BMRB Entry 53214

Name: NMR structure and zinc-induced folding of the eponymous novel zinc finger from the ZC4H2 protein
Published: 2025-07-31

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PDB ID: 9p3z
Entry in NMR Restraints Grid
Validation report in NRG-CING
Chem Shift validation: AVS_full
BMRB Entry DOI: doi:10.13018/BMR53214
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Nicholas Rego and David Koes
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Bioinformatics (2015) 31 (8): 1322-1324 doi:10.1093/bioinformatics/btu829

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Title:

NMR structure and zinc-induced folding of the eponymous novel zinc finger from the ZC4H2 protein

Deposition date:

2025-06-04

Original release date:

2025-07-31

Authors:

Alexandrescu, Andrei

Citation:

Citation: Harris, Rilee; Rua, Antonio; Alexandrescu, Andrei. "NMR structure and zinc-induced folding of the eponymous novel zinc finger from the ZC4H2 protein" Biomolecules ., .-..

Assembly members:

Assembly members:
entity_1, polymer, 29 residues, 3083.72 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: obtained from a vendor

Entity Sequences (FASTA):

Entity Sequences (FASTA):
entity_1: MKACLSCHQQIHRNAPICPL CKAKSRS

Data sets:

assigned_chemical_shifts
- assigned_chemical_shifts_1

Data type	Count
13C chemical shifts	77
15N chemical shifts	25
1H chemical shifts	186

Additional metadata:

Assembly
Samples and Experiments
Software
Spectrometers
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Assembly:

Entity Assembly ID	Entity Name	Entity ID
1	ZC4H2-ZL	1
2	Zn2+	2

Entities:

Entity 1, ZC4H2-ZL 29 residues - 3083.72 Da.

N-terminus is blocked by acetyl group (Ac-); C-terminus is blocked by amide group (-NH2); Peptide was synthesized this way so as to not introduce charges at the N-term (+) and C-term (-) of the domain, and therefore better represent the domain in the full-length protein.

1

ACE

MET

LYS

ALA

CYS

LEU

SER

CYS

HIS

GLN

2

GLN

ILE

HIS

ARG

ASN

ALA

PRO

ILE

CYS

PRO

3

LEU

CYS

LYS

ALA

LYS

SER

ARG

SER

NH2

Entity 2, Zn2+ - Zn - 65.409 Da.

1

ZN

Samples:

sample_1: ZC4H2-ZL 1.6 mM; zinc 1.6 mM; H2O 55 M

sample_2: ZC4H2-ZL 0.9 mM; zinc 0.9 mM; D2O 55 M

sample_conditions_1: pH: 6.0; pressure: 1 atm; temperature: 10 K

sample_conditions_2: pH: 5.9; pressure: 1 atm; temperature: 10 K

Experiments:

Name	Sample	Sample state	Sample conditions
2D 1H-1H TOCSY	sample_1	isotropic	sample_conditions_1
2D 1H-1H NOESY	sample_1	isotropic	sample_conditions_1
2D 1H-15N HSQC	sample_1	isotropic	sample_conditions_1
2D 1H-1H TOCSY	sample_2	isotropic	sample_conditions_2
2D 1H-1H NOESY	sample_2	isotropic	sample_conditions_2
2D 1H-13C HSQC	sample_2	isotropic	sample_conditions_2

Software:

CcpNMR Analysis v2.5.2 - chemical shift assignment, data analysis

iNMR v6.3.0 - processing

TOPSPIN v4.1 - collection

X-PLOR NIH v3.8 - structure solution

NMR spectrometers:

Bruker AVANCE NEO 800 MHz
Bruker AVANCE NEO 600 MHz