BMRB Entry 50901

Click here to enlarge.

PDB ID:
Entry in NMR Restraints Grid
Validation report in NRG-CING
Chem Shift validation: AVS_full
BMRB Entry DOI: doi:10.13018/BMR50901
MolProbity Validation Chart

NMR-STAR file interactive viewer.
NMR-STAR v3 text file.
XML gzip file.
RDF gzip file.
All files associated with the entry

Title:
SH3-PRR2 peptide complex
Deposition date:
2021-04-19
Original release date:
2022-07-09
Authors:
Sokolik, Chana; Chill, Jordan
Citation:

Citation: Twafra, Shams; Sokolik, Chana; Sneh, Tal; Srikanth, Kolluru; Genna, Alessandro; Samson, Avraham; Dessau, Moshe; Chill, Jordan; Gil-Henn, Hava. "Molecular and cellular aspects of cortactin inhibition by a Pyk2-derived peptide"  Mol. Cell ., .-..

Assembly members:

Assembly members:
entity_1, polymer, 57 residues, Formula weight is not available
entity_2, polymer, 19 residues, Formula weight is not available

Natural source:

Natural source:   Common Name: Mouse   Taxonomy ID: 10090   Superkingdom: Eukaryota   Kingdom: Metazoa   Genus/species: Mus musculus

Experimental source:

Experimental source:   Production method: recombinant technology   Host organism: Escherichia coli   Vector: pET28a+

Entity Sequences (FASTA):

Entity Sequences (FASTA):
entity_1: GITAIALYDYQAAGDDEISF DPDDIITNIEMIDDGWWRGV CKGRYGLFPANYVELRQ
entity_2: TAFQEPPPKPSRPKYRPPP

Data sets:
Data typeCount
13C chemical shifts133
15N chemical shifts60
1H chemical shifts467

Additional metadata:

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

Assembly:

Entity Assembly IDEntity NameEntity ID
1SH31
2PRR22

Entities:

Entity 1, SH3 57 residues - Formula weight is not available

1   GLYILETHRALAILEALALEUTYRASPTYR
2   GLNALAALAGLYASPASPGLUILESERPHE
3   ASPPROASPASPILEILETHRASNILEGLU
4   METILEASPASPGLYTRPTRPARGGLYVAL
5   CYSLYSGLYARGTYRGLYLEUPHEPROALA
6   ASNTYRVALGLULEUARGGLN

Entity 2, PRR2 19 residues - Formula weight is not available

1   THRALAPHEGLNGLUPROPROPROLYSPRO
2   SERARGPROLYSTYRARGPROPROPRO

Samples:

sample_1: Cortactin SH3 domain 0.75 ± 0.02 mM; Pyk2 PRR2 peptide 0.75 ± 0.02 mM; D2O 5 ± 0.1 %; NaPi pH 6.5 30 ± 0.06 mM; NaN3 0.02 ± 0.002 %

sample_2: Cortactin SH3 domain 0.75 ± 0.02 mM; Pyk2 PRR2 peptide 0.75 ± 0.02 mM; D2O 100 ± 0.1 %; NaPi pH 6.5 30 ± 0.06 mM; NaN3 0.02 ± 0.002 %

sample_3: Cortactin SH3 domain, [U-98% 13C; U-98% 15N], 0.45 ± 0.02 mM; Pyk2 PRR2 peptide 0.45 ± 0.02 mM; NaPi pH 6.5 30 ± 0.06 mM; NaN3 0.02 ± 0.002 %

sample_4: Cortactin SH3 domain, [U-98% 13C; U-98% 15N], 0.45 ± 0.02 mM; Pyk2 PRR2 peptide 0.45 ± 0.02 mM; NaPi pH 6.5 30 ± 0.06 mM; NaN3 0.02 ± 0.002 %

sample_5: Cortactin SH3 domain, [U-98% 2H; U-98% 15N], 0.45 ± 0.02 mM; Pyk2 PRR2 peptide 0.45 ± 0.02 mM; NaPi pH 6.5 30 ± 0.06 mM; NaN3 0.02 ± 0.002 %

sample_6: Pyk2 PRR2 peptide 0.45 ± 0.02 mM; NaPi pH 6.5 30 ± 0.06 mM; NaN3 0.02 ± 0.002 %

sample_conditions_1: ionic strength: 96 mM; pH: 6.5; pressure: 1 atm; temperature: 296 K

Experiments:

NameSampleSample stateSample conditions
2D 1H-15N HSQCsample_4isotropicsample_conditions_1
2D 1H-1H TOCSYsample_1isotropicsample_conditions_1
2D 1H-1H TOCSYsample_2isotropicsample_conditions_1
2D 1H-1H COSYsample_2isotropicsample_conditions_1
2D 1H-1H NOESYsample_1isotropicsample_conditions_1
2D 1H-1H NOESYsample_2isotropicsample_conditions_1
3D HNCACBsample_4isotropicsample_conditions_1
3D 15N-separated NOESYsample_6isotropicsample_conditions_1
2D 1H-1H NOESYsample_6isotropicsample_conditions_1
3D 1H-13C NOESY aliphaticsample_5isotropicsample_conditions_1
3D 1H-13C NOESY aromaticsample_5isotropicsample_conditions_1
2D 1H-1H TOCSYsample_6isotropicsample_conditions_1
2D 1H-1H NOESYsample_6isotropicsample_conditions_1

Software:

TOPSPIN v3.6.1 - chemical shift assignment, collection, data analysis, peak picking, processing

NMR spectrometers:

  • Bruker DRX 700 MHz

Related Database Links:

UniProt Q8BNA5 Q14289
AlphaFold Q8BNA5 Q6PID4

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