View & Download CD data for CD0004266000

E5


Citation: Dirk Windisch, Colin Ziegler, Stephan L. Grage, Jochen Buerck, Marcel Zeitler, Peter L. Gorkov, and Anne S. Ulrich 2015 Biophysical Journal 109 737 - 749


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 ---- Please select ---- Download
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Raw Sample Spectra Millidegrees (theta) Download
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Raw Sample Spectra 2 Millidegrees (theta) Download
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Raw Sample Spectra 3 Millidegrees (theta) Download
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Raw Baseline Spectra Millidegrees (theta) Download
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Raw Baseline Spectra 2 Millidegrees (theta) Download
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Raw Baseline Spectra 3 Millidegrees (theta) Download
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Average Sample Millidegrees (theta) Download
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Averaged Baseline Millidegrees (theta) Download
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HT / High Voltage / Dynode Spectra HT/Dynode Units Download
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HT / High Voltage / Dynode Spectra 2 HT/Dynode Units Download
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HT / High Voltage / Dynode Spectra 3 HT/Dynode Units Download
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Net Smoothed Spectrum Millidegrees (theta) Download
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Final Processed Spectrum Mean Residue Ellipticity Download
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Validation report compiled by Validichro v1.4.0, 2015-08-26, 4:13pm. - FLAG (Incomplete)

At a glance
Downloads 1585
Depositor Jochen Buerck
Uniprot Q6XHC0
Alpha Fold
PDB
EC
CATH Class
Protein Type membrane

Sample

Protein Name E5 ?
Alternative Protein Names No data provided ?
Source Organism none ?
Protein Supplier Institute of Biological Interfaces ?
Expression System or natural source E. coli ?
Expressed As Mutant (deletions) ?
Mutation Details delF36-F44 ?
Expression tags (if any) deltaLE_Trp_Leader ?
Ligands Present and Concentration or ratio No data provided ?
Macromolecular Partner(s) and Concentration or ratio No data provided ?
Deposition Date 2015-08-26 ?

Experiment

CD or SRCD SRCD ?
Protein Concentration (mg/ml) 1.044 ?
Concentration Quantification Method Nanodrop ?
Protein Purity (%) No data provided ?
Purity Quantification Method HPLC ?
Buffer Contents and Concentrations TCEP 10mM ?
Baseline Contents DNPC 23,2mM, TCEP 10mM, H2O ?
Experimental Temperature (C) 37 ?
Instrument or beamline UV-CD12 ?
Detector Angle (Scattering Angle) No data provided ?
Sample Cell Pathlength (cm) 0.0013 ?
Cell Pathlength Calibration Method Interferometry ?
Sample Cell Type Cylindrical-Demountable ?
Sample Cell Composition CaF2 ?
Sample Chamber Atmosphere Nitrogen ?
Number of repeat scans 3 ?
Continuous or Stepped scan Stepped ?
Maximum (highest) wavelength, nm 270 ?
Minimum (lowest) wavelength, nm 179 ?
Criteria for low wavelength cutoff HT value ?
Wavelength interval, nm 0.5 ?
Dwell or Averaging time, seconds 1.5 ?
Experimental Collection date 2012-12-06 ?
Local Spectrum Identifier No data provided ?

Calibration

CSA or ACS ACS ?
Dichroism Units for CSA Standard No data provided ?
Final Spectrum Calibrated YES ?
CSA/ACS Standard Concentration (mg/ml) 9.75 ?
CSA/ACS Pathlength (mm) 0.1 ?
CSA/ACS Zeroed at 230-240 nm ?
CSA/ACS Date Measured 2012-12-04 ?
CSA/ACS Ratio (192.5nm and 290.0 nm) 2.051 ?
CD signal at 290nm (mdeg) 30.44 ?
CSA/ACS Experiment temperature, C 25 ?

Data process.

Molecular Weight 4182.2 ?
Number of Residues 35 ?
Mean Residue Weight 123.01 ?
Data Processing Software Name CDTool ?
Data Processing Software Version 1.4 ?
Wavelength Range for Zeroing 250-260 nm ?
Number of Smoothing Points 15 ?

Sec. struct.

Secondary Structure Calculated from No data provided ?
DSSP value: alpha helix No data provided ?
DSSP value: 3-10 helix No data provided ?
DSSP value: pi helix No data provided ?
DSSP value: beta strand No data provided ?
DSSP value: beta bridge No data provided ?
DSSP value: bonded turn No data provided ?
DSSP value: bend No data provided ?
DSSP value: loop or irregular No data provided ?

Tertiary

PDB ID No data provided ?
UniProt ID Q6XHC0 ?
Enzyme Classification (EC) No data provided ?
Medline Entry No data provided ?
Cath Classification No data provided ?
Sequence GMPNLWFLLF LGLVAAMQLL LLLFLLLFFL VYWDH ?
Type of protein membrane ?
Keyword/phrase A E5 ?
Keyword/phrase B oncoprotein ?
Keyword/phrase C bovine papillomavirus ?
Keyword/phrase D small unilamellar DNPC lipid vesicles ?
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 Dirk Windisch, Colin Ziegler, Stephan L. Grage, Jochen Buerck, Marcel Zeitler, Peter L. Gorkov, and Anne S. Ulrich ?
Publication Year 2015 ?
Publication Journal Biophysical Journal ?
Publication Title Hydrophobic Mismatch Drives the Interaction of E5 with the Transmembrane Segment of PDGF Receptor ?
Publication Volume 109 ?
Publication Pages 737 - 749 ?

Depositor

Depositor Name Jochen Buerck ?
Department/School name Institute of Biological Interfaces (IBG-2) ?
University/Institution/Corporation Karlsruhe Institute of Technology ?
Depositor Country Germany ?
Name of Principal Investigator (if not depositor) Jochen Buerck ?

Validation report compiled by Validichro v1.4.0, 2015-08-26, 4:13pm. - FLAG (Incomplete)

Depositors Notes: Flag for concentration/path length non-optimal ratio: we used relatively low conc. of peptide due to high background absorption induced by unsaturated lipid to get good signal-to-noise ratio below 200 nm. Flag for UniProt sequence: deletions at C terminus F36-F44

Missing Wavelengths FAIL ?
Maximum Delta Epsilon INSUFFICIENT DATA ?
Minimal Level of Maximum Delta Epsilon INSUFFICIENT DATA ?
Peak Locations INSUFFICIENT DATA ?
Feature Width PASS ?
Experimental Temperature PASS ?
UniProt sequence FLAG ?
Molecular Weight PASS ?
Number of Residues PASS ?
Mean Residue Weight value PASS ?
Concentration and Pathlength FLAG ?
CSA / ACS peak ratio PASS ?
CSA / ACS Temperature PASS ?
Peak Shift test PASS ?
Standard Deviation PASS ?
Noise: 260-270nm INSUFFICIENT DATA ?
Flat topped peaks PASS ?
Wavelength range INSUFFICIENT DATA ?
Interval resolution PASS ?
High Tension Voltage 240-260nm PASS ?
Projection Test INSUFFICIENT DATA ?
Standard Deviation At Peak PASS ?
Depositor Note Flag for concentration/path length non-optimal ratio: we used relatively low conc. of peptide due to high background absorption induced by unsaturated lipid to get good signal-to-noise ratio below 200 nm. Flag for UniProt sequence: deletions at C terminus F36-F44 ?

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.