BMRB Entry 27464

Name: C-terminal tail of Protein Phosphatase 1, alpha isoform.
Published: 2019-04-26

Chem Shift validation: AVS_full
BMRB Entry DOI: doi:10.13018/BMR27464

NMR-STAR file interactive viewer.
NMR-STAR v3 text file.
XML gzip file.
RDF gzip file.
All files associated with the entry

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

Select model:

I am color blind

Download raw data. Direct link to this display. Help

Title:

C-terminal tail of Protein Phosphatase 1, alpha isoform.

Deposition date:

2018-04-23

Original release date:

2019-04-26

Authors:

Bajaj, Rakhi; Page, Rebecca; Peti, Wolfgang

Citation:

Citation: Bertran, M Teresa; Mouilleron, Stephane; Zhou, Yanxiang; Bajaj, Rakhi; Uliana, Federico; Kumar, Ganesan Senthil; van Drogen, Audrey; Lee, Rebecca; Banerjee, Jennifer; Hauri, Simon; O'Reilly, Nicola; Gstaiger, Matthias; Page, Rebecca; Peti, Wolfgang; Tapon, Nicolas. "ASPP proteins discriminate between PP1 catalytic subunits through their SH3 domain and the PP1 C-tail" Nat. Commun. 10, 771-771 (2019).
PubMed: 30770806

Assembly members:

Assembly members:
PP1_C-_ter, polymer, 34 residues, Formula weight is not available

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: pET-M30-MBP

Entity Sequences (FASTA):

Entity Sequences (FASTA):
PP1_C-_ter: GAMGKNKGKYGQFSGLNPGG RPITPPRNSAKAKK

Data sets:

assigned_chemical_shifts
- assigned_chem_shift_list_1

Data type	Count
13C chemical shifts	53
15N chemical shifts	27
1H chemical shifts	27

Additional metadata:

Assembly
Samples and Experiments
Software
Spectrometers
Hide all

Assembly:

Entity Assembly ID	Entity Name	Entity ID
1	Protein phosphatse 1	1

Entities:

Entity 1, Protein phosphatse 1 34 residues - Formula weight is not available

Residue 1 -4 GAMG is cloning artifact and residues 5-34 correspond to residues 301-330 of of Protein phosphatase 1 ( alpha isoform).

1

GLY

ALA

MET

GLY

LYS

ASN

LYS

GLY

LYS

TYR

2

GLY

GLN

PHE

SER

GLY

LEU

ASN

PRO

GLY

3

ARG

PRO

ILE

THR

PRO

ARG

ASN

SER

ALA

4

LYS

ALA

LYS

Samples:

sample_1: PP1 C- ter, [U-99% 13C; U-99% 15N], 0.4 mM; Bis-Tris pH=6.5 20 mM; sodium chloride 150 mM

sample_conditions_1: ionic strength: 0.15 M; pH: 6.5; pressure: 1 atm; temperature: 283 K

Experiments:

Name	Sample	Sample state	Sample conditions
2D 1H-15N HSQC	sample_1	isotropic	sample_conditions_1
3D HNCA	sample_1	isotropic	sample_conditions_1
3D HN(CO)CA	sample_1	isotropic	sample_conditions_1
3D CBCA(CO)NH	sample_1	isotropic	sample_conditions_1
3D HNCACB	sample_1	isotropic	sample_conditions_1

Software:

No software information available

NMR spectrometers:

Bruker Avance-NEO 600 MHz

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