BMRB Entry 50118

Name: Resonance assignment of human STIM1 CC1 R304W mutant
Published: 2020-09-05

Chem Shift validation: AVS_full
BMRB Entry DOI: doi:10.13018/BMR50118

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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:

Resonance assignment of human STIM1 CC1 R304W mutant

Deposition date:

2019-12-06

Original release date:

2020-09-05

Authors:

Rathner, Petr; Mueller, Norbert; Cerofolini, Linda; Ravera, Enrico; Luchinat, Claudio

Citation:

Citation: Rathner, Petr; Fahrner, Marc; Cerofolini, Linda; Grabmayr, Herwig; Horvath, Ferdinand; Krobath, Heinrich; Gupta, Agrim; Ravera, Enrico; Fragai, Marco; Bechmann, Matthias; Renger, Thomas; Luchinat, Claudio; Romanin, Christoph; Muller, Norbert. "Interhelical interactions within the STIM1 CC1 domain modulate CRAC channel activation" Nat. Chem. Biol. 17, 196-204 (2021).
PubMed: 33106661

Assembly members:

Assembly members:
entity_1, polymer, 115 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: pGEX 4T-1

Entity Sequences (FASTA):

Entity Sequences (FASTA):
entity_1: GSPEFNRYSKEHMKKMMKDL EGLHRAEQSLHDLQERLHKA QEEHRTVEVEKVHLEKKLRD EINLAKQEAQRLKELWEGTE NERSRQKYAEEELEQVREAL RKAEKELESHSSWYA

Data sets:

assigned_chemical_shifts
- assigned_chemical_shifts_1

Data type	Count
13C chemical shifts	295
15N chemical shifts	93
1H chemical shifts	369

Additional metadata:

Assembly
Samples and Experiments
Software
Spectrometers
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Assembly:

Entity Assembly ID	Entity Name	Entity ID
1	STIM1 CC1 R304W	1

Entities:

Entity 1, STIM1 CC1 R304W 115 residues - Formula weight is not available

1

GLY

SER

PRO

GLU

PHE

ASN

ARG

TYR

SER

LYS

2

GLU

HIS

MET

LYS

MET

LYS

ASP

LEU

3

GLU

GLY

LEU

HIS

ARG

ALA

GLU

GLN

SER

LEU

4

HIS

ASP

LEU

GLN

GLU

ARG

LEU

HIS

LYS

ALA

5

GLN

GLU

HIS

ARG

THR

VAL

GLU

VAL

GLU

6

LYS

VAL

HIS

LEU

GLU

LYS

LEU

ARG

ASP

7

GLU

ILE

ASN

LEU

ALA

LYS

GLN

GLU

ALA

GLN

8

ARG

LEU

LYS

GLU

LEU

TRP

GLU

GLY

THR

GLU

9

ASN

GLU

ARG

SER

ARG

GLN

LYS

TYR

ALA

GLU

10

GLU

LEU

GLU

GLN

VAL

ARG

GLU

ALA

LEU

11

ARG

LYS

ALA

GLU

LYS

GLU

LEU

GLU

SER

HIS

12

SER

TRP

TYR

ALA

Samples:

sample_1: TRIS 20 mM; SDS, [U-99% 2H], 7 mM; STIM1 CC1 R304W, [U-95% 13C; U-95% 15N], 0.3 mM; H2O, [U-99% 2H], 10 % w/v; H2O 90 % w/v

sample_conditions_1: ionic strength: 0.02 M; pH: 7.25; pressure: 1 atm; temperature: 310 K

Experiments:

Name	Sample	Sample state	Sample conditions
2D 1H-15N HSQC	sample_1	isotropic	sample_conditions_1
2D 1H-13C HSQC	sample_1	isotropic	sample_conditions_1
3D HNCO	sample_1	isotropic	sample_conditions_1
3D HNCA	sample_1	isotropic	sample_conditions_1
3D HNCACB	sample_1	isotropic	sample_conditions_1
3D HBHA(CO)NH	sample_1	isotropic	sample_conditions_1
3D HCCH-TOCSY	sample_1	isotropic	sample_conditions_1
CON	sample_1	isotropic	sample_conditions_1
3D 1H-15N NOESY	sample_1	isotropic	sample_conditions_1
3D 1H-13C NOESY	sample_1	isotropic	sample_conditions_1

Software:

CARA v1.8.4.2, Keller and Wuthrich - chemical shift assignment

TOPSPIN v3.5, 3.6, Bruker Biospin - collection

NMR spectrometers:

Bruker Avance 950 MHz
Bruker Avance 900 MHz
Bruker Avance III 700 MHz
Bruker Avance NEO 700 MHz

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