17

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PDB ID: 5uke
Entry in NMR Restraints Grid
Validation report in NRG-CING
Chem Shift validation: AVS_full, LACS
BMRB Entry DOI: doi:10.13018/BMR30237
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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 structure of monomeric human IRAK-M Death Domain R56D, Y61E mutant

Deposition date:

2017-01-20

Original release date:

2018-01-17

Authors:

Kwon, J.; Nicholson, L.

Citation:

Citation: Nechama, Morris; Kwon, Jeahoo; Wei, Shuo; Kyi, Adrian Tun; Welner, Robert; Ben-Dov, Iddo; Arredouani, Mohamed; Asara, John; Chen, Chun-Hau; Tsai, Cheng-Yu; Nelson, Kyle; Kobayashi, Koichi; Israel, Elliot; Zhou, Xiao Zhen; Nicholson, Linda; Lu, Kun Ping. "The IL-33-PIN1-IRAK-M axis is critical for type 2 immunity in IL-33-induced allergic airway inflammation." Nat. Commun. 9, 1603-1603 (2018).
PubMed: 29686383

Assembly members:

Assembly members:
entity_1, polymer, 124 residues, 13467.164 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: pMAL-c2X

Entity Sequences (FASTA):

Entity Sequences (FASTA):
entity_1: SEFGSMAGNCGARGALSAHT LLFDLPPALLGELCAVLDSC DGALGWRGLAERLSSSWLDV DHIEKEVDQGKSGTRELLWS WAQKNKTIGDLLQVLQEMGH RRAIHLITNYGAVLSPSEKS YQEG

Data sets:

assigned_chemical_shifts
- assigned_chemical_shifts_1

Data type	Count
13C chemical shifts	483
15N chemical shifts	131
1H chemical shifts	742

Additional metadata:

Assembly
Samples and Experiments
Software
Spectrometers
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Assembly:

Entity Assembly ID	Entity Name	Entity ID
1	entity_1	1

Entities:

Entity 1, entity_1 124 residues - 13467.164 Da.

1

SER

GLU

PHE

GLY

SER

MET

ALA

GLY

ASN

CYS

2

GLY

ALA

ARG

GLY

ALA

LEU

SER

ALA

HIS

THR

3

LEU

PHE

ASP

LEU

PRO

ALA

LEU

4

GLY

GLU

LEU

CYS

ALA

VAL

LEU

ASP

SER

CYS

5

ASP

GLY

ALA

LEU

GLY

TRP

ARG

GLY

LEU

ALA

6

GLU

ARG

LEU

SER

TRP

LEU

ASP

VAL

7

ASP

HIS

ILE

GLU

LYS

GLU

VAL

ASP

GLN

GLY

8

LYS

SER

GLY

THR

ARG

GLU

LEU

TRP

SER

9

TRP

ALA

GLN

LYS

ASN

LYS

THR

ILE

GLY

ASP

10

LEU

GLN

VAL

LEU

GLN

GLU

MET

GLY

HIS

11

ARG

ALA

ILE

HIS

LEU

ILE

THR

ASN

TYR

12

GLY

ALA

VAL

LEU

SER

PRO

SER

GLU

LYS

SER

13

TYR

GLN

GLU

GLY

Samples:

sample_1: IRAK-M Death Domain_R56D_Y61E, [U-99% 13C; U-99% 15N], 800 uM; TCEP 5 mM; TRIS 10 mM; sodium azide 5 mM; sodium chloride 20 mM

sample_conditions_1: ionic strength: 0.0229 M; pH: 6.67; pressure: 1 atm; temperature: 298 K

Experiments:

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

Software:

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

PINE v2.0, Bahrami, Markley, Assadi, and Eghbalnia - chemical shift assignment

PONDEROSA, NMRFAM (University of Wisconsin-Madison), WoongHee Lee - structure calculation

SPARKY v3.115, Goddard - data analysis

NMR spectrometers:

Varian INOVA 600 MHz

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