BMRB Entry 51336

Name: Backbone assignment of human PEX13 C-terminal region
Published: 2022-08-22

Chem Shift validation: AVS_full
BMRB Entry DOI: doi:10.13018/BMR51336

NMR-STAR file interactive viewer.
NMR-STAR v3 text file.
XML gzip file.
RDF gzip file.
All files associated with the entry

Nicholas Rego and David Koes
3Dmol.js: molecular visualization with WebGL
Bioinformatics (2015) 31 (8): 1322-1324 doi:10.1093/bioinformatics/btu829

Select model:

I am color blind

Download raw data. Direct link to this display. Help

Title:

Backbone assignment of human PEX13 C-terminal region

Deposition date:

2022-02-21

Original release date:

2022-08-22

Authors:

Gaussmann, Stefan; Sattler, Michael

Citation:

Citation: Gaussmann, Stefan; Peschel, Rebecca; Ott, Julia; Zak, Krzysztof; Sastre, Judit; Delhommel, Florent; Popowicz, Grzegorz; Boekhoven, Job; Schliebs, Wolfgang; Erdmann, Ralf; Sattler, Michael. "Modulation of peroxisomal import by the PEX13 SH3 domain and a proximal FxxxF binding motif" Nat. Commun. 15, 3317-3317 (2024).
PubMed: 38632234

Assembly members:

Assembly members:
entity_1, polymer, 143 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: pETM13S

Entity Sequences (FASTA):

Entity Sequences (FASTA):
entity_1: VTDSINWASGEDDHVVARAE YDFAAVSEEEISFRAGDMLN LALKEQQPKVRGWLLASLDG QTTGLIPANYVKILGKRKGR KTVESSKVSKQQQSFTNPTL TKGATVADSLDEQEAAFESV FVETNKVPVAPDSIGKDGEK QDL

Data sets:

assigned_chemical_shifts
- assigned_chemical_shifts_1

Data type	Count
13C chemical shifts	383
15N chemical shifts	121
1H chemical shifts	121

Additional metadata:

Assembly
Samples and Experiments
Software
Spectrometers
Hide all

Assembly:

Entity Assembly ID	Entity Name	Entity ID
1	PEX13 261-403	1

Entities:

Entity 1, PEX13 261-403 143 residues - Formula weight is not available

1

VAL

THR

ASP

SER

ILE

ASN

TRP

ALA

SER

GLY

2

GLU

ASP

HIS

VAL

ALA

ARG

ALA

GLU

3

TYR

ASP

PHE

ALA

VAL

SER

GLU

4

ILE

SER

PHE

ARG

ALA

GLY

ASP

MET

LEU

ASN

5

LEU

ALA

LEU

LYS

GLU

GLN

PRO

LYS

VAL

6

ARG

GLY

TRP

LEU

ALA

SER

LEU

ASP

GLY

7

GLN

THR

GLY

LEU

ILE

PRO

ALA

ASN

TYR

8

VAL

LYS

ILE

LEU

GLY

LYS

ARG

LYS

GLY

ARG

9

LYS

THR

VAL

GLU

SER

LYS

VAL

SER

LYS

10

GLN

SER

PHE

THR

ASN

PRO

THR

LEU

11

THR

LYS

GLY

ALA

THR

VAL

ALA

ASP

SER

LEU

12

ASP

GLU

GLN

GLU

ALA

PHE

GLU

SER

VAL

13

PHE

VAL

GLU

THR

ASN

LYS

VAL

PRO

VAL

ALA

14

PRO

ASP

SER

ILE

GLY

LYS

ASP

GLY

GLU

LYS

15

GLN

ASP

LEU

Samples:

sample_1: PEX13 261-403, [U-99% 13C; U-99% 15N], 400 uM; TRIS 20 mM; sodium chloride 50 mM; D2O, [U-2H], 10%

sample_conditions_1: pH: 7.5; pressure: 1 atm; temperature: 298 K

Experiments:

Name	Sample	Sample state	Sample conditions
1D 1H	sample_1	isotropic	sample_conditions_1
2D 1H-15N HSQC	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 HNCACO	sample_1	isotropic	sample_conditions_1
3D HNCO	sample_1	isotropic	sample_conditions_1

Software:

TOPSPIN vv3.5 pl7 - collection

CcpNMR vv2.4.2 - chemical shift assignment

NMRPipe vvLinux64:20210129 - processing

NMR spectrometers:

Bruker AVANCE III 600 MHz

SP	Q92968
AlphaFold	B2RCS1