BMRB Entry 30099

Name: Structure of human islet amyloid polypeptide in complex with an engineered binding protein
Published: 2016-09-22

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PDB ID: 5k5g
Entry in NMR Restraints Grid
Validation report in NRG-CING
Chem Shift validation: AVS_full, LACS
BMRB Entry DOI: doi:10.13018/BMR30099
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Nicholas Rego and David Koes
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Bioinformatics (2015) 31 (8): 1322-1324 doi:10.1093/bioinformatics/btu829

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Title: Structure of human islet amyloid polypeptide in complex with an engineered binding protein PubMed: 27641459

Deposition date: 2016-05-23 Original release date: 2016-09-22

Authors: Mirecka, E.; Feuerstein, S.; Gremer, L.; Schroeder, G.; Stoldt, M.; Willbold, D.; Hoyer, W.

Citation: Mirecka, E.; Feuerstein, S.; Gremer, L.; Schroeder, G.; Stoldt, M.; Willbold, D.; Hoyer, W.. "beta-Hairpin of Islet Amyloid Polypeptide Bound to an Aggregation Inhibitor" Sci. Rep. 6, 33474-33474 (2016).

Assembly members:
Islet amyloid polypeptide, polymer, 37 residues, 3909.304 Da.
HI18, polymer, 69 residues, 7804.660 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):
Islet amyloid polypeptide: KCNTATCATQRLANFLVHSS NNFGAILSSTNVGSNTY
HI18: MHHHHHHVNSVDNKFNKEME SAGGEIVYLPNLNPDQLCAF IHSIHDDPSQSANLLAEAKK LNDAQAPKW

Data sets:

assigned_chemical_shifts
- assigned_chemical_shifts_1

Data type	Count
13C chemical shifts	320
15N chemical shifts	98
1H chemical shifts	656

Additional metadata:

Assembly
Samples and Experiments
Software
Spectrometers
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Assembly:

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

Entities:

Entity 1, entity_1 37 residues - 3909.304 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

TYR

Entity 2, entity_2, 1 69 residues - 7804.660 Da.

1

MET

HIS

VAL

ASN

SER

2

VAL

ASP

ASN

LYS

PHE

ASN

LYS

GLU

MET

GLU

3

SER

ALA

GLY

GLU

ILE

VAL

TYR

LEU

PRO

4

ASN

LEU

ASN

PRO

ASP

GLN

LEU

CYS

ALA

PHE

5

ILE

HIS

SER

ILE

HIS

ASP

PRO

SER

GLN

6

SER

ALA

ASN

LEU

ALA

GLU

ALA

LYS

7

LEU

ASN

ASP

ALA

GLN

ALA

PRO

LYS

TRP

Samples:

sample_1: HI18 0.48 mM; ISLET AMYLOID POLYPEPTIDE, [U-13C; U-15N], 0.40 mM; sodium phosphate 20 mM; H2O 93%; D2O 7%

sample_2: HI18, [U-13C; U-15N], 0.40 mM; ISLET AMYLOID POLYPEPTIDE 0.48 mM; sodium phosphate 20 mM; H2O 93%; D2O 7%

sample_conditions_1: ionic strength: 20 mM; pH: 6.0; pressure: 1 atm; temperature: 298 K

Experiments:

Name	Sample	Sample state	Sample conditions
2D 1H-15N HSQC	sample_1	isotropic	sample_conditions_1
3D HNCA	sample_1	isotropic	sample_conditions_1
3D HNHA	sample_1	isotropic	sample_conditions_1
3D HNCACB	sample_1	isotropic	sample_conditions_1
3D 1H-15N NOESY	sample_1	isotropic	sample_conditions_1
3D HNCO	sample_1	isotropic	sample_conditions_1
3D HCCH-COSY	sample_1	isotropic	sample_conditions_1
3D 1H-13C NOESY	sample_1	isotropic	sample_conditions_1
2D 1H-15N HSQC	sample_2	isotropic	sample_conditions_1
3D HNCA	sample_2	isotropic	sample_conditions_1
3D HNHA	sample_2	isotropic	sample_conditions_1
3D HNCACB	sample_2	isotropic	sample_conditions_1
3D 1H-15N NOESY	sample_2	isotropic	sample_conditions_1
3D HCCH-COSY	sample_2	isotropic	sample_conditions_1
3D 1H-13C NOESY	sample_2	isotropic	sample_conditions_1

Software:

ARIA v2.3.2, Linge, O'Donoghue and Nilges - structure calculation

Analysis v2.3, CCPN - chemical shift assignment, peak picking

CNS v1.21, Brunger A. T. et.al. - refinement

NMRPipe v7.9, Delaglio, Grzesiek, Vuister, Zhu, Pfeifer and Bax - processing

VNMRJ v2.3A, Varian - collection

NMR spectrometers:

Varian VNMRS 800 MHz
Varian VNMRS 900 MHz

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