BMRB Entry 31151

Chem Shift validation: AVS_full
BMRB Entry DOI: doi:10.13018/BMR31151

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Title:
NMR solution structure of cell-permeant miniature protein ZF5.3
Deposition date:
2024-03-11
Original release date:
2024-04-23
Authors:
Giudice, J.; Kelly, M.; Schepartz, A.
Citation:

Citation: Giudice, J.; Brauer, D.; Vazquez Maldonado, A.; Zoltek, M.; Schepartz, A.. "Structural and mechanistic basis for efficient endosomal escape by designed mini-proteins"  To be published ., .-..

Assembly members:

Assembly members:
entity_1, polymer, 27 residues, 3203.776 Da.
entity_ZN, non-polymer, 65.409 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 BL21(DE3)

Entity Sequences (FASTA):

Entity Sequences (FASTA):
entity_1: YSCNVCGKAFVLSRHLNRHL RVHRRAT

Data sets:
Data typeCount
13C chemical shifts93
15N chemical shifts32
1H chemical shifts198

Additional metadata:

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

Assembly:

Entity Assembly IDEntity NameEntity ID
1unit_11
2unit_22

Entities:

Entity 1, unit_1 27 residues - 3203.776 Da.

1   TYRSERCYSASNVALCYSGLYLYSALAPHE
2   VALLEUSERARGHISLEUASNARGHISLEU
3   ARGVALHISARGARGALATHR

Entity 2, unit_2 - Zn - 65.409 Da.

1   ZN

Samples:

sample_1: ZF5.3, [U-13C; U-15N], 800 uM; TRIS 20 mM; sodium chloride 100 mM; TCEP 2 mM; ZnCl2 1.6 mM

sample_conditions_1: ionic strength: 150 mM; pH: 5.5; pressure: 1 atm; temperature: 298 K

Experiments:

NameSampleSample stateSample conditions
3D 1H-13C NOESYsample_1isotropicsample_conditions_1
2D 1H-13C HSQCsample_1isotropicsample_conditions_1
2D 1H-13C HSQC aromaticsample_1isotropicsample_conditions_1
2D 1H-15N HSQCsample_1isotropicsample_conditions_1
3D HCCH-TOCSYsample_1isotropicsample_conditions_1
3D 1H-15N NOESYsample_1isotropicsample_conditions_1
1D 1Hsample_1isotropicsample_conditions_1
1D 1Hsample_1isotropicsample_conditions_1

Software:

CcpNmr Analysis Assign v3.2.0, Laue E.D. - chemical shift assignment

TopSpin v4.3.0, Bruker Biospin - processing

X-PLOR NIH, Schwieters, Kuszewski, Tjandra and Clore - structure calculation

X-PLOR NIH v3.5, Schwieters, Kuszewski, Tjandra and Clore - refinement

ARTINA, Klukowski, P., Riek, R. and Guntert, P. - peak picking

NMR spectrometers:

  • Bruker AVANCE NEO 600 MHz
  • Bruker AVANCE NEO 800 MHz

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