BMRB Entry 31055

Name: NMR solution structure of lambda-MeuKTx-1
Published: 2022-11-17

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PDB ID: 8f2f
Entry in NMR Restraints Grid
Validation report in NRG-CING
Chem Shift validation: AVS_full
BMRB Entry DOI: doi:10.13018/BMR31055
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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 lambda-MeuKTx-1

Deposition date:

2022-11-07

Original release date:

2022-11-17

Authors:

Harvey, P.; Craik, D.

Citation:

Citation: Gao, B.; Harvey, P.; Craik, D.; Ronjat, M.; De Waard, M.; Zhu, S.. "Functional evolution of scorpion venom peptides with an inhibitor cystine knot fold." Biosci. Rep. 33, e00047-e00047 (2013).
PubMed: 23721518

Assembly members:

Assembly members:
entity_1, polymer, 38 residues, 4135.675 Da.

Natural source:

Natural source: Common Name: lesser Asian scorpion Taxonomy ID: 34648 Superkingdom: Eukaryota Kingdom: Metazoa Genus/species: Mesobuthus eupeus

Experimental source:

Experimental source: Production method: chemical synthesis

Entity Sequences (FASTA):

Entity Sequences (FASTA):
entity_1: GCNRLNKKCNSDADCCRYGE RCISTGVNYYCRPDVGPX

Data sets:

assigned_chemical_shifts
- assigned_chemical_shifts_1

Data type	Count
1H chemical shifts	218

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 38 residues - 4135.675 Da.

1

GLY

CYS

ASN

ARG

LEU

ASN

LYS

CYS

ASN

2

SER

ASP

ALA

ASP

CYS

ARG

TYR

GLY

GLU

3

ARG

CYS

ILE

SER

THR

GLY

VAL

ASN

TYR

4

CYS

ARG

PRO

ASP

VAL

GLY

PRO

NH2

Samples:

sample_1: peptide 1.0 mM

sample_2: peptide 1.0 mM

sample_conditions_1: pH: 3.0; pressure: 1 atm; temperature: 298 K

Experiments:

Name	Sample	Sample state	Sample conditions
2D 1H-1H TOCSY	sample_1	isotropic	sample_conditions_1
2D 1H-1H NOESY	sample_1	isotropic	sample_conditions_1
2D DQF-COSY	sample_1	isotropic	sample_conditions_1
2D 1H-13C HSQC aliphatic	sample_1	isotropic	sample_conditions_1
2D 1H-1H TOCSY	sample_2	isotropic	sample_conditions_1
2D 1H-1H NOESY	sample_2	isotropic	sample_conditions_1
2D ECOSY	sample_2	isotropic	sample_conditions_1

Software:

TopSpin, Bruker Biospin - processing

CcpNmr Analysis, CCPN - chemical shift assignment

CYANA, Guntert, Mumenthaler and Wuthrich - structure calculation

CNS, Brunger, Adams, Clore, Gros, Nilges and Read - refinement

NMR spectrometers:

Bruker AVANCE III HD 600 MHz