BMRB Entry 52322

Chem Shift validation: AVS_full
BMRB Entry DOI: doi:10.13018/BMR52322

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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, 223 residues, 21261.19 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: MHLNTLEGKKPGNNEGSGAP SPLSKSSPATTVTSPNSTPA KTIETSPPVDIFATASAAAP VSSAKPSSDLLDLQPDFSGA AAGAAAPVPPPTGGATAWGD LLGEDSLAALSSVPSEAPIS DPFAPEPSPPTTTTEPASAS ASATTAVTAATTEVDLFGDA FAASPGEAPAASEGATAPAT PAPVAAALDACSGNDPFAPS EGSAEAAPELDLFAMKPPET SAP

Data sets:
Data typeCount
13C chemical shifts479
15N chemical shifts172
1H chemical shifts172

Additional metadata:

  • Assembly
  • Samples and Experiments
  • Software
  • Spectrometers
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Assembly:

Entity Assembly IDEntity NameEntity ID
1AP180 281-5001

Entities:

Entity 1, AP180 281-500 223 residues - 21261.19 Da.

1   METHISLEUASNTHRLEUGLUGLYLYSLYS
2   PROGLYASNASNGLUGLYSERGLYALAPRO
3   SERPROLEUSERLYSSERSERPROALATHR
4   THRVALTHRSERPROASNSERTHRPROALA
5   LYSTHRILEGLUTHRSERPROPROVALASP
6   ILEPHEALATHRALASERALAALAALAPRO
7   VALSERSERALALYSPROSERSERASPLEU
8   LEUASPLEUGLNPROASPPHESERGLYALA
9   ALAALAGLYALAALAALAPROVALPROPRO
10   PROTHRGLYGLYALATHRALATRPGLYASP
11   LEULEUGLYGLUASPSERLEUALAALALEU
12   SERSERVALPROSERGLUALAPROILESER
13   ASPPROPHEALAPROGLUPROSERPROPRO
14   THRTHRTHRTHRGLUPROALASERALASER
15   ALASERALATHRTHRALAVALTHRALAALA
16   THRTHRGLUVALASPLEUPHEGLYASPALA
17   PHEALAALASERPROGLYGLUALAPROALA
18   ALASERGLUGLYALATHRALAPROALATHR
19   PROALAPROVALALAALAALALEUASPALA
20   CYSSERGLYASNASPPROPHEALAPROSER
21   GLUGLYSERALAGLUALAALAPROGLULEU
22   ASPLEUPHEALAMETLYSPROPROGLUTHR
23   SERALAPRO

Samples:

sample_1: Monomeric Clathrin Assembly Protein AP180, residues 281-500, [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:

NameSampleSample stateSample conditions
2D 1H-15N HSQCsample_1isotropicsample_conditions_1
3D HNCOsample_1isotropicsample_conditions_1
3D HN(CA)COsample_1isotropicsample_conditions_1
3D iHNCAsample_1isotropicsample_conditions_1
3D HN(CO)CAsample_1isotropicsample_conditions_1
3D iHNCACBsample_1isotropicsample_conditions_1
3D HN(CO)CACBsample_1isotropicsample_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