1EAG
Secreted aspartic proteinase (SAP2) from Candida albicans complexed with A70450
X-RAY DIFFRACTION
Crystallization
Crystal Properties | |
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Matthews coefficient | Solvent content |
2.52 | 50 |
Crystal Data
Unit Cell | |
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Length ( Å ) | Angle ( ˚ ) |
a = 76.2 | α = 90 |
b = 76.2 | β = 90 |
c = 126.1 | γ = 90 |
Symmetry | |
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Space Group | P 43 21 2 |
Diffraction
Diffraction Experiment | ||||||||||||||
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ID # | Crystal ID | Scattering Type | Data Collection Temperature | Detector | Detector Type | Details | Collection Date | Monochromator | Protocol | |||||
1 | 1 | x-ray | IMAGE PLATE | RIGAKU RAXIS IIC | 1993-11-16 | M |
Radiation Source | |||||
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ID # | Source | Type | Wavelength List | Synchrotron Site | Beamline |
1 |
Data Collection
Refinement
Statistics | |||||||||||||||||||
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Diffraction ID | Structure Solution Method | Resolution (High) | Resolution (Low) | Number Reflections (All) | Number Reflections (Observed) | Number Reflections (R-Free) | Percent Reflections (Observed) | R-Work | R-Free | Mean Isotropic B | |||||||||
X-RAY DIFFRACTION | 2.1 | 8 | 21780 | 21780 | 0.195 | 0.268 | 32.4 |
Temperature Factor Modeling | ||||||
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Anisotropic B[1][1] | Anisotropic B[1][2] | Anisotropic B[1][3] | Anisotropic B[2][2] | Anisotropic B[2][3] | Anisotropic B[3][3] | |
RMS Deviations | |
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Key | Refinement Restraint Deviation |
p_staggered_tor | 18.3 |
p_transverse_tor | 17.3 |
p_scangle_it | 2.45 |
p_planar_tor | 1.875 |
p_mcangle_it | 1.72 |
p_scbond_it | 1.49 |
p_mcbond_it | 0.97 |
p_multtor_nbd | 0.278 |
p_singtor_nbd | 0.205 |
p_xyhbond_nbd | 0.177 |
Non-Hydrogen Atoms Used in Refinement | |
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Non-Hydrogen Atoms | Number |
Protein Atoms | 2538 |
Nucleic Acid Atoms | |
Solvent Atoms | 119 |
Heterogen Atoms | 53 |
Software
Software | |
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Software Name | Purpose |
DENZO | data reduction |
PROLSQ | refinement |