View & Download CD data for CD0000089000

Neuraminidase (sialidase)


Citation: Ali Abdul-Gader, Andrew John Miles and B.A. Wallace 2011 Bioinformatics 27 1630-1636


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 DRS units Download
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Raw Sample Spectra DRS units Download
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Raw Baseline Spectra DRS units Download
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Average Sample DRS units Download
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Averaged Baseline DRS units Download
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HT / High Voltage / Dynode Spectra HT/Dynode Units Download
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Net Smoothed Spectrum DRS units Download
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Final Processed Spectrum Delta Epsilon Download
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Validation report compiled by Validichro v1.2.5, 2012-08-15, 3:14pm. - PASS

At a glance
Downloads 830
Depositor Andrew Miles
Uniprot P0C6E9
Alpha Fold P0C6E9
PDB 1kit
EC 3.2.1.18
CATH Class 2.60.120.200::2.120.10.10
Protein Type soluble_globular

Sample

Protein Name Neuraminidase ?
Alternative Protein Names Sialidase ?
Source Organism Vibrio cholerae ?
Protein Supplier Sigma Aldrich, UK. Cat no: N7885 ?
Expression System or natural source E. coli ?
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 2012-08-15 ?

Experiment

CD or SRCD SRCD ?
Protein Concentration (mg/ml) 5.80 ?
Concentration Quantification Method QAA ?
Protein Purity (%) No data provided ?
Purity Quantification Method No data provided ?
Buffer Contents and Concentrations H2O ?
Baseline Contents H2O ?
Experimental Temperature (C) 4 ?
Instrument or beamline Daresbury 12.1 ?
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 175 ?
Criteria for low wavelength cutoff HT value ?
Wavelength interval, nm 1 ?
Dwell or Averaging time, seconds 1 ?
Experimental Collection date 2003-09-17 ?
Local Spectrum Identifier r6372 ?

Calibration

CSA or ACS CSA ?
Dichroism Units for CSA Standard DRS units ?
Final Spectrum Calibrated YES ?
CSA/ACS Standard Concentration (mg/ml) 10.30 ?
CSA/ACS Pathlength (mm) 0.10 ?
CSA/ACS Zeroed at 235-240 ?
CSA/ACS Date Measured 2003-09-17 ?
CSA/ACS Ratio (192.5nm and 290.0 nm) 2.02 ?
CD signal at 290nm (mdeg) 48612 ?
CSA/ACS Experiment temperature, C 25 ?

Data process.

Molecular Weight 82978.0 ?
Number of Residues 757 ?
Mean Residue Weight 109.8 ?
Data Processing Software Name CDTool ?
Data Processing Software Version 1.4 ?
Wavelength Range for Zeroing 263-267 ?
Number of Smoothing Points 7 ?

Sec. struct.

Secondary Structure Calculated from Crystal structure ?
DSSP value: alpha helix 0.048 ?
DSSP value: 3-10 helix 0.012 ?
DSSP value: pi helix 0.000 ?
DSSP value: beta strand 0.503 ?
DSSP value: beta bridge 0.005 ?
DSSP value: bonded turn 0.125 ?
DSSP value: bend 0.110 ?
DSSP value: loop or irregular 0.197 ?

Tertiary

PDB ID 1kit ?
UniProt ID P0C6E9 ?
Enzyme Classification (EC) 3.2.1.18 ?
Medline Entry 21505036 ?
Cath Classification 2.60.120.200::2.120.10.10 ?
Sequence ALFDYNATGD TEFDSPAKQG WMQDNTNNGS GVLTNADGMP AWLVQGIGGR AQWTYSLSTN QHAQASSFGW RMTTEMKVLS GGMITNYYAN GTQRVLPIIS LDSSGNLVVE FEGQTGRTVL ATGTAATEYH KFELVFLPGS NPSASFYFDG KLIRDNIQPT ASKQNMIVWG NGSSNTDGVA AYRDIKFEIQ GDVIFRGPDR IPSIVASSVT PGVVTAFAEK RVGGGDPGAL SNTNDIITRT SRDGGITWDT ELNLTEQINV SDEFDFSDPR PIYDPSSNTV LVSYARWPTD AAQNGDRIKP WMPNGIFYSV YDVASGNWQA PIDVTDQVKE RSFQIAGWGG SELYRRNTSL NSQQDWQSNA KIRIVDGAAN QIQVADGSRK YVVTLSIDES GGLVANLNGV SAPIILQSEH AKVHSFHDYE LQYSALNHTT TLFVDGQQIT TWAGEVSQEN NIQFGNADAQ IDGRLHVQKI VLTQQGHNLV EFDAFYLAQQ TPEVEKDLEK LGWTKIKTGN TMSLYGNASV NPGPGHGITL TRQQNISGSQ NGRLIYPAIV LDRFFLNVMS IYSDDGGSNW QTGSTLPIPF RWKSSSILET LEPSEADMVE LQNGDLLLTA RLDFNQIVNG VNYSPRQQFL SKDGGITWSL LEANNANVFS NISTGTVDAS ITRFEQSDGS HFLLFTNPQG NPAGTNGRQN LGLWFSFDEG VTWKGPIQLV NGASAYSDIY QLDSENAIVI VETDNSNMRI LRMPITLLKQ KLTLSQN ?
Type of protein soluble_globular ?
Keyword/phrase A SMP180 ?
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 Ali Abdul-Gader, Andrew John Miles and B.A. Wallace ?
Publication Year 2011 ?
Publication Journal Bioinformatics ?
Publication Title A Reference Dataset for the Analyses of Membrane Protein Secondary Structures and Transmembrane Residues using Circular Dichroism Spectroscopy ?
Publication Volume 27 ?
Publication Pages 1630-1636 ?

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, 2012-08-15, 3:14pm. - 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.