BMRB Entry 51799

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PDB ID:
Entry in NMR Restraints Grid
Validation report in NRG-CING
Chem Shift validation: AVS_full
BMRB Entry DOI: doi:10.13018/BMR51799
MolProbity Validation Chart

NMR-STAR file interactive viewer.
NMR-STAR v3 text file.
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Title:
Complex of Wasp-interacting Protein (WIP) and the SH3 domain of cortactin
Deposition date:
2023-01-23
Original release date:
2025-02-10
Authors:
Sokolik, Chana; Chill, Jordan
Citation:

Citation: Sokolik, Chana; Chill, Jordan. "A triple-pose complex between an extended WIP motif and a C-terminal SH3 domain modulates cortactin activity"  J. Mol. Biol. ., .-. (2025).
PubMed: 39914658

Assembly members:

Assembly members:
entity_1, polymer, 57 residues, 6458.15 Da.
entity_2, polymer, 42 residues, 4489.05 Da.
entity_3, polymer, 19 residues, 2188.5 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   Vector: pET-28-a(+)

Entity Sequences (FASTA):

Entity Sequences (FASTA):
entity_1: GITAVALYDYQAAGDDEISF DPDDIITNIEMIDDGWWRGV CKGRYGLFPANYVELRQ
entity_2: GQRNRMPPPRPDVGSKPDSI PPPVPSTPRPIQSSPHNRGS PP
entity_3: QRNRMPPPRPDVGSKPDSI

Data sets:
Data typeCount
13C chemical shifts173
15N chemical shifts61
1H chemical shifts466

Additional metadata:

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

Entity Assembly IDEntity NameEntity ID
1Cort-SH31
2WIP(165-205)2
3WIP(165-183)3

Entities:

Entity 1, Cort-SH3 57 residues - 6458.15 Da.

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

Entity 2, WIP(165-205) 42 residues - 4489.05 Da.

1   GLYGLNARGASNARGMETPROPROPROARG
2   PROASPVALGLYSERLYSPROASPSERILE
3   PROPROPROVALPROSERTHRPROARGPRO
4   ILEGLNSERSERPROHISASNARGGLYSER
5   PROPRO

Entity 3, WIP(165-183) 19 residues - 2188.5 Da.

1   GLNARGASNARGMETPROPROPROARGPRO
2   ASPVALGLYSERLYSPROASPSERILE

Samples:

sample_1: C-terminal SH3 domain of human cortactin, [U-99% 13C; U-99% 15N], 0.22 ± 0.01 mM; WIP165-205 1.1 ± 0.05 mM; KPi 20 mM; NaCl 20 mM; DTT 1 mM; NaN3 0.02%

sample_2: C-terminal SH3 domain of human cortactin, [U-99% 13C; U-99% 15N], 0.22 mM; WIP165-183 1.1 mM; KPi 20 mM; NaCl 20 mM; DTT 1 mM; NaN3 0.02%

sample_3: C-terminal SH3 domain of human cortactin, [U-99% 15N; U-95% 2H], 0.22 mM; WIP165-183 1.1 mM; KPi 20 mM; NaCl 20 mM; DTT 1 mM; NaN3 0.02%

sample_4: C-terminal SH3 domain of human cortactin, [U-99% 15N; ~95% D2O], 0.22 mM; WIP165-183 1.1 mM; KPi 20 mM; NaCl 20 mM; DTT 1 mM; NaN3 0.02%

sample_conditions_1: ionic strength: 0.195 M; pH: 6.6; pressure: 1 atm; temperature: 298 K

Experiments:

NameSampleSample stateSample conditions
2D 1H-15N HSQCsample_1isotropicsample_conditions_1
2D 1H-13C TROSYsample_3isotropicsample_conditions_1
3D H(CCO)NHsample_1isotropicsample_conditions_1
3D CC(CO)NHsample_1isotropicsample_conditions_1
2D 1H-1H TOCSYsample_2isotropicsample_conditions_1
2D 1H-1H NOESYsample_2isotropicsample_conditions_1
2D 1H-1H TOCSYsample_4isotropicsample_conditions_1
2D 1H-1H NOESYsample_4isotropicsample_conditions_1
2D 1H-1H COSYsample_4isotropicsample_conditions_1

Software:

TOPSPIN v3.6.4 - peak picking, processing

NMR spectrometers:

  • Bruker DRX 700 MHz

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