View & Compare Raw Sample Spectra For CD0003899000

Microcin J25 Cyclic Branched (mccj25-lcm)


Citation: No citation information currently associated with this entry.


Citation: The PCDDB (protein circular dichroism data bank): A bioinformatics resource for protein characterisations and methods development.
Ramalli SG, Miles AJ, Janes RW, Wallace BA., J Mol Biol (2022)


Validation report compiled by Validichro v1.4.0, 2015-08-06, 8:30pm. - PASS (Incomplete)

Depositors Notes: The uniprot sequence corresponds to the 58-amino acid precursor peptide from microcin J25. The core peptide microcin J25 corresponds to the 21 C-terminal amino acids of the precursor sequence. The present peptide MccJ25-lcm is a non-lasso topoisomer of MccJ25, sharing the same amino acid sequence and macrolactam ring, but with the C-terminal tail not threaded within the macrolactam ring.

Missing Wavelengths PASS ?
Maximum Delta Epsilon PASS ?
Minimal Level of Maximum Delta Epsilon PASS ?
Peak Locations PASS ?
Feature Width PASS ?
Experimental Temperature PASS ?
UniProt sequence INSUFFICIENT DATA ?
Molecular Weight PASS ?
Number of Residues PASS ?
Mean Residue Weight value PASS ?
Concentration and Pathlength PASS ?
CSA / ACS peak ratio PASS ?
CSA / ACS Temperature PASS ?
Peak Shift test PASS ?
Standard Deviation PASS ?
Noise: 260-270nm PASS ?
Flat topped peaks PASS ?
Wavelength range PASS ?
Interval resolution PASS ?
High Tension Voltage 240-260nm PASS ?
Projection Test PASS ?
Standard Deviation At Peak PASS ?
Depositor Note The uniprot sequence corresponds to the 58-amino acid precursor peptide from microcin J25. The core peptide microcin J25 corresponds to the 21 C-terminal amino acids of the precursor sequence. The present peptide MccJ25-lcm is a non-lasso topoisomer of MccJ25, sharing the same amino acid sequence and macrolactam ring, but with the C-terminal tail not threaded within the macrolactam ring. ?

The PCDDB is a development of the Department of Biological Sciences, Institute of Structural and Molecular Biology, Birkbeck College, University of London and the School of Biological and Chemical Sciences, Queen Mary University of London, UK. It is supported by a grant from the BBSRC. Copyright of the design and implementation of this site are retained by the schools and the authors.