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 |
View Plot |
| Net Smoothed Spectrum | Download |
File not provided | |
| 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)
| 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.
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 | ? |
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 | ? |