BMRB Entry 36213

Name: Solution Structure of Bicyclic Peptide pb-13
Published: 2025-10-11

Click here to enlarge.

PDB ID: 6img
Entry in NMR Restraints Grid
Validation report in NRG-CING
Chem Shift validation: AVS_full
BMRB Entry DOI: doi:10.13018/BMR36213
MolProbity Validation Chart

NMR-STAR file interactive viewer.
NMR-STAR v3 text 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 Bicyclic Peptide pb-13

Deposition date:

2018-10-22

Original release date:

2025-10-11

Authors:

Yao, H.; Lin, P.; Zha, J.; Zha, M.; Zhao, Y.; Wu, C.

Citation:

Citation: Lin, Ping; Yao, Hongwei; Zha, Jun; Zhao, Yibing; Wu, Chuanliu. "Ordered and Isomerically Stable Bicyclic Peptide Scaffolds Constrained through Cystine Bridges and Proline Turns." Chembiochem. 20, 1514-1518 (2019).
PubMed: 30770638

Assembly members:

Assembly members:
(ACE)-GLY-CYS-PRO-CYS-ILE-TRP-PRO-GLU-LEU-CYS-PRO-TRP-ILE-ARG-SER-CYS-(NH2), polymer, 18 residues, 1888.306 Da.

Natural source:

Natural source: Common Name: not available Taxonomy ID: 1977402 Superkingdom: Viruses Kingdom: Loebvirae Genus/species: Inovirus not available

Experimental source:

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

Entity Sequences (FASTA):

Entity Sequences (FASTA):
(ACE)-GLY-CYS-PRO-CYS-ILE-TRP-PRO-GLU-LEU-CYS-PRO-TRP-ILE-ARG-SER-CYS-(NH2): XGCPCIWPELCPWIRSCX

Data sets:

assigned_chemical_shifts
- assigned_chemical_shifts_1

Data type	Count
13C chemical shifts	60
15N chemical shifts	17
1H chemical shifts	121

Additional metadata:

Assembly
Samples and Experiments
Software
Spectrometers
Hide all

Assembly:

Entity Assembly ID	Entity Name	Entity ID
1	entity_1	1

Entities:

Entity 1, entity_1 18 residues - 1888.306 Da.

1

ACE

GLY

CYS

PRO

CYS

ILE

TRP

PRO

GLU

LEU

2

CYS

PRO

TRP

ILE

ARG

SER

CYS

NH2

Samples:

sample_1: pb-13 4.3 ± 0.3 mM; acetonitrile 50%; H2O%; water 50%

sample_conditions_1: ionic strength: 0 Not defined; pH: 1.0; pressure: 1 atm; temperature: 278 K

sample_conditions_2: ionic strength: 0 Not defined; pH: 1.0 pD; pressure: 1 atm; temperature: 278 K

Experiments:

Name	Sample	Sample state	Sample conditions
2D 1H-15N HSQC	sample_1	isotropic	sample_conditions_1
2D 1H-13C HSQC	sample_1	isotropic	sample_conditions_1
2D 1H-1H TOCSY	sample_1	isotropic	sample_conditions_1
2D 1H-1H NOESY	sample_1	isotropic	sample_conditions_1
2D 1H-13C HSQC	sample_1	isotropic	sample_conditions_2
2D 1H-1H TOCSY	sample_1	isotropic	sample_conditions_2
2D 1H-1H NOESY	sample_1	isotropic	sample_conditions_2

Software:

X-PLOR NIH v2.48, Schwieters, Kuszewski, Tjandra and Clore - refinement

X-PLOR NIH v2.48, Schwieters, Kuszewski, Tjandra and Clore - structure calculation

Sparky, Goddard - chemical shift assignment

Sparky, Goddard - peak picking

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