BMRB Entry 53274

Name: Integrin alphaX(G1092L) transmembrane domain (q=0.5 bicelles)
Published: 2025-09-18

Chem Shift validation: AVS_full
BMRB Entry DOI: doi:10.13018/BMR53274

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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:

Integrin alphaX(G1092L) transmembrane domain (q=0.5 bicelles)

Deposition date:

2025-07-11

Original release date:

2025-09-18

Authors:

Vu, Han; Situ, Alan; Ulmer, Tobias

Citation:

Citation: Vu, Han; Lee, Minhyeong; Situ, Alan; An, Woojin; Ley, Klaus; Kim, Chungho; Ulmer, Tobias. "Functional unfolding of the integrin alphaX transmembrane helix" Proc. Natl. Acad. Sci. U. S. A. 122, e2507966122-e2507966122 (2025).
PubMed: 40956891

Assembly members:

Assembly members:
entity_1, polymer, 42 residues, Formula weight is not available

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: pET-44

Entity Sequences (FASTA):

Entity Sequences (FASTA):
entity_1: GEKYKVHNPTPLIVLSSIGG LLLLALITAVLYKVGFFKRQ YK

Data sets:

assigned_chemical_shifts
- assigned_chemical_shifts_1

Data type	Count
13C chemical shifts	38
15N chemical shifts	35
1H chemical shifts	35

Additional metadata:

Assembly
Samples and Experiments
Software
Spectrometers
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Assembly:

Entity Assembly ID	Entity Name	Entity ID
1	integrin alpha-X(G1092L) transmembrane domain	1

Entities:

Entity 1, integrin alpha-X(G1092L) transmembrane domain 42 residues - Formula weight is not available

1

GLY

GLU

LYS

TYR

LYS

VAL

HIS

ASN

PRO

THR

2

PRO

LEU

ILE

VAL

LEU

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: integrin alpha-X transmembrane domain, [U-100% 13C; U-100% 15N; U-80% 2H], 1.0 mM; 1,2-dimyristoyl-sn-glycero-3-phosphocholine 120 mM; 1,2-dihexanoly-sn-glycero-3-phosphocholine 240 mM; HEPES 25 mM; D2O 6%

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

Experiments:

Name	Sample	Sample state	Sample conditions
3D HNCA	sample_1	isotropic	sample_conditions_1

Software:

CARA - chemical shift assignment

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