BMRB Entry 17426

Name: Solution structure of SFTI-OPN, a pro-angiogenic peptide with osteopontin sequence grafted into SFTI-1 cyclic framework
Published: 2011-11-03

Chem Shift validation: AVS_full
BMRB Entry DOI: doi:10.13018/BMR17426

NMR-STAR file interactive viewer.
NMR-STAR v3 text file.
XML gzip file.
RDF gzip file.
All files associated with the entry

Nicholas Rego and David Koes
3Dmol.js: molecular visualization with WebGL
Bioinformatics (2015) 31 (8): 1322-1324 doi:10.1093/bioinformatics/btu829

Select model:

I am color blind

Download raw data. Direct link to this display. Help

Title:

Solution structure of SFTI-OPN, a pro-angiogenic peptide with osteopontin sequence grafted into SFTI-1 cyclic framework

Deposition date:

2011-01-24

Original release date:

2011-11-03

Authors:

Chan, Lai Yue; Daly, Norelle Lee

Citation:

Citation: Chan, Lai; Gunasekera, Sunithi; Henriques, Sonia; Worth, Nathalie; Le, Sarah-Jane; Clark, Richard; Campbell, Julie; Craik, David; Daly, Norelle. "Engineering pro-angiogenic peptides using stable, disulfide-rich cyclic scaffolds." Blood 118, 6709-6717 (2011).
PubMed: 22039263

Assembly members:

Assembly members:
SFTI-OPN, polymer, 14 residues, 1551.82 Da.

Natural source:

Natural source: Common Name: not available Taxonomy ID: not available Superkingdom: not available Kingdom: not available Genus/species: not available not available

Experimental source:

Experimental source: Production method: chemical synthesis

Entity Sequences (FASTA):

Entity Sequences (FASTA):
SFTI-OPN: GRCSVVYGLRCFPD

Data sets:

assigned_chemical_shifts
- assigned_chem_shift_list_1

Data type	Count
1H chemical shifts	83

Additional metadata:

Assembly
Samples and Experiments
Software
Spectrometers
Hide all

Assembly:

Entity Assembly ID	Entity Name	Entity ID
1	SFTI-OPN	1

Entities:

Entity 1, SFTI-OPN 14 residues - 1551.82 Da.

1

GLY

ARG

CYS

SER

VAL

TYR

GLY

LEU

ARG

2

CYS

PHE

PRO

ASP

Samples:

sample_1: SFTI-OPN 1 ± 0.1 mM; H2O 90%; D2O 10%

sample_conditions_1: pH: 5.0; temperature: 290 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
2D DQF-COSY	sample_1	isotropic	sample_conditions_1

Software:

CNS v1.1, Brunger, Adams, Clore, Gros, Nilges and Read - structure solution

TOPSPIN v2.1, Bruker Biospin - collection

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

SPARKY, Goddard - chemical shift assignment

NMR spectrometers:

Bruker Avance 600 MHz