BMRB Entry 27801

Chem Shift validation: AVS_full
BMRB Entry DOI: doi:10.13018/BMR27801

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Title:
Backbone 1H, 13C, and 15N chemical shift assignments for RCAN1 residues 128-164
Deposition date:
2019-02-25
Original release date:
2020-07-09
Authors:
Peti, Wolfgang; Page, Rebecca; Li, Yang; Sheftic, Sarah; Grigoriu, Simina
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:
RCAN1_residues_128-164, polymer, 40 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: THMT

Entity Sequences (FASTA):

Entity Sequences (FASTA):
RCAN1_residues_128-164: GHMNYDLLYAISKLGPGEKY ELHAATDTTPSVVITVCESD

Data sets:
Data typeCount
13C chemical shifts65
15N chemical shifts34
1H chemical shifts34

Additional metadata:

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

Assembly:

Entity Assembly IDEntity NameEntity ID
1RCAN1 residues 128-1641

Entities:

Entity 1, RCAN1 residues 128-164 40 residues - Formula weight is not available

GHM are cloning artefact; RCAN1 sequence starts with NYDL

1   GLYHISMETASNTYRASPLEULEUTYRALA
2   ILESERLYSLEUGLYPROGLYGLULYSTYR
3   GLULEUHISALAALATHRASPTHRTHRPRO
4   SERVALVALILETHRVALCYSGLUSERASP

Samples:

sample_1: RCAN1 residues 128-164, [U-99% 15N], 0.6 mM; sodium phosphate 20 mM; sodium chloride 50 mM; TCEP 0.5 mM

sample_2: RCAN1 residues 128-164, [U-99% 13C; U-99% 15N], 0.6 mM; sodium phosphate 20 mM; sodium chloride 50 mM; TCEP 0.5 mM

sample_conditions_1: ionic strength: 50 mM; pH: 6.8; pressure: 1 atm; temperature: 298 K

Experiments:

NameSampleSample stateSample conditions
2D 1H-15N HSQCsample_1isotropicsample_conditions_1
3D HNCAsample_2isotropicsample_conditions_1
3D HN(CO)CAsample_2isotropicsample_conditions_1
3D HNCACBsample_2isotropicsample_conditions_1
3D CBCA(CO)NHsample_2isotropicsample_conditions_1

Software:

TOPSPIN, Bruker Biospin - collection, processing

XEASY, 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