BMRB

Biological Magnetic Resonance Data Bank


A Repository for Data from NMR Spectroscopy on Proteins, Peptides, Nucleic Acids, and other Biomolecules
Member of WWPDB

BMRB Entry 30476

Title: Solution structure of the cyclic tetrapeptide, PYPV

Deposition date: 2018-06-08 Original release date: 2019-06-07

Authors: Shekhtman, A.; Breindel, L.; Zhang, Q.; Chen, H.

Citation: Shekhtman, A.; Breindel, L.; Zhang, Q.; Chen, H.. "Solution structure of the cyclic tetrapeptide, PYPV."  . ., .-..

Assembly members:
Cyclic tetrapeptide PYPV, polymer, 4 residues, 474.549 Da.

Natural source:   Common Name: Lactobacillus helveticus   Taxonomy ID: 1587   Superkingdom: Bacteria   Kingdom: not available   Genus/species: Lactobacillus helveticus

Experimental source:   Production method: chemical synthesis

Entity Sequences (FASTA):
Cyclic tetrapeptide PYPV: PYPV

Data sets:
Data typeCount
13C chemical shifts16
1H chemical shifts30

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 4 residues - 474.549 Da.

1   PROTYRPROVAL

Samples:

sample_1: cyclo(-L-Pro-L-Tyr-L-Pro-L-Val-) 1 ± 0.1 mM

sample_conditions_1: ionic strength: 0 Not defined; pH: 7.0 pH*; pressure: 1 bar; temperature: 293 K

Experiments:

NameSampleSample stateSample conditions
2D 1H-1H TOCSYsample_1isotropicsample_conditions_1
2D 1H-1H NOESYsample_1isotropicsample_conditions_1
2D 1H-1H ROESYsample_1isotropicsample_conditions_1
2D 1H-13C HSQCsample_1isotropicsample_conditions_1

Software:

CYANA v3.96, Guntert P., Guntert, Mumenthaler and Wuthrich - refinement, structure calculation

CARA, Keller and Wuthrich, Keller, Wuthrich - chemical shift assignment, peak picking

NMR spectrometers:

  • Bruker Avance III 600 MHz