BMRB Entry 17417

Title:
mutant C335A, K309C of the Nek2 kinase leucine zipper
Deposition date:
2011-01-20
Original release date:
2011-04-08
Authors:
Pfuhl, Mark
Citation:

Citation: Croasdale, Rebecca; Ivins, Frank; Muskett, Fred; Daviter, Tina; Scott, David; Hardy, Tara; Smerdon, Steven; Fry, Andrew; Pfuhl, Mark. "An undecided coiled coil: the leucine zipper of Nek2 kinase exhibits atypical conformational exchange dynamics."  J. Biol. Chem. 286, 27537-27547 (2011).
PubMed: 21669869

Assembly members:

Assembly members:
LZ5C335AK309C, polymer, 46 residues, 5438.1991 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: pETM-11

Entity Sequences (FASTA):

Entity Sequences (FASTA):
LZ5C335AK309C: GAMAVLSELKLCEIQLQERE RALKAREERLEQKEQELAVR ERLAED

Data sets:
Data typeCount
13C chemical shifts88
15N chemical shifts46
1H chemical shifts186

Additional metadata:

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

Assembly:

Entity Assembly IDEntity NameEntity ID
1LZ5, chain 11
2LZ5, chain 21

Entities:

Entity 1, LZ5, chain 1 46 residues - 5438.1991 Da.

residues 1-4 are a cloning artifact

1   GLYALAMETALAVALLEUSERGLULEULYS
2   LEUCYSGLUILEGLNLEUGLNGLUARGGLU
3   ARGALALEULYSALAARGGLUGLUARGLEU
4   GLUGLNLYSGLUGLNGLULEUALAVALARG
5   GLUARGLEUALAGLUASP

Samples:

sample_1: LZ5C335AK309C, [U-15N], 0.8 ± 0.1 mM; H2O 55 ± 0 M; sodium phosphate 20 ± 0.5 mM; sodium chloride 50 ± 0.5 mM; sodium azide 0.02 ± 0.0002 %; H2O 95%; D2O 5%

sample_2: LZ5C335AK309C, [U-13C; U-15N], 0.8 ± 0.1 mM; H2O 55 ± 0 M; sodium phosphate 20 ± 0.5 mM; sodium chloride 50 ± 0.5 mM; sodium azide 0.02 ± 0.0002 %; H2O 95%; D2O 5%

sample_conditions_1: ionic strength: 80 mM; pH: 7.2; pressure: 1 atm; temperature: 298 K

sample_conditions_2: ionic strength: 80 mM; pH: 6.0; 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 HNCACBsample_2isotropicsample_conditions_1
3D HBHA(CO)NHsample_2isotropicsample_conditions_1
3D CBCA(CO)NHsample_2isotropicsample_conditions_1
2D 1H-15N HSQCsample_1isotropicsample_conditions_2
3D 1H-15N NOESYsample_1isotropicsample_conditions_2

Software:

ANALYSIS v2.1, CCPN - chemical shift assignment, chemical shift calculation, peak picking

DANGLE v1.1, CCPN - calculate backbone torsion angles from chemical shifts

TOPSPIN v2.1, Bruker Biospin - processing

NMR spectrometers:

  • Bruker Avance 500 MHz

Related Database Links:

UNP NEK2_HUMAN

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