BMRB Entry 36214

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PDB ID:
Entry in NMR Restraints Grid
Validation report in NRG-CING
Chem Shift validation: AVS_full
BMRB Entry DOI: doi:10.13018/BMR36214
MolProbity Validation Chart

NMR-STAR file interactive viewer.
NMR-STAR v3 text file.
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Title:
Solution Structure of Bicyclic Peptide pb-18
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-GLU-PRO-SER-TYR-LEU-CYS-PRO-TRP-LEU-PRO-GLY-CYS-(NH2), polymer, 18 residues, 1749.086 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-GLU-PRO-SER-TYR-LEU-CYS-PRO-TRP-LEU-PRO-GLY-CYS-(NH2): XGCPCEPSYLCPWLPGCX

Data sets:
Data typeCount
13C chemical shifts55
15N chemical shifts14
1H chemical shifts105

Additional metadata:

  • Assembly
  • Samples and Experiments
  • Software
  • Spectrometers
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Assembly:

Entity Assembly IDEntity NameEntity ID
1entity_11

Entities:

Entity 1, entity_1 18 residues - 1749.086 Da.

1   ACEGLYCYSPROCYSGLUPROSERTYRLEU
2   CYSPROTRPLEUPROGLYCYSNH2

Samples:

sample_1: pb-18 0.9 ± 0.2 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:

NameSampleSample stateSample conditions
2D 1H-15N HSQCsample_1isotropicsample_conditions_1
2D 1H-13C HSQCsample_1isotropicsample_conditions_1
2D 1H-1H TOCSYsample_1isotropicsample_conditions_1
2D 1H-1H NOESYsample_1isotropicsample_conditions_1
2D 1H-13C HSQCsample_1isotropicsample_conditions_2
2D 1H-1H NOESYsample_1isotropicsample_conditions_2
2D 1H-1H TOCSYsample_1isotropicsample_conditions_2

Software:

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

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

Sparky, Goddard - peak picking

Sparky, Goddard - chemical shift assignment

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