BMRB Entry 34953

Name: Solution structure of homodimeric TMEM106B
Published: 2025-11-18

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PDB ID: 9gi8
Entry in NMR Restraints Grid
Validation report in NRG-CING
Chem Shift validation: AVS_full
BMRB Entry DOI: doi:10.13018/BMR34953
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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:

Solution structure of homodimeric TMEM106B

Deposition date:

2024-08-17

Original release date:

2025-11-18

Authors:

Schweimer, K.; Perez-Borrajero, C.; Hennig, J.

Citation:

Citation: Perez-Borrajero, C.; Hennig, J.. "Zinc-mediated regulation of TMEM106B function in the endolysosomal pathway revealed through systematic identification of TRIM2/3 ubiquitination substrates" .

Assembly members:

Assembly members:
entity_1, polymer, 39 residues, 4346.910 Da.
entity_ZN, non-polymer, 65.409 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: chemical synthesis

Entity Sequences (FASTA):

Entity Sequences (FASTA):
entity_1: TGRDSVTCPTCQGTGRIPRG QENQLVALIPYSDQRLRPR

Data sets:

assigned_chemical_shifts
- assigned_chemical_shifts_1

Data type	Count
13C chemical shifts	83
15N chemical shifts	30
1H chemical shifts	236

Additional metadata:

Assembly
Samples and Experiments
Software
Spectrometers
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Assembly:

Entity Assembly ID	Entity Name	Entity ID
1	unit_1	1
2	unit_2	1
3	unit_3	2

Entities:

Entity 1, unit_1 39 residues - 4346.910 Da.

1

THR

GLY

ARG

ASP

SER

VAL

THR

CYS

PRO

THR

2

CYS

GLN

GLY

THR

GLY

ARG

ILE

PRO

ARG

GLY

3

GLN

GLU

ASN

GLN

LEU

VAL

ALA

LEU

ILE

PRO

4

TYR

SER

ASP

GLN

ARG

LEU

ARG

PRO

ARG

Entity 2, unit_3 - Zn - 65.409 Da.

1

ZN

Samples:

sample_1: TMEM106B(54-92) 0.6 mM; ZINC ION 3 mM; sodium phosphate 20 mM; sodium chloride 100 mM; TCEP 0.5 mM

sample_2: TMEM106B(54-92) 1.8 mM; ZINC ION 5 mM; sodium phosphate 20 mM; sodium chloride 100 mM; TCEP 0.5 mM

sample_conditions_1: ionic strength: 120 mM; pH: 6.5; pressure: 1 atm; temperature: 298 K

Experiments:

Name	Sample	Sample state	Sample conditions
2D DQF-COSY	sample_1	isotropic	sample_conditions_1
2D 1H-1H TOCSY	sample_1	isotropic	sample_conditions_1
2D 1H-1H NOESY	sample_1	isotropic	sample_conditions_1
2D 1H-13C HSQC	sample_1	isotropic	sample_conditions_1
2D 1H-15N HSQC	sample_2	isotropic	sample_conditions_1

Software:

CYANA v3.98.15, Guntert, Mumenthaler and Wuthrich - structure calculation

NMRViewJ, OneMoon Scientific - chemical shift assignment

NMR spectrometers:

Bruker AVANCE III HD 600 MHz
Bruker AVANCE III HD 700 MHz
Bruker AVANCE III HD 1000 MHz

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