BMRB Entry 27912

Name: 1H, 13C and 15N NMR chemical shift assignments of cAMP-regulated phosphoprotein-19 and -16 (ARPP19 and ARPP16)
Published: 2020-09-28

Chem Shift validation: AVS_full
BMRB Entry DOI: doi:10.13018/BMR27912

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:

1H, 13C and 15N NMR chemical shift assignments of cAMP-regulated phosphoprotein-19 and -16 (ARPP19 and ARPP16)

Deposition date:

2019-05-15

Original release date:

2020-09-28

Authors:

Thapa, Chandan; Pentikainen, Ulla; Permi, Perttu

Citation:

Citation: Thapa, Chandan; Haataja, Tatu; Pentikainen, Ulla; Permi, Perttu. "1H, 13C and 15N NMR chemical shift assignments of cAMP-regulated phosphoprotein-19 and -16 (ARPP19 and ARPP16)" Biomol. NMR Assign. 14, 227-231 (2020).
PubMed: 32468417

Assembly members:

Assembly members:
ARPP-19, polymer, 116 residues, 12639.35 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: pGEX4T3 (modified)

Entity Sequences (FASTA):

Entity Sequences (FASTA):
ARPP-19: GAMGMSAEVPEAASAEEQKE MEDKVTSPEKAEEAKLKARY PHLGQKPGGSDFLRKRLQKG QKYFDSGDYNMAKAKMKNKQ LPTAAPDKTEVTGDHIPTPQ DLPQRKPSLVASKLAG

Data sets:

assigned_chemical_shifts
- assigned_chem_shift_list_1

Data type	Count
13C chemical shifts	325
15N chemical shifts	112
1H chemical shifts	215

Additional metadata:

Assembly
Samples and Experiments
Software
Spectrometers
Hide all

Assembly:

Entity Assembly ID	Entity Name	Entity ID
1	ARPP-19	1

Entities:

Entity 1, ARPP-19 116 residues - 12639.35 Da.

Residues 1-4 represent a cloning artifacts.

1

GLY

ALA

MET

GLY

MET

SER

ALA

GLU

VAL

PRO

2

GLU

ALA

SER

ALA

GLU

GLN

LYS

GLU

3

MET

GLU

ASP

LYS

VAL

THR

SER

PRO

GLU

LYS

4

ALA

GLU

ALA

LYS

LEU

LYS

ALA

ARG

TYR

5

PRO

HIS

LEU

GLY

GLN

LYS

PRO

GLY

SER

6

ASP

PHE

LEU

ARG

LYS

ARG

LEU

GLN

LYS

GLY

7

GLN

LYS

TYR

PHE

ASP

SER

GLY

ASP

TYR

ASN

8

MET

ALA

LYS

ALA

LYS

MET

LYS

ASN

LYS

GLN

9

LEU

PRO

THR

ALA

PRO

ASP

LYS

THR

GLU

10

VAL

THR

GLY

ASP

HIS

ILE

PRO

THR

PRO

GLN

11

ASP

LEU

PRO

GLN

ARG

LYS

PRO

SER

LEU

VAL

12

ALA

SER

LYS

LEU

ALA

GLY

Samples:

sample_1: ARPP-19, [U-98% 15N], 0.7 mM; NaH2PO4 50 mM

sample_2: ARPP-19, [U-98% 13C; U-98% 15N], 0.7 mM; KCl 100 mM

sample_conditions_1: ionic strength: 150 mM; pH: 6.5; pressure: 1 atm; temperature: 298 K

Experiments:

Name	Sample	Sample state	Sample conditions
2D 1H-15N HSQC	sample_1	isotropic	sample_conditions_1
3D HNCACB	sample_2	isotropic	sample_conditions_1
3D CBCA(CO)NH	sample_2	isotropic	sample_conditions_1
3D HNCO	sample_2	isotropic	sample_conditions_1
3D i(HCA)CO(CA)NH	sample_2	isotropic	sample_conditions_1
3D iHA(CA)NCO	sample_2	isotropic	sample_conditions_1
3D HA(CA)CON	sample_2	isotropic	sample_conditions_1
3D HA(CA)CON(CA)HA	sample_2	isotropic	sample_conditions_1

Software:

SPARKY v3.115, Goddard - chemical shift assignment, peak picking

NMR spectrometers:

Bruker Avance 800 MHz

UNP	P56211-1
AlphaFold	Q9UD70