BMRB Entry 51795

Chem Shift validation: AVS_full
BMRB Entry DOI: doi:10.13018/BMR51795

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Title:
Backbone 1H, 13C and 15N chemical shift assignments of the N-terminal portion of Annexin A11-PRD(residues 2-52)
Deposition date:
2023-01-23
Original release date:
2023-07-10
Authors:
Shihora, Aman; Elias, Ruben; Deshmukh, Lalit
Citation:

Citation: Shihora, Aman; Elias, Ruben; Hammond, R.; Ghirlando, Rodolfo; Deshmukh, Lalit. "ALS Variants of Annexin A11's Proline-Rich Domain Impair Its S100A6-Mediated Fibril Dissolution"  ACS Chem. Neurosci. 14, 2583-2589 (2023).
PubMed: 37433222

Assembly members:

Assembly members:
entity_1, polymer, 59 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: pET11a

Entity Sequences (FASTA):

Entity Sequences (FASTA):
entity_1: SYPGYPPPPGGYPPAAPGGG PWGGAAYPPPPSMPPIGLDN VATYAGQFNQDWSHPQFEK

Data sets:
Data typeCount
13C chemical shifts148
15N chemical shifts58
1H chemical shifts37

Additional metadata:

  • Assembly
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Assembly:

Entity Assembly IDEntity NameEntity ID
1proline-rich domain of Annexin A111

Entities:

Entity 1, proline-rich domain of Annexin A11 59 residues - Formula weight is not available

The primary seq is as follows: SYPGYPPPPGGYPPAAPGGGPWGGAAYPPPPSMPPIGLDNVATYAGQFNQDWSHPQFEK The first residue in the seq is Serine-2. The C-terminal residues (WSHPQFEK) represent non-native strep tag residues used for purification.

1   SERTYRPROGLYTYRPROPROPROPROGLY
2   GLYTYRPROPROALAALAPROGLYGLYGLY
3   PROTRPGLYGLYALAALATYRPROPROPRO
4   PROSERMETPROPROILEGLYLEUASPASN
5   VALALATHRTYRALAGLYGLNPHEASNGLN
6   ASPTRPSERHISPROGLNPHEGLULYS

Related Database Links:

UNP P50995

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