BMRB Entry 50537

Title:
Backbone Assignments for the Human Interleukin-17A Homodimer
Deposition date:
2020-10-28
Original release date:
2021-04-19
Authors:
Veverka, Vaclav; Waters, Lorna; Muskett, Frederick; Taylor, Richard; Henry, Alistair; Carr, Mark
Citation:

Citation: Waters, Lorna; Veverka, Vaclav; Strong, Sarah; Muskett, Frederick; Dedi, Neesha; Lawson, Alastair; Prosser, Christine; Taylor, Richard; Henry, Alistair; Carr, Mark. "Conformational dynamics in interleukin 17A and 17F functional complexes is a key determinant of receptor A affinity and specificity"  Cytokine 142, 155476-155476 (2021).
PubMed: 33706174

Assembly members:

Assembly members:
entity_1, polymer, 132 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: pET32

Data sets:
Data typeCount
13C chemical shifts299
15N chemical shifts93
1H chemical shifts93

Additional metadata:

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

Assembly:

Entity Assembly IDEntity NameEntity ID
1IL-17A - protomer 11
2IL-17A - protomer 21

Entities:

Entity 1, IL-17A - protomer 1 132 residues - Formula weight is not available

Mature sequence of human IL-17A

1   GLYILETHRILEPROARGASNPROGLYCYS
2   PROASNSERGLUASPLYSASNPHEPROARG
3   THRVALMETVALASNLEUASNILEHISASN
4   ARGASNTHRASNTHRASNPROLYSARGSER
5   SERASPTYRTYRASNARGSERTHRSERPRO
6   TRPASNLEUHISARGASNGLUASPPROGLU
7   ARGTYRPROSERVALILETRPGLUALALYS
8   CYSARGHISLEUGLYCYSILEASNALAASP
9   GLYASNVALASPTYRHISMETASNSERVAL
10   PROILEGLNGLNGLUILELEUVALLEUARG
11   ARGGLUPROPROHISCYSPROASNSERPHE
12   ARGLEUGLULYSILELEUVALSERVALGLY
13   CYSTHRCYSVALTHRPROILEVALHISHIS
14   VALALA

Samples:

sample_1: IL-17A dimer, [U-15N], 300 uM

sample_2: IL-17A dimer, [U-13C; U-15N; U-2H], 400 uM

sample_3: IL-17A dimer, [U-15N; U-2H], 450 uM

sample_conditions_1: ionic strength: 140 mM; pH: 6; pressure: 1 atm; temperature: 308 K

Experiments:

NameSampleSample stateSample conditions
2D 1H-15N HSQCsample_1isotropicsample_conditions_1
3D TROSY-HNCAsample_2isotropicsample_conditions_1
3D TROSY- HNCACBsample_2isotropicsample_conditions_1
3D TROSY-HNCOsample_2isotropicsample_conditions_1
3D TROSY-HN(CO)CACBsample_2isotropicsample_conditions_1
3D 15N/1H NOESY-HSQCsample_3isotropicsample_conditions_1

Software:

TOPSPIN - Data acquisition and processing

NMRPipe - Data processing

SPARKY - data analysis

NMR spectrometers:

  • Bruker DRX 600 MHz
  • Bruker Avance II 800 MHz

Related Database Links:

Uniprot Q16552
AlphaFold Q5T2P0

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