BMRB Entry 52944

Chem Shift validation: AVS_full
BMRB Entry DOI: doi:10.13018/BMR52944

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Title:
Partial assignment of the Annexin A11 low complexity domain (LCD)
Deposition date:
2025-02-28
Original release date:
2025-03-11
Authors:
Qamar, Seema; Wagstaff, Jane; Nixon-Abell, Jonathon; Freund, Stefan; St George-Hyslop, Peter
Citation:

Citation: Nixon-Abell, Jonathon; Ruggeri, Francesco; Qamar, Seema; Herling, Therese; Czekalska, Magdalena; Shen, Yi; Wang, Guzhen; King, Christopher; Fernandopulle, Michael; Sneideris, Tomas; Watson, Joseph; Pillai, Visakh; Meadows, William; Henderson, James; Chambers, Joseph; Wagstaff, Jane; Williams, Sioned; Coyle, Helena; Sneideriene, Greta; Lu, Yuqian; Zhang, Shuyuan; Marciniak, Stefan; Freund, Stefan; Derivery, Emmanuel; Ward, Michael; Vendruscolo, Michele; Knowles, Tuomas; St George-Hyslop, Peter. "ANXA11 biomolecular condensates facilitate protein-lipid phase coupling on lysosomal membranes"  Nat. Commun. ., .-..

Assembly members:

Assembly members:
entity_1, polymer, 185 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: pOPINS (Merck)

Entity Sequences (FASTA):

Entity Sequences (FASTA):
entity_1: MSYPGYPPPPGGYPPAAPGG GPWGGAAYPPPPSMPPIGLD NVATYAGQFNQDYLSGMAAN MSGTFGGANMPNLYPGAPGA GYPPVPPGGFGQPPSAQQPV PPYGMYPPPGGNPPSRMPSY PPYPGAPVPGQPMPPPGQQP PGAYPGQPPVTYPGQPPVPL PGQQQPVPSYPGYPGSGTVT PAVPP

Data sets:
Data typeCount
13C chemical shifts216
15N chemical shifts68
1H chemical shifts68

Additional metadata:

  • Assembly
  • Samples and Experiments
  • Software
  • Spectrometers
  • Hide all

Assembly:

Entity Assembly IDEntity NameEntity ID
1Annexin A111

Entities:

Entity 1, Annexin A11 185 residues - Formula weight is not available

1   METSERTYRPROGLYTYRPROPROPROPRO
2   GLYGLYTYRPROPROALAALAPROGLYGLY
3   GLYPROTRPGLYGLYALAALATYRPROPRO
4   PROPROSERMETPROPROILEGLYLEUASP
5   ASNVALALATHRTYRALAGLYGLNPHEASN
6   GLNASPTYRLEUSERGLYMETALAALAASN
7   METSERGLYTHRPHEGLYGLYALAASNMET
8   PROASNLEUTYRPROGLYALAPROGLYALA
9   GLYTYRPROPROVALPROPROGLYGLYPHE
10   GLYGLNPROPROSERALAGLNGLNPROVAL
11   PROPROTYRGLYMETTYRPROPROPROGLY
12   GLYASNPROPROSERARGMETPROSERTYR
13   PROPROTYRPROGLYALAPROVALPROGLY
14   GLNPROMETPROPROPROGLYGLNGLNPRO
15   PROGLYALATYRPROGLYGLNPROPROVAL
16   THRTYRPROGLYGLNPROPROVALPROLEU
17   PROGLYGLNGLNGLNPROVALPROSERTYR
18   PROGLYTYRPROGLYSERGLYTHRVALTHR
19   PROALAVALPROPRO

Samples:

sample_1: Annexin A11 LCD, [U-13C; U-15N; U-2H], 150 uM; D2O 5%; HEPES 25 mM; NaCl 225 mM

sample_2: Annexin A11 LCD, [U-99% 13C; U-99% 15N], 50 uM; D2O 5%; HEPES 25 mM; NaCl 225 mM

sample_conditions_1: ionic strength: 250 mM; pH: 7.4; pressure: 1 atm; temperature: 278 K

Experiments:

NameSampleSample stateSample conditions
2D 1H-15N BEST-TROSYsample_2isotropicsample_conditions_1
3D BEST-trHNCOsample_1isotropicsample_conditions_1
3D BEST-trHNCACOsample_1isotropicsample_conditions_1
3D BEST-trHNCOCAsample_1isotropicsample_conditions_1
3D BEST-trHNCAsample_1isotropicsample_conditions_1
3D BEST-trHNCOCACBsample_1isotropicsample_conditions_1
3D BEST-trHNCACBsample_1isotropicsample_conditions_1
c_hcacon_iasample_2isotropicsample_conditions_1
c_hcacon_ia3dsample_2isotropicsample_conditions_1
c_hcanco_ia3dsample_2isotropicsample_conditions_1
c_hcbcacon_ia3dsample_2isotropicsample_conditions_1

Software:

TOPSPIN v3.6.0 - collection

NMRPipe v10.4 - processing

NMRFAM-SPARKY v3.115 - peak picking

MARS v1.1 - chemical shift assignment

NMR spectrometers:

  • Bruker AVANCE III 700 MHz

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