BMRB Entry 34143

Title:
p130Cas SH3 domain Vinculin peptide chimera
Deposition date:
2017-05-22
Original release date:
2017-09-14
Authors:
Hexnerova, R.; Veverka, V.
Citation:

Citation: Gemperle, J.; Hexnerova, R.; Lepsik, M.; Tesina, P.; Dibus, M.; Novotny, M.; Brabek, J.; Veverka, V.; Rosel, D.. "Structural characterization of CAS SH3 domain selectivity and regulation reveals new CAS interaction partners."  Sci. Rep. 7, 8057-8057 (2017).
PubMed: 28808245

Assembly members:

Assembly members:
entity_1, polymer, 99 residues, 10623.104 Da.

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

Data sets:
Data typeCount
13C chemical shifts395
15N chemical shifts86
1H chemical shifts648

Additional metadata:

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

Assembly:

Entity Assembly IDEntity NameEntity ID
1entity_11

Entities:

Entity 1, entity_1 99 residues - 10623.104 Da.

1   GLYSERMETLYSTYRLEUASNVALLEUALA
2   LYSALALEUTYRASPASNVALALAGLUSER
3   PROASPGLULEUSERPHEARGLYSGLYASP
4   ILEMETTHRVALLEUGLUARGASPTHRGLN
5   GLYLEUASPGLYTRPTRPLEUCYSSERLEU
6   HISGLYARGGLNGLYILEVALPROGLYASN
7   ARGLEULYSILELEUVALGLYMETTYRASP
8   LYSLYSPROALAGLYSERGLYGLYSERGLY
9   SERGLYLEUTHRASPGLULEUALAPROPRO
10   LYSPROPROLEUPROGLUGLYGLUVAL

Samples:

sample_1: entity_1, [U-13C; U-15N], 0.45 mM; TCEP 1 M; sodium phosphate 25 mM

sample_conditions_1: ionic strength: 100 mM; pH: 7.5; pressure: 1 atm; temperature: 298 K

Experiments:

NameSampleSample stateSample conditions
2D 1H-15N HSQCsample_1isotropicsample_conditions_1
3D HNCACBsample_1isotropicsample_conditions_1
3D CBCA(CO)NHsample_1isotropicsample_conditions_1
3D 1H-15N NOESYsample_1isotropicsample_conditions_1
3D 1H-13C NOESYsample_1isotropicsample_conditions_1

Software:

CYANA, Guntert, Mumenthaler and Wuthrich - structure calculation

SPARKY, Goddard - chemical shift assignment

TOPSPIN, Bruker Biospin - collection, processing

YASARA, Krieger - refinement

NMR spectrometers:

  • Bruker AvanceIII 600 MHz
  • Bruker AvanceIII 850 MHz

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