BMRB Entry 31122

Name: Solution NMR structure of pro-IL-18
Published: 2024-05-21

Click here to enlarge.

PDB ID: 8urv
Entry in NMR Restraints Grid
Validation report in NRG-CING
Chem Shift validation: AVS_full
BMRB Entry DOI: doi:10.13018/BMR31122
MolProbity Validation Chart

NMR-STAR file interactive viewer.
NMR-STAR v3 text file.
XML gzip file.
RDF gzip file.
All files associated with the entry

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

Select model:

I am color blind

Download raw data. Direct link to this display. Help

Title:

Solution NMR structure of pro-IL-18

Deposition date:

2023-10-26

Original release date:

2024-05-21

Authors:

Bonin, J.; Aramini, J.; Kay, L.

Citation:

Citation: Dong, Ying; Bonin, Jeffrey; Devant, Pascal; Liang, Zhuoyi; Sever, Alexander; Mintseris, Julian; Aramini, James; Du, Gang; Gygi, Stephen; Kagan, Jonathan; Kay, Lewis; Wu, Hao. "Structural transitions enable interleukin-18 maturation and signaling" Immunity 57, 1533-1548 (2024).
PubMed: 38733997

Assembly members:

Assembly members:
entity_1, polymer, 193 residues, 22350.225 Da.

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

Entity Sequences (FASTA):

Entity Sequences (FASTA):
entity_1: MAAEPVEDNCINFVAMKFID NTLYFIAEDDENLESDYFGK LESKLSVIRNLNDQVLFIDQ GNRPLFEDMTDSDCRDNAPR TIFIISMYKDSQPRGMAVTI SVKCEKISTLSCENKIISFK EMNPPDNIKDTKSDIIFFQR SVPGHDNKMQFESSSYEGYF LACEKERDLFKLILKKEDEL GDRSIMFTVQNED

Data sets:

assigned_chemical_shifts
- assigned_chemical_shifts_1
spectral_peak_list
- spectral_peak_list_1

Data type	Count
13C chemical shifts	901
15N chemical shifts	203
1H chemical shifts	1380

Additional metadata:

Assembly
Samples and Experiments
Software
Spectrometers
Hide all

Assembly:

Entity Assembly ID	Entity Name	Entity ID
1	unit_1	1

Entities:

Entity 1, unit_1 193 residues - 22350.225 Da.

1

MET

ALA

GLU

PRO

VAL

GLU

ASP

ASN

CYS

2

ILE

ASN

PHE

VAL

ALA

MET

LYS

PHE

ILE

ASP

3

ASN

THR

LEU

TYR

PHE

ILE

ALA

GLU

ASP

4

GLU

ASN

LEU

GLU

SER

ASP

TYR

PHE

GLY

LYS

5

LEU

GLU

SER

LYS

LEU

SER

VAL

ILE

ARG

ASN

6

LEU

ASN

ASP

GLN

VAL

LEU

PHE

ILE

ASP

GLN

7

GLY

ASN

ARG

PRO

LEU

PHE

GLU

ASP

MET

THR

8

ASP

SER

ASP

CYS

ARG

ASP

ASN

ALA

PRO

ARG

9

THR

ILE

PHE

ILE

SER

MET

TYR

LYS

ASP

10

SER

GLN

PRO

ARG

GLY

MET

ALA

VAL

THR

ILE

11

SER

VAL

LYS

CYS

GLU

LYS

ILE

SER

THR

LEU

12

SER

CYS

GLU

ASN

LYS

ILE

SER

PHE

LYS

13

GLU

MET

ASN

PRO

ASP

ASN

ILE

LYS

ASP

14

THR

LYS

SER

ASP

ILE

PHE

GLN

ARG

15

SER

VAL

PRO

GLY

HIS

ASP

ASN

LYS

MET

GLN

16

PHE

GLU

SER

TYR

GLU

GLY

TYR

PHE

17

LEU

ALA

CYS

GLU

LYS

GLU

ARG

ASP

LEU

PHE

18

LYS

LEU

ILE

LEU

LYS

GLU

ASP

GLU

LEU

19

GLY

ASP

ARG

SER

ILE

MET

PHE

THR

VAL

GLN

20

ASN

GLU

ASP

Samples:

sample_1: pro-interleukin-18, [U-13C; U-15N], 0.5 mM; MES 20 mM; potassium chloride 50 mM; DTT 10 mM

sample_2: pro-interleukin-18, [U-13C; U-15N], 0.5 mM; MES 20 mM; potassium chloride 50 mM; DTT 10 mM

sample_3: pro-interleukin-18, [5% U-13C; U-15N], 0.5 mM; MES 20 mM; potassium chloride 50 mM; DTT 10 mM

sample_conditions_1: ionic strength: 50 mM; pH: 6.5; pressure: 1 atm; temperature: 298.1 K

sample_conditions_2: ionic strength: 50 mM; pH: 6.1 pD; pressure: 1 atm; temperature: 298.1 K

Experiments:

Name	Sample	Sample state	Sample conditions
3D HCH NOESY	sample_2	isotropic	sample_conditions_2
3D HNH NOESY	sample_1	isotropic	sample_conditions_1
3D NNH NOESY	sample_1	isotropic	sample_conditions_1
2D NH HSQC	sample_1	isotropic	sample_conditions_1
2D CH HSQC	sample_2	isotropic	sample_conditions_2
3D HNCO	sample_1	isotropic	sample_conditions_1
3D HN(CA)CO	sample_1	isotropic	sample_conditions_1
3D CBCA(CO)NH	sample_1	isotropic	sample_conditions_1
3D HNCACB	sample_1	isotropic	sample_conditions_1
3D HNN	sample_1	isotropic	sample_conditions_1
3D C(CO)NH TOCSY	sample_1	isotropic	sample_conditions_1
3D HBHA(CO)NH	sample_1	isotropic	sample_conditions_1
3D H(CCO)NH TOCSY	sample_1	isotropic	sample_conditions_1
3D C(CA)NH TOCSY	sample_1	isotropic	sample_conditions_1
2D CB(CGCD)HD	sample_2	isotropic	sample_conditions_2
2D CB(CGCDCE)HE	sample_2	isotropic	sample_conditions_2
2D CBCG(CE)HE	sample_2	isotropic	sample_conditions_2
2D CH CT-HSQC	sample_3	isotropic	sample_conditions_1

Software:

I-PINE, Lee, Bahrami, Dashti, Eghbalnia, Tonelli, Westler and Markley - chemical shift assignment

CYANA v3.98.15, Herrmann, Guntert and Wuthrich - structure calculation

Rosetta v3, Leaver-Fay et al. - refinement

NMRFAM-SPARKY, Lee, Tonelli and Markley - peak picking

NMR spectrometers:

Bruker AVANCE III HD 800 MHz
Bruker AVANCE III HD 600 MHz
Bruker AVANCE NEO 1000 MHz

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