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PDB ID: 9zo6
Entry in NMR Restraints Grid
Validation report in NRG-CING
Chem Shift validation: AVS_full
BMRB Entry DOI: doi:10.13018/BMR31288
MolProbity Validation Chart

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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:

Glargine insulin

Deposition date:

2025-12-15

Original release date:

2026-10-29

Authors:

Weiss, M.; Yang, Y.

Citation:

Citation: Yang, Yanwu; Dhayalan, Balamurugan; Ehnbom, Andreas; Weil-Ktorza, Orit; Metanis, Norman; Weiss, Michael. "Damping amyloid-associated conformational fluctuations in a protein by an engineered diselenide bridge " Protein Sci. 35, e70697-e70697 (2026).
PubMed: 42478539

Assembly members:

Assembly members:
entity_1, polymer, 21 residues, 2326.647 Da.
entity_2, polymer, 32 residues, 3748.340 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: chemical synthesis

Entity Sequences (FASTA):

Entity Sequences (FASTA):
entity_1: GIVEQCCTSICSLYQLENYC G
entity_2: FVNQHLCGSHLVEALYLVCG ERGFFYTPKTRR

Data sets:

assigned_chemical_shifts
- assigned_chemical_shifts_1

Data type	Count
13C chemical shifts	186
15N chemical shifts	53
1H chemical shifts	360

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 21 residues - 2326.647 Da.

1

GLY

ILE

VAL

GLU

GLN

CYS

THR

SER

ILE

2

CYS

SER

LEU

TYR

GLN

LEU

GLU

ASN

TYR

CYS

3

GLY

Entity 2, unit_2 32 residues - 3748.340 Da.

1

PHE

VAL

ASN

GLN

HIS

LEU

CYS

GLY

SER

HIS

2

LEU

VAL

GLU

ALA

LEU

TYR

LEU

VAL

CYS

GLY

3

GLU

ARG

GLY

PHE

TYR

THR

PRO

LYS

THR

4

ARG

Samples:

sample_1: glargine insulin 0.3 ± 0.01 mM

sample_2: glargine insulin 0.3 ± 0.01 mM

sample_conditions_1: ionic strength: 0.1 Not defined; pH: 2.1; pressure: 1 atm; temperature: 298 K

sample_conditions_2: ionic strength: 0.1 Not defined; pH: 2.1; 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-1H NOESY	sample_1	isotropic	sample_conditions_1
2D 1H-1H TOCSY	sample_1	isotropic	sample_conditions_1
2D 1H-13C HSQC aliphatic	sample_2	isotropic	sample_conditions_2
2D 1H-13C HSQC aromatic	sample_2	isotropic	sample_conditions_2
2D 1H-1H NOESY	sample_2	isotropic	sample_conditions_2
2D 1H-1H TOCSY	sample_2	isotropic	sample_conditions_2

Software:

TopSpin, Bruker Biospin - collection

Sparky, Goddard - chemical shift assignment, data analysis, peak picking

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

NMR spectrometers:

Bruker AVANCE NEO 700 MHz

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

BMRB Entry 31288