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 27911

Title: 1H, 13C and 15N NMR chemical shift assignments of cAMP-regulated phosphoprotein-19 and -16 (ARPP19 and ARPP16)   PubMed: 32468417

Deposition date: 2019-05-15 Original release date: 2020-09-28

Authors: Thapa, Chandan; Pentikainen, Ulla; Permi, Perttu

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).

Assembly members:
ARPP-16, polymer, 97 residues, 10722.26 Da.

Natural source:   Common Name: Human   Taxonomy ID: 9606   Superkingdom: Eukaryota   Kingdom: Metazoa   Genus/species: Homo sapiens

Experimental source:   Production method: recombinant technology   Host organism: Escherichia coli   Vector: pGTvL1-SGC

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

Data sets:
Data typeCount
13C chemical shifts279
15N chemical shifts96
1H chemical shifts185

Additional metadata:

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

Entity Assembly IDEntity NameEntity ID
1ARPP-161

Entities:

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

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

1   SERMETGLUASPLYSVALTHRSERPROGLU
2   LYSALAGLUGLUALALYSLEULYSALAARG
3   TYRPROHISLEUGLYGLNLYSPROGLYGLY
4   SERASPPHELEUARGLYSARGLEUGLNLYS
5   GLYGLNLYSTYRPHEASPSERGLYASPTYR
6   ASNMETALALYSALALYSMETLYSASNLYS
7   GLNLEUPROTHRALAALAPROASPLYSTHR
8   GLUVALTHRGLYASPHISILEPROTHRPRO
9   GLNASPLEUPROGLNARGLYSPROSERLEU
10   VALALASERLYSLEUALAGLY

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:

NameSampleSample stateSample conditions
2D 1H-15N HSQCsample_1isotropicsample_conditions_1
3D HNCACBsample_2isotropicsample_conditions_1
3D CBCA(CO)NHsample_2isotropicsample_conditions_1
3D HNCOsample_2isotropicsample_conditions_1
3D i(HCA)CO(CA)NHsample_2isotropicsample_conditions_1
3D iHA(CA)NCOsample_2isotropicsample_conditions_1
3D HA(CA)CONsample_2isotropicsample_conditions_1
3D HA(CA)CON(CA)HAsample_2isotropicsample_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 shifts
SPARKY: Backbone or all simulated shifts