BMRB

Biological Magnetic Resonance Data Bank


A Repository for Data from NMR Spectroscopy on Proteins, Peptides, Nucleic Acids, and other Biomolecules
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BMRB Entry 50114

Title: Resonance assignment of human STIM1 CC1 fragment

Deposition date: 2019-12-04 Original release date: 2020-08-31

Authors: Rathner, Petr; Cerofolini, Linda; Ravera, Enrico; Luchinat, Claudio; Romanin, Christoph; Mueller, Norbert

Citation: Rathner, Petr; Cerofolini, Linda; Ravera, Enrico; Luchinat, Claudio; Romanin, Christoph; Mueller, Norbert; Fahrner, Marc; Grabmayr, Herwig; Horvath, Ferdinand; Krobath, Heinrich; Fragai, Marco; Renger, Thomas. "Coiled-coil interactions within the STIM1 CC1 subdomain modulate CRAC channel activation"  Nat. Commun. ., .-..

Assembly members:
entity_1, polymer, 115 residues, Formula weight is not available

Natural source:   Common Name: Human   Taxonomy ID: 9606   Superkingdom: Eukaryota   Kingdom: Metazoa   Genus/species: Homo sapiens

Experimental source:   Production method: recombinant technology   Host organism: Escherichia coli

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

Data sets:
Data typeCount
13C chemical shifts340
15N chemical shifts94
1H chemical shifts524

Additional metadata:

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

Assembly:

Entity Assembly IDEntity NameEntity ID
1STIM1 CC1 wild-type1

Entities:

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

1   GLYSERPROGLUPHEASNARGTYRSERLYS
2   GLUHISMETLYSLYSMETMETLYSASPLEU
3   GLUGLYLEUHISARGALAGLUGLNSERLEU
4   HISASPLEUGLNGLUARGLEUHISLYSALA
5   GLNGLUGLUHISARGTHRVALGLUVALGLU
6   LYSVALHISLEUGLULYSLYSLEUARGASP
7   GLUILEASNLEUALALYSGLNGLUALAGLN
8   ARGLEULYSGLULEUARGGLUGLYTHRGLU
9   ASNGLUARGSERARGGLNLYSTYRALAGLU
10   GLUGLULEUGLUGLNVALARGGLUALALEU
11   ARGLYSALAGLULYSGLULEUGLUSERHIS
12   SERSERTRPTYRALA

Samples:

sample_1: TRIS 20 mM; SDS, [U-99% 2H], 7 mM; STIM1 CC1, [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: 310.15 K

Experiments:

NameSampleSample stateSample conditions
2D 1H-15N HSQCsample_1isotropicsample_conditions_1
2D 1H-13C HSQCsample_1isotropicsample_conditions_1
3D HNCOsample_1isotropicsample_conditions_1
3D HNCOsample_1isotropicsample_conditions_1
3D HNCAsample_1isotropicsample_conditions_1
3D HNCACBsample_1isotropicsample_conditions_1
3D HN(COCA)CBsample_1isotropicsample_conditions_1
3D 1H-15N TOCSYsample_1isotropicsample_conditions_1
3D 1H-15N NOESYsample_1isotropicsample_conditions_1
3D 1H-13C NOESY aliphaticsample_1isotropicsample_conditions_1
3D H(CCO)NHsample_1isotropicsample_conditions_1
3D C(CO)NHsample_1isotropicsample_conditions_1
CONsample_1isotropicsample_conditions_1
CBCACONsample_1isotropicsample_conditions_1
CANCOsample_1isotropicsample_conditions_1
CACOsample_1isotropicsample_conditions_1
CBCACOsample_1isotropicsample_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 MHz
  • Bruker Avance 900 MHz MHz
  • Bruker Avance 700 MHz MHz
  • Bruker Avance NEO 700 MHz MHz

Download simulated HSQC data in one of the following formats:
CSV: Backbone or all simulated shifts
SPARKY: Backbone or all simulated shifts