BMRB Entry 50540

Chem Shift validation: AVS_full
BMRB Entry DOI: doi:10.13018/BMR50540

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Title:
Backbone Assignments for the Human Interleukin-17AF Heterodimer
Deposition date:
2020-10-29
Original release date:
2021-04-19
Authors:
Waters, Lorna; Strong, Sarah; Muskett, Frederick; Prosser, Christine; 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, 153 residues, Formula weight is not available
entity_2, polymer, 133 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

Entity Sequences (FASTA):

Entity Sequences (FASTA):
entity_1: MGSSHHHHHHSSGENLYFQG SGITIPRNPGCPNSEDKNFP RTVMVNLNIHNRNTNTNPKR SSDYYNRSTSPWNLHRNEDP ERYPSVIWEAKCRHLGCINA DGNVDYHMNSVPIQQEILVL RREPPHCPNSFRLEKILVSV GCTCVTPIVHHVA
entity_2: RKIPKVGHTFFQKPESCPPV PGGSMKLDIGIINENQRVSM SRNIESRSTSPWNYTVTWDP NRYPSEVVQAQCRNLGCINA QGKEDISMNSVPIQQETLVV RRKHQGCSVSFQLEKVLVTV GCTCVTPVIHHVQ

Data sets:
Data typeCount
13C chemical shifts729
15N chemical shifts235
1H chemical shifts235

Additional metadata:

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

Assembly:

Entity Assembly IDEntity NameEntity ID
1IL-17A - protomer1
2IL-17F - protomer2

Entities:

Entity 1, IL-17A - protomer 153 residues - Formula weight is not available

Mature sequence of human IL-17A with N-terminal His-tag and linker

1   METGLYSERSERHISHISHISHISHISHIS
2   SERSERGLYGLUASNLEUTYRPHEGLNGLY
3   SERGLYILETHRILEPROARGASNPROGLY
4   CYSPROASNSERGLUASPLYSASNPHEPRO
5   ARGTHRVALMETVALASNLEUASNILEHIS
6   ASNARGASNTHRASNTHRASNPROLYSARG
7   SERSERASPTYRTYRASNARGSERTHRSER
8   PROTRPASNLEUHISARGASNGLUASPPRO
9   GLUARGTYRPROSERVALILETRPGLUALA
10   LYSCYSARGHISLEUGLYCYSILEASNALA
11   ASPGLYASNVALASPTYRHISMETASNSER
12   VALPROILEGLNGLNGLUILELEUVALLEU
13   ARGARGGLUPROPROHISCYSPROASNSER
14   PHEARGLEUGLULYSILELEUVALSERVAL
15   GLYCYSTHRCYSVALTHRPROILEVALHIS
16   HISVALALA

Entity 2, IL-17F - protomer 133 residues - Formula weight is not available

Mature sequence of human IL-17F

1   ARGLYSILEPROLYSVALGLYHISTHRPHE
2   PHEGLNLYSPROGLUSERCYSPROPROVAL
3   PROGLYGLYSERMETLYSLEUASPILEGLY
4   ILEILEASNGLUASNGLNARGVALSERMET
5   SERARGASNILEGLUSERARGSERTHRSER
6   PROTRPASNTYRTHRVALTHRTRPASPPRO
7   ASNARGTYRPROSERGLUVALVALGLNALA
8   GLNCYSARGASNLEUGLYCYSILEASNALA
9   GLNGLYLYSGLUASPILESERMETASNSER
10   VALPROILEGLNGLNGLUTHRLEUVALVAL
11   ARGARGLYSHISGLNGLYCYSSERVALSER
12   PHEGLNLEUGLULYSVALLEUVALTHRVAL
13   GLYCYSTHRCYSVALTHRPROVALILEHIS
14   HISVALGLN

Samples:

sample_1: His-IL-17A, [U-13C; U-15N; U-2H], 260 uM; IL-17F 260 uM

sample_2: His-IL-17A 110 uM; IL-17F, [U-13C; U-15N; U-2H], 110 uM

sample_3: His-IL-17A 400 uM; IL-17F, [U-13C; U-15N; U-2H], 400 uM

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

Experiments:

NameSampleSample stateSample conditions
2D 1H-15N TROSYsample_1isotropicsample_conditions_1
3D TROSY- HNCACBsample_1isotropicsample_conditions_1
3D TROSY-HNCOsample_1isotropicsample_conditions_1
3D TROSY-HN(CO)CACBsample_1isotropicsample_conditions_1
3D 15N/1H NOESY-TROSYsample_1isotropicsample_conditions_1
2D 1H-15N TROSYsample_2isotropicsample_conditions_1
3D TROSY-HNCOsample_2isotropicsample_conditions_1
3D TROSY-HNCACBsample_3isotropicsample_conditions_1
3D TROSY-HN(CO)CACBsample_3isotropicsample_conditions_1
3D 15N/1H NOESY-HSQCsample_3isotropicsample_conditions_1

Software:

TOPSPIN - Data acquisition and processing

NMRPipe - Data processing and NUS reconstruction

NMRFAM-SPARKY - data analysis

NMR spectrometers:

  • Bruker AVIII 600 MHz
  • Bruker AVII 800 MHz

Related Database Links:

Uniprot Q16552 Q96PD4
AlphaFold Q5T2P0 Q9NUE6

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