BMRB Entry 51175

Name: NMR assignments for the C-terminal domain of human RIPK3
Published: 2022-11-10

Chem Shift validation: AVS_full
BMRB Entry DOI: doi:10.13018/BMR51175

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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:

NMR assignments for the C-terminal domain of human RIPK3

Deposition date:

2021-11-10

Original release date:

2022-11-10

Authors:

Titaux Delgado, Gustavo Alfredo; Pham, Chi; Sunde, Margaret; Mompean, Miguel

Citation:

Citation: Pham, ChiL; Titaux-Delgado, GustavoA; Varghese, NikhilR; Polonio, Paula; Wilde, KarynL; Sunde, Margaret; Mompean, Miguel. "NMR characterization of an assembling RHIM (RIP Homotypic Interaction Motif) amyloid reveals a cryptic region for self-recognition" J. Biol. Chem. 299, 104568-104568 (2023).
PubMed: 36870681

Assembly members:

Assembly members:
entity_1, 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: pMAL

Entity Sequences (FASTA):

Entity Sequences (FASTA):
entity_1: GSSSDSMAQPPQTPETSTFR NQMPSPTSTGTPSPGPRGNQ GAERQGMNWSCRTPEPNPVT GRPLVNIYNCSGVQVGDNNY LTMQQTTALPTWGLAPSGKG RGLQHPPPVGSQEGPKDPEA WSRPQGWYNHSGK

Data sets:

assigned_chemical_shifts
- assigned_chemical_shifts_1
coupling_constants
- RIPK3_388_518_3JHNHA
heteronucl_T1_relaxation
- RIPK3_388_518_R1
heteronucl_T1rho_relaxation
- RIPK3_388_518_R1rho

Data type	Count
13C chemical shifts	449
15N chemical shifts	126
1H chemical shifts	428
T1 relaxation values	112
T1rho relaxation values	112
coupling constants	84

Additional metadata:

Assembly
Samples and Experiments
Software
Spectrometers
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Assembly:

Entity Assembly ID	Entity Name	Entity ID
1	C-terminal domain of RIPK3	1

Entities:

Entity 1, C-terminal domain of RIPK3 133 residues - Formula weight is not available

1

GLY

SER

ASP

SER

MET

ALA

GLN

PRO

2

PRO

GLN

THR

PRO

GLU

THR

SER

THR

PHE

ARG

3

ASN

GLN

MET

PRO

SER

PRO

THR

SER

THR

GLY

4

THR

PRO

SER

PRO

GLY

PRO

ARG

GLY

ASN

GLN

5

GLY

ALA

GLU

ARG

GLN

GLY

MET

ASN

TRP

SER

6

CYS

ARG

THR

PRO

GLU

PRO

ASN

PRO

VAL

THR

7

GLY

ARG

PRO

LEU

VAL

ASN

ILE

TYR

ASN

CYS

8

SER

GLY

VAL

GLN

VAL

GLY

ASP

ASN

TYR

9

LEU

THR

MET

GLN

THR

ALA

LEU

PRO

10

THR

TRP

GLY

LEU

ALA

PRO

SER

GLY

LYS

GLY

11

ARG

GLY

LEU

GLN

HIS

PRO

VAL

GLY

12

SER

GLN

GLU

GLY

PRO

LYS

ASP

PRO

GLU

ALA

13

TRP

SER

ARG

PRO

GLN

GLY

TRP

TYR

ASN

HIS

14

SER

GLY

LYS

Samples:

sample_1: C-terminal domain of RIPK3, [U-100% 13C; U-100% 15N], 18 uM; C-terminal domain of RIPK3, [U-100% 13C; U-100% 15N], 180 uM

sample_conditions_1: ionic strength: 0 M; pH: 4; pressure: 1 atm; temperature: 298 K

Experiments:

Name	Sample	Sample state	Sample conditions
2D 1H-15N HSQC	sample_1	isotropic	sample_conditions_1
3D HNCA	sample_1	isotropic	sample_conditions_1
3D HNCACB	sample_1	isotropic	sample_conditions_1
3D CBCA(CO)NH	sample_1	isotropic	sample_conditions_1
3D HNCO	sample_1	isotropic	sample_conditions_1
3D HN(CA)CO	sample_1	isotropic	sample_conditions_1
3D C(CO)NH	sample_1	isotropic	sample_conditions_1
3D HBHA(CO)NH	sample_1	isotropic	sample_conditions_1
3D HNHA	sample_1	isotropic	sample_conditions_1
3D HNHA gp	sample_1	isotropic	sample_conditions_1
HSQC T1 etf 3gpsi	sample_1	isotropic	sample_conditions_1
HSQC T ref 3gpsi	sample_1	isotropic	sample_conditions_1

Software:

NMRFAM-SPARKY - chemical shift assignment

NMR spectrometers:

Bruker AVANCE NEO 800 MHz

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