BMRB Entry 27467

Name: Solution structure of FAT10
Published: 2018-07-31

Chem Shift validation: AVS_anomalous, AVS_full, LACS
BMRB Entry DOI: doi:10.13018/BMR27467

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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 FAT10

Deposition date:

2018-04-28

Original release date:

2018-07-31

Authors:

Wiesner, Silke; Anders, Samira; Stotz, Sophie; Roessler, Philip

Citation:

Citation: Aichem, Annette; Anders, Samira; Catone, Nicola; Rossler, Philip; Stotz, Sophie; Berg, Andrej; Schwab, Ricarda; Scheuermann, Sophia; Bialas, Johanna; Schutz-Stoffregen, Mira; Schmidtke, Gunter; Peter, Christine; Groettrup, Marcus; Wiesner, Silke. "The structure of the ubiquitin-like modifier FAT10 reveals an alternative targeting mechanism for proteasomal degradation" Nat. Commun. 9, 3321-3321 (2018).
PubMed: 30127417

Assembly members:

Assembly members:
fat10_c, polymer, 85 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: pETM-41

Entity Sequences (FASTA):

Entity Sequences (FASTA):
fat10_c: GAMGDEELPLFLVESGDEAK RHLLQVRRSSSVAQVKAMIE TKTGIIPETQIVTLNGKRLE DGKMMADYGIRKGNLLFLAS YSIGG

Data sets:

assigned_chemical_shifts
- assigned_chem_shift_list_1

Data type	Count
13C chemical shifts	266
15N chemical shifts	83
1H chemical shifts	564

Additional metadata:

Assembly
Samples and Experiments
Software
Spectrometers
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Assembly:

Entity Assembly ID	Entity Name	Entity ID
1	FAT10 C-terminal domain	1

Entities:

Entity 1, FAT10 C-terminal domain 85 residues - Formula weight is not available

Residues 1-4 represent a non-native sequence resulting from the NcoI restriction site. The difference in amino acid numbers to the natural sequence is +80.

1

GLY

ALA

MET

GLY

ASP

GLU

LEU

PRO

LEU

2

PHE

LEU

VAL

GLU

SER

GLY

ASP

GLU

ALA

LYS

3

ARG

HIS

LEU

GLN

VAL

ARG

SER

4

SER

VAL

ALA

GLN

VAL

LYS

ALA

MET

ILE

GLU

5

THR

LYS

THR

GLY

ILE

PRO

GLU

THR

GLN

6

ILE

VAL

THR

LEU

ASN

GLY

LYS

ARG

LEU

GLU

7

ASP

GLY

LYS

MET

ALA

ASP

TYR

GLY

ILE

8

ARG

LYS

GLY

ASN

LEU

PHE

LEU

ALA

SER

9

TYR

SER

ILE

GLY

Samples:

sample_1: fat10_c, [U-100% 13C; U-100% 15N], 2 mM; sodium phosphate 20 mM; sodium chloride 150 mM

sample_conditions_1: ionic strength: 0.2 M; pH: 7.5; 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
2D 1H-1H NOESY	sample_1	isotropic	sample_conditions_1
3D CBCA(CO)NH	sample_1	isotropic	sample_conditions_1
3D HNCACB	sample_1	isotropic	sample_conditions_1
3D C(CO)NH	sample_1	isotropic	sample_conditions_1
3D HBHA(CO)NH	sample_1	isotropic	sample_conditions_1
3D HNHA	sample_1	isotropic	sample_conditions_1
3D 1H-15N NOESY	sample_1	isotropic	sample_conditions_1
3D 1H-13C NOESY	sample_1	isotropic	sample_conditions_1

Software:

XEASY, Keller and Wuthrich - chemical shift assignment, peak picking

NMR spectrometers:

Bruker Avance 600 MHz
Bruker Avance 800 MHz