BMRB Entry 20048

Name: NMR solution structure of an analgesic Mu-contoxin KIIIA
Published: 2009-04-04

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PDB ID: 2lxg
Entry in NMR Restraints Grid
Validation report in NRG-CING
Chem Shift validation: AVS_full
BMRB Entry DOI: doi:10.13018/BMR20048
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Bioinformatics (2015) 31 (8): 1322-1324 doi:10.1093/bioinformatics/btu829

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Title:

NMR solution structure of an analgesic Mu-contoxin KIIIA

Deposition date:

2008-09-28

Original release date:

2009-04-04

Authors:

Khoo, Keith; Feng, Zhiping; Norton, Raymond

Citation:

Citation: Khoo, Keith; Feng, Zhi-Ping; Smith, Brian; Zhang, Min-Min; Yoshikami, Doju; Olivera, Baldomero; Bulaj, Grzegorz; Norton, Raymond. "Structure of the Analgesic mu-Conotoxin KIIIA and Effects on the Structure and Function of Disulfide Deletion" Biochemistry 48, 1210-1219 (2009).
PubMed: 19170536

Assembly members:

Assembly members:
KIIIA, polymer, 16 residues, 1895.206 Da.

Natural source:

Natural source: Common Name: Conus kinoshitai Taxonomy ID: 376876 Superkingdom: Eukaryota Kingdom: Conidae Genus/species: Conus kinoshitai

Experimental source:

Experimental source: Production method: chemical synthesis

Entity Sequences (FASTA):

Entity Sequences (FASTA):
KIIIA: CCNCSSKWCRDHSRCC

Data sets:

assigned_chemical_shifts
- assigned_chem_shift_list_1
conformer_family_coord_set
- ensemble_coordinates

Data type	Count
13C chemical shifts	14
15N chemical shifts	15
1H chemical shifts	93

Additional metadata:

Assembly
Samples and Experiments
Software
Spectrometers
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Assembly:

Entity Assembly ID	Entity Name	Entity ID
1	KIIIA	1

Entities:

Entity 1, KIIIA 16 residues - 1895.206 Da.

1

CYS

ASN

CYS

SER

LYS

TRP

CYS

ARG

2

ASP

HIS

SER

ARG

CYS

Samples:

KIIIA_H2O: KIIIA 2.6 mM

KIIIA_D2O: KIIIA 2.3 mM

pH_2.9_278_K: pH: 2.9; temperature: 278 K

pH_2.9_283_K: pH: 2.9; temperature: 283 K

pH_4.8_278_K: pH: 4.8; temperature: 278 K

pH_4.8_293_K: pH: 4.8; temperature: 293 K

pH_5.3_278_K: pH: 5.3; temperature: 278 K

Experiments:

Name	Sample	Sample state	Sample conditions
2D 1H-15N HSQC	KIIIA_H2O	isotropic	pH_2.9_283_K
2D 1H-13C HSQC	KIIIA_H2O	isotropic	pH_2.9_278_K
2D 1H-1H TOCSY	KIIIA_H2O	isotropic	pH_4.8_278_K
2D DQF-COSY	KIIIA_H2O	isotropic	pH_4.8_278_K
2D 1H-1H NOESY	KIIIA_H2O	isotropic	pH_4.8_278_K
2D 1H-1H TOCSY	KIIIA_H2O	isotropic	pH_2.9_278_K
2D 1H-1H NOESY	KIIIA_H2O	isotropic	pH_2.9_278_K
2D 1H-1H TOCSY	KIIIA_D2O	isotropic	pH_5.3_278_K
2D 1H-1H NOESY	KIIIA_D2O	isotropic	pH_5.3_278_K

Software:

TOPSPIN v1.3, Bruker Biospin - collection, processing

XEASY v1.3.13, Bartels et al. - chemical shift assignment, peak picking

CYANA, Guntert, Mumenthaler and Wuthrich - structure solution

X-PLOR NIH, Schwieters, Kuszewski, Tjandra and Clore - geometry optimization, refinement

ProcheckNMR, Laskowski and MacArthur - data analysis

NMR spectrometers:

Bruker DRX 600 MHz
Bruker Avance 500 MHz

PDB	2LXG
SP	P0C195
AlphaFold	P0C195