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Open data
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Basic information
Entry | Database: PDB / ID: 1w50 | ||||||
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Title | Apo Structure of BACE (Beta Secretase) | ||||||
![]() | BETA-SECRETASE 1![]() | ||||||
![]() | ![]() ![]() ![]() ![]() ![]() ![]() ![]() ![]() ![]() ![]() | ||||||
Function / homology | ![]() ![]() ![]() ![]() ![]() ![]() ![]() ![]() ![]() ![]() ![]() ![]() ![]() ![]() ![]() ![]() ![]() ![]() ![]() ![]() ![]() ![]() ![]() ![]() ![]() ![]() ![]() ![]() Similarity search - Function | ||||||
Biological species | ![]() ![]() | ||||||
Method | ![]() ![]() ![]() | ||||||
![]() | Patel, S. / Vuillard, L. / Cleasby, A. / Murray, C.W. / Yon, J. | ||||||
![]() | ![]() Title: Apo and Inhibitor Complex Structures of Bace (Beta-Secretase) Authors: Patel, S. / Vuillard, L. / Cleasby, A. / Murray, C.W. / Yon, J. | ||||||
History |
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Remark 700 | SHEET THE SHEET STRUCTURE OF THIS MOLECULE IS BIFURCATED. IN ORDER TO REPRESENT THIS FEATURE IN ... SHEET THE SHEET STRUCTURE OF THIS MOLECULE IS BIFURCATED. IN ORDER TO REPRESENT THIS FEATURE IN THE SHEET RECORDS BELOW, TWO SHEETS ARE DEFINED. |
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Structure visualization
Structure viewer | Molecule: ![]() ![]() |
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Downloads & links
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Download
PDBx/mmCIF format | ![]() | 96.6 KB | Display | ![]() |
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PDB format | ![]() | 72.6 KB | Display | ![]() |
PDBx/mmJSON format | ![]() | Tree view | ![]() | |
Others | ![]() |
-Validation report
Arichive directory | ![]() ![]() | HTTPS FTP |
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-Related structure data
Related structure data | ![]() 1w51C ![]() 1fknS S: Starting model for refinement C: citing same article ( |
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Similar structure data |
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Links
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Assembly
Deposited unit | ![]()
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1 |
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Unit cell |
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Components
#1: Protein | ![]() Mass: 45822.445 Da / Num. of mol.: 1 / Fragment: ACTIVE PROTEASE DOMAIN, RESIDUES 43-453 / Mutation: YES Source method: isolated from a genetically manipulated source Source: (gene. exp.) ![]() ![]() ![]() ![]() ![]() ![]() | ||||||
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#2: Chemical | ChemComp-IOD / ![]() #3: Water | ChemComp-HOH / | ![]() Compound details | RESIDUES 56 AND 57 MUTATED TO LYS FROM ARGININE. THE MUTATION IS NOT VISIBLE IN THE STRUCTURE ...RESIDUES 56 AND 57 MUTATED TO LYS FROM ARGININE. THE MUTATION IS NOT VISIBLE IN THE STRUCTURE DEPOSITED. FUNCTION: RESPONSIBL | Sequence details | RESIDUES 56 AND 57 FROM THE UNIPROT REFERENCE BELOW HAVE HAVE BEEN MUTATED TO LYS FROM ARG. SINCE ...RESIDUES 56 AND 57 FROM THE UNIPROT REFERENCE BELOW HAVE HAVE BEEN MUTATED TO LYS FROM ARG. SINCE THIS MUTATION IS NOT VISIBLE IN THE STRUCTURE, THERE ARE NO SEQADV RECORDS GIVEN BELOW. | |
-Experimental details
-Experiment
Experiment | Method: ![]() |
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Sample preparation
Crystal | Density Matthews: 2.86 Å3/Da / Density % sol: 56.65 % |
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Crystal grow![]() | pH: 6.6 / Details: pH 6.60 |
-Data collection
Diffraction | Mean temperature: 100 K |
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Diffraction source | Source: ![]() ![]() ![]() |
Detector | Type: ADSC CCD / Detector: CCD |
Radiation | Protocol: SINGLE WAVELENGTH / Monochromatic (M) / Laue (L): M / Scattering type: x-ray |
Radiation wavelength | Wavelength![]() |
Reflection | Resolution: 1.75→39.5 Å / Num. obs: 51594 / % possible obs: 95.9 % / Observed criterion σ(I): 0 / Redundancy: 6.3 % / Rmerge(I) obs: 0.1 / Net I/σ(I): 4.6 |
Reflection shell | Resolution: 1.75→1.84 Å / Rmerge(I) obs: 0.45 / Mean I/σ(I) obs: 1.7 / % possible all: 97.2 |
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Processing
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Refinement | Method to determine structure![]() ![]() Starting model: PDB ENTRY 1FKN Resolution: 1.75→39.52 Å / Cor.coef. Fo:Fc: 0.933 / Cor.coef. Fo:Fc free: 0.915 / SU B: 3.063 / SU ML: 0.098 / Cross valid method: THROUGHOUT / ESU R: 0.132 / ESU R Free: 0.131 / Stereochemistry target values: MAXIMUM LIKELIHOOD Details: HYDROGENS HAVE BEEN ADDED IN THE RIDING POSITIONS. THIS ENTRY CONTAINS SOME ATOMS WHICH HAVE BEEN REFINED WITH AN OCCUPANCY OF 0.00. RESIDUES BETWEEN 157 AND 169 WERE NOT VISIBLE IN THE ELECTRON DENSITY MAPS
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Solvent computation | Ion probe radii: 0.8 Å / Shrinkage radii: 0.8 Å / VDW probe radii: 1.4 Å / Solvent model: BABINET MODEL WITH MASK | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Displacement parameters | Biso mean: 30.01 Å2
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Refinement step | Cycle: LAST / Resolution: 1.75→39.52 Å
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Refine LS restraints |
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