View & Download CD data for CD0003992001

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

Citation: Andrew J. Miles, Natalya U. Fedosova, Soren V. Hoffmann, B.A. Wallace, Mikael Esmann 2013 Biochemical and Biophysical Research Communications 435 300-305

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	View Plot
Raw Sample Spectra	Millidegrees (theta)	Download	View Plot
Raw Sample Spectra 2	Millidegrees (theta)	Download	View Plot
Raw Sample Spectra 3	Millidegrees (theta)	Download	View Plot
Raw Baseline Spectra	Millidegrees (theta)	Download	View Plot
Raw Baseline Spectra 2	Millidegrees (theta)	Download	View Plot
Raw Baseline Spectra 3	Millidegrees (theta)	Download	View Plot
Average Sample	Millidegrees (theta)	Download	View Plot
Averaged Baseline	Millidegrees (theta)	Download	View Plot
HT / High Voltage / Dynode Spectra	HT/Dynode Units	Download	View Plot
HT / High Voltage / Dynode Spectra 2	HT/Dynode Units	Download	View Plot
HT / High Voltage / Dynode Spectra 3	HT/Dynode Units	Download	View Plot
Net Smoothed Spectrum	Millidegrees (theta)	Download	View Plot
Final Processed Spectrum	Delta Epsilon	Download	View Plot

Validation report compiled by Validichro v1.2.5, 2012-08-20, 1:52pm. - PASS

At a glance

Downloads	1417
Depositor	Andrew Miles
Uniprot	P05024 P05027 Q58K79
Alpha Fold
PDB	3n23
EC	3.6.3.9
CATH Class	2.70.150.10, 1.20.1110.10, 3.40.50.1000, 3.40.1110.10
Protein Type	membrane

Go to section

Sample
Experiment
Calibration
Data Process.
Sec. Struct.
Tertiary
Depositor
Validation

Sample

Protein Name	Sodium/potassium-transporting ATPase	?
Alternative Protein Names	Na,K ATPase	?
Source Organism	Sus scrofa	?
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	0.1mM ouabain	?
Macromolecular Partner(s) and Concentration or ratio	No data provided	?
Deposition Date	2013-09-27	?

Experiment

CD or SRCD	SRCD	?
Protein Concentration (mg/ml)	4	?
Concentration Quantification Method	lowry (calibrated by QAA)	?
Protein Purity (%)	No data provided	?
Purity Quantification Method	No data provided	?
Buffer Contents and Concentrations	Tris 20 mM (SO4-salt), Na2HPO4 3 mM, MgSO4, 4 mM, Glycerol 25%, pH = 7.4, 0.1mM ouabain	?
Baseline Contents	Tris 20 mM (SO4-salt), Na2HPO4 3 mM, MgSO4, 4 mM, Glycerol 25%, pH = 7.4, 0.1mM ouabain	?
Experimental Temperature (C)	25	?
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	2011-08-22	?
Local Spectrum Identifier	a24678	?

Calibration

CSA or ACS	CSA	?
Dichroism Units for CSA Standard	Millidegrees (theta)	?
Final Spectrum Calibrated	YES	?
CSA/ACS Standard Concentration (mg/ml)	7.3	?
CSA/ACS Pathlength (mm)	0.1	?
CSA/ACS Zeroed at	235-240	?
CSA/ACS Date Measured	2011-08-22	?
CSA/ACS Ratio (192.5nm and 290.0 nm)	2.05	?
CD signal at 290nm (mdeg)	24.09	?
CSA/ACS Experiment temperature, C	25	?

Data process.

Molecular Weight	154415.7	?
Number of Residues	1384	?
Mean Residue Weight	111.7	?
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	0.353	?
DSSP value: 3-10 helix	0.033	?
DSSP value: pi helix	0.008	?
DSSP value: beta strand	0.135	?
DSSP value: beta bridge	0.009	?
DSSP value: bonded turn	0.117	?
DSSP value: bend	0.117	?
DSSP value: loop or irregular	0.228	?

Tertiary

PDB ID	3n23	?
UniProt ID	P05024,P05027,Q58K79	?
Enzyme Classification (EC)	3.6.3.9	?
Medline Entry	No data provided	?
Cath Classification	2.70.150.10, 1.20.1110.10, 3.40.50.1000, 3.40.1110.10	?
Sequence	GRDKYEPAAV SEHGDKKKAK KERDMDELKK EVSMDDHKLS LDELHRKYGT DLSRGLTPAR AAEILARDGP NALTPPPTTP EWVKFCRQLF GGFSMLLWIG AILCFLAYGI QAATEEEPQN DNLYLGVVLS AVVIITGCFS YYQEAKSSKI MESFKNMVPQ QALVIRNGEK MSINAEEVVV GDLVEVKGGD RIPADLRIIS ANGCKVDNSS LTGESEPQTR SPDFTNENPL ETRNIAFFST NCVEGTARGI VVYTGDRTVM GRIATLASGL EGGQTPIAAE IEHFIHIITG VAVFLGVSFF ILSLILEYTW LEAVIFLIGI IVANVPEGLL ATVTVCLTLT AKRMARKNCL VKNLEAVETL GSTSTICSDK TGTLTQNRMT VAHMWSDNQI HEADTTENQS GVSFDKTSAT WLALSRIAGL CNRAVFQANQ ENLPILKRAV AGDASESALL KCIELCCGSV KEMRERYTKI VEIPFNSTNK YQLSIHKNPN TAEPRHLLVM KGAPERILDR CSSILIHGKE QPLDEELKDA FQNAYLELGG LGERVLGFCH LFLPDEQFPE GFQFDTDDVN FPLDNLCFVG LISMIDPPRA AVPDAVGKCR SAGIKVIMVT GDHPITAKAI AKGVGIISEG NETVEDIAAR LNIPVSQVNP RDAKACVVHG SDLKDMTSEQ LDDILKYHTE IVFARTSPQQ KLIIVEGCQR QGAIVAVTGD GVNDSPASKK ADIGVAMGIA GSDVSKQAAD MILLDDNFAS IVTGVEEGRL IFDNLKKSIA YTLTSNIPEI TPFLIFIIAN IPLPLGTVTI LCIDLGTDMV PAISLAYEQA ESDIMKRQPR NPKTDKLVNE QLISMAYGQI GMIQALGGFF TYFVILAENG FLPIHLLGLR VNWDDRWIND VEDSYGQQWT YEQRKIVEFT CHTPFFVTIV VVQWADLVIC KTRRNSVFQQ GMKNKILIFG LFEETALAAF LSYCPGMGVA LRMYPLKPTW WFCAFPYSLL IFVYDEVRKL IIRRRPGGWV EKETYYMARG KAKEEGSWKK FIWNSEKKEF LGRTGGSWFK ILLFYVIFYG CLAGIFIGTI QVMLLTISEF KPTYQDRVAP PGLTQIPQSQ KTEISFRPND PQSYESYVVS IVRFLEKYKD LAQKDDMIFE DCGNVPSELK ERGEYNNERG ERKVCRFRLE WLGNCSGLND ETYGYKDGKP CVIIKLNRVL GFKPKPPKNE SLETYPVMKY NPYVLPVHCT GKRDEDKEKV GTMEYFGLGG YPGFPLQYYP YYGKLLQPKY LQPLMAVQFT NLTMDTEIRI ECKAYGENIG YSEKDRFQGR FDVKIEVKSM AGLSTDDGGS PKGDVDPFYY DYETVRNGGL IFAALAFIVG LIIILSKRLR CGGKKHRPIN EDEL	?
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, Natalya U. Fedosova, Soren V. Hoffmann, B.A. Wallace, Mikael Esmann	?
Publication Year	2013	?
Publication Journal	Biochemical and Biophysical Research Communications	?
Publication Title	Stabilisation of Na,K-ATPase structure by the cardiotonic steroid ouabain	?
Publication Volume	435	?
Publication Pages	300-305	?

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, 2012-08-20, 1:52pm. - 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		?