View & Download CD data for CD0003892000

Antithrombin-III (serpin c1)


Citation: No citation information currently associated with this entry.


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 Sample Spectra 4 Millidegrees (theta) Download
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Raw Sample Spectra 5 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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Raw Baseline Spectra 4 Millidegrees (theta) Download
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Raw Baseline Spectra 5 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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HT / High Voltage / Dynode Spectra 4 HT/Dynode Units Download
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HT / High Voltage / Dynode Spectra 5 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 v1.4.0, 2015-04-01, 3:33pm. - PASS

At a glance
Downloads 2526
Depositor Frank Wien
Uniprot P01008
Alpha Fold
PDB 1SR5
EC
CATH Class 2.30.39.10.3.30.497.10
Protein Type soluble globular

Sample

Protein Name Antithrombin-III ?
Alternative Protein Names Serpin C1 ?
Source Organism Homo sapiens ?
Protein Supplier Jzsef Dob, Institute of Enzymology ?
Expression System or natural source E. coli ?
Expressed As Wild-type ?
Mutation Details na. ?
Expression tags (if any) na. ?
Ligands Present and Concentration or ratio na. ?
Macromolecular Partner(s) and Concentration or ratio na. ?
Deposition Date 2015-04-01 ?

Experiment

CD or SRCD SRCD ?
Protein Concentration (mg/ml) 3.57 ?
Concentration Quantification Method QAA ?
Protein Purity (%) >95% ?
Purity Quantification Method SDS gels ?
Buffer Contents and Concentrations 20mMTris-Cl, 0,1mM EDTA,10mM NaCl, 10mM PO4 pH7 ?
Baseline Contents dialysate ?
Experimental Temperature (C) 25 ?
Instrument or beamline Soleil DISCO ?
Detector Angle (Scattering Angle) 60 ?
Sample Cell Pathlength (cm) 0.0012 ?
Cell Pathlength Calibration Method Interferometry ?
Sample Cell Type Cylindrical-Demountable ?
Sample Cell Composition CaF2 ?
Sample Chamber Atmosphere Nitrogen ?
Number of repeat scans 5 ?
Continuous or Stepped scan Stepped ?
Maximum (highest) wavelength, nm 275 ?
Minimum (lowest) wavelength, nm 180 ?
Criteria for low wavelength cutoff HT value ?
Wavelength interval, nm 1 ?
Dwell or Averaging time, seconds 1.2 ?
Experimental Collection date 2012-09-08 ?
Local Spectrum Identifier paprika3 ?

Calibration

CSA or ACS CSA ?
Dichroism Units for CSA Standard Millidegrees \(theta\) ?
Final Spectrum Calibrated YES ?
CSA/ACS Standard Concentration (mg/ml) 6.3 ?
CSA/ACS Pathlength (mm) 0.1 ?
CSA/ACS Zeroed at 245-230 ?
CSA/ACS Date Measured 2012-09-08 ?
CSA/ACS Ratio (192.5nm and 290.0 nm) 2.13 ?
CD signal at 290nm (mdeg) 19.15 ?
CSA/ACS Experiment temperature, C 25 ?

Data process.

Molecular Weight 49039.1 ?
Number of Residues 432 ?
Mean Residue Weight 113.78 ?
Data Processing Software Name CDTool ?
Data Processing Software Version latest ?
Wavelength Range for Zeroing 263-267 ?
Number of Smoothing Points 7 ?

Sec. struct.

Secondary Structure Calculated from DSSP - 1sr5.pdb Chain A ?
DSSP value: alpha helix 0.238 ?
DSSP value: 3-10 helix 0.028 ?
DSSP value: pi helix 0.0 ?
DSSP value: beta strand 0.231 ?
DSSP value: beta bridge 0.007 ?
DSSP value: bonded turn 0.097 ?
DSSP value: bend 0.113 ?
DSSP value: loop or irregular 0.285 ?

Tertiary

PDB ID 1SR5 ?
UniProt ID P01008 ?
Enzyme Classification (EC) No data provided ?
Medline Entry No data provided ?
Cath Classification 2.30.39.10.3.30.497.10 ?
Sequence HGSPVDICTA KPRDIPMNPM CIYRSPEKKA TEDEGSEQKI PEATNRRVWE LSKANSRFAT TFYQHLADSK NDNDNIFLSP LSISTAFAMT KLGACNDTLQ QLMEVFKFDT ISEKTSDQIH FFFAKLNCRL YRKANKSSKL VSANRLFGDK SLTFNETYQD ISELVYGAKL QPLDFKENAE QSRAAINKWV SNKTEGRITD VIPSEAINEL TVLVLVNTIY FKGLWKSKFS PENTRKELFY KADGESCSAS MMYQEGKFRY RRVAEGTQVL ELPFKGDDIT MVLILPKPEK SLAKVEKELT PEVLQEWLDE LEEMMLVVHM PRFRIEDGFS LKEQLQDMGL VDLFSPEKSK LPGIVAEGRD DLYVSDAFHK AFLEVNEEGS EAAASTAVVI AGRSLNPNRV TFKANRPFLV FIREVPLNTI IFMGRVANPC VK ?
Type of protein soluble globular ?
Keyword/phrase A Hydrolase/hydrolase inhibitor ?
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 No data provided ?
Publication Year No data provided ?
Publication Journal No data provided ?
Publication Title No data provided ?
Publication Volume No data provided ?
Publication Pages No data provided ?

Depositor

Depositor Name Frank Wien ?
Department/School name Experiences ?
University/Institution/Corporation SOLEIL Synchrotron ?
Depositor Country France ?
Name of Principal Investigator (if not depositor) József Kardos ?

Validation report compiled by Validichro v1.4.0, 2015-04-01, 3:33pm. - PASS

Depositors Notes: To be resubmitted replacing the originally submitted antithrombin spectra.

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 To be resubmitted replacing the originally submitted antithrombin spectra. ?

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.