View & Download CD data for CD0006424001

Immunoglobulin G1 (pH 2, 3 Hours) (igg1 (ph 2, 3 hours))


Citation: Hiroshi Imamura, Ayako Ooishi, Shinya Honda


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) File not provided
Raw Sample Spectra Millidegrees_(theta) Download
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Raw Baseline Spectra Millidegrees_(theta) Download
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Average Sample Download
File not provided
Averaged Baseline Download
File not provided
HT / High Voltage / Dynode Spectra HT/Dynode Units Download
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Net Smoothed Spectrum Download
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Final Processed Spectrum Mean_Residue_Ellipticity Download
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Validation report compiled by Validichro v1.4.0.1, 2023-01-05 08:11:33. - PASS (incomplete)

At a glance
Downloads 679
Depositor Hiroshi Imamura
Uniprot unavailable
Alpha Fold
PDB
EC
CATH Class
Protein Type soluble_globular

Sample

Protein Name immunoglobulin G1 (pH 2, 3 hours) ?
Alternative Protein Names IgG1 (pH 2, 3 hours) ?
Source Organism mouse/human (chimera) ?
Protein Supplier pharmaceutical company ?
Expression System or natural source Other-Specify ?
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 2022-12-15 ?

Experiment

CD or SRCD CD ?
Protein Concentration (mg/ml) 1.1 ?
Concentration Quantification Method A280 or A280-denatured ?
Protein Purity (%) No data provided ?
Purity Quantification Method No data provided ?
Buffer Contents and Concentrations 0.1 M glycine-HCl buffer solution, pH 2.0 ?
Baseline Contents 0.1 M glycine-HCl buffer solution, pH 2.0 ?
Experimental Temperature (C) 25.0 ?
Instrument or beamline Jasco ?
Detector Angle (Scattering Angle) No data provided ?
Sample Cell Pathlength (cm) 0.02 ?
Cell Pathlength Calibration Method Manufacturers Spec. ?
Sample Cell Type Cylindrical ?
Sample Cell Composition Quartz ?
Sample Chamber Atmosphere Nitrogen ?
Number of repeat scans 4 ?
Continuous or Stepped scan Unknown ?
Maximum (highest) wavelength, nm 300 ?
Minimum (lowest) wavelength, nm 195 ?
Criteria for low wavelength cutoff HT value ?
Wavelength interval, nm 0.5 ?
Dwell or Averaging time, seconds 2 ?
Experimental Collection date 2017-03-16 ?
Local Spectrum Identifier ph2_3h_10d_2_sub ?

Calibration

CSA or ACS CSA ?
Dichroism Units for CSA Standard Millidegrees_(theta) ?
Final Spectrum Calibrated NO ?
CSA/ACS Standard Concentration (mg/ml) No data provided ?
CSA/ACS Pathlength (mm) No data provided ?
CSA/ACS Zeroed at No data provided ?
CSA/ACS Date Measured No data provided ?
CSA/ACS Ratio (192.5nm and 290.0 nm) No data provided ?
CD signal at 290nm (mdeg) No data provided ?
CSA/ACS Experiment temperature, C No data provided ?

Data process.

Molecular Weight 999 ?
Number of Residues 999 ?
Mean Residue Weight 109 ?
Data Processing Software Name Other-Specify ?
Data Processing Software Version Spectra Manager for Windows 95/NT version 1.53.02 ?
Wavelength Range for Zeroing No data provided ?
Number of Smoothing Points No data provided ?

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 unavailable ?
Enzyme Classification (EC) No data provided ?
Medline Entry No data provided ?
Cath Classification No data provided ?
Sequence x-x-x ?
Type of protein soluble_globular ?
Keyword/phrase A monoclonal antibody ?
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 Hiroshi Imamura, Ayako Ooishi, Shinya Honda ?
Publication Year No data provided ?
Publication Journal No data provided ?
Publication Title Getting Smaller by Denaturation: Acid-Induced Compaction of Antibodies ?
Publication Volume No data provided ?
Publication Pages No data provided ?

Depositor

Depositor Name Hiroshi Imamura ?
Department/School name Department of Bio-science ?
University/Institution/Corporation Nagahama Institute of Bio-Science and Technology ?
Depositor Country Japan ?
Name of Principal Investigator (if not depositor) Shinya Honda ?

Validation report compiled by Validichro v1.4.0.1, 2023-01-05 08:11:33. - PASS (incomplete)

Depositors Notes: hidden

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 ?
Molecular Weight PASS ?
Number of Residues PASS ?
Mean Residue Weight value PASS ?
Concentration and Pathlength PASS ?
CSA / ACS peak ratio INSUFFICIENT DATA ?
CSA / ACS Temperature INSUFFICIENT DATA ?
Peak Shift test INSUFFICIENT DATA ?
Standard Deviation INSUFFICIENT DATA ?
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 INSUFFICIENT DATA ?
Depositor Note hidden ?

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.