BMRB Entry 31215

Name: Structure of the human integrin alphaX transmembrane domain
Published: 2025-09-24

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PDB ID: 9ecm
Entry in NMR Restraints Grid
Validation report in NRG-CING
Chem Shift validation: AVS_full
BMRB Entry DOI: doi:10.13018/BMR31215
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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 of the human integrin alphaX transmembrane domain

Deposition date:

2024-11-14

Original release date:

2025-09-24

Authors:

Ulmer, T.; Vu, H.; Situ, A.

Citation:

Citation: Ulmer, T.; Vu, H.; Situ, A.. "Transmembrane Helix Destabilization Regulates Integrin alphaXbeta2 Signaling" .

Assembly members:

Assembly members:
entity_1, polymer, 42 residues, 4640.578 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 'BL21-Gold(DE3)pLysS AG'

Entity Sequences (FASTA):

Entity Sequences (FASTA):
entity_1: GEKYKVHNPTPLIVGSSIGG LLLLALITAVLYKVGFFKRQ YK

Data sets:

assigned_chemical_shifts
- assigned_chemical_shifts_1

Data type	Count
13C chemical shifts	103
15N chemical shifts	37
1H chemical shifts	37

Additional metadata:

Assembly
Samples and Experiments
Software
Spectrometers
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Assembly:

Entity Assembly ID	Entity Name	Entity ID
1	unit_1	1

Entities:

Entity 1, unit_1 42 residues - 4640.578 Da.

1

GLY

GLU

LYS

TYR

LYS

VAL

HIS

ASN

PRO

THR

2

PRO

LEU

ILE

VAL

GLY

SER

ILE

GLY

3

LEU

ALA

LEU

ILE

THR

ALA

VAL

4

LEU

TYR

LYS

VAL

GLY

PHE

LYS

ARG

GLN

5

TYR

LYS

Samples:

sample_1: alphaX peptide, [U-100% 13C; U-100% 15N; U-80% 2H], 1.2 mM; 1,2-dihexanoly-sn-glycero-3-phosphocholine, none, 350 mM; 1-palmitoyl-2-oleoyl-sn-glycero-3-phosphocholine, none, 105 mM; HEPES, none, 25 mM

sample_conditions_1: ionic strength: 0.025 M; pH: 7.4 pH*; pressure: 1 atm; temperature: 313.2 K

Experiments:

Name	Sample	Sample state	Sample conditions
3D HNCA	sample_1	isotropic	sample_conditions_1
3D HNCACB	sample_1	isotropic	sample_conditions_1
3D HNCO	sample_1	isotropic	sample_conditions_1
3D HN(CA)CO	sample_1	isotropic	sample_conditions_1
2D 1H-15N HSQC	sample_1	isotropic	sample_conditions_1

Software:

CARA, Keller and Wuthrich - chemical shift assignment

X-PLOR NIH, Schwieters, Kuszewski, Tjandra and Clore - structure calculation

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

NMR spectrometers:

Bruker AVANCE 700 MHz

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