BMRB Entry 35004

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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/BMR35004
MolProbity Validation Chart

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Title:
PIN1 WW Domain Binding Mode with LYR-tide
Deposition date:
2025-06-25
Original release date:
2026-09-01
Authors:
Jiang, M.; Sun, M.; Mott, H.; Creixell, P.
Citation:

Citation: Jiang, M.; Sun, M.; Nuo, C.; Ord, M.; Augustin, T.; Li, A.; Shah, N.; Rinehart, J.; Mott, H.; Creixell, P.. "Identifying molecular determinants of epistasis and engineering protein superbinders with combinatorial deep mutational scanning libraries "  .

Assembly members:

Assembly members:
entity_1, polymer, 37 residues, 4360.806 Da.
entity_2, polymer, 12 residues, 1161.249 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: EKLPPGWEKRMSRSSGRVYY FNHITNASQWERPSGNS
entity_2: XGLYRXPPLPGX

Data sets:
Data typeCount
13C chemical shifts115
15N chemical shifts30
1H chemical shifts299

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 37 residues - 4360.806 Da.

1   GLULYSLEUPROPROGLYTRPGLULYSARG
2   METSERARGSERSERGLYARGVALTYRTYR
3   PHEASNHISILETHRASNALASERGLNTRP
4   GLUARGPROSERGLYASNSER

Entity 2, unit_2 12 residues - 1161.249 Da.

1   ACEGLYLEUTYRARGSEPPROPROLEUPRO
2   GLYNH2

Samples:

sample_1: Peptidyl-prolyl cis-trans isomerase NIMA-interacting 1 (PIN1) WW Domain 1000 uM; LYR-tide LYRpSPPLP 2000 uM; sodium chloride 100 mM; sodium phosphate 50 mM; D2O, [U-99% 2H], 10%

sample_conditions_1: ionic strength: 200 mM; pH: 7; pressure: 1 atm; temperature: 298 K

Experiments:

NameSampleSample stateSample conditions
2D 1H-1H NOESYsample_1isotropicsample_conditions_1
2D 1H-13C HSQCsample_1isotropicsample_conditions_1
2D 1H-1H TOCSYsample_1isotropicsample_conditions_1
2D DQF-COSYsample_1isotropicsample_conditions_1
2D 1H-15N HSQCsample_1isotropicsample_conditions_1

Software:

CcpNmr Analysis v3.2.10, Skinner, S.P., Fogh, R.H., Boucher, W., Ragan, T.J., Mureddu, L.G., and Vuister, G.W - chemical shift assignment, peak picking

TopSpin v3.1, Bruker Biospin - collection

ARIA, Linge, O'Donoghue and Nilges - structure calculation

NMR spectrometers:

  • Bruker AVANCE 600 MHz

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