BMRB

Biological Magnetic Resonance Data Bank


A Repository for Data from NMR Spectroscopy on Proteins, Peptides, Nucleic Acids, and other Biomolecules
Member of WWPDB

BMRB Entry 34141

Title: p130Cas SH3 domain   PubMed: 28808245

Authors: Hexnerova, R.; Veverka, V.

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).

Assembly members:
entity_1, polymer, 81 residues, 9053.410 Da.

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: GSMKYLNVLAKALYDNVAES PDELSFRKGDIMTVLERDTQ GLDGWWLCSLHGRQGIVPGN RLKILVGMYDKKPAGEFIVT D

Data sets:
Data typeCount
13C chemical shifts336
15N chemical shifts80
1H chemical shifts549

Additional metadata:

  • Assembly
  • Samples and Experiments
  • Software
  • Spectrometers
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Assembly:

Entity Assembly IDEntity NameEntity ID
1entity_11

Entities:

Entity 1, entity_1 81 residues - 9053.410 Da.

1   GLYSERMETLYSTYRLEUASNVALLEUALA
2   LYSALALEUTYRASPASNVALALAGLUSER
3   PROASPGLULEUSERPHEARGLYSGLYASP
4   ILEMETTHRVALLEUGLUARGASPTHRGLN
5   GLYLEUASPGLYTRPTRPLEUCYSSERLEU
6   HISGLYARGGLNGLYILEVALPROGLYASN
7   ARGLEULYSILELEUVALGLYMETTYRASP
8   LYSLYSPROALAGLYGLUPHEILEVALTHR
9   ASP

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 AvanceII 600 MHz
  • Bruker Avance 850 MHz

Related Database Links: