BMRB Entry 19663

Name: Somatostatin-14 solution structure in 5% D-mannitol
Published: 2014-05-05

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PDB ID: 2mi1
Entry in NMR Restraints Grid
Validation report in NRG-CING
Chem Shift validation: AVS_full, SPARTA
BMRB Entry DOI: doi:10.13018/BMR19663
MolProbity Validation Chart

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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:

Somatostatin-14 solution structure in 5% D-mannitol

Deposition date:

2013-12-08

Original release date:

2014-05-05

Authors:

Anoop, A.; Ranganathan, Srivastav; Pratihar, Supriya

Citation:

Citation: Anoop, Arunagiri; Ranganathan, Srivastav; Dhaked, Bhagwan Das; Jha, Narendra Nath; Pratihar, Supriya; Ghosh, Saikat; Sahay, Shruti; Kumar, Santosh; Das, Subhadeep; Kombrabail, Mamata; Agarwal, Kumud; Jacob, Reeba; Singru, Praful; Bhaumik, Prasenjit; Padinhateeri, Ranjith; Kumar, Ashutosh; Maji, Samir. "Elucidating the Role of Disulfide Bond on Amyloid Formation and Fibril Reversibility of Somatostatin-14: RELEVANCE TO ITS STORAGE AND SECRETION." J. Biol. Chem. 289, 16884-16903 (2014).
PubMed: 24782311

Assembly members:

Assembly members:
Somatostatin-14, polymer, 14 residues, 1641.918 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):
Somatostatin-14: AGCKNFFWKTFTSC

Data sets:

assigned_chemical_shifts
- assigned_chem_shift_list_1

Data type	Count
1H chemical shifts	74

Additional metadata:

Assembly
Samples and Experiments
Software
Spectrometers
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Assembly:

Entity Assembly ID	Entity Name	Entity ID
1	Somatostatin-14	1

Entities:

Entity 1, Somatostatin-14 14 residues - 1641.918 Da.

1

ALA

GLY

CYS

LYS

ASN

PHE

TRP

LYS

THR

2

PHE

THR

SER

CYS

Samples:

sample_1: H2O 90%; D2O 10%; D-mannitol 5 w/v %

sample_conditions_1: pH: 5.6; pressure: 1 atm; temperature: 298 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:

CYANA v2.1, Guntert, Mumenthaler and Wuthrich - structure solution

SPARKY v3.114, Goddard - chemical shift assignment

NMR spectrometers:

Bruker Avance 500 MHz