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 26651

Title: 1H, 13C, and 15N assignments of the Pleckstrin Homology Domain of Akt1.   PubMed: 26391397

Deposition date: 2015-09-08 Original release date: 2015-10-22

Authors: Saad, Jamil; Ghanam, Ruba; Agamasu, Constance

Citation: Agamasu, Constance; Ghanam, Ruba; Saad, Jamil. "Structural and Biophysical Characterization of the Interactions between Calmodulin and the Pleckstrin Homology Domain of Akt"  J. Biol. Chem. 290, 27403-27413 (2015).

Assembly members:
Akt_PHD, polymer, 113 residues, 13456.2528 Da.

Natural source:   Common Name: Mouse   Taxonomy ID: 10090   Superkingdom: Eukaryota   Kingdom: Metazoa   Genus/species: Mus musculus

Experimental source:   Production method: recombinant technology   Host organism: Escherichia coli   Vector: pET-28

Entity Sequences (FASTA):
Akt_PHD: SNDVAIVKEGWLHKRGEYIK TWRPRYFLLKNDGTFIGYKE RPQDVDQRESPLNNFSVAQC QLMKTERPRPNTFIIRCLQW TTVIERTFHVETPEEREEWA TAIQTVADGLKRQ

Data sets:
Data typeCount
13C chemical shifts197
15N chemical shifts97
1H chemical shifts97

Additional metadata:

  • Assembly
  • Samples and Experiments
  • Software
  • Spectrometers
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Assembly:

Entity Assembly IDEntity NameEntity ID
1Akt PHD1

Entities:

Entity 1, Akt PHD 113 residues - 13456.2528 Da.

1   SERASNASPVALALAILEVALLYSGLUGLY
2   TRPLEUHISLYSARGGLYGLUTYRILELYS
3   THRTRPARGPROARGTYRPHELEULEULYS
4   ASNASPGLYTHRPHEILEGLYTYRLYSGLU
5   ARGPROGLNASPVALASPGLNARGGLUSER
6   PROLEUASNASNPHESERVALALAGLNCYS
7   GLNLEUMETLYSTHRGLUARGPROARGPRO
8   ASNTHRPHEILEILEARGCYSLEUGLNTRP
9   THRTHRVALILEGLUARGTHRPHEHISVAL
10   GLUTHRPROGLUGLUARGGLUGLUTRPALA
11   THRALAILEGLNTHRVALALAASPGLYLEU
12   LYSARGGLN

Samples:

15N: Akt_PHD, [U-100% 15N], 0.2 mM; H2O 95%; D2O 5%

15N-13C: Akt_PHD, [U-100% 15N], 0.2 mM; H2O 95%; D2O 5%

AKT(PHD): ionic strength: 0.450 M; pH: 6.500; pressure: 1.000 atm; temperature: 303.000 K

Experiments:

NameSampleSample stateSample conditions
3D 1H-15N NOESY15NisotropicAKT(PHD)
2D 1H-15N HSQC/HMQC15NisotropicAKT(PHD)
3D HNCA15N-13CisotropicAKT(PHD)
HNcoCA_9 (H[N[co[{CA|ca[C]}]]])15N-13CisotropicAKT(PHD)
3D HNCO15N-13CisotropicAKT(PHD)

Software:

CcpNmr_Analysis v2.4, CCPN - Data Analysis

NMR_PIPE v2014, Delaglio, Grzesiek, Vuister, Zhu, Pfeifer and Bax - Data processing

NMR spectrometers:

  • Bruker AMX 700 MHz

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