View & Download CD data for CD0003675012

Lysozyme (1,4-beta-n-acetylmuramidase c)

Citation: Filip Meersman, Canan Atilgan, Andrew J. Miles, Reto Bader, Weifeng Shang, Andr Matagne, B.A. Wallace, Michel H.J. Koch 2010 Biophysical Journal 99 2255-2263

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)

CSA/ACS Standard Spectrum	Millidegrees (theta)	Download	View Plot
Raw Sample Spectra	Millidegrees (theta)	Download	View Plot
Raw Sample Spectra 2	Millidegrees (theta)	Download	View Plot
Raw Sample Spectra 3	Millidegrees (theta)	Download	View Plot
Raw Baseline Spectra	Millidegrees (theta)	Download	View Plot
Raw Baseline Spectra 2	Millidegrees (theta)	Download	View Plot
Raw Baseline Spectra 3	Millidegrees (theta)	Download	View Plot
Average Sample	Millidegrees (theta)	Download	View Plot
Averaged Baseline	Millidegrees (theta)	Download	View Plot
HT / High Voltage / Dynode Spectra	HT/Dynode Units	Download	View Plot
HT / High Voltage / Dynode Spectra 2	HT/Dynode Units	Download	View Plot
HT / High Voltage / Dynode Spectra 3	HT/Dynode Units	Download	View Plot
Net Smoothed Spectrum	Millidegrees (theta)	Download	View Plot
Final Processed Spectrum	Delta Epsilon	Download	View Plot

Validation report compiled by Validichro v1.2.5, 2012-08-14, 2:13pm. - FLAG

At a glance

Downloads	1042
Depositor	Andrew Miles
Uniprot	P00698
Alpha Fold
PDB	193l
EC	3.2.1.17
CATH Class	1.10.530.10
Protein Type	soluble globular

Go to section

Sample
Experiment
Calibration
Data Process.
Sec. Struct.
Tertiary
Depositor
Validation

Sample

Protein Name	lysozyme	?
Alternative Protein Names	1,4-beta-N-acetylmuramidase C	?
Source Organism	Gallus gallus	?
Protein Supplier	Worthington Biochemicals corporation, LS002933	?
Expression System or natural source	Natural source	?
Expressed As	Wild-type	?
Mutation Details	No data provided	?
Expression tags (if any)	No data provided	?
Ligands Present and Concentration or ratio	No data provided	?
Macromolecular Partner(s) and Concentration or ratio	No data provided	?
Deposition Date	2012-08-15	?

Experiment

CD or SRCD	SRCD	?
Protein Concentration (mg/ml)	1.17	?
Concentration Quantification Method	Nanodrop	?
Protein Purity (%)	No data provided	?
Purity Quantification Method	No data provided	?
Buffer Contents and Concentrations	H2O	?
Baseline Contents	H2O	?
Experimental Temperature (C)	80	?
Instrument or beamline	ISA CD1	?
Detector Angle (Scattering Angle)	No data provided	?
Sample Cell Pathlength (cm)	0.01	?
Cell Pathlength Calibration Method	Interferometry	?
Sample Cell Type	Cylindrical	?
Sample Cell Composition	Suprasil	?
Sample Chamber Atmosphere	Nitrogen	?
Number of repeat scans	3	?
Continuous or Stepped scan	Stepped	?
Maximum (highest) wavelength, nm	270	?
Minimum (lowest) wavelength, nm	175	?
Criteria for low wavelength cutoff	HT value	?
Wavelength interval, nm	1	?
Dwell or Averaging time, seconds	2	?
Experimental Collection date	2009-08-01	?
Local Spectrum Identifier	a14971	?

Calibration

CSA or ACS	CSA	?
Dichroism Units for CSA Standard	Millidegrees (theta)	?
Final Spectrum Calibrated	YES	?
CSA/ACS Standard Concentration (mg/ml)	6.6	?
CSA/ACS Pathlength (mm)	0.1	?
CSA/ACS Zeroed at	235-245	?
CSA/ACS Date Measured	2009-08-01	?
CSA/ACS Ratio (192.5nm and 290.0 nm)	2.1	?
CD signal at 290nm (mdeg)	21.68	?
CSA/ACS Experiment temperature, C	25	?

Data process.

Molecular Weight	14313	?
Number of Residues	129	?
Mean Residue Weight	111.8	?
Data Processing Software Name	CDTool	?
Data Processing Software Version	1.4	?
Wavelength Range for Zeroing	263-270	?
Number of Smoothing Points	7	?

Sec. struct.

Secondary Structure Calculated from	Crystal structure	?
DSSP value: alpha helix	0.302	?
DSSP value: 3-10 helix	0.101	?
DSSP value: pi helix	0.000	?
DSSP value: beta strand	0.062	?
DSSP value: beta bridge	0.047	?
DSSP value: bonded turn	0.240	?
DSSP value: bend	0.093	?
DSSP value: loop or irregular	0.155	?

Tertiary

PDB ID	193l	?
UniProt ID	P00698	?
Enzyme Classification (EC)	3.2.1.17	?
Medline Entry	20923660	?
Cath Classification	1.10.530.10	?
Sequence	KVFGRCELAA AMKRHGLDNY RGYSLGNWVC AAKFESNFNT QATNRNTDGS TDYGILQINS RWWCNDGRTP GSRNLCNIPC SALLSSDITA SVNCAKKIVS DGNGMNAWVA WRNRCKGTDV QAWIRGCRL	?
Type of protein	soluble globular	?
Keyword/phrase A	Thermal stability	?
Keyword/phrase B	No data provided	?
Keyword/phrase C	No data provided	?
Keyword/phrase D	No data provided	?
Keyword/phrase E	No data provided	?
Keyword/phrase F	No data provided	?
Keyword/phrase G	No data provided	?
Keyword/phrase H	No data provided	?
Keyword/phrase I	No data provided	?
Keyword/phrase J	No data provided	?
Publication Authors	Filip Meersman, Canan Atilgan, Andrew J. Miles, Reto Bader, Weifeng Shang, Andr Matagne, B.A. Wallace, Michel H.J. Koch	?
Publication Year	2010	?
Publication Journal	Biophysical Journal	?
Publication Title	Consistent picture of the reversible thermal unfolding of hen egg-white lysozyme from experiment and molecular dynamics.	?
Publication Volume	99	?
Publication Pages	2255-2263	?

Depositor

Depositor Name	Andrew Miles	?
Department/School name	crystallography	?
University/Institution/Corporation	Birkbeck	?
Depositor Country	United Kingdom	?
Name of Principal Investigator (if not depositor)	B.A.Wallace	?

Validation report compiled by Validichro v1.2.5, 2012-08-14, 2:13pm. - FLAG

Depositors Notes: Standard deviation is flagged because the spectrum is noisy at this temperature. Projection test is flagged because the denatured protein has an unusual spectrum

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	PASS	?
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	FLAG	?
Noise: 260-270nm	PASS	?
Flat topped peaks	PASS	?
Wavelength range	PASS	?
Interval resolution	PASS	?
High Tension Voltage 240-260nm	PASS	?
Projection Test	FLAG	?
Standard Deviation At Peak	PASS	?
Depositor Note	Standard deviation is flagged because the spectrum is noisy at this temperature. Projection test is flagged because the denatured protein has an unusual spectrum	?