BMRB Entry 50538

Name: Backbone Assignments for the Human Interleukin-17F Homodimer
Published: 2021-04-19

Chem Shift validation: AVS_full
BMRB Entry DOI: doi:10.13018/BMR50538

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Nicholas Rego and David Koes
3Dmol.js: molecular visualization with WebGL
Bioinformatics (2015) 31 (8): 1322-1324 doi:10.1093/bioinformatics/btu829

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Title:

Backbone Assignments for the Human Interleukin-17F 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, 134 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: MRKIPKVGHTFFQKPESCPP VPGGSMKLDIGIINENQRVS MSRNIESRSTSPWNYTVTWD PNRYPSEVVQAQCRNLGCIN AQGKEDISMNSVPIQQETLV VRRKHQGCSVSFQLEKVLVT VGCTCVTPVIHHVQ

Data sets:

assigned_chemical_shifts
- assigned_chemical_shifts_1

Data type	Count
13C chemical shifts	339
15N chemical shifts	108
1H chemical shifts	108

Additional metadata:

Assembly
Samples and Experiments
Software
Spectrometers
Hide all

Assembly:

Entity Assembly ID	Entity Name	Entity ID
1	IL-17F - protomer 1	1
2	IL-17F - protomer 2	1

Entities:

Entity 1, IL-17F - protomer 1 134 residues - Formula weight is not available

Mature sequence of human IL-17F, with an additional N-terminal Met

1

MET

ARG

LYS

ILE

PRO

LYS

VAL

GLY

HIS

THR

2

PHE

GLN

LYS

PRO

GLU

SER

CYS

PRO

3

VAL

PRO

GLY

SER

MET

LYS

LEU

ASP

ILE

4

GLY

ILE

ASN

GLU

ASN

GLN

ARG

VAL

SER

5

MET

SER

ARG

ASN

ILE

GLU

SER

ARG

SER

THR

6

SER

PRO

TRP

ASN

TYR

THR

VAL

THR

TRP

ASP

7

PRO

ASN

ARG

TYR

PRO

SER

GLU

VAL

GLN

8

ALA

GLN

CYS

ARG

ASN

LEU

GLY

CYS

ILE

ASN

9

ALA

GLN

GLY

LYS

GLU

ASP

ILE

SER

MET

ASN

10

SER

VAL

PRO

ILE

GLN

GLU

THR

LEU

VAL

11

VAL

ARG

LYS

HIS

GLN

GLY

CYS

SER

VAL

12

SER

PHE

GLN

LEU

GLU

LYS

VAL

LEU

VAL

THR

13

VAL

GLY

CYS

THR

CYS

VAL

THR

PRO

VAL

ILE

14

HIS

VAL

GLN

Samples:

sample_1: IL-17F dimer, [U-15N], 210 uM

sample_2: IL-17F dimer, [U-13C; U-15N; U-2H], 90 uM

sample_3: IL-17F dimer, [U-15N; U-2H], 200 uM

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

Experiments:

Name	Sample	Sample state	Sample conditions
2D 1H-15N HSQC	sample_1	isotropic	sample_conditions_1
3D TROSY- HNCACB	sample_2	isotropic	sample_conditions_1
3D TROSY-HNCO	sample_2	isotropic	sample_conditions_1
3D TROSY-HN(CO)CACB	sample_2	isotropic	sample_conditions_1
3D 15N/1H NOESY-HSQC	sample_3	isotropic	sample_conditions_1
3D TROSY-HN(CO)CA	sample_2	isotropic	sample_conditions_1

Software:

TOPSPIN - Data acquisition and processing

NMRPipe - Data processing

SPARKY - data analysis

NMR spectrometers:

Bruker Avance 600 MHz
Bruker Avance II 800 MHz

Uniprot	Q96PD4
AlphaFold	Q9NUE6