BMRB Entry 36009

Name: Solution NMR structure of Humanin containing a D-isomerized serine residue
Published: 2016-09-08

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PDB ID: 5giw
Entry in NMR Restraints Grid
Validation report in NRG-CING
Chem Shift validation: AVS_anomalous, AVS_full
BMRB Entry DOI: doi:10.13018/BMR36009
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Nicholas Rego and David Koes
3Dmol.js: molecular visualization with WebGL
Bioinformatics (2015) 31 (8): 1322-1324 doi:10.1093/bioinformatics/btu829

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Title:

Solution NMR structure of Humanin containing a D-isomerized serine residue

Deposition date:

2016-06-25

Original release date:

2016-09-08

Authors:

Sugiki, T.; Furuita, K.; Alsanousi, N.; Fujiwara, T.; Kojima, C.

Citation:

Citation: Alsanousi, N.; Sugiki, T.; Furuita, K.; So, M.; Lee, Y.; Fujiwara, T.; Kojima, C.. "Solution NMR structure and inhibitory effect against amyloid-beta fibrillation of Humanin containing a d-isomerized serine residue" Biochem. Biophys. Res. Commun. 477, 647-653 (2016).
PubMed: 27349871

Assembly members:

Assembly members:
entity_1, polymer, 24 residues, 2691.264 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: chemical synthesis

Entity Sequences (FASTA):

Entity Sequences (FASTA):
entity_1: MAPRGFSCLLLLTXEIDLPV KRRA

Data sets:

assigned_chemical_shifts
- assigned_chemical_shifts_1

Data type	Count
15N chemical shifts	22
1H chemical shifts	158

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 24 residues - 2691.264 Da.

1

MET

ALA

PRO

ARG

GLY

PHE

SER

CYS

LEU

2

LEU

THR

DSN

GLU

ILE

ASP

LEU

PRO

VAL

3

LYS

ARG

ALA

Samples:

sample_1: D-Ser-containing humanin 2.0 mM; trifluoroethanol, U-99% D, 30%; H2O 70%

sample_conditions_1: ionic strength: 0 mM; pH: 7; 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
2D 1H-15N HSQC	sample_1	isotropic	sample_conditions_1

Software:

CYANA v3.97, Guntert, Mumenthaler and Wuthrich - structure calculation

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

SPARKY, Goddard - chemical shift assignment

X-PLOR NIH, Schwieters, Kuszewski, Tjandra and Clore - refinement

NMR spectrometers:

Bruker AvanceIII HD 600 MHz

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