BMRB Entry 25481

Title:
Backbone 1H, 13C and 15N chemical shift assignment for perforin C2 quad mutant
Deposition date:
2015-02-09
Original release date:
2016-11-02
Authors:
Yagi, Hiromasa; Conroy, Paul; Leung, Eleanor; Law, Ruby; Whisstock, James; Norton, Raymond
Citation:

Citation: Yagi, Hiromasa; Conroy, Paul; Leung, Eleanor; Law, Ruby; Whisstock, James; Norton, Raymond. "Structural Basis for Ca2+-mediated Interaction of the Perforin C2 Domain with Lipid Membranes"  J. Biol. Chem. 290, 25213-25226 (2015).
PubMed: 26306037

Assembly members:

Assembly members:
perforin_C2_domain, polymer, 125 residues, Formula weight is not available

Natural source:

Natural source:   Common Name: house mouse   Taxonomy ID: 10090   Superkingdom: Eukaryota   Kingdom: Metazoa   Genus/species: Mus musculus

Experimental source:

Experimental source:   Production method: recombinant technology   Host organism: Escherichia coli   Vector: pComb3X

Data sets:
Data typeCount
13C chemical shifts211
15N chemical shifts108
1H chemical shifts108

Additional metadata:

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

Assembly:

Entity Assembly IDEntity NameEntity ID
1perforin C2 quad mutant1

Entities:

Entity 1, perforin C2 quad mutant 125 residues - Formula weight is not available

An extra Alanine is remained at N-terminal as a result of cleavage of the signal sequence. Gly + His6 tag are attached at C-terminal.

1   ALAGLNARGGLYLEUALAHISLEUVALVAL
2   SERASNPHEARGALAGLUHISLEUALAGLY
3   ASPALATHRTHRALATHRASPALATYRLEU
4   LYSVALPHEPHEGLYGLYGLNGLUPHEARG
5   THRGLYVALVALTRPASNASNASNASNPRO
6   ARGTRPTHRASPLYSMETASPPHEGLUASN
7   VALLEULEUSERTHRGLYGLYPROLEUARG
8   VALGLNVALTRPASPALAASPALAGLYALA
9   ASPASPASPLEULEUGLYSERCYSASPARG
10   SERPROHISSERGLYPHEHISGLUVALTHR
11   CYSGLULEUASNHISGLYARGVALLYSPHE
12   SERTYRHISALALYSSERLEUPROGLYHIS
13   HISHISHISHISHIS

Samples:

sample_1: perforin C2 domain, [U-99% 13C; U-99% 15N], 0.5 mM; HEPES 20 mM; sodium chloride 150 mM; D2O 10%; H2O 90%

sample_conditions_1: ionic strength: 150 mM; pH: 7.0; pressure: 1 atm; temperature: 298 K

Experiments:

NameSampleSample stateSample conditions
2D 1H-15N HSQCsample_1isotropicsample_conditions_1
3D CBCA(CO)NHsample_1isotropicsample_conditions_1
3D HNCAsample_1isotropicsample_conditions_1
3D HNCACBsample_1isotropicsample_conditions_1
3D HN(CO)CAsample_1isotropicsample_conditions_1

Software:

SPARKY v3.115, Goddard - chemical shift assignment, data analysis, peak picking

TOPSPIN v3.2, Bruker Biospin - collection, processing

NMR spectrometers:

  • Bruker Avance 600 MHz

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