BMRB Entry 27994

Name: chemical shift assignments for RCAN1 residues 89-197
Published: 2020-07-09

Chem Shift validation: AVS_full
BMRB Entry DOI: doi:10.13018/BMR27994

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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:

chemical shift assignments for RCAN1 residues 89-197

Deposition date:

2019-08-09

Original release date:

2020-07-09

Authors:

Peti, Wolfgang; Li, Yang; Page, Rebecca; Grigoriu, Simina; Peti, Wolfgang

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_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):

Entity Sequences (FASTA):
RCAN1_residues_89-197: GHMLHIGSSHLAPPNPDKQF LISPPASPPVGWKQVEDATP VINYDLLYAISKLGPGEKYE LHAATDTTPSVVVHVCESDQ EKEEEEEMERMRRPKPKIIQ TRRPEYTPIHLS

Data sets:

assigned_chemical_shifts
- assigned_chem_shift_list_1

Data type	Count
13C chemical shifts	172
15N chemical shifts	89
1H chemical shifts	89

Additional metadata:

Assembly
Samples and Experiments
Software
Spectrometers
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Assembly:

Entity Assembly ID	Entity Name	Entity ID
1	RCAN1	1

Entities:

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

GHM are cloning artifact; RCAN1 sequence starts with LHIG

1

GLY

HIS

MET

LEU

HIS

ILE

GLY

SER

HIS

2

LEU

ALA

PRO

ASN

PRO

ASP

LYS

GLN

PHE

3

LEU

ILE

SER

PRO

ALA

SER

PRO

VAL

4

GLY

TRP

LYS

GLN

VAL

GLU

ASP

ALA

THR

PRO

5

VAL

ILE

ASN

TYR

ASP

LEU

TYR

ALA

ILE

6

SER

LYS

LEU

GLY

PRO

GLY

GLU

LYS

TYR

GLU

7

LEU

HIS

ALA

THR

ASP

THR

PRO

SER

8

VAL

HIS

VAL

CYS

GLU

SER

ASP

GLN

9

GLU

LYS

GLU

MET

GLU

ARG

10

MET

ARG

PRO

LYS

PRO

LYS

ILE

GLN

11

THR

ARG

PRO

GLU

TYR

THR

PRO

ILE

HIS

12

LEU

SER

Samples:

sample_1: RCAN1 residues 89-197, [U-99% 13C; U-99% 15N], 0.2 mM; sodium phosphate 20 mM; sodium chloride 50 mM; TCEP 0.5 mM

sample_conditions_1: ionic strength: 50 mM; pH: 6.2; 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_1	isotropic	sample_conditions_1
3D HNCA	sample_1	isotropic	sample_conditions_1

Software:

CARA, Keller and Wuthrich - chemical shift assignment

TOPSPIN, Bruker Biospin - collection, processing

NMR spectrometers:

Bruker Avance 850 MHz

UNP	P53805-2
AlphaFold	Q9UME4