BMRB Entry 31151

Name: NMR solution structure of cell-permeant miniature protein ZF5.3
Published: 2024-04-23

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PDB ID: 9azi
Entry in NMR Restraints Grid
Validation report in NRG-CING
Chem Shift validation: AVS_full
BMRB Entry DOI: doi:10.13018/BMR31151
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Nicholas Rego and David Koes
3Dmol.js: molecular visualization with WebGL
Bioinformatics (2015) 31 (8): 1322-1324 doi:10.1093/bioinformatics/btu829

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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:

assigned_chemical_shifts
- assigned_chemical_shifts_1

Data type	Count
13C chemical shifts	93
15N chemical shifts	32
1H chemical shifts	198

Additional metadata:

Assembly
Samples and Experiments
Software
Spectrometers
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Assembly:

Entity Assembly ID	Entity Name	Entity ID
1	unit_1	1
2	unit_2	2

Entities:

Entity 1, unit_1 27 residues - 3203.776 Da.

1

TYR

SER

CYS

ASN

VAL

CYS

GLY

LYS

ALA

PHE

2

VAL

LEU

SER

ARG

HIS

LEU

ASN

ARG

HIS

LEU

3

ARG

VAL

HIS

ARG

ALA

THR

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:

Name	Sample	Sample state	Sample conditions
3D 1H-13C NOESY	sample_1	isotropic	sample_conditions_1
2D 1H-13C HSQC	sample_1	isotropic	sample_conditions_1
2D 1H-13C HSQC aromatic	sample_1	isotropic	sample_conditions_1
2D 1H-15N HSQC	sample_1	isotropic	sample_conditions_1
3D HCCH-TOCSY	sample_1	isotropic	sample_conditions_1
3D 1H-15N NOESY	sample_1	isotropic	sample_conditions_1
1D 1H	sample_1	isotropic	sample_conditions_1
1D 1H	sample_1	isotropic	sample_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