View & Download CD data for CD0006158000

Acetomicrobium Hydrogeniformans Esterase (ahest recombinant protein)


Citation: Kumagai PS, Gutierrez RF, Lopes JLS, Martins JM, Jameson DM, Castro AM, Martins LF, DeMarco R, Bossolan NRS, Wallace BA, Araujo APU 2018 Extremophile


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 ---- Please select ---- 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 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
Average Sample Millidegrees (theta) Download
File not provided
Averaged Baseline ---- Please select ---- Download
File not provided
HT / High Voltage / Dynode Spectra HT/Dynode Units Download
View Plot
HT / High Voltage / Dynode Spectra 2 HT/Dynode Units Download
View Plot
HT / High Voltage / Dynode Spectra 3 HT/Dynode Units Download
View Plot
Net Smoothed Spectrum ---- Please select ---- Download
File not provided
Final Processed Spectrum Delta Epsilon Download
View Plot

Validation report compiled by Validichro v1.4.0.1, 2018-08-16, 7:22pm. - FLAG

At a glance
Downloads 1223
Depositor Jose Lopes
Uniprot
Alpha Fold
PDB
EC 3.1.1.x
CATH Class
Protein Type soluble globular

Sample

Protein Name Acetomicrobium hydrogeniformans esterase ?
Alternative Protein Names AhEst recombinant protein ?
Source Organism Acetomicrobium hydrogeniformans ?
Protein Supplier APU Araujo, IF-USP, Brazil ?
Expression System or natural source E. coli ?
Expressed As Wild-type ?
Mutation Details No data provided ?
Expression tags (if any) hexahistidineSUMO protein, cleaved ?
Ligands Present and Concentration or ratio no ligands ?
Macromolecular Partner(s) and Concentration or ratio no partner ?
Deposition Date 2018-08-17 ?

Experiment

CD or SRCD SRCD ?
Protein Concentration (mg/ml) 0.7 ?
Concentration Quantification Method Nanodrop ?
Protein Purity (%) No data provided ?
Purity Quantification Method SDS gels ?
Buffer Contents and Concentrations 10 mM sodium phosphate (pH 7.0) ?
Baseline Contents 10 mM sodium phosphate (pH 7.0) ?
Experimental Temperature (C) 25 ?
Instrument or beamline ISA CD1 ?
Detector Angle (Scattering Angle) No data provided ?
Sample Cell Pathlength (cm) 0.0098 ?
Cell Pathlength Calibration Method Interferometry ?
Sample Cell Type Cylindrical ?
Sample Cell Composition Quartz ?
Sample Chamber Atmosphere Nitrogen ?
Number of repeat scans 3 ?
Continuous or Stepped scan Stepped ?
Maximum (highest) wavelength, nm 280 ?
Minimum (lowest) wavelength, nm 170 ?
Criteria for low wavelength cutoff HT value ?
Wavelength interval, nm 1 ?
Dwell or Averaging time, seconds 2 ?
Experimental Collection date 2016-11-01 ?
Local Spectrum Identifier 52298 ?

Calibration

CSA or ACS CSA ?
Dichroism Units for CSA Standard No data provided ?
Final Spectrum Calibrated YES ?
CSA/ACS Standard Concentration (mg/ml) 7.4 ?
CSA/ACS Pathlength (mm) 0.099 ?
CSA/ACS Zeroed at 230-235 ?
CSA/ACS Date Measured 0000-00-00 ?
CSA/ACS Ratio (192.5nm and 290.0 nm) 2.07 ?
CD signal at 290nm (mdeg) No data provided ?
CSA/ACS Experiment temperature, C 25 ?

Data process.

Molecular Weight 28287.94 ?
Number of Residues 256 ?
Mean Residue Weight 110.9 ?
Data Processing Software Name CDTool ?
Data Processing Software Version No data provided ?
Wavelength Range for Zeroing 263-270 ?
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 No data provided ?
Enzyme Classification (EC) 3.1.1.x ?
Medline Entry No data provided ?
Cath Classification No data provided ?
Sequence GLAGTNPLLQ RAEGAQTLKE EIITYNHEDT VLEGYLVYEE SVKDKRPGVI IIHEWMGLSE YEKMRARQIA ELGYVAFAAD IYGKGVRPKN ADEAAQLAGK FRSDRNLLRE RGQAALSVLQ NHPLVDPERI ATMGYCFGGG ASLELARSGA PIRGAISFHG NLDTPNPDDA KNIKGSILVL HGADDPMVPM EQVIAFQEEM RSANVDWQMI FYGNTVHSFT NPNAGNNPEI GVAYNPISER RSFEAMKAFF DEIFAK ?
Type of protein soluble globular ?
Keyword/phrase A esterase ?
Keyword/phrase B enhanced oil recovery (EOR) ?
Keyword/phrase C enzyme ?
Keyword/phrase D thermo stable protein ?
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 Kumagai PS, Gutierrez RF, Lopes JLS, Martins JM, Jameson DM, Castro AM, Martins LF, DeMarco R, Bossolan NRS, Wallace BA, Araujo APU ?
Publication Year 2018 ?
Publication Journal Extremophile ?
Publication Title Characterization of esterase activity from an Acetomicrobium hydrogeniformans enzyme with high structural stability in extreme conditions ?
Publication Volume No data provided ?
Publication Pages No data provided ?

Depositor

Depositor Name Jose Lopes ?
Department/School name Crystallography ?
University/Institution/Corporation Birkbeck College ?
Depositor Country U.K. ?
Name of Principal Investigator (if not depositor) BA Wallace ?

Validation report compiled by Validichro v1.4.0.1, 2018-08-16, 7:22pm. - FLAG

Depositors Notes: 1) A 27-residue signal peptide at N-terminus was removed from sequence deposited in UniProt

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 FLAG ?
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 calculation failed ?
Projection Test PASS ?
Standard Deviation At Peak PASS ?
Depositor Note 1) A 27-residue signal peptide at N-terminus was removed from sequence deposited in UniProt ?

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.