BMRB Entry 34069

Name: Solution structure of oxidized and amidated human IAPP (1-37), the diabetes II peptide.
Published: 2017-03-23

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PDB ID: 5mgq
Entry in NMR Restraints Grid
Validation report in NRG-CING
Chem Shift validation: AVS_full
BMRB Entry DOI: doi:10.13018/BMR34069
MolProbity Validation Chart

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Bioinformatics (2015) 31 (8): 1322-1324 doi:10.1093/bioinformatics/btu829

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Title: Solution structure of oxidized and amidated human IAPP (1-37), the diabetes II peptide. PubMed: 28287098

Deposition date: 2016-11-21 Original release date: 2017-03-23

Authors: Rodriguez Camargo, D.; Tripsianes, K.; Reif, B.

Citation: Rodriguez Camargo, D.; Tripsianes, K.; Buday, K.; Franko, A.; Gobl, C.; Hartlmuller, C.; Sarkar, R.; Aichler, M.; Mettenleiter, G.; Schulz, M.; Boddrich, A.; Erck, C.; Martens, H.; Walch, A.; Madl, T.; Wanker, E.; Conrad, M.; de Angelis, M.; Reif, B.. "The redox environment triggers conformational changes and aggregation of hIAPP in Type II Diabetes." Sci. Rep. 7, 44041-44041 (2017).

Assembly members:
entity_1, polymer, 37 residues, 3908.319 Da.

Natural source: Common Name: Human Taxonomy ID: 9606 Superkingdom: Eukaryota Kingdom: Metazoa Genus/species: Homo sapiens

Experimental source: Production method: recombinant technology Host organism: Escherichia coli BL21(DE3)

Entity Sequences (FASTA):
entity_1: KCNTATCATQRLANFLVHSS NNFGAILSSTNVGSNTX

Data sets:

assigned_chemical_shifts
- assigned_chemical_shifts_1

Data type	Count
13C chemical shifts	56
15N chemical shifts	42
1H chemical shifts	238

Additional metadata:

Assembly
Samples and Experiments
Software
Spectrometers
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Assembly:

Entity Assembly ID	Entity Name	Entity ID
1	entity_1	1

Entities:

Entity 1, entity_1 37 residues - 3908.319 Da.

1

LYS

CYS

ASN

THR

ALA

THR

CYS

ALA

THR

GLN

2

ARG

LEU

ALA

ASN

PHE

LEU

VAL

HIS

SER

3

ASN

PHE

GLY

ALA

ILE

LEU

SER

THR

4

ASN

VAL

GLY

SER

ASN

THR

TYC

Samples:

sample_1: Islet Amyloid Polypeptide (IAPP or Amylin), [U-99% 13C; U-99% 15N], 150 uM

sample_conditions_1: pH: 5.3; pressure: 1 atm; temperature: 278 K

Experiments:

Name	Sample	Sample state	Sample conditions
2D 1H-15N HSQC	sample_1	isotropic	sample_conditions_1
2D 1H-13C HSQC	sample_1	isotropic	sample_conditions_1
3D HNCACB	sample_1	isotropic	sample_conditions_1
3D CBCA(CO)NH	sample_1	isotropic	sample_conditions_1
3D HCCH-TOCSY	sample_1	isotropic	sample_conditions_1
3D 1H-15N NOESY	sample_1	isotropic	sample_conditions_1

Software:

CNS, Brunger A. T. et.al. - refinement

CYANA, Guntert, Mumenthaler and Wuthrich - structure calculation

SPARKY, Goddard - chemical shift assignment, peak picking

TOPSPIN, Bruker Biospin - processing

NMR spectrometers:

Bruker Bruker Avance 500 MHz
Bruker Bruker Avance 600 MHz
Bruker Bruker Avance 750 MHz

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