BMRB Entry 35012

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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/BMR35012
MolProbity Validation Chart

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

Title:
Human WASP/WIP complex
Deposition date:
2025-08-06
Original release date:
2026-08-14
Authors:
Sasson, I.; Halle-Bikovski, A.; Chill, J.
Citation:

Citation: Sasson, I.; Baluom, S.; Halle-Bikovski, A.; Sher, I.; Chill, J.. "Structure of the human WASP-EVH1/WIP complex: Molecular basis of the WIP chaperone function "  .

Assembly members:

Assembly members:
entity_1, polymer, 141 residues, 16167.181 Da.
entity_2, polymer, 53 residues, 6167.616 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

Entity Sequences (FASTA):

Entity Sequences (FASTA):
entity_1: SGQNIPSTLLQDHENQRLFE MLGRKCLTLATAVVQLYLAL PPGAEHWTKEHCGAVCFVKD NPQKSYFIRLYGLQAGRLLW EQELYSQLVYSTPTPFFHTF AGDDCQAGLNFADEDEAQAF RALVQEKIQKRNQRQSGDRR Q
entity_2: SGQDSPCEDEWESRFYFHPI SDLPPPEPYVQTTKSYPSKL ARNESRSGSNRRE

Data sets:
Data typeCount
13C chemical shifts771
15N chemical shifts175
1H chemical shifts1147

Additional metadata:

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

Entity Assembly IDEntity NameEntity ID
1unit_11
2unit_22

Entities:

Entity 1, unit_1 141 residues - 16167.181 Da.

1   SERGLYGLNASNILEPROSERTHRLEULEU
2   GLNASPHISGLUASNGLNARGLEUPHEGLU
3   METLEUGLYARGLYSCYSLEUTHRLEUALA
4   THRALAVALVALGLNLEUTYRLEUALALEU
5   PROPROGLYALAGLUHISTRPTHRLYSGLU
6   HISCYSGLYALAVALCYSPHEVALLYSASP
7   ASNPROGLNLYSSERTYRPHEILEARGLEU
8   TYRGLYLEUGLNALAGLYARGLEULEUTRP
9   GLUGLNGLULEUTYRSERGLNLEUVALTYR
10   SERTHRPROTHRPROPHEPHEHISTHRPHE
11   ALAGLYASPASPCYSGLNALAGLYLEUASN
12   PHEALAASPGLUASPGLUALAGLNALAPHE
13   ARGALALEUVALGLNGLULYSILEGLNLYS
14   ARGASNGLNARGGLNSERGLYASPARGARG
15   GLN

Entity 2, unit_2 53 residues - 6167.616 Da.

1   SERGLYGLNASPSERPROCYSGLUASPGLU
2   TRPGLUSERARGPHETYRPHEHISPROILE
3   SERASPLEUPROPROPROGLUPROTYRVAL
4   GLNTHRTHRLYSSERTYRPROSERLYSLEU
5   ALAARGASNGLUSERARGSERGLYSERASN
6   ARGARGGLU

Samples:

sample_1: WIP(442-492), [U-98% 13C; U-98% 15N], 0.5 mM; WASp(20-158), [U-98% 13C; U-98% 15N], 0.5 mM; DTT 1 mM; sodium chloride 50 mM; sodium phosphate 20 mM; D2O, [U-2H], 7%; H2O 93%

sample_conditions_1: ionic strength: 0.2 M; pH: 6.8; pressure: 1 atm; temperature: 303 K

Experiments:

NameSampleSample stateSample conditions
2D 1H-15N HSQCsample_1isotropicsample_conditions_1
3D HNCOsample_1isotropicsample_conditions_1
3D HNCAsample_1isotropicsample_conditions_1
3D HNCACBsample_1isotropicsample_conditions_1
3D HBHA(CO)NHsample_1isotropicsample_conditions_1

Software:

TopSpin v3.2, Bruker Biospin - collection

TopSpin, Bruker Biospin - chemical shift assignment

CNS, Brunger, Adams, Clore, Gros, Nilges and Read - refinement, structure calculation

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