BMRB Entry 16314

Name: Three-Dimensional NMR Structure of Rat Islet Amyloid Polypeptide in DPC micelles.
Published: 2009-05-29

Chem Shift validation: AVS_full
BMRB Entry DOI: doi:10.13018/BMR16314

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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:

Three-Dimensional NMR Structure of Rat Islet Amyloid Polypeptide in DPC micelles.

Deposition date:

2009-05-22

Original release date:

2009-05-29

Authors:

Nanga, Ravi P R; Jeffrey, Brender; Xu, Jiadi; Hartman, Kevin; Subramanian, Vivekanandan; Ramamoorthy, Ayyalusamy

Citation:

Citation: Nanga, Ravi P. R.; Jeffrey, Brender; Xu, Jiadi; Hartman, Kevin; Subramanian, Vivekanandan; Ramamoorthy, Ayyalusamy. "Three-Dimensional Structure and Orientation of Rat Islet Amyloid Polypeptide Protein in a Membrane Environment by Solution NMR Spectroscopy." J. Am. Chem. Soc. 131, 8252-8261 (2009).
PubMed: 19456151

Assembly members:

Assembly members:
IAPP, polymer, 37 residues, 3926.447 Da.

Natural source:

Natural source: Common Name: Norway Rat Taxonomy ID: 10116 Superkingdom: Eukaryota Kingdom: Metazoa Genus/species: Rattus norvegicus

Experimental source:

Experimental source: Production method: chemical synthesis

Entity Sequences (FASTA):

Entity Sequences (FASTA):
IAPP: KCNTATCATQRLANFLVRSS NNLGPVLPPTNVGSNTY

Data sets:

assigned_chemical_shifts
- assigned_chem_shift_list_1

Data type	Count
1H chemical shifts	212

Additional metadata:

Assembly
Samples and Experiments
Software
Spectrometers
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Assembly:

Entity Assembly ID	Entity Name	Entity ID
1	IAPP	1

Entities:

Entity 1, IAPP 37 residues - 3926.447 Da.

1

LYS

CYS

ASN

THR

ALA

THR

CYS

ALA

THR

GLN

2

ARG

LEU

ALA

ASN

PHE

LEU

VAL

ARG

SER

3

ASN

LEU

GLY

PRO

VAL

LEU

PRO

THR

4

ASN

VAL

GLY

SER

ASN

THR

TYR

Samples:

sample_1: sodium phosphate 20 mM; sodium azide 0.02%; sodium chloride 120 mM; D2O, 99.9%, 10%; DPC, 98% deuterated, 200 mM; entity 2.5 mM; H2O 90%

sample_conditions_1: ionic strength: 120 mM; pH: 7.3; pressure: 1 atm; temperature: 303 K

Experiments:

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

Software:

NMRPipe, Delaglio, Grzesiek, Vuister, Zhu, Pfeifer and Bax - processing

TOPSPIN, Bruker Biospin - collection, data analysis, processing

SPARKY, Goddard - chemical shift assignment, chemical shift calculation, peak picking

X-PLOR NIH, Schwieters, Kuszewski, Tjandra and Clore - geometry optimization, refinement, structure solution

Molmol, Koradi, Billeter and Wuthrich - structure solution

NMR spectrometers:

Bruker Avance 900 MHz

BMRB	20046
PDB	2KJ7
DBJ	BAA22051
EMBL	CAA37003
GB	AAA37874 AAA40730 AAA41359 AAH27527 EDL10633
REF	NP_034621 NP_036718 XP_006155144 XP_006155145 XP_006237676
SP	P12968 P12969
AlphaFold	P12968 P12969