BMRB Entry 30437

Title:
Solution structure of SH3 domain from Shank2
Deposition date:
2018-03-13
Original release date:
2018-08-07
Authors:
Ishida, H.; Vogel, H.
Citation:

Citation: Ishida, Hiroaki; Skorobogatov, Anton; Yamniuk, Aaron; Vogel, Hans. "Solution structures of the SH3 domains from Shank scaffold proteins and their interactions with Cav1.3 calcium channels"  FEBS Lett. 592, 2786-2797 (2018).
PubMed: 30058071

Assembly members:

Assembly members:
entity_1, polymer, 61 residues, 6741.667 Da.

Natural source:

Natural source:   Common Name: Rat   Taxonomy ID: 10116   Superkingdom: Eukaryota   Kingdom: Metazoa   Genus/species: Rattus norvegicus

Experimental source:

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

Entity Sequences (FASTA):

Data sets:
Data typeCount
13C chemical shifts173
15N chemical shifts55
1H chemical shifts55

Additional metadata:

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

Assembly:

Entity Assembly IDEntity NameEntity ID
1entity_11

Entities:

Entity 1, entity_1 61 residues - 6741.667 Da.

1   METVALPROGLYARGLEUPHEVALALAILE
2   LYSPROTYRGLNPROGLNVALASPGLYGLU
3   ILEPROLEUHISARGGLYASPARGVALLYS
4   VALLEUSERILEGLYGLUGLYGLYPHETRP
5   GLUGLYSERALAARGGLYHISILEGLYTRP
6   PHEPROALAGLUCYSVALGLUGLUVALGLN
7   SER

Samples:

sample_1: Shank2 SH3, [U-99% 13C; U-99% 15N], 1 mM; Bis-Tris 20 mM; KCl 100 mM

sample_2: Shank2 SH3, [U-99% 13C; U-99% 15N], 1 mM; Bis-Tris 20 mM; KCl 100 mM

sample_3: Shank2 SH3, [U-99% 13C; U-99% 15N], 1 mM; Bis-Tris 20 mM; KCl 100 mM

sample_4: Shank2 SH3 1 mM; Bis-Tris 20 mM; KCl 100 mM

sample_conditions_1: ionic strength: 100 mM; pH: 6.8; pressure: 1 atm; temperature: 298 K

Experiments:

NameSampleSample stateSample conditions
2D 1H-15N HSQCsample_3isotropicsample_conditions_1
3D CBCA(CO)NHsample_1isotropicsample_conditions_1
3D HNCACBsample_1isotropicsample_conditions_1
3D HNCOsample_1isotropicsample_conditions_1
3D HN(CA)COsample_1isotropicsample_conditions_1
3D H(CCO)NHsample_1isotropicsample_conditions_1
3D C(CO)NHsample_1isotropicsample_conditions_1
3D HBHA(CO)NHsample_1isotropicsample_conditions_1
3D 1H-13C NOESYsample_2isotropicsample_conditions_1
2D NOESYsample_4isotropicsample_conditions_1
3D 1H-15N NOESYsample_3isotropicsample_conditions_1

Software:

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

NMRView, Johnson, One Moon Scientific - data analysis

CYANA v2.0, Guntert, Mumenthaler and Wuthrich - structure calculation

NMR spectrometers:

  • Bruker Avance 500 MHz

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