BMRB Entry 30944

Name: The solution structure of remipede double-ICK toxin phi-Xibalbin3-Xt3a
Published: 2022-08-26

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PDB ID: 7rz3
Entry in NMR Restraints Grid
Validation report in NRG-CING
Chem Shift validation: AVS_full
BMRB Entry DOI: doi:10.13018/BMR30944
MolProbity Validation Chart

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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:

The solution structure of remipede double-ICK toxin phi-Xibalbin3-Xt3a

Deposition date:

2021-08-27

Original release date:

2022-08-26

Authors:

Maxwell, M.; Chin, Y.; Mobli, M.

Citation:

Citation: Maxwell, Michael; Thekkedam, Chris; Lamboley, Cedric; Chin, Yanni K-Y; Crawford, Theo; Smith, Jennifer; Liu, Junyu; Jia, Xinying; Vetter, Irina; Laver, Derek; Launikonis, Bradley; Dulhunty, Angela; Undheim, Eivind; Mobli, Mehdi. "A bivalent remipede toxin promotes calcium release via ryanodine receptor activation" Nat. Commun. 14, 1036-1036 (2023).
PubMed: 36823422

Assembly members:

Assembly members:
entity_1, polymer, 82 residues, 8856.960 Da.

Natural source:

Natural source: Common Name: Xibalbanus tulumensis Taxonomy ID: 1519145 Superkingdom: Eukaryota Kingdom: Metazoa Genus/species: Xibalbanus tulumensis

Experimental source:

Experimental source: Production method: recombinant technology Host organism: Escherichia coli

Entity Sequences (FASTA):

Entity Sequences (FASTA):
entity_1: SAVLWNQQYDKTVCNQEGEF CSKSGVDCCAGLSCRKYNLM GYGVCAAQTCSEEGTFCSLS DSDCCSGLKCKRRGHGYGEC SK

Data sets:

assigned_chemical_shifts
- assigned_chemical_shifts_1
spectral_peak_list

Data type	Count
13C chemical shifts	288
15N chemical shifts	78
1H chemical shifts	472

Additional metadata:

Assembly
Samples and Experiments
Software
Spectrometers
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Assembly:

Entity Assembly ID	Entity Name	Entity ID
1	unit_1	1

Entities:

Entity 1, unit_1 82 residues - 8856.960 Da.

1

SER

ALA

VAL

LEU

TRP

ASN

GLN

TYR

ASP

2

LYS

THR

VAL

CYS

ASN

GLN

GLU

GLY

GLU

PHE

3

CYS

SER

LYS

SER

GLY

VAL

ASP

CYS

ALA

4

GLY

LEU

SER

CYS

ARG

LYS

TYR

ASN

LEU

MET

5

GLY

TYR

GLY

VAL

CYS

ALA

GLN

THR

CYS

6

SER

GLU

GLY

THR

PHE

CYS

SER

LEU

SER

7

ASP

SER

ASP

CYS

SER

GLY

LEU

LYS

CYS

8

LYS

ARG

GLY

HIS

GLY

TYR

GLY

GLU

CYS

9

SER

LYS

Name	Sample	Sample state	Sample conditions
2D 1H-15N HSQC	sample_1	isotropic	sample_conditions_1
2D 1H-13C HSQC	sample_1	isotropic	sample_conditions_1
3D 1H-13C NOESY aliphatic	sample_1	isotropic	sample_conditions_1
3D 1H-13C NOESY aromatic	sample_1	isotropic	sample_conditions_1
3D 1H-15N NOESY	sample_1	isotropic	sample_conditions_1
3D HNCO	sample_1	isotropic	sample_conditions_1
3D HNCACB	sample_2	isotropic	sample_conditions_1
3D HCACO	sample_1	isotropic	sample_conditions_1
3D CBCA(CO)NH	sample_2	isotropic	sample_conditions_1
3D HBHA(CO)NH	sample_2	isotropic	sample_conditions_1
2D CB(CGCC-TOCSY)Haro	sample_1	isotropic	sample_conditions_1

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

BMRB Entry 30944

Additional metadata:

Assembly:

Entities:

Samples:

Experiments:

Software:

NMR spectrometers: