BMRB Entry 25304

Title:
obscurin Ig1 bound to titin M10
Deposition date:
2014-10-29
Original release date:
2015-08-25
Authors:
Wright, Nathan; Rudloff, Michael; Woosley, Alec
Citation:

Citation: Rudloff, Michael; Woosley, Alec; Wright, Nathan. "Biophysical characterization of naturally occurring titin M10 mutations"  Protein Sci. 24, 946-955 (2015).
PubMed: 25739468

Assembly members:

Assembly members:
Ig1_bound_to_M10, 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: pET24a

Data sets:
Data typeCount
15N chemical shifts76
1H chemical shifts76

Additional metadata:

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

Assembly:

Entity Assembly IDEntity NameEntity ID
1Ig11

Entities:

Entity 1, Ig1 112 residues - Formula weight is not available

1   METASPGLNPROGLNPHESERGLYALAPRO
2   ARGPHELEUTHRARGPROLYSALAPHEVAL
3   VALSERVALGLYLYSASPALATHRLEUSER
4   CYSGLNILEVALGLYASNPROTHRPROGLN
5   VALSERTRPGLULYSASPGLNGLNPROVAL
6   THRALAGLYALAARGPHEARGLEUALAGLN
7   ASPGLYASPLEUTYRARGLEUTHRILELEU
8   ASPLEUALALEUGLYASPSERGLYGLNTYR
9   VALCYSARGALAARGASNALAILEGLYGLU
10   ALAPHEALAALAVALGLYLEUGLNVALASP
11   ALAGLUALAALALEUGLUHISHISHISHIS
12   HISHIS

Samples:

sample_1: Ig1 bound to M10, [U-99% 13C; U-99% 15N], 0.5 – 2.5 mM; TRIS 20 mM; NaCl 20 mM; NaN3 0.35 mM; H2O 90%; D2O 10%

sample_conditions_1: ionic strength: .02 M; pH: 7.5; pressure: 1 atm; temperature: 298 K

Experiments:

NameSampleSample stateSample conditions
2D 1H-15N HSQCsample_1isotropicsample_conditions_1
3D HNCOsample_1isotropicsample_conditions_1
3D HNCACBsample_1isotropicsample_conditions_1
3D CBCA(CO)NHsample_1isotropicsample_conditions_1
3D HCACOsample_1isotropicsample_conditions_1

Software:

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

NMR spectrometers:

  • Bruker Avance 600 MHz

Related Database Links:

BMRB 25301
PDB

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