BMRB

Biological Magnetic Resonance Data Bank


A Repository for Data from NMR Spectroscopy on Proteins, Peptides, Nucleic Acids, and other Biomolecules
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BMRB Entry 20049

Title: NMR solution structure of Mu-KIIIA[C1A,C9A]   PubMed: 19170536

Authors: Khoo, Keith; Feng, Zhiping; Norton, Raymond

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).

Assembly members:
KIIIA[Ala1,9], polymer, 16 residues, 1831.085 Da.

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

Experimental source:   Production method: recombinant technology

Entity Sequences (FASTA):
KIIIA[Ala1,9]: ACNCSSKWARDHSRCC

Data sets:
Data typeCount
13C chemical shifts15
15N chemical shifts12
1H chemical shifts94

Additional metadata:

  • Assembly
  • Samples and Experiments
  • Software
  • Spectrometers
  • Hide all

Assembly:

Entity Assembly IDEntity NameEntity ID
1KIIIA[Ala1,9]1

Entities:

Entity 1, KIIIA[Ala1,9] 16 residues - 1831.085 Da.

1   ALACYSASNCYSSERSERLYSTRPALAARG
2   ASPHISSERARGCYSCYS

Samples:

KIIIA(Ala1_9)_H2O: KIIIA[Ala1,9] 3.7 mM

KIIIA(Ala1_9)_D2O: KIIIA[Ala1,9] 3.7 mM

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

pH_5.3_283_K: pH: 5.3; temperature: 283 K

pH_5.3_293_K: pH: 5.3; temperature: 293 K

pH_3.2_278_K: pH: 3.2; temperature: 278 K

pH_4.2_278_K: pH: 4.2; temperature: 278 K

Experiments:

NameSampleSample stateSample conditions
2D 1H-15N HSQCKIIIA(Ala1_9)_H2OisotropicpH_5.3_283_K
2D 1H-13C HSQCKIIIA(Ala1_9)_H2OisotropicpH_5.3_278_K
2D 1H-1H TOCSYKIIIA(Ala1_9)_H2OisotropicpH_5.3_278_K
2D DQF-COSYKIIIA(Ala1_9)_H2OisotropicpH_5.3_278_K
2D 1H-1H NOESYKIIIA(Ala1_9)_H2OisotropicpH_5.3_278_K
2D 1H-1H TOCSYKIIIA(Ala1_9)_H2OisotropicpH_3.2_278_K
2D 1H-1H NOESYKIIIA(Ala1_9)_H2OisotropicpH_3.2_278_K
2D 1H-1H TOCSYKIIIA(Ala1_9)_D2OisotropicpH_4.2_278_K
2D 1H-1H NOESYKIIIA(Ala1_9)_D2OisotropicpH_4.2_278_K
2D 1H-1H NOESYKIIIA(Ala1_9)_H2OisotropicpH_5.3_293_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, structure solution

ProcheckNMR, Laskowski and MacArthur - data analysis

NMR spectrometers:

  • Bruker DRX 600 MHz
  • Bruker Avance 500 MHz

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