BMRB Entry 52325

Name: An extended interaction site determines binding between AP180 and AP2 in clathrin mediated endocytosis
Published: 2024-06-25

Chem Shift validation: AVS_full
BMRB Entry DOI: doi:10.13018/BMR52325

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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:

An extended interaction site determines binding between AP180 and AP2 in clathrin mediated endocytosis

Deposition date:

2024-02-16

Original release date:

2024-06-25

Authors:

Naudi-Fabra, Samuel; Elena-Real, Carlos; Vedel, Ida; Tengo, Maud; Motzny, Kathrin; Jiang, Pin-Lian; Schmieder, Peter; Liu, Fan; Milles, Sigrid

Citation:

Citation: Naudi-Fabra, Samuel; Elena-Real, Carlos; Vedel, Ida; Tengo, Maud; Motzny, Kathrin; Jiang, Pin-Lian; Schmieder, Peter; Liu, Fan; Milles, Sigrid. "An extended interaction site determines binding between AP180 and AP2 in clathrin mediated endocytosis" Nat. Commun. 15, 5884-5884 (2024).
PubMed: 39003270

Assembly members:

Assembly members:
entity_1, polymer, 201 residues, 19439.29 Da.

Natural source:

Natural source: Common Name: Rat Taxonomy ID: 10116 Superkingdom: Eukaryota Kingdom: Metazoa Genus/species: Rattus norvegicus

Experimental source:

Experimental source: Production method: recombinant technology Host organism: Escherichia coli Vector: pET-28

Entity Sequences (FASTA):

Entity Sequences (FASTA):
entity_1: AAATTTATTSAAAAATAAAP PALDIFGDLFDSAPEVAAAS KPDVAPSIDLFGTDAFSSPP RGASPVPESSLTADLLSVDA FAAPSPASTASPAKAESSGV IDLFGDAFGSSASETQPAPQ AVSSSSASADLLAGFGGSFM APSTTPVTPAQNNLLQPNFE AAFGTTPSTSSSSSFDPSGD LLMPTMAPSGQPAPVSMVPP S

Data sets:

assigned_chemical_shifts
- assigned_chemical_shifts_1

Data type	Count
13C chemical shifts	243
15N chemical shifts	125
1H chemical shifts	125

Additional metadata:

Assembly
Samples and Experiments
Software
Spectrometers
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Assembly:

Entity Assembly ID	Entity Name	Entity ID
1	AP180 540-740	1

Entities:

Entity 1, AP180 540-740 201 residues - 19439.29 Da.

1

ALA

THR

ALA

THR

SER

2

ALA

THR

ALA

PRO

3

PRO

ALA

LEU

ASP

ILE

PHE

GLY

ASP

LEU

PHE

4

ASP

SER

ALA

PRO

GLU

VAL

ALA

SER

5

LYS

PRO

ASP

VAL

ALA

PRO

SER

ILE

ASP

LEU

6

PHE

GLY

THR

ASP

ALA

PHE

SER

PRO

7

ARG

GLY

ALA

SER

PRO

VAL

PRO

GLU

SER

8

LEU

THR

ALA

ASP

LEU

SER

VAL

ASP

ALA

9

PHE

ALA

PRO

SER

PRO

ALA

SER

THR

ALA

10

SER

PRO

ALA

LYS

ALA

GLU

SER

GLY

VAL

11

ILE

ASP

LEU

PHE

GLY

ASP

ALA

PHE

GLY

SER

12

SER

ALA

SER

GLU

THR

GLN

PRO

ALA

PRO

GLN

13

ALA

VAL

SER

ALA

SER

ALA

ASP

14

LEU

ALA

GLY

PHE

GLY

SER

PHE

MET

15

ALA

PRO

SER

THR

PRO

VAL

THR

PRO

ALA

16

GLN

ASN

LEU

GLN

PRO

ASN

PHE

GLU

17

ALA

PHE

GLY

THR

PRO

SER

THR

SER

18

SER

PHE

ASP

PRO

SER

GLY

ASP

19

LEU

MET

PRO

THR

MET

ALA

PRO

SER

GLY

20

GLN

PRO

ALA

PRO

VAL

SER

MET

VAL

PRO

21

SER

Samples:

sample_4: Monomeric Clathrin Assembly Protein AP180, residues 540-740, [U-100% 13C; U-100% 15N], 100 uM; Na-phosphate 50 mM; NaCl 150 mM; DTT 2 mM

sample_conditions_1: ionic strength: 0.375 M; pH: 6; pressure: 1 atm; temperature: 298.15 K

Experiments:

Name	Sample	Sample state	Sample conditions
2D 1H-15N HSQC	sample_4	isotropic	sample_conditions_1
3D HNCO	sample_4	isotropic	sample_conditions_1
3D HN(CA)CO	sample_4	isotropic	sample_conditions_1
3D iHNCA	sample_4	isotropic	sample_conditions_1
3D HN(CO)CA	sample_4	isotropic	sample_conditions_1

Software:

MARS - chemical shift assignment

NMR spectrometers:

Bruker AVANCE III 600 MHz

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