BMRB Entry 52871

Name: human PC1 prodomain
Published: 2025-09-03

Chem Shift validation: AVS_full
BMRB Entry DOI: doi:10.13018/BMR52871

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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:

human PC1 prodomain

Deposition date:

2025-01-20

Original release date:

2025-09-03

Authors:

Marzaro, Simone; Klaushofer, Rupert; Brandstetter, Hans; Dahms, Sven; Schubert, Mario

Citation:

Citation: Klaushofer, Rupert; Bloch, Konstantin; Eder, Luisa Susanna; Marzaro, Simone; Schubert, Mario; Bottcher-Friebertshauser, Eva; Brandstetter, Hans; Dahms, Sven. "Structural insights into proprotein convertase activation facilitate the engineering of highly specific furin inhibitors" Nat. Commun. 16, 8206-8206 (2025).
PubMed: 40897699

Assembly members:

Assembly members:
entity_1, polymer, 83 residues, Formula weight is not available

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 Vector: hPC1pro_WT

Entity Sequences (FASTA):

Entity Sequences (FASTA):
entity_1: KRQFVNEWAAEIPGGPEAAS AIAEELGYDLLGQIGSLENH YLFKHKNHPRRSRRSAFHIT KRLSDDDRVIWAEQQYEKER SKR

Data sets:

assigned_chemical_shifts
- assigned_chemical_shifts_1

Data type	Count
13C chemical shifts	373
15N chemical shifts	85
1H chemical shifts	560

Additional metadata:

Assembly
Samples and Experiments
Software
Spectrometers
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Assembly:

Entity Assembly ID	Entity Name	Entity ID
1	PC1 prodomain	1

Entities:

Entity 1, PC1 prodomain 83 residues - Formula weight is not available

1

LYS

ARG

GLN

PHE

VAL

ASN

GLU

TRP

ALA

2

GLU

ILE

PRO

GLY

PRO

GLU

ALA

SER

3

ALA

ILE

ALA

GLU

LEU

GLY

TYR

ASP

LEU

4

LEU

GLY

GLN

ILE

GLY

SER

LEU

GLU

ASN

HIS

5

TYR

LEU

PHE

LYS

HIS

LYS

ASN

HIS

PRO

ARG

6

ARG

SER

ARG

SER

ALA

PHE

HIS

ILE

THR

7

LYS

ARG

LEU

SER

ASP

ARG

VAL

ILE

8

TRP

ALA

GLU

GLN

TYR

GLU

LYS

GLU

ARG

9

SER

LYS

ARG

Samples:

sample_1: PC1 prodomain, [U-99% 15N], 0.4 mM; D2O, [U-100% 2H], 7%; sodium phosphate 100 mM

sample_2: D2O, [U-100% 2H], 7%; sodium phosphate 100 mM; PC1 prodomain, [U-99% 13C; U-99% 15N], 0.4 mM

sample_conditions_1: ionic strength: 265 mM; pH: 7.4; pressure: 1 atm; temperature: 298 K

Experiments:

Name	Sample	Sample state	Sample conditions
2D 1H-15N HSQC	sample_1	isotropic	sample_conditions_1
2D 1H-15N HSQC	sample_2	isotropic	sample_conditions_1
3D 15N-separated NOESY	sample_1	isotropic	sample_conditions_1
2D 1H-1H NOESY	sample_1	isotropic	sample_conditions_1
2D 1H-13C HSQC aliphatic	sample_2	isotropic	sample_conditions_1
2D 1H-13C HSQC aromatic	sample_2	isotropic	sample_conditions_1
3D HNCA	sample_2	isotropic	sample_conditions_1
3D CBCA(CO)NH	sample_2	isotropic	sample_conditions_1
3D HNCO	sample_2	isotropic	sample_conditions_1
3D HNCACB	sample_2	isotropic	sample_conditions_1
3D HN(CA)CO	sample_2	isotropic	sample_conditions_1
3D CCH-TOCSY	sample_2	isotropic	sample_conditions_1
3D 13C-separated NOESY	sample_2	isotropic	sample_conditions_1

Software:

TOPSPIN - collection, processing

SPARKY - data analysis

NMR spectrometers:

Bruker AVANCE III 600 MHz

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