Alkaline Phosphatase (apase)

Citation: Lees, J.G., Wien, F., Miles, A.J. & Wallace, B.A., 2006 Bioinformatics 22 1955-1962

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 v1.4.0.1, 2022-09-27 10:12:17. - PASS

At a glance

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Sample

Protein Name	Alkaline phosphatase	?
Alternative Protein Names	APase	?
Source Organism	E.coli	?
Protein Supplier	Worthington Biochemical Corp	?
Expression System or natural source	E. coli	?
Expressed As	Wild-type	?
Mutation Details	none	?
Expression tags (if any)	none	?
Ligands Present and Concentration or ratio	none	?
Macromolecular Partner(s) and Concentration or ratio	n	?
Deposition Date	2015-04-27	?

Experiment

CD or SRCD	SRCD	?
Protein Concentration (mg/ml)	2.7	?
Concentration Quantification Method	Nanodrop	?
Protein Purity (%)	>95%	?
Purity Quantification Method	Supplier value	?
Buffer Contents and Concentrations	water	?
Baseline Contents	water	?
Experimental Temperature (C)	4	?
Instrument or beamline	ISA CD1	?
Detector Angle (Scattering Angle)	No data provided	?
Sample Cell Pathlength (cm)	0.0024	?
Cell Pathlength Calibration Method	Interferometry	?
Sample Cell Type	Cylindrical-Demountable	?
Sample Cell Composition	Suprasil	?
Sample Chamber Atmosphere	Nitrogen	?
Number of repeat scans	3	?
Continuous or Stepped scan	Stepped	?
Maximum (highest) wavelength, nm	280	?
Minimum (lowest) wavelength, nm	173	?
Criteria for low wavelength cutoff	HT value	?
Wavelength interval, nm	1	?
Dwell or Averaging time, seconds	2	?
Experimental Collection date	2014-09-21	?
Local Spectrum Identifier	a41158	?

Calibration

CSA or ACS	CSA	?
Dichroism Units for CSA Standard	Millidegrees (theta)	?
Final Spectrum Calibrated	YES	?
CSA/ACS Standard Concentration (mg/ml)	7.3	?
CSA/ACS Pathlength (mm)	0.1	?
CSA/ACS Zeroed at	235-240	?
CSA/ACS Date Measured	2014-09-21	?
CSA/ACS Ratio (192.5nm and 290.0 nm)	2.12	?
CD signal at 290nm (mdeg)	25.99	?
CSA/ACS Experiment temperature, C	25	?

Data process.

Molecular Weight	47199	?
Number of Residues	450	?
Mean Residue Weight	105.1	?
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	0.278	?
DSSP value: 3-10 helix	0.033	?
DSSP value: pi helix	0.00	?
DSSP value: beta strand	0.185	?
DSSP value: beta bridge	0.027	?
DSSP value: bonded turn	0.127	?
DSSP value: bend	0.122	?
DSSP value: loop or irregular	0.227	?

Tertiary

PDB ID	1ed9	?
UniProt ID	P00634	?
Enzyme Classification (EC)	3.1.3.1	?
Medline Entry	16787970 (pubmed)	?
Cath Classification	3.40.720.10	?
Sequence	RTPEMPVLEN RAAQGDITAP GGARRLTGDQ TAALRDSLSD KPAKNIILLI GDGMGDSEIT AARNYAEGAG GFFKGIDALP LTGQYTHYAL NKKTGKPDYV TDSAASATAW STGVKTYNGA LGVDIHEKDH PTILEMAKAA GLATGNVSTA ELQDATPAAL VAHVTSRKCY GPSATSEKCP GNALEKGGKG SITEQLLNAR ADVTLGGGAK TFAETATAGE WQGKTLREQA QARGYQLVSD AASLNSVTEA NQQKPLLGLF ADGNMPVRWL GPKATYHGNI DKPAVTCTPN PQRNDSVPTL AQMTDKAIEL LSKNEKGFFL QVEGASIDKQ DHAANPCGQI GETVDLDEAV QRALEFAKKE GNTLVIVTAD HAHASQIVAP DTKAPGLTQA LNTKDGAVMV MSYGNSEEDS QEHTGSQLRI AAYGPHAANV VGLTDQTDLF YTMKAALGLK	?
Type of protein	soluble globular	?
Keyword/phrase A	SP175	?
Keyword/phrase B	single domain	?
Keyword/phrase C	mixed alpha beta	?
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	Lees, J.G., Wien, F., Miles, A.J. & Wallace, B.A.,	?
Publication Year	2006	?
Publication Journal	Bioinformatics	?
Publication Title	A reference database for circular dichroism spectroscopy covering fold and secondary structure space	?
Publication Volume	22	?
Publication Pages	1955-1962	?

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 v1.4.0.1, 2022-09-27 10:12:17. - PASS

Depositors Notes:

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		?
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		?