BMRB Entry 30562

Name: Solution structure of SFTI-KLK5 inhibitor
Published: 2019-03-28

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PDB ID: 6nox
Entry in NMR Restraints Grid
Validation report in NRG-CING
Chem Shift validation: AVS_anomalous, AVS_full
BMRB Entry DOI: doi:10.13018/BMR30562
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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 structure of SFTI-KLK5 inhibitor

Deposition date:

2019-01-16

Original release date:

2019-03-28

Authors:

White, A.

Citation:

Citation: Li, C.; de Veer, S.; White, A.; Chen, X.; Harris, J.; Swedberg, J.; Craik, D.. "Amino Acid Scanning at P5' within the Bowman-Birk Inhibitory Loop Reveals Specificity Trends for Diverse Serine Proteases." J. Med. Chem. 62, 3696-3706 (2019).
PubMed: 30888159

Assembly members:

Assembly members:
entity_1, polymer, 14 residues, 1694.889 Da.

Natural source:

Natural source: Common Name: common sunflower Taxonomy ID: 4232 Superkingdom: Eukaryota Kingdom: Viridiplantae Genus/species: Helianthus annuus

Experimental source:

Experimental source: Production method: chemical synthesis

Entity Sequences (FASTA):

Entity Sequences (FASTA):
entity_1: GFCHRSYPPECWPN

Data sets:

assigned_chemical_shifts
- assigned_chemical_shifts_1

Data type	Count
13C chemical shifts	36
15N chemical shifts	14
1H chemical shifts	88

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 14 residues - 1694.889 Da.

1

GLY

PHE

CYS

HIS

ARG

SER

TYR

PRO

GLU

2

CYS

TRP

PRO

ASN

Samples:

sample_1: SFTI-KLK5 1.5 ± 0.2 mM

sample_conditions_1: pH: 3.5; pressure: 1 atm; temperature: 298 K

sample_conditions_2: pH: 3.5; 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
2D 1H-13C HSQC	sample_1	isotropic	sample_conditions_1
2D 1H-1H COSY	sample_1	isotropic	sample_conditions_2
2D 1H-13C HSQC	sample_1	isotropic	sample_conditions_2

Software:

CcpNMR, CCPN - chemical shift assignment, peak picking

CYANA, Guntert, Mumenthaler and Wuthrich - structure calculation

CNS, Brunger, Adams, Clore, Gros, Nilges and Read - refinement, structure calculation

TOPSPIN, Bruker Biospin - collection

TALOS, Cornilescu, Delaglio and Bax - structure calculation

NMR spectrometers:

Bruker AvanceIII 600 MHz

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