BMRB Entry 26651

Name: 1H, 13C, and 15N assignments of the Pleckstrin Homology Domain of Akt1.
Published: 2015-10-22

Chem Shift validation: AVS_full
BMRB Entry DOI: doi:10.13018/BMR26651

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Nicholas Rego and David Koes
3Dmol.js: molecular visualization with WebGL
Bioinformatics (2015) 31 (8): 1322-1324 doi:10.1093/bioinformatics/btu829

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Title:

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

Deposition date:

2015-09-08

Original release date:

2015-10-22

Authors:

Saad, Jamil; Ghanam, Ruba; Agamasu, Constance

Citation:

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).
PubMed: 26391397

Assembly members:

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

Natural source:

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

Experimental source:

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

Entity Sequences (FASTA):

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

Data sets:

assigned_chemical_shifts
- assigned_chem_shift_list

Data type	Count
13C chemical shifts	197
15N chemical shifts	97
1H chemical shifts	97

Additional metadata:

Assembly
Samples and Experiments
Software
Spectrometers
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Assembly:

Entity Assembly ID	Entity Name	Entity ID
1	Akt PHD	1

Entities:

Entity 1, Akt PHD 113 residues - 13456.2528 Da.

1

SER

ASN

ASP

VAL

ALA

ILE

VAL

LYS

GLU

GLY

2

TRP

LEU

HIS

LYS

ARG

GLY

GLU

TYR

ILE

LYS

3

THR

TRP

ARG

PRO

ARG

TYR

PHE

LEU

LYS

4

ASN

ASP

GLY

THR

PHE

ILE

GLY

TYR

LYS

GLU

5

ARG

PRO

GLN

ASP

VAL

ASP

GLN

ARG

GLU

SER

6

PRO

LEU

ASN

PHE

SER

VAL

ALA

GLN

CYS

7

GLN

LEU

MET

LYS

THR

GLU

ARG

PRO

ARG

PRO

8

ASN

THR

PHE

ILE

ARG

CYS

LEU

GLN

TRP

9

THR

VAL

ILE

GLU

ARG

THR

PHE

HIS

VAL

10

GLU

THR

PRO

GLU

ARG

GLU

TRP

ALA

11

THR

ALA

ILE

GLN

THR

VAL

ALA

ASP

GLY

LEU

12

LYS

ARG

GLN

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:

Name	Sample	Sample state	Sample conditions
3D 1H-15N NOESY	15N	isotropic	AKT(PHD)
2D 1H-15N HSQC/HMQC	15N	isotropic	AKT(PHD)
3D HNCA	15N-13C	isotropic	AKT(PHD)
HNcoCA_9 (H[N[co[{CA\|ca[C]}]]])	15N-13C	isotropic	AKT(PHD)
3D HNCO	15N-13C	isotropic	AKT(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 peaks
SPARKY: Backbone or all simulated peaks