BMRB Entry 27605

Chem Shift validation: AVS_full
BMRB Entry DOI: doi:10.13018/BMR27605

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Title:
Dynamics of the leucine zipper of Nek2 kinase
Deposition date:
2018-09-12
Original release date:
2019-01-17
Authors:
Pfuhl, Mark; Gutmans, Daniel
Citation:

Citation: Gutmans, Daniel; Whittaker, Sara B-M; Asiani, Karishma; Atkinson, R Andrew; Oregioni, Alain; Pfuhl, Mark. "Controlling the dynamics of the Nek2 leucine zipper by engineering of "kinetic" disulphide bonds."  PLoS ONE 14, e0210352-e0210352 (2019).
PubMed: 30707691

Assembly members:

Assembly members:
LZ2, polymer, 49 residues, 5700 Da.

Natural source:

Natural source:   Common Name: Human   Taxonomy ID: 9606   Superkingdom: Eukaryota   Kingdom: Metazoa   Genus/species: Homo sapiens

Experimental source:

Experimental source:   Production method: recombinant technology   Host organism: Escherichia coli   Vector: pLEICS-07

Entity Sequences (FASTA):

Entity Sequences (FASTA):
LZ2: GAMASSPVLSELKLKEIQLQ ERERALKAREERLEQKEQEL AVRERLACD

Data sets:
Data typeCount
13C chemical shifts224
15N chemical shifts98
1H chemical shifts522

Additional metadata:

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

Assembly:

Entity Assembly IDEntity NameEntity ID
1monomer 1 conformer A1
2monomer 2 conformer A1
3monomer 1 conformer B1
4monomer 2 conformer B1

Entities:

Entity 1, monomer 1 conformer A 49 residues - 5700 Da.

residues 295-298 are leftover of the his-tag. The real sequence starts at S299

1   GLYALAMETALASERSERPROVALLEUSER
2   GLULEULYSLEULYSGLUILEGLNLEUGLN
3   GLUARGGLUARGALALEULYSALAARGGLU
4   GLUARGLEUGLUGLNLYSGLUGLNGLULEU
5   ALAVALARGGLUARGLEUALACYSASP

Samples:

sample_1: LZ2, [U-98% 15N], 1 ± 0.05 mM; NaCl 50 mM

sample_2: LZ2, [U-95% 13C; U-90% 15N], 1 ± 0.05 mM; NaCl 50 mM

sample_conditions_1: ionic strength: 0.05 M; pH: 7.2; pressure: 1 atm; temperature: 298 K

Experiments:

NameSampleSample stateSample conditions
2D 1H-15N HSQCsample_1isotropicsample_conditions_1
3D 1H-15N NOESYsample_1isotropicsample_conditions_1
3D 1H-15N TOCSYsample_1isotropicsample_conditions_1
3D HNCAsample_2isotropicsample_conditions_1
3D HNCACBsample_2isotropicsample_conditions_1
3D HNCOsample_2isotropicsample_conditions_1
3D HNHBsample_1isotropicsample_conditions_1

Software:

TOPSPIN v3.1, Bruker Biospin - processing

CCPN_Analysis v2.4, CCPN - chemical shift assignment, data analysis, peak picking

NMR spectrometers:

  • Bruker Avance 900 MHz
  • Bruker Avance 700 MHz
  • Bruker Avance 600 MHz
  • Bruker Avance 800 MHz

Related Database Links:

UNP P51955
AlphaFold Q96QN9

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