BMRB Entry 36258

Name: Structure of Glargine insulin in 20% acetic acid-d4 (pH 1.9)
Published: 2020-07-15

Click here to enlarge.

PDB ID: 6k59
Entry in NMR Restraints Grid
Validation report in NRG-CING
Chem Shift validation: AVS_full
BMRB Entry DOI: doi:10.13018/BMR36258
MolProbity Validation Chart

NMR-STAR file interactive viewer.
NMR-STAR v3 text file.
XML gzip file.
RDF gzip file.
All files associated with the entry

Nicholas Rego and David Koes
3Dmol.js: molecular visualization with WebGL
Bioinformatics (2015) 31 (8): 1322-1324 doi:10.1093/bioinformatics/btu829

Select model:

I am color blind

Download raw data. Direct link to this display. Help

Title:

Structure of Glargine insulin in 20% acetic acid-d4 (pH 1.9)

Deposition date:

2019-05-28

Original release date:

2020-07-15

Authors:

Ratha, B.; Kar, R.; Bhunia, A.

Citation:

Citation: Ratha, B.; Kar, R.; Bednarikova, Z.; Gazova, Z.; Kotler, S.; Raha, S.; De, S.; Maiti, N.; Bhunia, A.. "Molecular Details of a Salt Bridge and Its Role in Insulin Fibrillation by NMR and Raman Spectroscopic Analysis." J. Phys. Chem. B 124, 1125-1136 (2020).
PubMed: 31958230

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: not available Taxonomy ID: 32630 Superkingdom: not available Kingdom: not available Genus/species: not available not available

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
1H chemical shifts	333

Additional metadata:

Assembly
Samples and Experiments
Software
Spectrometers
Hide all

Assembly:

Entity Assembly ID	Entity Name	Entity ID
1	entity_1	1
2	entity_2	2

Entities:

Entity 1, entity_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, entity_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: PEPTIDE CHAIN A 350 uM; PEPTIDE CHAIN B 350 uM; acetic acid-d4, [U-2H], 20%; H2O 80%

sample_conditions_1: ionic strength: 0 mM; pH: 1.9 pD; pressure: 1 atm; temperature: 298 K

Experiments:

Name	Sample	Sample state	Sample conditions
2D 1H-1H NOESY	sample_1	isotropic	sample_conditions_1
2D 1H-1H TOCSY	sample_1	isotropic	sample_conditions_1

Software:

Amber, Case, Darden, Cheatham III, Simmerling, Wang, Duke, Luo, ... and Kollman - refinement, structure calculation

Sparky, Goddard - chemical shift assignment, peak picking

TopSpin, Bruker Biospin - collection

NMR spectrometers:

Bruker AVANCE III 600 MHz