View & Download CD data for CD0000129000

BH1501 Protein (nachbac, bacterial voltage gated sodium channel)


Citation: Powl, A.M, O'Reilly, A.O, Miles, A.M. and Wallace, B.A. 2010 PNAS 107 14064-14069


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 v1.2.5, 2011-09-05, 10:10am. - PASS

At a glance
Downloads 1423
Depositor Andrew Miles
Uniprot Q9KCR8
Alpha Fold
PDB
EC
CATH Class
Protein Type membrane

Sample

Protein Name BH1501 protein ?
Alternative Protein Names NaChBac, Bacterial voltage gated sodium channel ?
Source Organism Bacillus halodurans ?
Protein Supplier A.Powl, (Wallace group) Birkbeck college, Uni. London ?
Expression System or natural source E. coli ?
Expressed As Wild-type ?
Mutation Details No data provided ?
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 2011-09-07 ?

Experiment

CD or SRCD SRCD ?
Protein Concentration (mg/ml) 1.03 ?
Concentration Quantification Method Nanodrop ?
Protein Purity (%) 95 ?
Purity Quantification Method SDS gels ?
Buffer Contents and Concentrations 20mM phosphate pH 7.6, 50mM NaCl, 0.3% cymal 5 ?
Baseline Contents 20mM phosphate pH 7.6, 50mM NaCl, 0.3% cymal 5 ?
Experimental Temperature (C) 4 ?
Instrument or beamline Soleil DISCO ?
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 Continuous ?
Maximum (highest) wavelength, nm 280 ?
Minimum (lowest) wavelength, nm 183 ?
Criteria for low wavelength cutoff HT value ?
Wavelength interval, nm 1 ?
Dwell or Averaging time, seconds 1 ?
Experimental Collection date 2009-10-21 ?
Local Spectrum Identifier as00148 ?

Calibration

CSA or ACS CSA ?
Dichroism Units for CSA Standard Millidegrees (theta) ?
Final Spectrum Calibrated YES ?
CSA/ACS Standard Concentration (mg/ml) 5.87 ?
CSA/ACS Pathlength (mm) 0.10 ?
CSA/ACS Zeroed at - ?
CSA/ACS Date Measured 2010-10-21 ?
CSA/ACS Ratio (192.5nm and 290.0 nm) 1.93 ?
CD signal at 290nm (mdeg) 21.7 ?
CSA/ACS Experiment temperature, C 25 ?

Data process.

Molecular Weight 33619.6 ?
Number of Residues 294 ?
Mean Residue Weight 114.7 ?
Data Processing Software Name CDTool ?
Data Processing Software Version 1.4 ?
Wavelength Range for Zeroing 264-271 ?
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 20663949 ?
Cath Classification No data provided ?
Sequence MGSSHHHHHH SSGLVPRGSH MKMEARQKQN SFTSKMQKIV NHRAFTFTVI ALILFNALIV GIETYPRIYA DHKWLFYRID LVLLWIFTIE IAMRFLASNP KSAFFRSSWN WFDFLIVAAG HIFAGAQFVT VLRILRVLRV LRAISVVPSL RRLVDALVMT IPALGNILIL MSIFFYIFAV IGTMLFQHVS PEYFGNLQLS LLTLFQVVTL ESWASGVMRP IFAEVPWSWL YFVSFVLIGT FIIFNLFIGV IVNNVEKAEL TDNEEDGEAD GLKQEISALR KDVAELKSLL KQSK ?
Type of protein membrane ?
Keyword/phrase A voltage-gated sodium channel ?
Keyword/phrase B c-terminal domain ?
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 Powl, A.M, O'Reilly, A.O, Miles, A.M. and Wallace, B.A. ?
Publication Year 2010 ?
Publication Journal PNAS ?
Publication Title Synchrotron radiation circular dichroism spectroscopy-defined structure of the C-terminal domain of NaChBac and its role in channel assembly. ?
Publication Volume 107 ?
Publication Pages 14064-14069 ?

Depositor

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

Validation report compiled by Validichro v1.2.5, 2011-09-05, 10:10am. - 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 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 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.