BMRB Entry 52964

Name: Vimentin Tail Domain
Published: 2025-03-19

Chem Shift validation: AVS_full
BMRB Entry DOI: doi:10.13018/BMR52964

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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:

Vimentin Tail Domain

Deposition date:

2025-03-11

Original release date:

2025-03-19

Authors:

Carranza, Estely; Heffern, Marie; Murray, Dylan

Citation:

Citation: Carranza, Estely; Heffern, Marie; Murray, Dylan. "Metal Ion Binding of Human Vimentin Tail Domain Fragments" .

Assembly members:

Assembly members:
entity_1, polymer, 67 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: pHIS VimT

Entity Sequences (FASTA):

Entity Sequences (FASTA):
entity_1: GAMDPEGEESRISLPLPNFS SLNLRETNLDSLPLVDTHSK RTLLIKTVETRDGQVINETS QHHDDLE

Data sets:

assigned_chemical_shifts
- assigned_chemical_shifts_1

Data type	Count
13C chemical shifts	144
15N chemical shifts	51
1H chemical shifts	51

Additional metadata:

Assembly
Samples and Experiments
Software
Spectrometers
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Assembly:

Entity Assembly ID	Entity Name	Entity ID
1	Human Vimentin Tail Domain	1

Entities:

Entity 1, Human Vimentin Tail Domain 67 residues - Formula weight is not available

1

GLY

ALA

MET

ASP

PRO

GLU

GLY

GLU

SER

2

ARG

ILE

SER

LEU

PRO

LEU

PRO

ASN

PHE

SER

3

SER

LEU

ASN

LEU

ARG

GLU

THR

ASN

LEU

ASP

4

SER

LEU

PRO

LEU

VAL

ASP

THR

HIS

SER

LYS

5

ARG

THR

LEU

ILE

LYS

THR

VAL

GLU

THR

6

ARG

ASP

GLY

GLN

VAL

ILE

ASN

GLU

THR

SER

7

GLN

HIS

ASP

LEU

GLU

Samples:

sample_1: Vimentin Tail Domain monomer, [U-100% 13C; U-100% 15N], 44 uM; D2O, [U-99% 2H], 10%; H2O 90%; sodium phosphate 20 mM

sample_conditions_1: ionic strength: 0.02 M; pH: 6.5; pressure: 1 atm; temperature: 298.2 K

Experiments:

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

Software:

NMRFAM-SPARKY - chemical shift assignment, data analysis

NMRPipe - data analysis

NMR spectrometers:

Bruker AVANCE III 600 MHz