BMRB Entry 36460

Name: Solution structures of a disulfide-rich peptide that can bind KEAP1
Published: 2025-11-03

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PDB ID: 7w8t
Entry in NMR Restraints Grid
Validation report in NRG-CING
Chem Shift validation: AVS_full
BMRB Entry DOI: doi:10.13018/BMR36460
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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 structures of a disulfide-rich peptide that can bind KEAP1

Deposition date:

2021-12-08

Original release date:

2025-11-03

Authors:

Fan, S.; Wu, Y.; Wu, C.

Citation:

Citation: Wu, Yapei; Fan, Shihui; Dong, Meng; Li, Jinjing; Kong, Chuilian; Zhuang, Jie; Meng, Xiaoting; Lu, Shuaimin; Zhao, Yibing; Wu, Chuanliu. "Structure-guided design of CPPC-paired disulfide-rich peptide libraries for ligand and drug discovery." Chem. Sci. 13, 7780-7789 (2022).
PubMed: 35865895

Assembly members:

Assembly members:
DRP3, polymer, 26 residues, 2748.033 Da.

Natural source:

Natural source: Common Name: not available Taxonomy ID: 32630 Superkingdom: not available Kingdom: not available Genus/species: not available not available

Experimental source:

Experimental source: Production method: chemical synthesis Host organism: unidentified

Entity Sequences (FASTA):

Entity Sequences (FASTA):
DRP3: GCPPCASGCSPETGEFCWRE DDCPPC

Data sets:

assigned_chemical_shifts
- chem_shift_list_1

Data type	Count
13C chemical shifts	60
15N chemical shifts	21
1H chemical shifts	128

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 26 residues - 2748.033 Da.

1

GLY

CYS

PRO

CYS

ALA

SER

GLY

CYS

SER

2

PRO

GLU

THR

GLY

GLU

PHE

CYS

TRP

ARG

GLU

3

ASP

CYS

PRO

CYS

Samples:

sample_1: drp3 1 mM; perdeuterated acetonitrile, [U-?% 2H], 50%; H2O 50%

sample_conditions_1: ionic strength: 0 Not defined; pH: 7; pressure: 1 atm; temperature: 298 K

Experiments:

Name	Sample	Sample state	Sample conditions
2D 1H-13C HSQC	sample_1	anisotropic	sample_conditions_1
2D 1H-15N HSQC	sample_1	anisotropic	sample_conditions_1
2D 1H-1H NOESY	sample_1	anisotropic	sample_conditions_1
2D 1H-1H TOCSY	sample_1	anisotropic	sample_conditions_1

Software:

CNS, Brunger A. T. et.al. - refinement

ARIA, Linge, O'Donoghue and Nilges - structure calculation

NMRFAM-SPARKY, Lee W, Tonelli M, Markley JL - chemical shift assignment

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

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

NMR spectrometers:

Bruker AVANCE III 850 MHz

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