BMRB Entry 27911

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/BMR27911

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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 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-16, polymer, 97 residues, 10722.26 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: pGTvL1-SGC

Entity Sequences (FASTA):

Entity Sequences (FASTA):
ARPP-16: SMEDKVTSPEKAEEAKLKAR YPHLGQKPGGSDFLRKRLQK GQKYFDSGDYNMAKAKMKNK QLPTAAPDKTEVTGDHIPTP QDLPQRKPSLVASKLAG

Data sets:

assigned_chemical_shifts
- assigned_chem_shift_list_1

Data type	Count
13C chemical shifts	279
15N chemical shifts	96
1H chemical shifts	185

Additional metadata:

Assembly
Samples and Experiments
Software
Spectrometers
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Assembly:

Entity Assembly ID	Entity Name	Entity ID
1	ARPP-16	1

Entities:

Entity 1, ARPP-16 97 residues - 10722.26 Da.

Residue 1 represent cloning artifact. Residue remained after TEV protease cleavage

1

SER

MET

GLU

ASP

LYS

VAL

THR

SER

PRO

GLU

2

LYS

ALA

GLU

ALA

LYS

LEU

LYS

ALA

ARG

3

TYR

PRO

HIS

LEU

GLY

GLN

LYS

PRO

GLY

4

SER

ASP

PHE

LEU

ARG

LYS

ARG

LEU

GLN

LYS

5

GLY

GLN

LYS

TYR

PHE

ASP

SER

GLY

ASP

TYR

6

ASN

MET

ALA

LYS

ALA

LYS

MET

LYS

ASN

LYS

7

GLN

LEU

PRO

THR

ALA

PRO

ASP

LYS

THR

8

GLU

VAL

THR

GLY

ASP

HIS

ILE

PRO

THR

PRO

9

GLN

ASP

LEU

PRO

GLN

ARG

LYS

PRO

SER

LEU

10

VAL

ALA

SER

LYS

LEU

ALA

GLY

Samples:

sample_1: ARPP-16, [U-98% 15N], 0.4 mM; NaH2PO4 50 mM

sample_2: ARPP-16, [U-98% 13C; U-98% 15N], 0.4 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

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