BMRB Entry 50567

Name: Structure of PCSK9 antagonist P9-38
Published: 2020-11-24

Chem Shift validation: AVS_anomalous, AVS_full
BMRB Entry DOI: doi:10.13018/BMR50567

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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: Structure of PCSK9 antagonist P9-38 PubMed: 33356222

Deposition date: 2020-11-11 Original release date: 2020-11-24

Authors: Tombling, Benjamin

Citation: Tombling, Benjamin; Lammi, Carmen; Lawrence, Nicole; Gilding, Edward; Grazioso, Giovanni; Craik, David; Wang, Conan. "Bioactive cyclization optimizes the affinity of a proprotein convertase subtilisin/kexin type 9 (PCSK9) peptide inhibitor" J. Med. Chem. 64, 2523-2533 (2021).

Assembly members:
entity_1, polymer, 22 residues, Formula weight is not available

Natural source: Common Name: not available Taxonomy ID: not available Superkingdom: not available Kingdom: not available Genus/species: not available not available

Experimental source: Production method: recombinant technology Host organism: Escherichia coli Vector: pComb3

Entity Sequences (FASTA):
entity_1: CTVFTSWEEYLDWNNLHPRN SC

Data sets:

assigned_chemical_shifts
- assigned_chemical_shifts_1

Data type	Count
13C chemical shifts	54
15N chemical shifts	21
1H chemical shifts	139

Additional metadata:

Assembly
Samples and Experiments
Software
Spectrometers
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Assembly:

Entity Assembly ID	Entity Name	Entity ID
1	P9-38	1

Entities:

Entity 1, P9-38 22 residues - Formula weight is not available

1

CYS

THR

VAL

PHE

THR

SER

TRP

GLU

TYR

2

LEU

ASP

TRP

ASN

LEU

HIS

PRO

ARG

ASN

3

SER

CYS

Samples:

sample_1: P9-38 0.75 mM

sample_conditions_1: pH: 3.25; pressure: 1 atm; temperature: 298 K

Experiments:

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

Software:

CcpNMR - chemical shift assignment

NMR spectrometers:

Bruker AVANCE III 600 MHz

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