View & Download CD data for CD0001197000

Sodium/potassium-transporting ATPase (na,k,atpase)


Citation: Andrew J. Miles, B. A. Wallace, and Mikael Esmann 2011 BBA biomembranes 1808 2573-2580


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, 2012-02-02, 2:27pm. - PASS

At a glance
Downloads 1707
Depositor Andrew Miles
Uniprot Q4H132
Q70Q12
Alpha Fold
PDB 2zxe
EC -
CATH Class 2.70.150.10 1.20.1110.10 3.40.50.1000 3.40.1110.10
Protein Type membrane

Sample

Protein Name Sodium/potassium-transporting ATPase ?
Alternative Protein Names Na,K,ATPase ?
Source Organism Squalus acanthias ?
Protein Supplier M.Esmann, Uni. Aarhus, Denmark ?
Expression System or natural source Natural source ?
Expressed As Wild-type ?
Mutation Details No data provided ?
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 2012-02-02 ?

Experiment

CD or SRCD SRCD ?
Protein Concentration (mg/ml) 4.01 ?
Concentration Quantification Method Lowery (Calibrated by QAA) ?
Protein Purity (%) No data provided ?
Purity Quantification Method No data provided ?
Buffer Contents and Concentrations membrane +10 mM Tris, 25 mM K2SO4 and 25% glycerol (pH 7.4) ?
Baseline Contents membrane +10 mM Tris, 25 mM K2SO4 and 25% glycerol (pH 7.4) ?
Experimental Temperature (C) 35 ?
Instrument or beamline ISA CD1 ?
Detector Angle (Scattering Angle) No data provided ?
Sample Cell Pathlength (cm) 0.0015 ?
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 2 ?
Experimental Collection date 2010-04-30 ?
Local Spectrum Identifier a17431 ?

Calibration

CSA or ACS CSA ?
Dichroism Units for CSA Standard Millidegrees (theta) ?
Final Spectrum Calibrated YES ?
CSA/ACS Standard Concentration (mg/ml) 6.00 ?
CSA/ACS Pathlength (mm) 0.10 ?
CSA/ACS Zeroed at 235-240 ?
CSA/ACS Date Measured 2010-04-30 ?
CSA/ACS Ratio (192.5nm and 290.0 nm) 2.06 ?
CD signal at 290nm (mdeg) 20.01 ?
CSA/ACS Experiment temperature, C 25 ?

Data process.

Molecular Weight 121388.5 ?
Number of Residues 1102 ?
Mean Residue Weight 110.3 ?
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 0.363 ?
DSSP value: 3-10 helix 0.036 ?
DSSP value: pi helix 0.004 ?
DSSP value: beta strand 0.132 ?
DSSP value: beta bridge 0.009 ?
DSSP value: bonded turn 0.102 ?
DSSP value: bend 0.081 ?
DSSP value: loop or irregular 0.273 ?

Tertiary

PDB ID 2zxe ?
UniProt ID Q4H132,Q70Q12 ?
Enzyme Classification (EC) - ?
Medline Entry 19458722 ?
Cath Classification 2.70.150.10 1.20.1110.10 3.40.50.1000 3.40.1110.10 ?
Sequence MGKGTASDKY EPAATSENAT KSKKKGKKDK IDKKRDLDEL KKEVSMDDHK LSLDELHNKY GTDLTRGLTN ARAKEILARD GPNSLTPPPT TPEWIKFCRQ LFGGFSILLW IGAILCFLAY GIQAATEDEP ANDNLYLGVV LSTVVIVTGC FSYYQEAKSS RIMDSFKNMV PQQALVIRDG EKSTINAEFV VAGDLVEVKG GDRIPADLRI ISAHGCKVDN SSLTGESEPQ TRSPEFSSEN PLETRNIAFF STNCVEGTAR GVVVYTGDRT VMGRIATLAS GLEVGRTPIA IEIEHFIHII TGVAVFLGVS FFILSLILGY SWLEAVIFLI GIIVANVPEG LLATVTVCLT LTAKRMARKN CLVKNLEAVE TLGSTSTICS DKTGTLTQNR MTVAHMWFDN QIHEADTTEN QSGAAFDKTS ATWSALSRIA ALCNRAVFQA GQDNVPILKR SVAGDASESA LLKCIELCCG SVQGMRDRNP KIVEIPFNST NKYQLSIHEN EKSSESRYLL VMKGAPERIL DRCSTILLNG AEEPLKEDMK EAFQNAYLEL GGLGERVLGF CHFALPEDKY NEGYPFDADE PNFPTTDLCF VGLMAMIDPP RAAVPDAVGK CRSAGIKVIM VTGDHPITAK AIAKGVGIIS EGNETIEDIA ARLNIPIGQV NPRDAKACVV HGSDLKDLST EVLDDILHYH TEIVFARTSP QQKLIIVEGC QRQGAIVAVT GDGVNDSPAL KKADIGVAMG ISGSDVSKQA ADMILLDDNF ASIVTGVEEG RLIFDNLKKS IAYTLTSNIP EITPFLVFII GNVPLPLGTV TILCIDLGTD MVPAISLAYE QAESDIMKRQ PRNPKTDKLV NERLISMAYG QIGMIQALGG FFSYFVILAE NGFLPMDLIG KRVRWDDRWI SDVEDSFGQQ WTYEQRKIVE FTCHTSFFIS IVVVQWADLI ICKTRRNSIF QQGMKNKILI FGLFEETALA AFLSYCPGTD VALRMYPLKP SWWFCAFPYS LIIFLYDEMR RFIIRRSPGG WVEQETYYMD PEGPDNDERF TYDYYRLRVV GLIVAAVLCV IGIIILLAGK CRCKFNQNKR TRSNSGTATA QHLLQPGEAT EC ?
Type of protein membrane ?
Keyword/phrase A Thermal stability ?
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 Andrew J. Miles, B. A. Wallace, and Mikael Esmann ?
Publication Year 2011 ?
Publication Journal BBA biomembranes ?
Publication Title Correlation of structural and functional thermal stability of the integral membrane protein Na,K-ATPase ?
Publication Volume 1808 ?
Publication Pages 2573-2580 ?

Depositor

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

Validation report compiled by Validichro v1.2.5, 2012-02-02, 2:27pm. - 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.