BMRB Entry 30727

Name: NMR solution structure of natural scorpion toxin Cl13
Published: 2020-07-05

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PDB ID: 6vxw
Entry in NMR Restraints Grid
Validation report in NRG-CING
Chem Shift validation: AVS_anomalous, AVS_full
BMRB Entry DOI: doi:10.13018/BMR30727
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:

NMR solution structure of natural scorpion toxin Cl13

Deposition date:

2020-02-24

Original release date:

2020-07-05

Authors:

del Rio Portilla, F.; Delepierre, M.; Lopez Giraldo, A.

Citation:

Citation: Lopez-Giraldo, A.; Olamendi-Portugal, T.; Riano-Umbarila, L.; Becerril, B.; Possani, L.; Delepierre, M.; Rio-Portilla, F.. "The three-dimensional structure of the toxic peptide Cl13 from the scorpion Centruroides limpidus." Toxicon 184, 158-166 (2020).
PubMed: 32569846

Assembly members:

Assembly members:
entity_1, polymer, 67 residues, 7866.033 Da.

Natural source:

Natural source: Common Name: Mexican scorpion Taxonomy ID: 6876 Superkingdom: Eukaryota Kingdom: Metazoa Genus/species: Centruroides limpidus

Experimental source:

Experimental source: Production method: .

Entity Sequences (FASTA):

Entity Sequences (FASTA):
entity_1: KEGYLVDYHTGCKYTCAKLG DNDYCVRECRLRYYQSAHGY CYAFACWCTHLYEQAVVWPL PNKRCKX

Data sets:

assigned_chemical_shifts
- assigned_chemical_shifts_1
spectral_peak_list
- spectral_peak_list_1

Data type	Count
13C chemical shifts	241
15N chemical shifts	65
1H chemical shifts	459

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 67 residues - 7866.033 Da.

1

LYS

GLU

GLY

TYR

LEU

VAL

ASP

TYR

HIS

THR

2

GLY

CYS

LYS

TYR

THR

CYS

ALA

LYS

LEU

GLY

3

ASP

ASN

ASP

TYR

CYS

VAL

ARG

GLU

CYS

ARG

4

LEU

ARG

TYR

GLN

SER

ALA

HIS

GLY

TYR

5

CYS

TYR

ALA

PHE

ALA

CYS

TRP

CYS

THR

HIS

6

LEU

TYR

GLU

GLN

ALA

VAL

TRP

PRO

LEU

7

PRO

ASN

LYS

ARG

CYS

LYS

NH2

Name	Sample	Sample state	Sample conditions
2D 1H-1H TOCSY	sample_1	isotropic	sample_conditions_2
2D 1H-1H NOESY	sample_1	isotropic	sample_conditions_2
2D DQF-COSY	sample_1	isotropic	sample_conditions_2
2D 1H-1H TOCSY	sample_1	isotropic	sample_conditions_1
2D 1H-1H TOCSY	sample_1	isotropic	sample_conditions_2
2D 1H-1H TOCSY	sample_1	isotropic	sample_conditions_3
2D 1H-1H TOCSY	sample_1	isotropic	sample_conditions_5
2D 1H-1H TOCSY	sample_1	isotropic	sample_conditions_4
2D 1H-1H NOESY	sample_1	isotropic	sample_conditions_5
2D 1H-1H NOESY	sample_1	isotropic	sample_conditions_4
2D 1H-1H NOESY	sample_1	isotropic	sample_conditions_3
2D 1H-1H NOESY	sample_1	isotropic	sample_conditions_2
2D 1H-1H NOESY	sample_1	isotropic	sample_conditions_1
2D DQF-COSY	sample_1	isotropic	sample_conditions_5
2D DQF-COSY	sample_1	isotropic	sample_conditions_4
2D DQF-COSY	sample_1	isotropic	sample_conditions_3
2D DQF-COSY	sample_1	isotropic	sample_conditions_2
2D DQF-COSY	sample_1	isotropic	sample_conditions_1
13C HMBC	sample_1	isotropic	sample_conditions_2
13C HSQCTOCSY	sample_1	isotropic	sample_conditions_2
2D 1H-13C HSQC	sample_1	isotropic	sample_conditions_2
2D 1H-15N HSQC	sample_1	isotropic	sample_conditions_2

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

BMRB Entry 30727

Additional metadata:

Assembly:

Entities:

Samples:

Experiments:

Software:

NMR spectrometers: