BMRB Entry 30471

Title:
Human Titin ZIg10
Deposition date:
2018-05-31
Original release date:
2019-08-16
Authors:
Wright, N.
Citation:

Citation: Letourneau, A.; Wright, N.. "Structural Insights on the Obscurin-Binding Domains in Titin"  Protein Pept. Lett. 25, 973-979 (2018).
PubMed: 30289063

Assembly members:

Assembly members:
Titin, polymer, 119 residues, 13965.898 Da.

Natural source:

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

Experimental source:

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

Data sets:
Data typeCount
13C chemical shifts299
15N chemical shifts94
1H chemical shifts623

Additional metadata:

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

Assembly:

Entity Assembly IDEntity NameEntity ID
1entity_11

Entities:

Entity 1, entity_1 119 residues - 13965.898 Da.

1   ARGMETALAHISGLUGLYALALEUTHRGLY
2   VALTHRTHRASPGLNLYSGLULYSGLNLYS
3   PROASPILEVALLEUTYRPROGLUPROVAL
4   ARGVALLEUGLUGLYGLUTHRALAARGPHE
5   ARGCYSARGVALTHRGLYTYRPROGLNPRO
6   LYSVALASNTRPTYRLEUASNGLYGLNLEU
7   ILEARGLYSSERLYSARGPHEARGVALARG
8   TYRASPGLYILEHISTYRLEUASPILEVAL
9   ASPCYSLYSSERTYRASPTHRGLYGLUVAL
10   LYSVALTHRALAGLUASNPROGLUGLYVAL
11   ILEGLUHISLYSVALLYSLEUGLUILEGLN
12   GLNLEUGLUHISHISHISHISHISHIS

Samples:

sample_1: TRIS 20 mM; sodium chloride 50 mM; Human Titin ZIg10, [U-99% 13C; U-99% 15N], 1 mM

sample_conditions_1: ionic strength: 50 mM; pH: 7.5; 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 HNCACBsample_1isotropicsample_conditions_1
3D C(CO)NHsample_1isotropicsample_conditions_1
3D H(CCO)NHsample_1isotropicsample_conditions_1
3D HN(CA)COsample_1isotropicsample_conditions_1
3D HNCOsample_1isotropicsample_conditions_1
3D 1H-15N TOCSYsample_1isotropicsample_conditions_1
3D 1H-15N NOESYsample_1isotropicsample_conditions_1
3D 1H-13C NOESYsample_1isotropicsample_conditions_1

Software:

X-PLOR NIH, Schwieters, Kuszewski, Tjandra and Clore - structure calculation

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

SPARKY, Goddard - chemical shift assignment, peak picking

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