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package org.rcsb.cif.schema.mm;
import org.rcsb.cif.model.*;
import org.rcsb.cif.schema.*;
import javax.annotation.Generated;
/**
* Data items in the PDBX_SOLN_SCATTER category record details about a
* solution scattering experiment
*/
@Generated("org.rcsb.cif.schema.generator.SchemaGenerator")
public class PdbxSolnScatter extends DelegatingCategory {
public PdbxSolnScatter(Category delegate) {
super(delegate);
}
@Override
protected Column createDelegate(String columnName, Column column) {
switch (columnName) {
case "entry_id":
return getEntryId();
case "id":
return getId();
case "type":
return getType();
case "source_beamline":
return getSourceBeamline();
case "source_beamline_instrument":
return getSourceBeamlineInstrument();
case "detector_type":
return getDetectorType();
case "detector_specific":
return getDetectorSpecific();
case "source_type":
return getSourceType();
case "source_class":
return getSourceClass();
case "num_time_frames":
return getNumTimeFrames();
case "sample_pH":
return getSamplePH();
case "temperature":
return getTemperature();
case "concentration_range":
return getConcentrationRange();
case "buffer_name":
return getBufferName();
case "mean_guiner_radius":
return getMeanGuinerRadius();
case "mean_guiner_radius_esd":
return getMeanGuinerRadiusEsd();
case "min_mean_cross_sectional_radii_gyration":
return getMinMeanCrossSectionalRadiiGyration();
case "min_mean_cross_sectional_radii_gyration_esd":
return getMinMeanCrossSectionalRadiiGyrationEsd();
case "max_mean_cross_sectional_radii_gyration":
return getMaxMeanCrossSectionalRadiiGyration();
case "max_mean_cross_sectional_radii_gyration_esd":
return getMaxMeanCrossSectionalRadiiGyrationEsd();
case "protein_length":
return getProteinLength();
case "data_reduction_software_list":
return getDataReductionSoftwareList();
case "data_analysis_software_list":
return getDataAnalysisSoftwareList();
default:
return new DelegatingColumn(column);
}
}
/**
* This data item is a pointer to _entry.id in the ENTRY category.
* @return StrColumn
*/
public StrColumn getEntryId() {
return delegate.getColumn("entry_id", DelegatingStrColumn::new);
}
/**
* The value of _pdbx_soln_scatter.id must
* uniquely identify the sample in the category PDBX_SOLN_SCATTER
* @return StrColumn
*/
public StrColumn getId() {
return delegate.getColumn("id", DelegatingStrColumn::new);
}
/**
* The type of solution scattering experiment carried out
* @return StrColumn
*/
public StrColumn getType() {
return delegate.getColumn("type", DelegatingStrColumn::new);
}
/**
* The beamline name used for the experiment
* @return StrColumn
*/
public StrColumn getSourceBeamline() {
return delegate.getColumn("source_beamline", DelegatingStrColumn::new);
}
/**
* The instrumentation used on the beamline
* @return StrColumn
*/
public StrColumn getSourceBeamlineInstrument() {
return delegate.getColumn("source_beamline_instrument", DelegatingStrColumn::new);
}
/**
* The general class of the radiation detector.
* @return StrColumn
*/
public StrColumn getDetectorType() {
return delegate.getColumn("detector_type", DelegatingStrColumn::new);
}
/**
* The particular radiation detector. In general this will be a
* manufacturer, description, model number or some combination of
* these.
* @return StrColumn
*/
public StrColumn getDetectorSpecific() {
return delegate.getColumn("detector_specific", DelegatingStrColumn::new);
}
/**
* The make, model, name or beamline of the source of radiation.
* @return StrColumn
*/
public StrColumn getSourceType() {
return delegate.getColumn("source_type", DelegatingStrColumn::new);
}
/**
* The general class of the radiation source.
* @return StrColumn
*/
public StrColumn getSourceClass() {
return delegate.getColumn("source_class", DelegatingStrColumn::new);
}
/**
* The number of time frame solution scattering images used.
* @return IntColumn
*/
public IntColumn getNumTimeFrames() {
return delegate.getColumn("num_time_frames", DelegatingIntColumn::new);
}
/**
* The pH value of the buffered sample.
* @return FloatColumn
*/
public FloatColumn getSamplePH() {
return delegate.getColumn("sample_pH", DelegatingFloatColumn::new);
}
/**
* The temperature in kelvins at which the experiment
* was conducted
* @return FloatColumn
*/
public FloatColumn getTemperature() {
return delegate.getColumn("temperature", DelegatingFloatColumn::new);
}
/**
* The concentration range (mg/mL) of the complex in the
* sample used in the solution scattering experiment to
* determine the mean radius of structural elongation.
* @return StrColumn
*/
public StrColumn getConcentrationRange() {
return delegate.getColumn("concentration_range", DelegatingStrColumn::new);
}
/**
* The name of the buffer used for the sample in the solution scattering
* experiment.
* @return StrColumn
*/
public StrColumn getBufferName() {
return delegate.getColumn("buffer_name", DelegatingStrColumn::new);
}
/**
* The mean radius of structural elongation of the sample.
* In a given solute-solvent contrast, the radius of gyration
* R_G is a measure of structural elongation if the internal
* inhomogeneity of scattering densities has no effect. Guiner
* analysis at low Q gives the R_G and the forward scattering at
* zero angle I(0).
*
* lnl(Q) = lnl(0) - R_G^2Q^2/3
*
* where
* Q = 4(pi)sin(theta/lamda)
* 2theta = scattering angle
* lamda = wavelength
*
* The above expression is valid in a QR_G range for extended
* rod-like particles. The relative I(0)/c values ( where
* c = sample concentration) for sample measurements in a
* constant buffer for a single sample data session, gives the
* relative masses of the protein(s) studied when referenced
* against a standard.
*
* see: O.Glatter & O.Kratky, (1982). Editors of "Small angle
* X-ray Scattering, Academic Press, New York.
* O.Kratky. (1963). X-ray small angle scattering with
* substances of biological interest in diluted solutions.
* Prog. Biophys. Chem., 13, 105-173.
*
* G.D.Wignall & F.S.Bates, (1987). The small-angle approximation
* of X-ray and neutron scatter from rigid rods of non-uniform
* cross section and finite length. J.Appl. Crystallog., 18, 452-460.
*
* If the structure is elongated, the mean radius of gyration
* of the cross-sectional structure R_XS and the mean cross sectional
* intensity at zero angle [I(Q).Q]_Q->0 is obtained from
*
* ln[I(Q).Q] = ln[l(Q).(Q)]_Q->0 - ((R_XS)^2Q^2)/2
* @return FloatColumn
*/
public FloatColumn getMeanGuinerRadius() {
return delegate.getColumn("mean_guiner_radius", DelegatingFloatColumn::new);
}
/**
* The estimated standard deviation for the
* mean radius of structural elongation of the sample.
* In a given solute-solvent contrast, the radius of gyration
* R_G is a measure of structural elongation if the internal
* inhomogeneity of scattering densities has no effect. Guiner
* analysis at low Q give the R_G and the forward scattering at
* zero angle I(0).
*
* lnl(Q) = lnl(0) - R_G^2Q^2/3
*
* where
* Q = 4(pi)sin(theta/lamda)
* 2theta = scattering angle
* lamda = wavelength
*
* The above expression is valid in a QR_G range for extended
* rod-like particles. The relative I(0)/c values ( where
* c = sample concentration) for sample measurements in a
* constant buffer for a single sample data session, gives the
* relative masses of the protein(s) studied when referenced
* against a standard.
*
* see:
* O.Glatter & O.Kratky, (1982). Editors of "Small angle
* X-ray Scattering, Academic Press, New York.
* O.Kratky. (1963). X-ray small angle scattering with
* substances of biological interest in diluted solutions.
* Prog. Biophys. Chem., 13, 105-173.
* G.D.Wignall & F.S.Bates, (1987). The small-angle approximation
* of X-ray and neutron scatter from rigid rods of non-uniform
* cross section and finite length. J.Appl. Crystallog., 18, 452-460.
*
* If the structure is elongated, the mean radius of gyration
* of the cross-sectional structure R_XS and the mean cross sectional
* intensity at zero angle [I(Q).Q]_Q->0 is obtained from
* ln[I(Q).Q] = ln[l(Q).(Q)]_Q->0 - ((R_XS)^2Q^2)/2
* @return FloatColumn
*/
public FloatColumn getMeanGuinerRadiusEsd() {
return delegate.getColumn("mean_guiner_radius_esd", DelegatingFloatColumn::new);
}
/**
* The minimum mean radius of structural elongation of the sample.
* In a given solute-solvent contrast, the radius of gyration
* R_G is a measure of structural elongation if the internal
* inhomogeneity of scattering densities has no effect. Guiner
* analysis at low Q give the R_G and the forward scattering at
* zero angle I(0).
*
* lnl(Q) = lnl(0) - R_G^2Q^2/3
*
* where
* Q = 4(pi)sin(theta/lamda)
* 2theta = scattering angle
* lamda = wavelength
*
* The above expression is valid in a QR_G range for extended
* rod-like particles. The relative I(0)/c values ( where
* c = sample concentration) for sample measurements in a
* constant buffer for a single sample data session, gives the
* relative masses of the protein(s) studied when referenced
* against a standard.
*
* see:
* O.Glatter & O.Kratky, (1982). Editors of "Small angle
* X-ray Scattering, Academic Press, New York.
* O.Kratky. (1963). X-ray small angle scattering with
* substances of biological interest in diluted solutions.
* Prog. Biophys. Chem., 13, 105-173.
* G.D.Wignall & F.S.Bates, (1987). The small-angle approximation
* of X-ray and neutron scatter from rigid rods of non-uniform
* cross section and finite length. J.Appl. Crystallog., 18, 452-460.
*
* If the structure is elongated, the mean radius of gyration
* of the cross-sectional structure R_XS and the mean cross sectional
* intensity at zero angle [I(Q).Q]_Q->0 is obtained from
* ln[I(Q).Q] = ln[l(Q).(Q)]_Q->0 - ((R_XS)^2Q^2)/2
* @return FloatColumn
*/
public FloatColumn getMinMeanCrossSectionalRadiiGyration() {
return delegate.getColumn("min_mean_cross_sectional_radii_gyration", DelegatingFloatColumn::new);
}
/**
* The estimated standard deviation for the
* minimum mean radius of structural elongation of the sample.
* In a given solute-solvent contrast, the radius of gyration
* R_G is a measure of structural elongation if the internal
* inhomogeneity of scattering densities has no effect. Guiner
* analysis at low Q give the R_G and the forward scattering at
* zero angle I(0).
*
* lnl(Q) = lnl(0) - R_G^2Q^2/3
*
* where
* Q = 4(pi)sin(theta/lamda)
* 2theta = scattering angle
* lamda = wavelength
*
* The above expression is valid in a QR_G range for extended
* rod-like particles. The relative I(0)/c values ( where
* c = sample concentration) for sample measurements in a
* constant buffer for a single sample data session, gives the
* relative masses of the protein(s) studied when referenced
* against a standard.
*
* see:
* O.Glatter & O.Kratky, (1982). Editors of "Small angle
* X-ray Scattering, Academic Press, New York.
* O.Kratky. (1963). X-ray small angle scattering with
* substances of biological interest in diluted solutions.
* Prog. Biophys. Chem., 13, 105-173.
* G.D.Wignall & F.S.Bates, (1987). The small-angle approximation
* of X-ray and neutron scatter from rigid rods of non-uniform
* cross section and finite length. J.Appl. Crystallog., 18, 452-460.
*
* If the structure is elongated, the mean radius of gyration
* of the cross-sectional structure R_XS and the mean cross sectional
* intensity at zero angle [I(Q).Q]_Q->0 is obtained from
*
* ln[I(Q).Q] = ln[l(Q).(Q)]_Q->0 - ((R_XS)^2Q^2)/2
* @return FloatColumn
*/
public FloatColumn getMinMeanCrossSectionalRadiiGyrationEsd() {
return delegate.getColumn("min_mean_cross_sectional_radii_gyration_esd", DelegatingFloatColumn::new);
}
/**
* The maximum mean radius of structural elongation of the sample.
* In a given solute-solvent contrast, the radius of gyration
* R_G is a measure of structural elongation if the internal
* inhomogeneity of scattering densities has no effect. Guiner
* analysis at low Q give the R_G and the forward scattering at
* zero angle I(0).
*
* lnl(Q) = lnl(0) - R_G^2Q^2/3
*
* where
* Q = 4(pi)sin(theta/lamda)
* 2theta = scattering angle
* lamda = wavelength
*
* The above expression is valid in a QR_G range for extended
* rod-like particles. The relative I(0)/c values ( where
* c = sample concentration) for sample measurements in a
* constant buffer for a single sample data session, gives the
* relative masses of the protein(s) studied when referenced
* against a standard.
*
* see:
* O.Glatter & O.Kratky, (1982). Editors of "Small angle
* X-ray Scattering, Academic Press, New York.
* O.Kratky. (1963). X-ray small angle scattering with
* substances of biological interest in diluted solutions.
* Prog. Biophys. Chem., 13, 105-173.
* G.D.Wignall & F.S.Bates, (1987). The small-angle approximation
* of X-ray and neutron scatter from rigid rods of non-uniform
* cross section and finite length. J.Appl. Crystallog., 18, 452-460.
*
* If the structure is elongated, the mean radius of gyration
* of the cross-sectional structure R_XS and the mean cross sectional
* intensity at zero angle [I(Q).Q]_Q->0 is obtained from
* ln[I(Q).Q] = ln[l(Q).(Q)]_Q->0 - ((R_XS)^2Q^2)/2
* @return FloatColumn
*/
public FloatColumn getMaxMeanCrossSectionalRadiiGyration() {
return delegate.getColumn("max_mean_cross_sectional_radii_gyration", DelegatingFloatColumn::new);
}
/**
* The estimated standard deviation for the
* minimum mean radius of structural elongation of the sample.
* In a given solute-solvent contrast, the radius of gyration
* R_G is a measure of structural elongation if the internal
* inhomogeneity of scattering densities has no effect. Guiner
* analysis at low Q give the R_G and the forward scattering at
* zero angle I(0).
*
* lnl(Q) = lnl(0) - R_G^2Q^2/3
*
* where
* Q = 4(pi)sin(theta/lamda)
* 2theta = scattering angle
* lamda = wavelength
*
* The above expression is valid in a QR_G range for extended
* rod-like particles. The relative I(0)/c values ( where
* c = sample concentration) for sample measurements in a
* constant buffer for a single sample data session, gives the
* relative masses of the protein(s) studied when referenced
* against a standard.
*
* see:
* O.Glatter & O.Kratky, (1982). Editors of "Small angle
* X-ray Scattering, Academic Press, New York.
* O.Kratky. (1963). X-ray small angle scattering with
* substances of biological interest in diluted solutions.
* Prog. Biophys. Chem., 13, 105-173.
* G.D.Wignall & F.S.Bates, (1987). The small-angle approximation
* of X-ray and neutron scatter from rigid rods of non-uniform
* cross section and finite length. J.Appl. Crystallog., 18, 452-460.
*
* If the structure is elongated, the mean radius of gyration
* of the cross-sectional structure R_XS and the mean cross sectional
* intensity at zero angle [I(Q).Q]_Q->0 is obtained from
* ln[I(Q).Q] = ln[l(Q).(Q)]_Q->0 - ((R_XS)^2Q^2)/2
* @return FloatColumn
*/
public FloatColumn getMaxMeanCrossSectionalRadiiGyrationEsd() {
return delegate.getColumn("max_mean_cross_sectional_radii_gyration_esd", DelegatingFloatColumn::new);
}
/**
* The length (or range) of the protein sample under study.
* If the solution structure is approximated as an elongated elliptical
* cyclinder the length L is determined from,
*
* L = sqrt [12( (R_G)^2 - (R_XS)^2 ) ]
*
* The length should also be given by
*
* L = pi I(0) / [ I(Q).Q]_Q->0
* @return StrColumn
*/
public StrColumn getProteinLength() {
return delegate.getColumn("protein_length", DelegatingStrColumn::new);
}
/**
* A list of the software used in the data reduction
* @return StrColumn
*/
public StrColumn getDataReductionSoftwareList() {
return delegate.getColumn("data_reduction_software_list", DelegatingStrColumn::new);
}
/**
* A list of the software used in the data analysis
* @return StrColumn
*/
public StrColumn getDataAnalysisSoftwareList() {
return delegate.getColumn("data_analysis_software_list", DelegatingStrColumn::new);
}
}
