BMRB Entry 16105

Name: THE DYNAMIC ALPHA-HELIX STRUCTURE OF MICELLE-BOUND HUMAN AMYLIN.
Published: 2009-03-17

Chem Shift validation: AVS_full
BMRB Entry DOI: doi:10.13018/BMR16105

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

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Title:

THE DYNAMIC ALPHA-HELIX STRUCTURE OF MICELLE-BOUND HUMAN AMYLIN.

Deposition date:

2009-01-02

Original release date:

2009-03-17

Authors:

Patil, Sharadrao; Xu, Shihao; Sheftic, Sarah; Alexandrescu, Andrei

Citation:

Citation: Patil, Sharadrao; Xu, Shihao; Sheftic, Sarah; Alexandrescu, Andrei. "THE DYNAMIC ALPHA-HELIX STRUCTURE OF MICELLE-BOUND HUMAN AMYLIN." J. Biol. Chem. 284, 11982-11991 (2009).
PubMed: 19244249

Assembly members:

Assembly members:
alpha-helix, polymer, 37 residues, 3909.330 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: recombinant technology Host organism: Escherichia coli Vector: purchased from rPeptide

Entity Sequences (FASTA):

Entity Sequences (FASTA):
alpha-helix: KCNTATCATQRLANFLVHSS NNFGAILSSTNVGSNTY

Data sets:

assigned_chemical_shifts
- assigned_chem_shift_list_1

Data type	Count
15N chemical shifts	44
1H chemical shifts	192

Additional metadata:

Assembly
Samples and Experiments
Software
Spectrometers
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Assembly:

Entity Assembly ID	Entity Name	Entity ID
1	alpha-helix	1

Entities:

Entity 1, alpha-helix 37 residues - 3909.330 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

Samples:

sample_2: amylin, [U-100% 15N], 0.5 mM; sodium dodecyl sulfate, [U-99% 2H], 100 mM; acetic acid, [U-99% 2H], 60 mM

sample_1: amylin, [U-99% 15N], 0.5 mM; SDS, [U-2H], 100 mM; acetic acid 60 mM

sample_conditions_1: ionic strength: 60 mM; pH: 4.6; pressure: 1.0 atm; temperature: 310 K

sample_conditions_2: ionic strength: 60 mM; pH*: 4.2; temperature: 310 K

Experiments:

Name	Sample	Sample state	Sample conditions
3D 1H-15N NOESY	sample_1	isotropic	sample_conditions_1
3D HNCA	sample_1	isotropic	sample_conditions_1
3D HNHB	sample_1	isotropic	sample_conditions_1
2D 1H-1H NOESY	sample_1	isotropic	sample_conditions_1
3D TROSY	sample_1	isotropic	sample_conditions_1
3D TOCSY	sample_1	isotropic	sample_conditions_1

Software:

X-PLOR v3.851, Brunger - structure solution

NMR spectrometers:

Varian INOVA 600 MHz

BMRB	16104 17394 18795 20045
PDB	2G48 2KB8 2L86 3G7V 3G7W 3HGZ
DBJ	BAG73319
EMBL	CAA33032 CAA37002 CAA39504 CAA48724 CAB57803
GB	AAA35524 AAA35983 AAA51728 AAA52281 AAI11850
REF	NP_000406 XP_001144800 XP_003265632 XP_003265633 XP_003828947
SP	P10997
AlphaFold	P10997