BMRB Entry 27995

Title:
chemical shift assignments for phosphorylated RCAN1 residues 89-197
Deposition date:
2019-08-09
Original release date:
2020-07-09
Authors:
Peti, Wolfgang; Li, Yang; Page, Rebecca
Citation:

Citation: Li, Yang; Sheftic, Sarah; Grigoriu, Simina; Schwieters, Charles; Page, Rebecca; Peti, Wolfgang. "The structure of the RCAN1:CN complex explains the inhibition of and substrate recruitment by calcineurin"  Sci. Adv. 6, 3681-3681 (2020).
PubMed: 32936779

Assembly members:

Assembly members:
phosphorylated_RCAN1_89-197, polymer, 112 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: pTHMT

Entity Sequences (FASTA):

Data sets:
Data typeCount
13C chemical shifts170
15N chemical shifts87
1H chemical shifts87

Additional metadata:

  • Assembly
  • Samples and Experiments
  • Software
  • Spectrometers
  • Hide all

Assembly:

Entity Assembly IDEntity NameEntity ID
1RCAN11

Entities:

Entity 1, RCAN1 112 residues - Formula weight is not available

GHM are cloning artifact; RCAN1 sequence starts with LHIG; residues S108, S112, T124, T152, T153 and T192 are phosphorylated.

1   GLYHISMETLEUHISILEGLYSERSERHIS
2   LEUALAPROPROASNPROASPLYSGLNPHE
3   LEUILESEPPROPROALASEPPROPROVAL
4   GLYTRPLYSGLNVALGLUASPALATPOPRO
5   VALILEASNTYRASPLEULEUTYRALAILE
6   SERLYSLEUGLYPROGLYGLULYSTYRGLU
7   LEUHISALAALATHRASPTPOTPOPROSER
8   VALVALILETHRVALCYSGLUSERASPGLN
9   GLULYSGLUGLUGLUGLUGLUMETGLUARG
10   METARGARGPROLYSPROLYSILEILEGLN
11   THRARGARGPROGLUTYRTPOPROILEHIS
12   LEUSER

Samples:

sample_1: phosphorylated RCAN1 89-197, [U-99% 13C; U-99% 15N], 0.4 mM; HEPES 20 mM; sodium chloride 50 mM; TCEP 0.5 mM

sample_conditions_1: ionic strength: 50 mM; pH: 6.8; pressure: 1 atm; temperature: 283 K

Experiments:

NameSampleSample stateSample conditions
2D 1H-15N HSQCsample_1isotropicsample_conditions_1
3D HNCACBsample_1isotropicsample_conditions_1
3D HNCAsample_1isotropicsample_conditions_1
3D HN(CO)CAsample_1isotropicsample_conditions_1
3D CBCA(CO)NHsample_1isotropicsample_conditions_1

Software:

TOPSPIN, Bruker Biospin - collection, processing

CARA, Keller and Wuthrich - chemical shift assignment

NMR spectrometers:

  • Bruker Avance 600 MHz

Related Database Links:

UNP P53805-2
AlphaFold Q9UME4

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