BMRB Entry 26990

Title:
1H, 15N and 13C Chemical Shift Assignments of the Regulatory Domain of Human Calcineurin
Deposition date:
2017-01-05
Original release date:
2017-06-20
Authors:
Yadav, Dinesh; Tata, Sri Ramya; Hunt, John; Cook, Erik; Creamer, Trevor; Fitzkee, Nicholas
Citation:

Citation: Yadav, Dinesh; Tata, Sri Ramya; Hunt, John; Cook, Erik; Creamer, Trevor; Fitzkee, Nicholas. "1H, 15N, and 13C chemical shift assignments of the regulatory domain of human calcineurin"  Biomol. NMR Assign. 11, 215-219 (2017).
PubMed: 28803387

Assembly members:

Assembly members:
Regulatory_Domain_of_Calcineurin, polymer, 97 residues, 10359.8 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: pETRD

Entity Sequences (FASTA):

Data sets:
Data typeCount
13C chemical shifts376
15N chemical shifts95
1H chemical shifts285

Additional metadata:

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

Assembly:

Entity Assembly IDEntity NameEntity ID
1Regulatory domain of Calcineurin1

Entities:

Entity 1, Regulatory domain of Calcineurin 97 residues - 10359.8 Da.

A partially disordered region of Calcineurin with Calmodulin binding sequence. The first 3 residues at the N-terminus, and the last 13 residues at the C-terminus, are extraneous and correspond to additional sequence used in the cloning vector. Residues 4 to 89 correspond to residues 388-468 of Calcineurin chain A isoform alpha (NCBI Reference Sequence NP_000935).

1   METALAGLYTHRALAALAALAARGLYSGLU
2   VALILEARGASNLYSILEARGALAILEGLY
3   LYSMETALAARGVALPHESERVALLEUARG
4   GLUGLUSERGLUSERVALLEUTHRLEULYS
5   GLYLEUTHRPROTHRGLYMETLEUPROSER
6   GLYVALLEUSERGLYGLYLYSGLNTHRLEU
7   GLNSERALATHRVALGLUALAILEGLUALA
8   ASPGLUALAILELYSGLYPHESERPROGLN
9   HISLYSILETHRGLYTRPGLYGLYGLYLEU
10   GLUHISHISHISHISHISHIS

Samples:

sample_1: D2O, [U-100% 2H], 6%; Regulatory Domain of Calcineurin, [U-100% 13C; U-100% 15N], 0.2 mM; DTT 10 mM; sodium chloride 100 mM; PIPES Buffer 20 mM; H2O 94%

sample_2: D2O, [U-100% 2H], 6%; DTT 10 mM; sodium chloride 100 mM; PIPES Buffer 20 mM; Regulatory Domain of Calcineurin, [U-100% 13C; U-100% 15N], 250 mM; H2O 94%

sample_conditions_1: ionic strength: 0.1 M; pH: 5.5; pressure: 1 atm; temperature: 288 K

Experiments:

NameSampleSample stateSample conditions
2D 1H-15N HSQCsample_1isotropicsample_conditions_1
3D HNCOsample_1isotropicsample_conditions_1
3D HNCAsample_1isotropicsample_conditions_1
3D HNCACBsample_1isotropicsample_conditions_1
3D CBCA(CO)NHsample_1isotropicsample_conditions_1
3D HN(CO)CAsample_1isotropicsample_conditions_1
3D 1H-15N TOCSYsample_1isotropicsample_conditions_1
3D H(CCO)NHsample_1isotropicsample_conditions_1
3D (HACA)N(CA)CONsample_2isotropicsample_conditions_1
2D HACACONsample_2isotropicsample_conditions_1

Software:

NMRPipe, Delaglio, Grzesiek, Vuister, Zhu, Pfeifer and Bax - processing

SPARKY, Goddard - chemical shift assignment

TOPSPIN v3.1, Bruker Biospin - collection

NMR spectrometers:

  • Bruker Avance 600 MHz

Related Database Links:

PDB

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