CREB Binding Protein Nuclear Coactivator Binding Domain (2059-2117) (cbp-ncbd)

Citation: Gabor Nagy, Soren V Hoffman, Nykola C Jones, Helmut Grubmuller 2024 Applied Spectroscopy 78/9 897-911

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 Sample Spectra 4	Millidegrees_(theta)	Download	View Plot
Raw Sample Spectra 5	Millidegrees_(theta)	Download	View Plot
Raw Sample Spectra 6	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
Raw Baseline Spectra 4	Millidegrees_(theta)	Download	View Plot
Raw Baseline Spectra 5	Millidegrees_(theta)	Download	View Plot
Raw Baseline Spectra 6	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
Net Smoothed Spectrum	Millidegrees_(theta)	Download	View Plot
Final Processed Spectrum	Delta_Epsilon	Download	View Plot

Validation report compiled by Validichro v1.4.0.1, 2025-04-07 15:06:34. - PASS

At a glance

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Sample

Protein Name	CREB Binding Protein Nuclear Coactivator Binding Domain (2059-2117)	?
Alternative Protein Names	CBP-NCBD	?
Source Organism	Mouse	?
Protein Supplier	Karebay Biochem Inc.	?
Expression System or natural source	Other- custom peptide synthesis	?
Expressed As	Mutant	?
Mutation Details	P2060N	?
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	2023-11-03	?

Experiment

CD or SRCD	SRCD	?
Protein Concentration (mg/ml)	0.80	?
Concentration Quantification Method	Extinction Coefficient (214 nm)	?
Protein Purity (%)	95	?
Purity Quantification Method	Supplier value	?
Buffer Contents and Concentrations	Na2HPO4 buffer 10 mM, NaF 50 mM	?
Baseline Contents	Na2HPO4 buffer 10 mM, NaF 50 mM	?
Experimental Temperature (C)	25	?
Instrument or beamline	AU-CD beamline, ISA-ASTRID2	?
Detector Angle (Scattering Angle)	No data provided	?
Sample Cell Pathlength (cm)	0.01023	?
Cell Pathlength Calibration Method	Interferometry	?
Sample Cell Type	Cylindrical-Demountable	?
Sample Cell Composition	Suprasil	?
Sample Chamber Atmosphere	Nitrogen	?
Number of repeat scans	8	?
Continuous or Stepped scan	Continuous	?
Maximum (highest) wavelength, nm	280	?
Minimum (lowest) wavelength, nm	178	?
Criteria for low wavelength cutoff	HT value	?
Wavelength interval, nm	1	?
Dwell or Averaging time, seconds	2	?
Experimental Collection date	2016-11-23	?
Local Spectrum Identifier	52747	?

Calibration

CSA or ACS	CSA	?
Dichroism Units for CSA Standard	Millidegrees_(theta)	?
Final Spectrum Calibrated	NO	?
CSA/ACS Standard Concentration (mg/ml)	7.4	?
CSA/ACS Pathlength (mm)	1.0	?
CSA/ACS Zeroed at	No data provided	?
CSA/ACS Date Measured	2016-11-23	?
CSA/ACS Ratio (192.5nm and 290.0 nm)	2.051	?
CD signal at 290nm (mdeg)	25.5968	?
CSA/ACS Experiment temperature, C	25	?

Data process.

Molecular Weight	6563.0	?
Number of Residues	59	?
Mean Residue Weight	113.1	?
Data Processing Software Name	Spectra Manager	?
Data Processing Software Version	No data provided	?
Wavelength Range for Zeroing	No data provided	?
Number of Smoothing Points	7	?

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	P45481	?
Enzyme Classification (EC)	No data provided	?
Medline Entry	No data provided	?
Cath Classification	No data provided	?
Sequence	PNRSISPSAL QDLLRTLKSP SSPQQQQQVL NILKSNPQLM AAFIKQRTAK YVANQPGMQ	?
Type of protein	intrinsically_disordered	?
Keyword/phrase A	CBP	?
Keyword/phrase B	NCBD	?
Keyword/phrase C	CBP-NCBD	?
Keyword/phrase D	Cbpn	?
Keyword/phrase E	IDP	?
Keyword/phrase F	IDP8	?
Keyword/phrase G	molten globule	?
Keyword/phrase H	CBP-IBID	?
Keyword/phrase I	No data provided	?
Keyword/phrase J	No data provided	?
Publication Authors	Gabor Nagy, Soren V Hoffman, Nykola C Jones, Helmut Grubmuller	?
Publication Year	2024	?
Publication Journal	Applied Spectroscopy	?
Publication Title	Reference Data Set for Circular Dichroism Spectroscopy Comprised of Validated Intrinsically Disordered Protein Models	?
Publication Volume	78/9	?
Publication Pages	897-911	?

Depositor

Depositor Name	Gabor Nagy	?
Department/School name	Theoreritical and Computational Biophysics	?
University/Institution/Corporation	Max Planck Institute for Multidisciplinary Sciences	?
Depositor Country	Germany	?
Name of Principal Investigator (if not depositor)	Helmut Grubmuller	?

Validation report compiled by Validichro v1.4.0.1, 2025-04-07 15:06:34. - 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		?
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		?