View & Download CD data for CD0006121000

Translocated Actin Recruiting Phosphoprotein (tarp)


Citation: James Tolchard, Samuel J. Walpole, Andrew J. Miles, Robin M. Maytum, Lawrence A. Eaglen, Ted Hackstadt, B. A. Wallace, Tharin M. A. Blumenschein 2018 Nature, Scientific Reports Article number: 1960 8


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
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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 Delta Epsilon Download
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Validation report compiled by Validichro v1.4.0.1, 2019-11-20, 3:30pm. - FLAG (Incomplete)

At a glance
Downloads 1012
Depositor Andrew Miles
Uniprot Q6GX35
Alpha Fold
PDB
EC
CATH Class
Protein Type soluble globular

Sample

Protein Name translocated actin recruiting phosphoprotein ?
Alternative Protein Names Tarp ?
Source Organism Chlamydia trachomatis ?
Protein Supplier author ?
Expression System or natural source E. coli ?
Expressed As Wild-type ?
Mutation Details 726-825 ?
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 2019-11-21 ?

Experiment

CD or SRCD SRCD ?
Protein Concentration (mg/ml) 1.75 ?
Concentration Quantification Method Nanodrop ?
Protein Purity (%) No data provided ?
Purity Quantification Method No data provided ?
Buffer Contents and Concentrations 2mM Tris, 2mM CaCl2, 0.2mM ATP ?
Baseline Contents 2mM Tris, 2mM CaCl2, 0.2mM ATP ?
Experimental Temperature (C) 25 ?
Instrument or beamline ISA CD1 ?
Detector Angle (Scattering Angle) No data provided ?
Sample Cell Pathlength (cm) 0.00507 ?
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 Continuous ?
Maximum (highest) wavelength, nm 280 ?
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 2013-08-29 ?
Local Spectrum Identifier a35215 ?

Calibration

CSA or ACS CSA ?
Dichroism Units for CSA Standard Millidegrees (theta) ?
Final Spectrum Calibrated YES ?
CSA/ACS Standard Concentration (mg/ml) 7.25 ?
CSA/ACS Pathlength (mm) 0.1 ?
CSA/ACS Zeroed at - ?
CSA/ACS Date Measured 2013-08-28 ?
CSA/ACS Ratio (192.5nm and 290.0 nm) 2.07 ?
CD signal at 290nm (mdeg) 25.5 ?
CSA/ACS Experiment temperature, C 25 ?

Data process.

Molecular Weight 10411 ?
Number of Residues 105 ?
Mean Residue Weight 100 ?
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 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 Q6GX35 ?
Enzyme Classification (EC) No data provided ?
Medline Entry No data provided ?
Cath Classification No data provided ?
Sequence GPLGSDDSGS VSSSESDKNA SVGNDGPAMK DILSAVRKHL DVVYPGDNGG STEGPLQANQ TLGDIVQDME TTGTSQETVV SPWKGSTSST GSAGGSGSVQ TLLPS ?
Type of protein soluble globular ?
Keyword/phrase A IDP ?
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 James Tolchard, Samuel J. Walpole, Andrew J. Miles, Robin M. Maytum, Lawrence A. Eaglen, Ted Hackstadt, B. A. Wallace, Tharin M. A. Blumenschein ?
Publication Year 2018 ?
Publication Journal Nature, Scientific Reports Article number: 1960 ?
Publication Title The Intrinsically Disordered Chlamydia Tarp Protein Binds Actin With A Partially Preformed Helix ?
Publication Volume 8 ?
Publication Pages No data provided ?

Depositor

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

Validation report compiled by Validichro v1.4.0.1, 2019-11-20, 3:30pm. - FLAG (Incomplete)

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 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 FLAG ?
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 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.