View & Download CD data for CD0006395001

BH1501 Protein T1 Chimera (nachbac bacterial voltage gated sodium channel t1 chimera)


Citation: O’Reilly A.O., Powl A.M., D’Avanzo N., Miles A.J., Nichols C.G., Wallace B.A. 2022 FEBS letters


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 Download
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Raw Baseline Spectra Download
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Average Sample Download
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Averaged Baseline Download
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HT / High Voltage / Dynode Spectra HT/Dynode Units Download
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Net Smoothed Spectrum Download
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Final Processed Spectrum Delta_Epsilon Download
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Validation report compiled by Validichro v1.4.0.1, 2022-01-01 18:27:44. - PASS (incomplete)

At a glance
Downloads 564
Depositor Andrew Miles
Uniprot Q9KCR8
Alpha Fold
PDB
EC
CATH Class
Protein Type membrane

Sample

Protein Name BH1501 protein T1 chimera ?
Alternative Protein Names NachBac Bacterial voltage gated sodium channel T1 chimera ?
Source Organism B. halodurans ?
Protein Supplier A. O. O'Reilly ?
Expression System or natural source E. coli ?
Expressed As deletion and insertion ?
Mutation Details C, termination at position 239. Addition at N of T1-tetramerisation domain of the Kv1.2 channel ?
Expression tags (if any) N,MGSSHHHHHHSSGLVPRGSH ?
Ligands Present and Concentration or ratio No data provided ?
Macromolecular Partner(s) and Concentration or ratio No data provided ?
Deposition Date 2022-01-01 ?

Experiment

CD or SRCD CD ?
Protein Concentration (mg/ml) 1.35 ?
Concentration Quantification Method Nanodrop ?
Protein Purity (%) 95 ?
Purity Quantification Method SDS gels ?
Buffer Contents and Concentrations 20 mM sodium phosphate; pH 7.6, 100 mM NaCl, % Cymal-5 ?
Baseline Contents 20 mM sodium phosphate; pH 7.6, 100 mM NaCl, 0.3 % Cymal-5 ?
Experimental Temperature (C) 20 ?
Instrument or beamline Aviv ?
Detector Angle (Scattering Angle) No data provided ?
Sample Cell Pathlength (cm) 0.005 ?
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 180 ?
Criteria for low wavelength cutoff HT value ?
Wavelength interval, nm 1 ?
Dwell or Averaging time, seconds 1 ?
Experimental Collection date 2010-02-21 ?
Local Spectrum Identifier KBach #1 ?

Calibration

CSA or ACS CSA ?
Dichroism Units for CSA Standard Millidegrees_(theta) ?
Final Spectrum Calibrated YES ?
CSA/ACS Standard Concentration (mg/ml) 5.9 ?
CSA/ACS Pathlength (mm) 0.1 ?
CSA/ACS Zeroed at 235-245 ?
CSA/ACS Date Measured 2009-09-09 ?
CSA/ACS Ratio (192.5nm and 290.0 nm) 2.1 ?
CD signal at 290nm (mdeg) 22.8 ?
CSA/ACS Experiment temperature, C 25 ?

Data process.

Molecular Weight 46239 ?
Number of Residues 400 ?
Mean Residue Weight 116 ?
Data Processing Software Name CDTool ?
Data Processing Software Version 1.4 ?
Wavelength Range for Zeroing 255-260 ?
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 Q9KCR8 ?
Enzyme Classification (EC) No data provided ?
Medline Entry No data provided ?
Cath Classification No data provided ?
Sequence MGSSHHHHHH SSGLVPRGSH MTVATGDPAD EAAALPGHPQ DTYDPEADHE CCERVVINIS GLRFETQLKT LAQFPETLLG DPKKRMRYFD PLRNEYFFDR NRPSFDAILY YYQSGGRLRR PVNVPLDIFS EEIRFYELGE EAMEMFREDE GYIKEEERPL PENEFQKQNS FTSKMQKIVN HRAFTFTVIA LILFNALIVG IETYPRIYAD HKWLFYRIDL VLLWIFTIEI AMRFLASNPK SAFFRSSWNW FDFLIVAAGH IFAGAQFVTV LRILRVLRVL RAISVVPSLR RLVDALVMTI PALGNILILM SIFFYIFAVI GTMLFQHVSP EYFGNLQLSL LTLFQVVTLE SWASGVMRPI FAEVPWSWLY FVSFVLIGTF IIFNLFIGVI VNNVEKAELT ?
Type of protein membrane ?
Keyword/phrase A NaChBac voltage gated sodium channel ?
Keyword/phrase B T1 chimera ?
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 O’Reilly A.O., Powl A.M., D’Avanzo N., Miles A.J., Nichols C.G., Wallace B.A. ?
Publication Year 2022 ?
Publication Journal FEBS letters ?
Publication Title The T1-tetramerization Domain of Kv1.2 Rescues Expression and Preserves Function of a Truncated NaChBac Sodium Channel ?
Publication Volume No data provided ?
Publication Pages No data provided ?

Depositor

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

Validation report compiled by Validichro v1.4.0.1, 2022-01-01 18:27:44. - PASS (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 ?
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 INSUFFICIENT DATA ?
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 INSUFFICIENT DATA ?
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.