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3l81

Crystal structure of adaptor protein complex 4 (AP-4) mu4 subunit C-terminal domain, in complex with a sorting peptide from the amyloid precursor protein (APP)

Method: X-RAY DIFFRACTION Dmax: 80.2 Å Quality: GOOD
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1. Protein Identity and Related Structures Protein Identity & Related Structures

AP-4 complex subunit mu-1

Homo sapiens

UniProt O00189

State in the Current Structure

Assembly Oligomeric State Construct Mutations and Modifications Ligands, Ions and Associated Components Method and Experimental Conditions Structure Quality
1 Protein heterocomplex Heteromer Protein × 2 PDB declaration: dimeric（2） Consistent with protein copy count Chain A； UniProt 160–453 Fragment：C-terminus, residues 160-453 Mutation：C235S,C431S Amyloid beta A4 protein × 1 （P05067） GOL GLYCEROL × 3 X-RAY DIFFRACTION X-ray crystallization conditions：VAPOR DIFFUSION, HANGING DROP；pH 7；295 K；10% PEG 3350, 10mM magnesium chloride, 0.1M HEPES, pH 7.0, VAPOR DIFFUSION, HANGING DROP, temperature 295K X-ray crystallization conditions：VAPOR DIFFUSION, HANGING DROP；pH 7；295 K；15% PEG 6000, 3% trimethylamine N-oxide dihydrate, 0.1M HEPES, pH 7.0, VAPOR DIFFUSION, HANGING DROP, temperature 295K Resolution 1.60 Å R-free 0.252

Other States of the Same Protein in the Database

Each row is a biological assembly of the same UniProt protein in another PDB entry. The “Difference from current entry” column identifies evidence-level differences; no tag means the currently parsed fields agree.

Other PDB Difference from Current Entry 3L81 Assembly / Oligomeric State Construct Mutations and Modifications Ligands, Ions and Non-polymers Method and Experimental Conditions Structure Quality
4MDR Crystal structure of adaptor protein complex 4 (AP-4) mu4 subunit C-terminal domain D190A mutant, in complex with a sorting peptide from the amyloid precursor protein (APP) Deposited 2013-08-23 Different mutation/modification Different ligand/ion Different experimental conditions Different structure-quality metrics Assembly 1 Protein heterocomplex Heteromer；Protein × 2 PDB declaration: dimeric
Chain A 160–453（294 aa） Fragment：C-terminus, residues 160-453
Mutation：D190A,C235S,C431S No recorded non-water small molecule X-RAY DIFFRACTION
X-ray crystallization conditions VAPOR DIFFUSION, HANGING DROP；pH 7；295 K；15% PEG 6000, 3% trimethylamine N-oxide dihydrate, 0.1M HEPES, pH 7.0, VAPOR DIFFUSION, HANGING DROP, temperature 295.0K
Resolution 1.85 Å R-free 0.260
9U9I M4-CTD-undocked AP-4 core in apo form Deposited 2025-03-28 Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental method Different experimental conditions Different structure-quality metrics Assembly 1 Protein heterocomplex Heteromer；Protein × 4 PDB declaration: tetrameric
Chain M 1–453（453 aa）
Not recorded No recorded non-water small molecule ELECTRON MICROSCOPY
cryo-EM buffer pH 8
Resolution 4.00 Å
9U9J M4-CTD-docked AP-4 core in apo form Deposited 2025-03-28 Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental method Different experimental conditions Different structure-quality metrics Assembly 1 Protein heterocomplex Heteromer；Protein × 4 PDB declaration: tetrameric
Chain M 1–453（453 aa）
Not recorded No recorded non-water small molecule ELECTRON MICROSCOPY
cryo-EM buffer pH 8
Resolution 4.20 Å
9U9R ARF1(Q71L) bound M4-CTD-undocked AP-4 core Deposited 2025-03-29 Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental method Different experimental conditions Different structure-quality metrics Assembly 1 Protein heterocomplex Heteromer；Protein × 5 PDB declaration: pentameric
Chain M 1–453（453 aa）
Not recorded No recorded non-water small molecule ELECTRON MICROSCOPY
cryo-EM buffer pH 8
Resolution 6.60 Å
9U9S ARF1(Q71L) bound M4-CTD-docked AP-4 core Deposited 2025-03-29 Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental method Different experimental conditions Different structure-quality metrics Assembly 1 Protein heterocomplex Heteromer；Protein × 5 PDB declaration: pentameric
Chain M 1–453（453 aa）
Not recorded No recorded non-water small molecule ELECTRON MICROSCOPY
cryo-EM buffer pH 8
Resolution 6.80 Å

5 other PDB entries and 5 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name AP4M1_HUMAN
Isoform —
PDB entities 1
Chains and sequence ranges Author chain A； PDBConstruct 8–301； UniProt 160–453

Amyloid beta A4 protein

OrganismNot specified

UniProt P05067

State in the Current Structure

Assembly Oligomeric State Construct Mutations and Modifications Ligands, Ions and Associated Components Method and Experimental Conditions Structure Quality
1 Protein heterocomplex Heteromer Protein × 2 PDB declaration: dimeric（2） Consistent with protein copy count Chain B； UniProt 761–767 Fragment：C-terminus, residues 761-767 AP-4 complex subunit mu-1 × 1 （O00189） GOL GLYCEROL × 3 X-RAY DIFFRACTION X-ray crystallization conditions：VAPOR DIFFUSION, HANGING DROP；pH 7；295 K；10% PEG 3350, 10mM magnesium chloride, 0.1M HEPES, pH 7.0, VAPOR DIFFUSION, HANGING DROP, temperature 295K X-ray crystallization conditions：VAPOR DIFFUSION, HANGING DROP；pH 7；295 K；15% PEG 6000, 3% trimethylamine N-oxide dihydrate, 0.1M HEPES, pH 7.0, VAPOR DIFFUSION, HANGING DROP, temperature 295K Resolution 1.60 Å R-free 0.252

Other States of the Same Protein in the Database

Each row is a biological assembly of the same UniProt protein in another PDB entry. The “Difference from current entry” column identifies evidence-level differences; no tag means the currently parsed fields agree.

Other PDB Difference from Current Entry 3L81 Assembly / Oligomeric State Construct Mutations and Modifications Ligands, Ions and Non-polymers Method and Experimental Conditions Structure Quality
11EN Structure of Rapidly twisting Amyloid-beta 40 fibril , RT-Ab40(2_1) Deposited 2026-02-19 Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental method Different experimental conditions Different structure-quality metrics Assembly 1 Protein homooligomer Homooligomer；Protein × 6 PDB declaration: hexameric
Chain A 672–711（40 aa）
Chain B 672–711（40 aa）
Chain C 672–711（40 aa）
Chain D 672–711（40 aa）
Chain E 672–711（40 aa）
Chain F 672–711（40 aa）
Not recorded No recorded non-water small molecule ELECTRON MICROSCOPY
cryo-EM buffer pH 7.4
cryo-EM vitrification conditions Cryogen ETHANE
Resolution 2.50 Å
11EO Structure of Rapidly twisting Amyloid-beta 40 fibril , RT-Ab40(C2) Deposited 2026-02-19 Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental method Different experimental conditions Different structure-quality metrics Assembly 1 Protein homooligomer Homooligomer；Protein × 6 PDB declaration: hexameric
Chain A 672–711（40 aa）
Chain B 672–711（40 aa）
Chain C 672–711（40 aa）
Chain D 672–711（40 aa）
Chain E 672–711（40 aa）
Chain F 672–711（40 aa）
Not recorded No recorded non-water small molecule ELECTRON MICROSCOPY
cryo-EM buffer pH 7.4
cryo-EM vitrification conditions Cryogen ETHANE
Resolution 2.73 Å
11EP Structure of Rapidly twisting Amyloid-beta 40 fibril , RT-Ab40(C1) Deposited 2026-02-19 Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental method Different experimental conditions Different structure-quality metrics Assembly 1 Protein homooligomer Homooligomer；Protein × 6 PDB declaration: hexameric
Chain A 672–711（40 aa）
Chain B 672–711（40 aa）
Chain C 672–711（40 aa）
Chain D 672–711（40 aa）
Chain E 672–711（40 aa）
Chain F 672–711（40 aa）
Not recorded No recorded non-water small molecule ELECTRON MICROSCOPY
cryo-EM buffer pH 7.4
cryo-EM vitrification conditions Cryogen ETHANE
Resolution 2.75 Å
12GB High Resolution Structure of Monomorphic AB1-40 Fibrils Deposited 2026-04-03 Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental method Different experimental conditions Different structure-quality metrics Assembly 1 Protein homooligomer Homooligomer；Protein × 20 PDB declaration: 20-meric
Chain A 672–711（40 aa）
Chain B 672–711（40 aa）
Chain C 672–711（40 aa）
Chain D 672–711（40 aa）
Chain E 672–711（40 aa）
Chain F 672–711（40 aa）
Chain G 672–711（40 aa）
Chain H 672–711（40 aa）
Chain I 672–711（40 aa）
Chain J 672–711（40 aa）
Chain K 672–711（40 aa）
Chain L 672–711（40 aa）
Chain M 672–711（40 aa）
Chain N 672–711（40 aa）
Chain O 672–711（40 aa）
Chain P 672–711（40 aa）
Chain Q 672–711（40 aa）
Chain R 672–711（40 aa）
Chain S 672–711（40 aa）
Chain T 672–711（40 aa）
Not recorded No recorded non-water small molecule SOLID-STATE NMR
NMR measurement conditions pH 7.4；277 K；Ionic strength (raw mmCIF value) 20；Pressure 1
NMR sample composition 350 uM [U-13C; U-15N] Amyloid-beta 1-40 fibrils, 95% H2O/5% D2O | 95% H2O/5% D2O
Resolution not provided
1AAP X-RAY CRYSTAL STRUCTURE OF THE PROTEASE INHIBITOR DOMAIN OF ALZHEIMER'S AMYLOID BETA-PROTEIN PRECURSOR Deposited 1990-09-14 Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental conditions Different structure-quality metrics Assembly 1 Protein homooligomer Homooligomer；Protein × 2 PDB declaration: dimeric
Chain A 287–344（58 aa） Fragment：INHIBITOR DOMAIN
Chain B 287–344（58 aa） Fragment：INHIBITOR DOMAIN
Not recorded No recorded non-water small molecule X-RAY DIFFRACTION mmCIF provides none of the parsed conditions Resolution 1.50 Å
1AMB SOLUTION STRUCTURE OF RESIDUES 1-28 OF THE AMYLOID BETA-PEPTIDE Deposited 1994-10-21 Different construct Different oligomeric state Different ligand/ion Different experimental method Different experimental conditions Different structure-quality metrics Assembly 1 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric
Chain A 672–699（28 aa）
Not recorded No recorded non-water small molecule SOLUTION NMR mmCIF provides none of the parsed conditions Resolution not provided
1AMC SOLUTION STRUCTURE OF RESIDUES 1-28 OF THE AMYLOID BETA-PEPTIDE Deposited 1994-11-14 Different construct Different oligomeric state Different ligand/ion Different experimental method Different experimental conditions Different structure-quality metrics Assembly 1 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric
Chain A 672–699（28 aa）
Not recorded No recorded non-water small molecule SOLUTION NMR mmCIF provides none of the parsed conditions Resolution not provided
1AML THE ALZHEIMER`S DISEASE AMYLOID A4 PEPTIDE (RESIDUES 1-40) Deposited 1995-02-13 Different construct Different oligomeric state Different ligand/ion Different experimental method Different experimental conditions Different structure-quality metrics Assembly 1 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric
Chain A 672–711（40 aa）
Not recorded No recorded non-water small molecule SOLUTION NMR mmCIF provides none of the parsed conditions Resolution not provided
1BA4 THE SOLUTION STRUCTURE OF AMYLOID BETA-PEPTIDE (1-40) IN A WATER-MICELLE ENVIRONMENT. IS THE MEMBRANE-SPANNING DOMAIN WHERE WE THINK IT IS? NMR, 10 STRUCTURES Deposited 1998-04-07 Different construct Different oligomeric state Different ligand/ion Different experimental method Different experimental conditions Different structure-quality metrics Assembly 1 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric
Chain A 672–711（40 aa） Fragment：ABETA
Not recorded No recorded non-water small molecule SOLUTION NMR
NMR measurement conditions pH 5.1；298 K
Resolution not provided
1BA6 SOLUTION STRUCTURE OF THE METHIONINE-OXIDIZED AMYLOID BETA-PEPTIDE (1-40). DOES OXIDATION AFFECT CONFORMATIONAL SWITCHING? NMR, 10 STRUCTURES Deposited 1998-04-22 Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental method Different experimental conditions Different structure-quality metrics Assembly 1 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric
Chain A 672–711（40 aa） Fragment：ABETA
Mutation：INS(MO) Non-standard monomer：Yes (specific site not provided by mmCIF) No recorded non-water small molecule SOLUTION NMR
NMR measurement conditions pH 5.3；298 K
Resolution not provided
1BJB SOLUTION NMR STRUCTURE OF AMYLOID BETA[E16], RESIDUES 1-28, 14 STRUCTURES Deposited 1998-06-23 Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental method Different experimental conditions Different structure-quality metrics Assembly 1 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric
Chain A 672–699（28 aa） Fragment：ABETA [F16], RESIDUES 1-28
Mutation：K16E No recorded non-water small molecule SOLUTION NMR
NMR measurement conditions pH 5.6；296 K；Pressure 1
NMR sample composition SDS MICELLES (100MM)/D2O, H2O
Resolution not provided
1BJC SOLUTION NMR STRUCTURE OF AMYLOID BETA[F16], RESIDUES 1-28, 15 STRUCTURES Deposited 1998-06-23 Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental method Different experimental conditions Different structure-quality metrics Assembly 1 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric
Chain A 672–699（28 aa） Fragment：ABETA [F16], RESIDUES 1-28
Mutation：K16F No recorded non-water small molecule SOLUTION NMR
NMR measurement conditions pH 5.8；296 K；Pressure 1
NMR sample composition SDS MICELLES (100MM)/D2O, H2O
Resolution not provided
1BRC RELOCATING A NEGATIVE CHARGE IN THE BINDING POCKET OF TRYPSIN Deposited 1992-12-17 Different construct Different ligand/ion Different experimental conditions Different structure-quality metrics Assembly 1 Protein heterocomplex Heteromer；Protein × 2 PDB declaration: dimeric
Chain I 287–342（56 aa）
Not recorded No recorded non-water small molecule X-RAY DIFFRACTION mmCIF provides none of the parsed conditions Resolution 2.50 Å
1CA0 BOVINE CHYMOTRYPSIN COMPLEXED TO APPI Deposited 1997-01-23 Different construct Different oligomeric state Different ligand/ion Different experimental conditions Different structure-quality metrics Assembly 1 Protein heterocomplex Heteromer；Protein × 4 PDB declaration: tetrameric
Chain D 289–342（54 aa）
Not recorded No recorded non-water small molecule X-RAY DIFFRACTION
X-ray crystallization conditions pH 4.5；pH 4.5
Resolution 2.10 Å R-free 0.323
1CA0 BOVINE CHYMOTRYPSIN COMPLEXED TO APPI Deposited 1997-01-23 Different construct Different oligomeric state Different ligand/ion Different experimental conditions Different structure-quality metrics Assembly 2 Protein heterocomplex Heteromer；Protein × 4 PDB declaration: tetrameric
Chain I 289–342（54 aa）
Not recorded No recorded non-water small molecule X-RAY DIFFRACTION
X-ray crystallization conditions pH 4.5；pH 4.5
Resolution 2.10 Å R-free 0.323
1HZ3 ALZHEIMER'S DISEASE AMYLOID-BETA PEPTIDE (RESIDUES 10-35) Deposited 2001-01-23 Different construct Different oligomeric state Different ligand/ion Different experimental method Different experimental conditions Different structure-quality metrics Assembly 1 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric
Chain A 681–706（26 aa） Fragment：RESIDUES 10-35
Not recorded No recorded non-water small molecule SOLUTION NMR
NMR measurement conditions pH 5.6；283 K；Ionic strength (raw mmCIF value) <1mM；Pressure ambient
NMR sample composition 300uM A-Beta(10-35); 90% H2O, 10% D2O | 90% H2O/10% D2O
NMR sample composition 300uM A-Beta(1-40) U-15N; 90% H2O, 10% D2O | 90% H2O/10% D2O
NMR sample composition 300 uM A-Beta(10-35) 2H-Val12, -Leu17, -Val18, -Phe19, -Ile32 and -Leu34; 15N-Phe19, -Val24, -Gly25 and -Gly29; 13C-Val24; 13C-Ala21 Beta Methyl; 13C-Ala30 Beta Methyl; 13C-Met35 Delta Methyl | 90% H2O/10% D2O
NMR sample composition 300 uM A-Beta(10-35) 2H-Val12, -Leu17, -Phe19, -Val24, -Ile31 and -Leu34; 15N-Val 18, -Phe20, -Gly25, -Gly29 and -Gly33; 13C-Val24; 13C-Ala21 Beta Methyl; 13C-Ala30 Beta Methyl; 13C-Met35 Delta Methyl | 90% H2O/10% D2O
Resolution not provided
1IYT Solution structure of the Alzheimer's disease amyloid beta-peptide (1-42) Deposited 2002-09-06 Different construct Different oligomeric state Different ligand/ion Different experimental method Different experimental conditions Different structure-quality metrics Assembly 1 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric
Chain A 672–713（42 aa） Fragment：beta-peptide
Not recorded No recorded non-water small molecule SOLUTION NMR
NMR measurement conditions 300 K；Pressure ambient
NMR sample composition 2mM amyloid beta-peptide (TFA pretreated); 20% H2O, 80% hexafluoroisopropanol-d2 | 20% H2O, 80% hexafluoroisopropanol-d2 (v/v)
NMR sample composition 2.5mM amyloid beta-peptide (TFA pretreated); 20% D2O, 80% hexafluoroisopropanol-d2 | 20% D2O, 80% hexafluoroisopropanol-d2 (v/v)
Resolution not provided
1MWP N-TERMINAL DOMAIN OF THE AMYLOID PRECURSOR PROTEIN Deposited 1999-03-09 Different construct Different oligomeric state Different ligand/ion Different experimental conditions Different structure-quality metrics Assembly 1 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric
Chain A 28–123（96 aa） Fragment：HEPARIN BINDING DOMAIN
Not recorded No recorded non-water small molecule X-RAY DIFFRACTION
X-ray crystallization conditions pH 7.5；pH 7.5
Resolution 1.80 Å R-free 0.242
1OWT Structure of the Alzheimer's disease amyloid precursor protein copper binding domain Deposited 2003-03-30 Different construct Different oligomeric state Different ligand/ion Different experimental method Different experimental conditions Different structure-quality metrics Assembly 1 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric
Chain A 124–189（66 aa） Fragment：Copper binding domain
Not recorded No recorded non-water small molecule SOLUTION NMR
NMR measurement conditions pH 6.9；303 K；Ionic strength (raw mmCIF value) 0.3；Pressure 1
NMR sample composition 0.5mM CuBD U-15N,13C; 20mM phosphate buffer | 90% H2O, 10% D20
Resolution not provided
1QCM AMYLOID BETA PEPTIDE (25-35), NMR, 20 STRUCTURES Deposited 1996-07-19 Different construct Different oligomeric state Different ligand/ion Different experimental method Different experimental conditions Different structure-quality metrics Assembly 1 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric
Chain A 696–706（11 aa） Fragment：RESIDUES 25 - 35
Not recorded No recorded non-water small molecule SOLUTION NMR mmCIF provides none of the parsed conditions Resolution not provided
1QWP NMR analysis of 25-35 fragment of beta amyloid peptide Deposited 2003-09-03 Different construct Different oligomeric state Different ligand/ion Different experimental method Different experimental conditions Different structure-quality metrics Assembly 1 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric
Chain A 696–706（11 aa）
Not recorded No recorded non-water small molecule SOLUTION NMR
NMR measurement conditions pH 4.5；300 K；Pressure ambient
NMR sample composition 2mM abeta(25-35) peptide | hexafluoroisopropanol/water mixture 80/20 v:v
Resolution not provided
1QXC NMR structure of the fragment 25-35 of beta amyloid peptide in 20/80 v:v hexafluoroisopropanol/water mixture Deposited 2003-09-05 Different construct Different oligomeric state Different ligand/ion Different experimental method Different experimental conditions Different structure-quality metrics Assembly 1 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric
Chain A 696–706（11 aa）
Not recorded No recorded non-water small molecule SOLUTION NMR
NMR measurement conditions pH 4.5；300 K；Pressure ambient
NMR sample composition 2mM abeta(25-35) peptide | hexafluoroisopropanol/water 20/80 v:v mixture
Resolution not provided
1QYT Solution structure of fragment (25-35) of beta amyloid peptide in SDS micellar solution Deposited 2003-09-12 Different construct Different oligomeric state Different ligand/ion Different experimental method Different experimental conditions Different structure-quality metrics Assembly 1 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric
Chain A 696–706（11 aa）
Not recorded No recorded non-water small molecule SOLUTION NMR
NMR measurement conditions pH 4.15；300 K；Pressure ambient
NMR sample composition 2mM abeta(25-35) peptide | 100mM SDS solution
Resolution not provided
1TAW BOVINE TRYPSIN COMPLEXED TO APPI Deposited 1996-12-19 Different construct Different oligomeric state Different ligand/ion Different experimental conditions Different structure-quality metrics Assembly 1 Protein heterocomplex Heteromer；Protein × 4 PDB declaration: tetrameric
Chain B 287–344（58 aa） Fragment：;RESIDUES 289 - 342 OF ALZHEIMER'S AMYLOID BETA-PROTEIN PRECURSOR ;
Not recorded CA CALCIUM ION × 2 X-RAY DIFFRACTION
X-ray crystallization conditions pH 6.5；pH 6.5
Resolution 1.80 Å
1TKN Solution structure of CAPPD*, an independently folded extracellular domain of human Amyloid-beta Precursor Protein Deposited 2004-06-08 Different construct Different oligomeric state Different ligand/ion Different experimental method Different experimental conditions Different structure-quality metrics Assembly 1 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric
Chain A 460–569（110 aa）
Not recorded No recorded non-water small molecule SOLUTION NMR
NMR measurement conditions pH 6.4；300 K；Ionic strength (raw mmCIF value) 250 mM NaCl, 300 mM guanidinium chloride；Pressure 1
NMR sample composition 0.85 mM U-15N CAPPD*, 50mM sodium phosphate, 250 mM NaCl, 300 mM guanidinium chloride | 95% H2O/5% D2O
NMR sample composition 0.85 mM U-15N,13C CAPPD*, 50mM sodium phosphate, 250 mM NaCl, 300 mM guanidinium chloride | 95% H2O/5% D2O
NMR sample composition 0.8 mM 10% 13C CAPPD*, 50mM sodium phosphate, 250 mM NaCl, 300 mM guanidinium chloride | 95% H2O/5% D2O
Resolution not provided
1X11 X11 PTB DOMAIN Deposited 1997-07-28 Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental conditions Different structure-quality metrics Assembly 1 Protein heterocomplex Heteromer；Protein × 4 PDB declaration: tetrameric
Chain C 754–766（13 aa）
Chain D 754–766（13 aa）
Not recorded No recorded non-water small molecule X-RAY DIFFRACTION
X-ray crystallization conditions pH 7.5；pH 7.5
Resolution 2.50 Å R-free 0.304
1X11 X11 PTB DOMAIN Deposited 1997-07-28 Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental conditions Different structure-quality metrics Assembly 2 Protein heterocomplex Heteromer；Protein × 8 PDB declaration: octameric
Chain C 754–766（13 aa）
Chain D 754–766（13 aa）
Not recorded No recorded non-water small molecule X-RAY DIFFRACTION
X-ray crystallization conditions pH 7.5；pH 7.5
Resolution 2.50 Å R-free 0.304
1X11 X11 PTB DOMAIN Deposited 1997-07-28 Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental conditions Different structure-quality metrics Assembly 3 Protein heterocomplex Heteromer；Protein × 4 PDB declaration: tetrameric
Chain C 754–766（13 aa）
Chain D 754–766（13 aa）
Not recorded No recorded non-water small molecule X-RAY DIFFRACTION
X-ray crystallization conditions pH 7.5；pH 7.5
Resolution 2.50 Å R-free 0.304
1Z0Q Aqueous Solution Structure of the Alzheimer's Disease Abeta Peptide (1-42) Deposited 2005-03-02 Different construct Different oligomeric state Different ligand/ion Different experimental method Different experimental conditions Different structure-quality metrics Assembly 1 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric
Chain A 672–713（42 aa） Fragment：Beta-peptide
Not recorded No recorded non-water small molecule SOLUTION NMR
NMR measurement conditions 300 K；Pressure ambient
NMR sample composition 2mM beta peptide (TFA pretreated); 70% H2O, 30% hexafluoroisopropanol-d2 | 70% H2O, 30% hexafluoroisopropanol-d2
Resolution not provided
1ZE7 Zinc-binding domain of Alzheimer's disease amyloid beta-peptide in water solution at pH 6.5 Deposited 2005-04-18 Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental method Different experimental conditions Different structure-quality metrics Assembly 1 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric
Chain A 672–687（16 aa）
Non-standard monomer：Yes (specific site not provided by mmCIF) No recorded non-water small molecule SOLUTION NMR
NMR measurement conditions pH 6.5；278 K；Ionic strength (raw mmCIF value) 0.1；Pressure ambient
NMR sample composition 2.8mM in 50mM sodium phosphate buffer | 90% H2O/10% D2O
Resolution not provided
1ZE9 Zinc-binding domain of Alzheimer's disease amyloid beta-peptide complexed with a zinc (II) cation Deposited 2005-04-18 Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental method Different experimental conditions Different structure-quality metrics Assembly 1 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric
Chain A 672–687（16 aa）
Non-standard monomer：Yes (specific site not provided by mmCIF) ZN ZINC ION × 1 SOLUTION NMR
NMR measurement conditions pH 6.5；278 K；Ionic strength (raw mmCIF value) 0.1；Pressure ambient
NMR sample composition 2.8mM in 50mM sodium phosphate buffer | 90% H2O/10% D2O
Resolution not provided
1ZJD Crystal Structure of the Catalytic Domain of Coagulation Factor XI in Complex with Kunitz Protease Inhibitor Domain of Protease Nexin II Deposited 2005-04-28 Different construct Different ligand/ion Different experimental conditions Different structure-quality metrics Assembly 1 Protein heterocomplex Heteromer；Protein × 2 PDB declaration: dimeric
Chain B 289–345（57 aa） Fragment：Inhibitory Domain
Not recorded No recorded non-water small molecule X-RAY DIFFRACTION
X-ray crystallization conditions VAPOR DIFFUSION, HANGING DROP；283 K；Sodium Formate, VAPOR DIFFUSION, HANGING DROP, temperature 283K
Resolution 2.60 Å R-free 0.255
21FB Structure of minor species of Abeta fibrils from AppNL-FPsen1P117L mice Deposited 2025-12-10 Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental method Different experimental conditions Different structure-quality metrics Assembly 1 Protein homooligomer Homooligomer；Protein × 12 PDB declaration: dodecameric
Chain A 672–713（42 aa）
Chain B 672–713（42 aa）
Chain C 672–713（42 aa）
Chain D 672–713（42 aa）
Chain E 672–713（42 aa）
Chain F 672–713（42 aa）
Chain G 672–713（42 aa）
Chain H 672–713（42 aa）
Chain I 672–713（42 aa）
Chain J 672–713（42 aa）
Chain K 672–713（42 aa）
Chain L 672–713（42 aa）
Not recorded No recorded non-water small molecule ELECTRON MICROSCOPY
cryo-EM buffer pH 7.4
cryo-EM vitrification conditions Cryogen ETHANE
Resolution 3.40 Å
2BEG 3D Structure of Alzheimer's Abeta(1-42) fibrils Deposited 2005-10-24 Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental method Different experimental conditions Different structure-quality metrics Assembly 1 Protein homooligomer Homooligomer；Protein × 5 PDB declaration: pentameric
Chain A 672–713（42 aa） Fragment：Beta-amyloid protein 42
Chain B 672–713（42 aa） Fragment：Beta-amyloid protein 42
Chain C 672–713（42 aa） Fragment：Beta-amyloid protein 42
Chain D 672–713（42 aa） Fragment：Beta-amyloid protein 42
Chain E 672–713（42 aa） Fragment：Beta-amyloid protein 42
Not recorded No recorded non-water small molecule SOLUTION NMR mmCIF provides none of the parsed conditions Resolution not provided
2BP4 Zinc-binding domain of Alzheimer's disease amyloid beta-peptide in TFE-water (80-20) solution Deposited 2005-04-18 Different construct Different oligomeric state Different ligand/ion Different experimental method Different experimental conditions Different structure-quality metrics Assembly 1 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric
Chain A 672–687（16 aa） Fragment：;16-MER FRAGMENT BETWEEN THE BETA AND ALPHA SECRETASES CLEAVAGE SITES OF ALZHEIMER'S DISEASE AMYLOID A4 PROTEIN, RESIDUES 672-687 ;
Not recorded No recorded non-water small molecule SOLUTION NMR
NMR measurement conditions pH 3；298 K；Pressure 1.0
NMR sample composition 80 % TFE-D2OH / 20 % H2O
Resolution not provided
2FJZ Structure of the Alzheimer's Amyloid Precursor Protein (APP) copper binding domain (residues 133 to 189) in 'small unit cell' form, metal-free Deposited 2006-01-03 Different construct Different oligomeric state Different ligand/ion Different experimental conditions Different structure-quality metrics Assembly 1 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric
Chain A 133–189（57 aa） Fragment：Residues 133 to 189
Not recorded No recorded non-water small molecule X-RAY DIFFRACTION
X-ray crystallization conditions VAPOR DIFFUSION, HANGING DROP；pH 8；295 K；28 - 32 % (w/v) PEG 10000, 0.1 M HEPES pH 8.0, VAPOR DIFFUSION, HANGING DROP, temperature 295K
Resolution 1.61 Å R-free 0.209
2FK1 Structure of the Alzheimer's Amyloid Precursor Protein (APP) Copper Binding Domain in 'small unit cell' form, Cu(II)-bound Deposited 2006-01-03 Different construct Different oligomeric state Different ligand/ion Different experimental conditions Different structure-quality metrics Assembly 1 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric
Chain A 133–189（57 aa） Fragment：Residues 133 to 189
Not recorded CU COPPER (II) ION × 1 X-RAY DIFFRACTION
X-ray crystallization conditions VAPOR DIFFUSION, HANGING DROP；pH 8；295 K；0.1 M HEPES pH 8.0, 28 - 32 % (w/v) PEG 10000, VAPOR DIFFUSION, HANGING DROP, temperature 295K
Resolution 1.60 Å R-free 0.232
2FK2 Structure of the Alzheimer's Amyloid Precursor Protein (APP) Copper Binding Domain in 'small unit cell' form, Cu(I)-bound Deposited 2006-01-03 Different construct Different oligomeric state Different ligand/ion Different experimental conditions Different structure-quality metrics Assembly 1 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric
Chain A 133–189（57 aa） Fragment：Residues 133 to 189
Not recorded CU1 COPPER (I) ION × 1 X-RAY DIFFRACTION
X-ray crystallization conditions VAPOR DIFFUSION, HANGING DROP；pH 8；295 K；0.1 M HEPES pH 8.0, 28 - 32 % (w/v) PEG 10000, VAPOR DIFFUSION, HANGING DROP, temperature 295K
Resolution 1.65 Å R-free 0.249
2FK3 Structure of the Alzheimer's Amyloid Precursor Protein (APP) Copper Binding Domain in 'large unit cell' form Deposited 2006-01-04 Different construct Different oligomeric state Different ligand/ion Different experimental conditions Different structure-quality metrics Assembly 1 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric
Chain A 133–189（57 aa） Fragment：Residues 133 to 189
Not recorded CU COPPER (II) ION × 4 X-RAY DIFFRACTION
X-ray crystallization conditions VAPOR DIFFUSION, HANGING DROP；pH 5.4；295 K；0.1 M MES pH 5.4 - 5.6, 0.4 M NaCOOH, 10 - 15 % (w/v) PEG 4000, VAPOR DIFFUSION, HANGING DROP, temperature 295K
Resolution 2.40 Å R-free 0.248
2FK3 Structure of the Alzheimer's Amyloid Precursor Protein (APP) Copper Binding Domain in 'large unit cell' form Deposited 2006-01-04 Different construct Different oligomeric state Different ligand/ion Different experimental conditions Different structure-quality metrics Assembly 2 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric
Chain B 133–189（57 aa） Fragment：Residues 133 to 189
Not recorded CU COPPER (II) ION × 2 X-RAY DIFFRACTION
X-ray crystallization conditions VAPOR DIFFUSION, HANGING DROP；pH 5.4；295 K；0.1 M MES pH 5.4 - 5.6, 0.4 M NaCOOH, 10 - 15 % (w/v) PEG 4000, VAPOR DIFFUSION, HANGING DROP, temperature 295K
Resolution 2.40 Å R-free 0.248
2FK3 Structure of the Alzheimer's Amyloid Precursor Protein (APP) Copper Binding Domain in 'large unit cell' form Deposited 2006-01-04 Different construct Different oligomeric state Different ligand/ion Different experimental conditions Different structure-quality metrics Assembly 3 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric
Chain C 133–189（57 aa） Fragment：Residues 133 to 189
Not recorded CU COPPER (II) ION × 3 X-RAY DIFFRACTION
X-ray crystallization conditions VAPOR DIFFUSION, HANGING DROP；pH 5.4；295 K；0.1 M MES pH 5.4 - 5.6, 0.4 M NaCOOH, 10 - 15 % (w/v) PEG 4000, VAPOR DIFFUSION, HANGING DROP, temperature 295K
Resolution 2.40 Å R-free 0.248
2FK3 Structure of the Alzheimer's Amyloid Precursor Protein (APP) Copper Binding Domain in 'large unit cell' form Deposited 2006-01-04 Different construct Different oligomeric state Different ligand/ion Different experimental conditions Different structure-quality metrics Assembly 4 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric
Chain D 133–189（57 aa） Fragment：Residues 133 to 189
Not recorded CU COPPER (II) ION × 2 X-RAY DIFFRACTION
X-ray crystallization conditions VAPOR DIFFUSION, HANGING DROP；pH 5.4；295 K；0.1 M MES pH 5.4 - 5.6, 0.4 M NaCOOH, 10 - 15 % (w/v) PEG 4000, VAPOR DIFFUSION, HANGING DROP, temperature 295K
Resolution 2.40 Å R-free 0.248
2FK3 Structure of the Alzheimer's Amyloid Precursor Protein (APP) Copper Binding Domain in 'large unit cell' form Deposited 2006-01-04 Different construct Different oligomeric state Different ligand/ion Different experimental conditions Different structure-quality metrics Assembly 5 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric
Chain E 133–189（57 aa） Fragment：Residues 133 to 189
Not recorded CU COPPER (II) ION × 3 X-RAY DIFFRACTION
X-ray crystallization conditions VAPOR DIFFUSION, HANGING DROP；pH 5.4；295 K；0.1 M MES pH 5.4 - 5.6, 0.4 M NaCOOH, 10 - 15 % (w/v) PEG 4000, VAPOR DIFFUSION, HANGING DROP, temperature 295K
Resolution 2.40 Å R-free 0.248
2FK3 Structure of the Alzheimer's Amyloid Precursor Protein (APP) Copper Binding Domain in 'large unit cell' form Deposited 2006-01-04 Different construct Different oligomeric state Different ligand/ion Different experimental conditions Different structure-quality metrics Assembly 6 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric
Chain F 133–189（57 aa） Fragment：Residues 133 to 189
Not recorded CU COPPER (II) ION × 3 X-RAY DIFFRACTION
X-ray crystallization conditions VAPOR DIFFUSION, HANGING DROP；pH 5.4；295 K；0.1 M MES pH 5.4 - 5.6, 0.4 M NaCOOH, 10 - 15 % (w/v) PEG 4000, VAPOR DIFFUSION, HANGING DROP, temperature 295K
Resolution 2.40 Å R-free 0.248
2FK3 Structure of the Alzheimer's Amyloid Precursor Protein (APP) Copper Binding Domain in 'large unit cell' form Deposited 2006-01-04 Different construct Different oligomeric state Different ligand/ion Different experimental conditions Different structure-quality metrics Assembly 7 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric
Chain G 133–189（57 aa） Fragment：Residues 133 to 189
Not recorded No recorded non-water small molecule X-RAY DIFFRACTION
X-ray crystallization conditions VAPOR DIFFUSION, HANGING DROP；pH 5.4；295 K；0.1 M MES pH 5.4 - 5.6, 0.4 M NaCOOH, 10 - 15 % (w/v) PEG 4000, VAPOR DIFFUSION, HANGING DROP, temperature 295K
Resolution 2.40 Å R-free 0.248
2FK3 Structure of the Alzheimer's Amyloid Precursor Protein (APP) Copper Binding Domain in 'large unit cell' form Deposited 2006-01-04 Different construct Different oligomeric state Different ligand/ion Different experimental conditions Different structure-quality metrics Assembly 8 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric
Chain H 133–189（57 aa） Fragment：Residues 133 to 189
Not recorded CU COPPER (II) ION × 2 X-RAY DIFFRACTION
X-ray crystallization conditions VAPOR DIFFUSION, HANGING DROP；pH 5.4；295 K；0.1 M MES pH 5.4 - 5.6, 0.4 M NaCOOH, 10 - 15 % (w/v) PEG 4000, VAPOR DIFFUSION, HANGING DROP, temperature 295K
Resolution 2.40 Å R-free 0.248
2FKL Structure of the Alzheimer's Amyloid Precursor Protein (APP) Copper Binding Domain (Residues 126- 189 of APP) Deposited 2006-01-04 Different construct Different oligomeric state Different ligand/ion Different experimental conditions Different structure-quality metrics Assembly 1 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric
Chain A 124–189（66 aa） Fragment：Residues 124 to 189
Not recorded No recorded non-water small molecule X-RAY DIFFRACTION
X-ray crystallization conditions VAPOR DIFFUSION, HANGING DROP；pH 4.05；295 K；1.5 M (NH4)H2PO4, pH 4.05, VAPOR DIFFUSION, HANGING DROP, temperature 295K
Resolution 2.50 Å R-free 0.263
2FKL Structure of the Alzheimer's Amyloid Precursor Protein (APP) Copper Binding Domain (Residues 126- 189 of APP) Deposited 2006-01-04 Different construct Different oligomeric state Different ligand/ion Different experimental conditions Different structure-quality metrics Assembly 2 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric
Chain B 124–189（66 aa） Fragment：Residues 124 to 189
Not recorded No recorded non-water small molecule X-RAY DIFFRACTION
X-ray crystallization conditions VAPOR DIFFUSION, HANGING DROP；pH 4.05；295 K；1.5 M (NH4)H2PO4, pH 4.05, VAPOR DIFFUSION, HANGING DROP, temperature 295K
Resolution 2.50 Å R-free 0.263
2FMA Structure of the Alzheimer's Amyloid Precursor Protein (APP) Copper Binding Domain in 'small unit cell' form, atomic resolution Deposited 2006-01-08 Different construct Different oligomeric state Different ligand/ion Different experimental conditions Different structure-quality metrics Assembly 1 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric
Chain A 133–189（57 aa） Fragment：Copper Binding Domain(residues 133-189)
Not recorded GOL GLYCEROL × 1 X-RAY DIFFRACTION
X-ray crystallization conditions VAPOR DIFFUSION, HANGING DROP；pH 8；295 K；0.1M HEPES pH 8.0, 28-32% (w/v) PEG 10000, VAPOR DIFFUSION, HANGING DROP, temperature 295K
Resolution 0.85 Å R-free 0.150
2LFM A partially folded structure of amyloid-beta(1 40) in an aqueous environment Deposited 2011-07-06 Different construct Different oligomeric state Different ligand/ion Different experimental method Different experimental conditions Different structure-quality metrics Assembly 1 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric
Chain A 672–711（40 aa）
Not recorded No recorded non-water small molecule SOLUTION NMR
NMR measurement conditions pH 7.3；15 K；Ionic strength (raw mmCIF value) 0.07；Pressure ambient
NMR sample composition 20 mM potassium phosphate, 50 mM sodium chloride, 93% H2O/7% D2O | 93% H2O/7% D2O
Resolution not provided
2LLM Structure of amyloid precursor protein's transmembrane domain Deposited 2011-11-15 Different construct Different oligomeric state Different ligand/ion Different experimental method Different experimental conditions Different structure-quality metrics Assembly 1 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric
Chain A 686–726（41 aa） Fragment：UNP residues 686-726
Not recorded No recorded non-water small molecule SOLUTION NMR
NMR measurement conditions pH 4.6；318 K；Ionic strength (raw mmCIF value) 20；Pressure ambient
NMR sample composition 0.3-1 mM [U-100% 13C; U-100% 15N] APPjmtm, 21-70 mM [U-100% 2H] DPC, 95% H2O/5% D2O | 95% H2O/5% D2O
NMR sample composition 0.3-1 mM [U-100% 15N] APPjmtm, 21-70 mM DPC, 95% H2O/5% D2O | 95% H2O/5% D2O
Resolution not provided
2LMN Structural Model for a 40-Residue Beta-Amyloid Fibril with Two-Fold Symmetry, Positive Stagger Deposited 2011-12-08 Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental method Different experimental conditions Different structure-quality metrics Assembly 1 Protein homooligomer Homooligomer；Protein × 12 PDB declaration: dodecameric
Chain A 672–711（40 aa）
Chain B 672–711（40 aa）
Chain C 672–711（40 aa）
Chain D 672–711（40 aa）
Chain E 672–711（40 aa）
Chain F 672–711（40 aa）
Chain G 672–711（40 aa）
Chain H 672–711（40 aa）
Chain I 672–711（40 aa）
Chain J 672–711（40 aa）
Chain K 672–711（40 aa）
Chain L 672–711（40 aa）
Not recorded No recorded non-water small molecule SOLID-STATE NMR
NMR measurement conditions pH 7.4；300 K；Ionic strength (raw mmCIF value) 10；Pressure ambient
NMR sample composition selective 13C and 15N beta-amyloid, 10 mM phosphate buffer | 10 mM phosphate buffer
Resolution not provided
2LMO Structural Model for a 40-Residue Beta-Amyloid Fibril with Two-Fold Symmetry, Negative Stagger Deposited 2011-12-08 Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental method Different experimental conditions Different structure-quality metrics Assembly 1 Protein homooligomer Homooligomer；Protein × 12 PDB declaration: dodecameric
Chain A 672–711（40 aa）
Chain B 672–711（40 aa）
Chain C 672–711（40 aa）
Chain D 672–711（40 aa）
Chain E 672–711（40 aa）
Chain F 672–711（40 aa）
Chain G 672–711（40 aa）
Chain H 672–711（40 aa）
Chain I 672–711（40 aa）
Chain J 672–711（40 aa）
Chain K 672–711（40 aa）
Chain L 672–711（40 aa）
Not recorded No recorded non-water small molecule SOLID-STATE NMR
NMR measurement conditions pH 7.4；300 K；Ionic strength (raw mmCIF value) 10；Pressure ambient
NMR sample composition selective 13C and 15N beta-amyloid, 10 mM phosphate buffer | 10 mM phosphate buffer
Resolution not provided
2LMP Structural Model for a 40-residue Beta-Amyloid Fibril with Three-Fold Symmetry, Positive Stagger Deposited 2011-12-08 Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental method Different experimental conditions Different structure-quality metrics Assembly 1 Protein homooligomer Homooligomer；Protein × 18 PDB declaration: octadecameric
Chain A 672–711（40 aa）
Chain B 672–711（40 aa）
Chain C 672–711（40 aa）
Chain D 672–711（40 aa）
Chain E 672–711（40 aa）
Chain F 672–711（40 aa）
Chain G 672–711（40 aa）
Chain H 672–711（40 aa）
Chain I 672–711（40 aa）
Chain J 672–711（40 aa）
Chain K 672–711（40 aa）
Chain L 672–711（40 aa）
Chain M 672–711（40 aa）
Chain N 672–711（40 aa）
Chain O 672–711（40 aa）
Chain P 672–711（40 aa）
Chain Q 672–711（40 aa）
Chain R 672–711（40 aa）
Not recorded No recorded non-water small molecule SOLID-STATE NMR
NMR measurement conditions pH 7.4；300 K；Ionic strength (raw mmCIF value) 10；Pressure ambient
NMR sample composition selective 13C and 15N beta-amyloid, 10 mM phosphate buffer | 10 mM phosphate buffer
Resolution not provided
2LMQ Structural Model for a 40-residue Beta-Amyloid Fibril with Three-Fold Symmetry, Negative Stagger Deposited 2011-12-09 Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental method Different experimental conditions Different structure-quality metrics Assembly 1 Protein homooligomer Homooligomer；Protein × 18 PDB declaration: octadecameric
Chain A 672–711（40 aa）
Chain B 672–711（40 aa）
Chain C 672–711（40 aa）
Chain D 672–711（40 aa）
Chain E 672–711（40 aa）
Chain F 672–711（40 aa）
Chain G 672–711（40 aa）
Chain H 672–711（40 aa）
Chain I 672–711（40 aa）
Chain J 672–711（40 aa）
Chain K 672–711（40 aa）
Chain L 672–711（40 aa）
Chain M 672–711（40 aa）
Chain N 672–711（40 aa）
Chain O 672–711（40 aa）
Chain P 672–711（40 aa）
Chain Q 672–711（40 aa）
Chain R 672–711（40 aa）
Not recorded No recorded non-water small molecule SOLID-STATE NMR
NMR measurement conditions pH 7.4；300 K；Ionic strength (raw mmCIF value) 10；Pressure ambient
NMR sample composition selective 13C and 15N beta-amyloid, 10 mM phosphate buffer | 10 mM phosphate buffer
Resolution not provided
2LNQ 40-residue D23N beta amyloid fibril Deposited 2012-01-03 Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental method Different experimental conditions Different structure-quality metrics Assembly 1 Protein homooligomer Homooligomer；Protein × 8 PDB declaration: octameric
Chain A 672–711（40 aa）
Chain B 672–711（40 aa）
Chain C 672–711（40 aa）
Chain D 672–711（40 aa）
Chain E 672–711（40 aa）
Chain F 672–711（40 aa）
Chain G 672–711（40 aa）
Chain H 672–711（40 aa）
Mutation：D23N Mutation：D23N Mutation：D23N Mutation：D23N Mutation：D23N Mutation：D23N Mutation：D23N Mutation：D23N No recorded non-water small molecule SOLID-STATE NMR
NMR measurement conditions pH 7.4；279 K；Pressure ambient
NMR sample composition 25 uM [U-13C] protein, H2O | H2O
Resolution not provided
2LOH Dimeric structure of transmembrane domain of amyloid precursor protein in micellar environment Deposited 2012-01-24 Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental method Different experimental conditions Different structure-quality metrics Assembly 1 Protein homooligomer Homooligomer；Protein × 2 PDB declaration: dimeric
Chain A 686–726（41 aa） Fragment：UNP residues 686-726
Chain B 686–726（41 aa） Fragment：UNP residues 686-726
Not recorded No recorded non-water small molecule SOLUTION NMR
NMR measurement conditions pH 6.2；318 K；Ionic strength (raw mmCIF value) 20；Pressure ambient
NMR sample composition 0.9 mM [U-100% 15N] APPjmtm, 36 mM DPC, 95% H2O/5% D2O | 95% H2O/5% D2O
NMR sample composition 0.75 mM [U-100% 13C; U-100% 15N] APPjmtm, 0.75 mM APPjmtm, 60 mM [U-98% 2H] DPC, 100% D2O | 100% D2O
Resolution not provided
2LP1 The solution NMR structure of the transmembrane C-terminal domain of the amyloid precursor protein (C99) Deposited 2012-01-30 Different construct Different oligomeric state Different ligand/ion Different experimental method Different experimental conditions Different structure-quality metrics Assembly 1 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric
Chain A 671–770（100 aa） Fragment：UNP residues 683-728
Not recorded No recorded non-water small molecule SOLUTION NMR
NMR measurement conditions pH 6.5；318 K；Pressure ambient
NMR sample composition 10 % lyso myristoyl phosphatidylglycerol, 10 % [U-2H] D2O, 100 mM imidazole, 250 uM [U-100% 15N] APP_C99, 1 mM EDTA, 90% H2O/10% D2O | 90% H2O/10% D2O
Resolution not provided
2LZ3 Solution NMR structure of transmembrane domain of amyloid precursor protein WT Deposited 2012-09-23 Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental method Different experimental conditions Different structure-quality metrics Assembly 1 Protein homooligomer Homooligomer；Protein × 2 PDB declaration: dimeric
Chain A 699–726（28 aa）
Chain B 699–726（28 aa）
Not recorded No recorded non-water small molecule SOLUTION NMR
NMR measurement conditions pH 7.2；313 K；Ionic strength (raw mmCIF value) 0；Pressure ambient
NMR sample composition 0.5 mM [U-100% 13C; U-100% 15N] peptide, sodium phosphate, 10% D2O | 10% D2O
NMR sample composition 0.5 mM [U-100% 13C; U-100% 15N] peptide, sodium phosphate, 100% D2O | 100% D2O
NMR sample composition 0.5 mM [U-99% 15N] peptide, sodium phosphate, 90% H2O/10% D2O | 90% H2O/10% D2O
Resolution not provided
2LZ4 Solution NMR structure of transmembrane domain of amyloid precursor protein V44M Deposited 2012-09-23 Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental method Different experimental conditions Different structure-quality metrics Assembly 1 Protein homooligomer Homooligomer；Protein × 2 PDB declaration: dimeric
Chain A 699–726（28 aa）
Chain B 699–726（28 aa）
Mutation：V21M Mutation：V21M No recorded non-water small molecule SOLUTION NMR
NMR measurement conditions pH 7.2；313 K；Ionic strength (raw mmCIF value) 0；Pressure ambient
NMR sample composition 0.5 mM [U-100% 13C; U-100% 15N] peptide, sodium chloride, 90% H2O/10% D2O | 90% H2O/10% D2O
NMR sample composition 0.5 mM [U-100% 13C; U-100% 15N] peptide, sodium phosphate, 100% D2O | 100% D2O
NMR sample composition 0.5 mM [U-99% 15N] peptide, sodium chloride, 90% H2O/10% D2O | 90% H2O/10% D2O
Resolution not provided
2M4J 40-residue beta-amyloid fibril derived from Alzheimer's disease brain Deposited 2013-02-05 Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental method Different experimental conditions Different structure-quality metrics Assembly 1 Protein homooligomer Homooligomer；Protein × 9 PDB declaration: nonameric
Chain A 672–711（40 aa） Fragment：UNP residues 672-711
Chain B 672–711（40 aa） Fragment：UNP residues 672-711
Chain C 672–711（40 aa） Fragment：UNP residues 672-711
Chain D 672–711（40 aa） Fragment：UNP residues 672-711
Chain E 672–711（40 aa） Fragment：UNP residues 672-711
Chain F 672–711（40 aa） Fragment：UNP residues 672-711
Chain G 672–711（40 aa） Fragment：UNP residues 672-711
Chain H 672–711（40 aa） Fragment：UNP residues 672-711
Chain I 672–711（40 aa） Fragment：UNP residues 672-711
Not recorded No recorded non-water small molecule SOLID-STATE NMR
NMR measurement conditions pH 7.4；288 K；Ionic strength (raw mmCIF value) 10；Pressure ambient
NMR sample composition 1-2 mg selectively and uniformly labeled samples beta-amyloid peptide | none
Resolution not provided
2M9R 3D NMR structure of a complex between the amyloid beta peptide (1-40) and the polyphenol epsilon-viniferin glucoside Deposited 2013-06-19 Different construct Different oligomeric state Different ligand/ion Different experimental method Different experimental conditions Different structure-quality metrics Assembly 1 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric
Chain A 672–711（40 aa） Fragment：UNP residues 672-711
Not recorded 23Y (2S,3S)-3-(3,5-dihydroxyphenyl)-2-(4-hydroxyphenyl)-4-[(E)-2-(4-hydroxyphenyl)ethenyl]-2,3-dihydro-1-benzofuran-6-yl beta-D-glucopyranoside × 2 SOLUTION NMR
NMR measurement conditions 300 K；Pressure ambient
NMR sample composition 1 mM amyloid peptide, 100% DMSO-d6 | 100% DMSO-d6
Resolution not provided
2M9S 3D NMR structure of a complex between the amyloid beta peptide (1-40) and the polyphenol epsilon-viniferin glucoside Deposited 2013-06-19 Different construct Different oligomeric state Different ligand/ion Different experimental method Different experimental conditions Different structure-quality metrics Assembly 1 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric
Chain A 672–711（40 aa） Fragment：UNP residues 672-711
Not recorded 23Y (2S,3S)-3-(3,5-dihydroxyphenyl)-2-(4-hydroxyphenyl)-4-[(E)-2-(4-hydroxyphenyl)ethenyl]-2,3-dihydro-1-benzofuran-6-yl beta-D-glucopyranoside × 2 SOLUTION NMR
NMR measurement conditions 300 K；Pressure ambient
NMR sample composition 1 mM amyloid peptide, 100% DMSO-d6 | 100% DMSO-d6
Resolution not provided
2MGT Zinc induced dimer of the metal binding domain 1-16 of human amyloid beta-peptide with Alzheimer's disease pathogenic English mutation H6R Deposited 2013-11-06 Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental method Different experimental conditions Different structure-quality metrics Assembly 1 Protein homooligomer Homooligomer；Protein × 2 PDB declaration: dimeric
Chain A 672–687（16 aa） Fragment：metal binding domain, UNP residues 672-687
Chain B 672–687（16 aa） Fragment：metal binding domain, UNP residues 672-687
Mutation：H6R Non-standard monomer：Yes (specific site not provided by mmCIF) Mutation：H6R Non-standard monomer：Yes (specific site not provided by mmCIF) ZN ZINC ION × 1 SOLUTION NMR
NMR measurement conditions pH 6.8；274 K；Pressure ambient
NMR measurement conditions 278 K；Pressure ambient
NMR sample composition 2 mM protein_1-1, 20 mM [U-99% 2H] bis-Tris-2, 40 uM d4 (100%) TSP-3, 90% H2O/10% D2O | 90% H2O/10% D2O
NMR sample composition 2 mM protein_1-4, 20 mM [U-99% 2H] bis-Tris-5, 40 uM d4 (100%) TSP-6, 100% D2O | 100% D2O
NMR sample composition 2 mM protein_1-7, 1 mM zinc cloride-8, 20 mM [U-99% 2H] bis-Tris-9, 40 uM d4 (100%) TSP-10, 90% H2O/10% D2O | 90% H2O/10% D2O
NMR sample composition 2 mM protein_1-11, 1 mM zinc cloride-12, 20 mM [U-99% 2H] bis-Tris-13, 40 uM d4 (100%) TSP-14, 100% D2O | 100% D2O
Resolution not provided
2MJ1 NMR structure of the soluble A beta 17-34 peptide Deposited 2013-12-23 Different construct Different oligomeric state Different ligand/ion Different experimental method Different experimental conditions Different structure-quality metrics Assembly 1 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric
Chain A 688–705（18 aa） Fragment：UNP RESIDUES 688-705
Not recorded No recorded non-water small molecule SOLUTION NMR
NMR measurement conditions pH 7；278 K；Ionic strength (raw mmCIF value) 0.12；Pressure ambient
NMR sample composition 50 mM sodium phosphate-1, 0.2 uM sodium azide-2, 95% H2O/5% D2O | 95% H2O/5% D2O
Resolution not provided
2MPZ Atomic model of the Abeta D23N "Iowa" mutant using solid-state NMR, EM and Rosetta modeling Deposited 2014-06-10 Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental method Different experimental conditions Different structure-quality metrics Assembly 1 Protein homooligomer Homooligomer；Protein × 27 PDB declaration: 27-meric
Chain A 686–711（26 aa）
Chain B 686–711（26 aa）
Chain C 686–711（26 aa）
Chain D 686–711（26 aa）
Chain E 686–711（26 aa）
Chain F 686–711（26 aa）
Chain G 686–711（26 aa）
Chain H 686–711（26 aa）
Chain I 686–711（26 aa）
Chain J 686–711（26 aa）
Chain K 686–711（26 aa）
Chain L 686–711（26 aa）
Chain M 686–711（26 aa）
Chain N 686–711（26 aa）
Chain O 686–711（26 aa）
Chain P 686–711（26 aa）
Chain Q 686–711（26 aa）
Chain R 686–711（26 aa）
Chain S 686–711（26 aa）
Chain T 686–711（26 aa）
Chain U 686–711（26 aa）
Chain V 686–711（26 aa）
Chain W 686–711（26 aa）
Chain X 686–711（26 aa）
Chain Y 686–711（26 aa）
Chain Z 686–711（26 aa）
Chain a 686–711（26 aa）
Not recorded No recorded non-water small molecule SOLID-STATE NMR
NMR measurement conditions pH 7.4；298 K；Ionic strength (raw mmCIF value) 10；Pressure ambient
NMR sample composition 25 uM [U-99% 13C; U-99% 15N] Abeta D23N, solid
Resolution not provided
2MVX Atomic-resolution 3D structure of amyloid-beta fibrils: the Osaka mutation Deposited 2014-10-17 Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental method Different experimental conditions Different structure-quality metrics Assembly 1 Protein homooligomer Homooligomer；Protein × 10 PDB declaration: decameric
Chain A 672–711（40 aa） Fragment：UNP residues 672-711
Chain B 672–711（40 aa） Fragment：UNP residues 672-711
Chain C 672–711（40 aa） Fragment：UNP residues 672-711
Chain D 672–711（40 aa） Fragment：UNP residues 672-711
Chain E 672–711（40 aa） Fragment：UNP residues 672-711
Chain F 672–711（40 aa） Fragment：UNP residues 672-711
Chain G 672–711（40 aa） Fragment：UNP residues 672-711
Chain H 672–711（40 aa） Fragment：UNP residues 672-711
Chain I 672–711（40 aa） Fragment：UNP residues 672-711
Chain J 672–711（40 aa） Fragment：UNP residues 672-711
Mutation：E22Delta Mutation：E22Delta Mutation：E22Delta Mutation：E22Delta Mutation：E22Delta Mutation：E22Delta Mutation：E22Delta Mutation：E22Delta Mutation：E22Delta Mutation：E22Delta No recorded non-water small molecule SOLID-STATE NMR
NMR measurement conditions pH 7；283 K；Ionic strength (raw mmCIF value) 0；Pressure ambient
NMR sample composition 15 mg/mL [U-100% 13C; U-100% 15N] amyloid beta, 100% H2O | 100% H2O
NMR sample composition 15 mg/mL [U-100% 13C] amyloid beta, 100% H2O | 100% H2O
NMR sample composition 15 mg/mL [U-100% 13C]/[U-100% 15N] amyloid beta, 100% H2O | 100% H2O
NMR sample composition 15 mg/mL [U-100% 2-13C-glucose; U-100% 15N] amyloid beta, 100% H2O | 100% H2O
NMR sample composition 15 mg/mL [U-100% 13C; U-100% 15N]/natural abundance amyloid beta, 100% H2O | 100% H2O
Resolution not provided
2MXU 42-Residue Beta Amyloid Fibril Deposited 2015-01-14 Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental method Different experimental conditions Different structure-quality metrics Assembly 1 Protein homooligomer Homooligomer；Protein × 12 PDB declaration: dodecameric
Chain A 672–713（42 aa） Fragment：UNP residues 672-713
Chain B 672–713（42 aa） Fragment：UNP residues 672-713
Chain C 672–713（42 aa） Fragment：UNP residues 672-713
Chain D 672–713（42 aa） Fragment：UNP residues 672-713
Chain E 672–713（42 aa） Fragment：UNP residues 672-713
Chain F 672–713（42 aa） Fragment：UNP residues 672-713
Chain G 672–713（42 aa） Fragment：UNP residues 672-713
Chain H 672–713（42 aa） Fragment：UNP residues 672-713
Chain I 672–713（42 aa） Fragment：UNP residues 672-713
Chain J 672–713（42 aa） Fragment：UNP residues 672-713
Chain K 672–713（42 aa） Fragment：UNP residues 672-713
Chain L 672–713（42 aa） Fragment：UNP residues 672-713
Not recorded No recorded non-water small molecule SOLID-STATE NMR
NMR measurement conditions pH 7.4；283 K；Pressure ambient
NMR sample composition 50 uM [U-100% 13C; U-100% 15N] AB42, 10 mM sodium phosphate, 100% H2O | 100% H2O
Resolution not provided
2NAO Atomic resolution structure of a disease-relevant Abeta(1-42) amyloid fibril Deposited 2016-01-07 Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental method Different experimental conditions Different structure-quality metrics Assembly 1 Protein homooligomer Homooligomer；Protein × 6 PDB declaration: hexameric
Chain A 672–713（42 aa）
Chain B 672–713（42 aa）
Chain C 672–713（42 aa）
Chain D 672–713（42 aa）
Chain E 672–713（42 aa）
Chain F 672–713（42 aa）
Not recorded No recorded non-water small molecule SOLUTION NMR
NMR measurement conditions pH 7.4；277 K；Pressure ambient
NMR sample composition 100 mM sodium chloride, 100 mM sodium phosphate, 100 uM zinc chloride, 95% H2O/5% D2O | 95% H2O/5% D2O
Resolution not provided
2OTK Structure of Alzheimer Ab peptide in complex with an engineered binding protein Deposited 2007-02-08 Different construct Different oligomeric state Different ligand/ion Different experimental method Different experimental conditions Different structure-quality metrics Assembly 1 Protein heterocomplex Heteromer；Protein × 3 PDB declaration: trimeric
Chain C 672–711（40 aa） Fragment：residues 672-711
Not recorded No recorded non-water small molecule SOLUTION NMR
NMR measurement conditions pH 7.2；298 K；Ionic strength (raw mmCIF value) 20 mM sodium phophate；Pressure ambient
NMR measurement conditions pH 7.2；298 K；Ionic strength (raw mmCIF value) 20 mM sodium phosphate；Pressure ambient
NMR sample composition 400 uM [U-100% 13C; U-100% 15N] Abeta peptide, 400 uM ZAb3 dimers, 20 mM Na-phosphate buffer, 90% H2O/10% D2O | 90% H2O/10% D2O
NMR sample composition 400 uM Abeta peptide, 400 uM [U-100% 13C; U-100% 15N] ZAb3 dimers, 20 mM Na-phosphate buffer, 90% H2O/10% D2O | 90% H2O/10% D2O
Resolution not provided
2R0W PFA2 FAB complexed with Abeta1-8 Deposited 2007-08-21 Different construct Different oligomeric state Different ligand/ion Different experimental conditions Different structure-quality metrics Assembly 1 Protein heterocomplex Heteromer；Protein × 3 PDB declaration: trimeric
Chain Q 672–679（8 aa） Fragment：octapeptide
Not recorded NA SODIUM ION × 1 X-RAY DIFFRACTION
X-ray crystallization conditions VAPOR DIFFUSION；pH 5.3；295 K；25% PEG-MME 5000, 0.1 M OAc, pH 5.3, VAPOR DIFFUSION, temperature 295K
Resolution 2.50 Å R-free 0.277
2WK3 Crystal structure of human insulin-degrading enzyme in complex with amyloid-beta (1-42) Deposited 2009-06-05 Different construct Different ligand/ion Different experimental conditions Different structure-quality metrics Assembly 1 Protein heterocomplex Heteromer；Protein × 2 PDB declaration: dimeric
Chain D 672–713（42 aa） Fragment：BETA-AMYLOID PROTEIN 42, RESIDUES 672-713
Not recorded ZN ZINC ION × 1 X-RAY DIFFRACTION mmCIF provides none of the parsed conditions Resolution 2.59 Å R-free 0.232
2WK3 Crystal structure of human insulin-degrading enzyme in complex with amyloid-beta (1-42) Deposited 2009-06-05 Different construct Different ligand/ion Different experimental conditions Different structure-quality metrics Assembly 2 Protein heterocomplex Heteromer；Protein × 2 PDB declaration: dimeric
Chain C 672–713（42 aa） Fragment：BETA-AMYLOID PROTEIN 42, RESIDUES 672-713
Not recorded ZN ZINC ION × 1 X-RAY DIFFRACTION mmCIF provides none of the parsed conditions Resolution 2.59 Å R-free 0.232
2Y29 Structure of segment KLVFFA from the amyloid-beta peptide (Ab, residues 16-21), alternate polymorph III Deposited 2010-12-14 Different construct Different oligomeric state Different ligand/ion Different experimental conditions Different structure-quality metrics Assembly 1 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric
Chain A 687–692（6 aa） Fragment：SEGMENT KLVFFA, RESIDUES 687-692
Not recorded No recorded non-water small molecule X-RAY DIFFRACTION
X-ray crystallization conditions pH 8.5；AB16-21 FORM III CRYSTALS WERE OBTAINED AFTER THE SEGMENT WAS DISSOLVED IN WATER AT 5 MG/ML AND MIXED WITH 0.2M AMMONIUM ACETATE, 0.1 M TRIS BUFFER PH 8.5 AND 30% ISOPROPANOL.
Resolution 2.30 Å R-free 0.260
2Y2A Structure of segment KLVFFA from the amyloid-beta peptide (Ab, residues 16-21), alternate polymorph I Deposited 2010-12-14 Different construct Different oligomeric state Different ligand/ion Different experimental conditions Different structure-quality metrics Assembly 1 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric
Chain A 687–692（6 aa） Fragment：SEGMENT KLVFFA, RESIDUES 687-692
Not recorded ACT ACETATE ION × 1 X-RAY DIFFRACTION
X-ray crystallization conditions pH 5.5；AB16-21 FORM I CRYSTALS WERE OBTAINED AFTER THE SEGMENT WAS DISSOLVED IN WATER AT 5 MG/ML AND MIXED WITH 0.2 M AMMONIUM ACETATE, 0.1 M BIS-TRIS PH 5.5, 45 % V/V MPD
Resolution 1.91 Å R-free 0.248
2Y3J Structure of segment AIIGLM from the amyloid-beta peptide (Ab, residues 30-35) Deposited 2010-12-21 Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental conditions Different structure-quality metrics Assembly 1 Protein homooligomer Homooligomer；Protein × 4 PDB declaration: tetrameric
Chain A 701–706（6 aa） Fragment：RESIDUES 701-706
Chain B 701–706（6 aa） Fragment：RESIDUES 701-706
Chain C 701–706（6 aa） Fragment：RESIDUES 701-706
Chain D 701–706（6 aa） Fragment：RESIDUES 701-706
Not recorded No recorded non-water small molecule X-RAY DIFFRACTION
X-ray crystallization conditions pH 7；AB3035 WAS DISSOLVED IN WATER AT 1MG/ML AND MIXED WITH 2 M SODIUM CHLORIDE, pH 7
Resolution 1.99 Å R-free 0.267
2Y3J Structure of segment AIIGLM from the amyloid-beta peptide (Ab, residues 30-35) Deposited 2010-12-21 Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental conditions Different structure-quality metrics Assembly 2 Protein homooligomer Homooligomer；Protein × 4 PDB declaration: tetrameric
Chain E 701–706（6 aa） Fragment：RESIDUES 701-706
Chain F 701–706（6 aa） Fragment：RESIDUES 701-706
Chain G 701–706（6 aa） Fragment：RESIDUES 701-706
Chain H 701–706（6 aa） Fragment：RESIDUES 701-706
Not recorded No recorded non-water small molecule X-RAY DIFFRACTION
X-ray crystallization conditions pH 7；AB3035 WAS DISSOLVED IN WATER AT 1MG/ML AND MIXED WITH 2 M SODIUM CHLORIDE, pH 7
Resolution 1.99 Å R-free 0.267
2Y3K Structure of segment MVGGVVIA from the amyloid-beta peptide (Ab, residues 35-42), alternate polymorph 1 Deposited 2010-12-21 Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental conditions Different structure-quality metrics Assembly 1 Protein homooligomer Homooligomer；Protein × 2 PDB declaration: dimeric
Chain A 706–713（8 aa） Fragment：RESIDUES 706-713
Chain B 706–713（8 aa） Fragment：RESIDUES 706-713
Not recorded No recorded non-water small molecule X-RAY DIFFRACTION
X-ray crystallization conditions pH 5.6；AB3542 CRYSTALS (FIRST DISSOLVED IN WATER) WERE FOUND IN 1.5-YEAR-OLD TRAYS SET AT 0.5 MG/ML IN 1.26 M NA PHOSPHATE MONOBASIC MONOHYDRATE, 0.14 M K PHOSPHATE DIBASIC, PH 5.6 (CRYSTAL FORM I)
Resolution 1.90 Å R-free 0.231
2Y3K Structure of segment MVGGVVIA from the amyloid-beta peptide (Ab, residues 35-42), alternate polymorph 1 Deposited 2010-12-21 Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental conditions Different structure-quality metrics Assembly 2 Protein homooligomer Homooligomer；Protein × 2 PDB declaration: dimeric
Chain C 706–713（8 aa） Fragment：RESIDUES 706-713
Chain D 706–713（8 aa） Fragment：RESIDUES 706-713
Not recorded No recorded non-water small molecule X-RAY DIFFRACTION
X-ray crystallization conditions pH 5.6；AB3542 CRYSTALS (FIRST DISSOLVED IN WATER) WERE FOUND IN 1.5-YEAR-OLD TRAYS SET AT 0.5 MG/ML IN 1.26 M NA PHOSPHATE MONOBASIC MONOHYDRATE, 0.14 M K PHOSPHATE DIBASIC, PH 5.6 (CRYSTAL FORM I)
Resolution 1.90 Å R-free 0.231
2Y3K Structure of segment MVGGVVIA from the amyloid-beta peptide (Ab, residues 35-42), alternate polymorph 1 Deposited 2010-12-21 Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental conditions Different structure-quality metrics Assembly 3 Protein homooligomer Homooligomer；Protein × 2 PDB declaration: dimeric
Chain E 706–713（8 aa） Fragment：RESIDUES 706-713
Chain F 706–713（8 aa） Fragment：RESIDUES 706-713
Not recorded No recorded non-water small molecule X-RAY DIFFRACTION
X-ray crystallization conditions pH 5.6；AB3542 CRYSTALS (FIRST DISSOLVED IN WATER) WERE FOUND IN 1.5-YEAR-OLD TRAYS SET AT 0.5 MG/ML IN 1.26 M NA PHOSPHATE MONOBASIC MONOHYDRATE, 0.14 M K PHOSPHATE DIBASIC, PH 5.6 (CRYSTAL FORM I)
Resolution 1.90 Å R-free 0.231
2Y3K Structure of segment MVGGVVIA from the amyloid-beta peptide (Ab, residues 35-42), alternate polymorph 1 Deposited 2010-12-21 Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental conditions Different structure-quality metrics Assembly 4 Protein homooligomer Homooligomer；Protein × 2 PDB declaration: dimeric
Chain G 706–713（8 aa） Fragment：RESIDUES 706-713
Chain H 706–713（8 aa） Fragment：RESIDUES 706-713
Not recorded No recorded non-water small molecule X-RAY DIFFRACTION
X-ray crystallization conditions pH 5.6；AB3542 CRYSTALS (FIRST DISSOLVED IN WATER) WERE FOUND IN 1.5-YEAR-OLD TRAYS SET AT 0.5 MG/ML IN 1.26 M NA PHOSPHATE MONOBASIC MONOHYDRATE, 0.14 M K PHOSPHATE DIBASIC, PH 5.6 (CRYSTAL FORM I)
Resolution 1.90 Å R-free 0.231
2Y3L Structure of segment MVGGVVIA from the amyloid-beta peptide (Ab, residues 35-42), alternate polymorph 2 Deposited 2010-12-21 Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental conditions Different structure-quality metrics Assembly 1 Protein homooligomer Homooligomer；Protein × 4 PDB declaration: tetrameric
Chain A 706–713（8 aa） Fragment：RESIDUES 706-713
Chain B 706–713（8 aa） Fragment：RESIDUES 706-713
Chain C 706–713（8 aa） Fragment：RESIDUES 706-713
Chain G 706–713（8 aa） Fragment：RESIDUES 706-713
Not recorded No recorded non-water small molecule X-RAY DIFFRACTION
X-ray crystallization conditions pH 7.5；AB3542 CRYSTALS (FIRST DISSOLVED IN WATER) WERE FOUND IN 1.5-YEAR-OLD TRAYS SET AT 0.5 MG/ML IN 0.1 M HEPES PH 7.5, 0.5 M MG FORMATE (CRYSTAL FORM II)
Resolution 2.10 Å R-free 0.247
3AYU Crystal structure of MMP-2 active site mutant in complex with APP-drived decapeptide inhibitor Deposited 2011-05-17 Different construct Different ligand/ion Different experimental conditions Different structure-quality metrics Assembly 1 Protein heterocomplex Heteromer；Protein × 2 PDB declaration: dimeric
Chain B 586–595（10 aa） Fragment：UNP residues 586-595
Not recorded ZN ZINC ION × 2 CA CALCIUM ION × 3 X-RAY DIFFRACTION mmCIF provides none of the parsed conditions Resolution 2.00 Å R-free 0.205
3DXC Crystal structure of the intracellular domain of human APP in complex with Fe65-PTB2 Deposited 2008-07-24 Different construct Different ligand/ion Different experimental conditions Different structure-quality metrics Assembly 1 Protein heterocomplex Heteromer；Protein × 2 PDB declaration: dimeric
Chain B 739–770（32 aa） Fragment：APP intracellular domain, UNP residues 739-770
Not recorded No recorded non-water small molecule X-RAY DIFFRACTION
X-ray crystallization conditions VAPOR DIFFUSION；pH 4.6；293 K；3.2 M NaCl,0.1 M sodium acetate , pH 4.6, VAPOR DIFFUSION, temperature 293K
Resolution 2.10 Å R-free 0.238
3DXC Crystal structure of the intracellular domain of human APP in complex with Fe65-PTB2 Deposited 2008-07-24 Different construct Different ligand/ion Different experimental conditions Different structure-quality metrics Assembly 2 Protein heterocomplex Heteromer；Protein × 2 PDB declaration: dimeric
Chain D 739–770（32 aa） Fragment：APP intracellular domain, UNP residues 739-770
Not recorded No recorded non-water small molecule X-RAY DIFFRACTION
X-ray crystallization conditions VAPOR DIFFUSION；pH 4.6；293 K；3.2 M NaCl,0.1 M sodium acetate , pH 4.6, VAPOR DIFFUSION, temperature 293K
Resolution 2.10 Å R-free 0.238
3DXD Crystal structure of the intracellular domain of human APP (T668E mutant) in complex with Fe65-PTB2 Deposited 2008-07-24 Different construct Different mutation/modification Different ligand/ion Different experimental conditions Different structure-quality metrics Assembly 1 Protein heterocomplex Heteromer；Protein × 2 PDB declaration: dimeric
Chain B 739–770（32 aa） Fragment：APP intracellular domain, UNP residues 739-770
Mutation：T668E No recorded non-water small molecule X-RAY DIFFRACTION
X-ray crystallization conditions VAPOR DIFFUSION；pH 4.6；293 K；3.2 M NaCl, 0.1 M sodium acetate , pH 4.6, VAPOR DIFFUSION, temperature 293K
Resolution 2.20 Å R-free 0.247
3DXD Crystal structure of the intracellular domain of human APP (T668E mutant) in complex with Fe65-PTB2 Deposited 2008-07-24 Different construct Different mutation/modification Different ligand/ion Different experimental conditions Different structure-quality metrics Assembly 2 Protein heterocomplex Heteromer；Protein × 2 PDB declaration: dimeric
Chain D 739–770（32 aa） Fragment：APP intracellular domain, UNP residues 739-770
Mutation：T668E No recorded non-water small molecule X-RAY DIFFRACTION
X-ray crystallization conditions VAPOR DIFFUSION；pH 4.6；293 K；3.2 M NaCl, 0.1 M sodium acetate , pH 4.6, VAPOR DIFFUSION, temperature 293K
Resolution 2.20 Å R-free 0.247
3DXE Crystal structure of the intracellular domain of human APP (T668A mutant) in complex with Fe65-PTB2 Deposited 2008-07-24 Different construct Different mutation/modification Different ligand/ion Different experimental conditions Different structure-quality metrics Assembly 1 Protein heterocomplex Heteromer；Protein × 2 PDB declaration: dimeric
Chain B 739–770（32 aa） Fragment：APP intracellular domain, UNP residues 739-770
Mutation：T668A No recorded non-water small molecule X-RAY DIFFRACTION
X-ray crystallization conditions VAPOR DIFFUSION；pH 4.6；293 K；3.2 M NaCl, 0.1 M sodium acetate , pH 4.6, VAPOR DIFFUSION, temperature 293K
Resolution 2.00 Å R-free 0.241
3DXE Crystal structure of the intracellular domain of human APP (T668A mutant) in complex with Fe65-PTB2 Deposited 2008-07-24 Different construct Different mutation/modification Different ligand/ion Different experimental conditions Different structure-quality metrics Assembly 2 Protein heterocomplex Heteromer；Protein × 2 PDB declaration: dimeric
Chain D 739–770（32 aa） Fragment：APP intracellular domain, UNP residues 739-770
Mutation：T668A No recorded non-water small molecule X-RAY DIFFRACTION
X-ray crystallization conditions VAPOR DIFFUSION；pH 4.6；293 K；3.2 M NaCl, 0.1 M sodium acetate , pH 4.6, VAPOR DIFFUSION, temperature 293K
Resolution 2.00 Å R-free 0.241
3GCI Crystal Structure of the Complex Formed Between a New Isoform of Phospholipase A2 with C-terminal Amyloid Beta Heptapeptide at 2 A Resolution Deposited 2009-02-22 Different construct Different ligand/ion Different experimental conditions Different structure-quality metrics Assembly 1 Protein heterocomplex Heteromer；Protein × 2 PDB declaration: dimeric
Chain P 707–713（7 aa） Fragment：UNP residues 707-713
Not recorded CA CALCIUM ION × 1 X-RAY DIFFRACTION
X-ray crystallization conditions VAPOR DIFFUSION, HANGING DROP；pH 6；290 K；10mM Sodium phosphate, pH 6.0, 1mM CaCl2, VAPOR DIFFUSION, HANGING DROP, temperature 290K
Resolution 2.04 Å R-free 0.221
3IFL X-ray structure of amyloid beta peptide:antibody (Abeta1-7:12A11) complex Deposited 2009-07-24 Different construct Different oligomeric state Different ligand/ion Different experimental conditions Different structure-quality metrics Assembly 1 Protein heterocomplex Heteromer；Protein × 3 PDB declaration: trimeric
Chain P 672–678（7 aa） Fragment：residues 672-678
Not recorded No recorded non-water small molecule X-RAY DIFFRACTION
X-ray crystallization conditions VAPOR DIFFUSION, HANGING DROP；pH 9；295 K；Protein: 15 mg/ml, 10 mM Hepes, pH 7.5, 75 mM NaCl. Protein:peptide molar ratio: 1:1.1. Reservoir: 32% PEG400, 0.1M Tris pH 9.0, VAPOR DIFFUSION, HANGING DROP, temperature 295K
Resolution 1.50 Å R-free 0.206
3IFN X-ray structure of amyloid beta peptide:antibody (Abeta1-40:12A11) complex Deposited 2009-07-24 Different construct Different oligomeric state Different ligand/ion Different experimental conditions Different structure-quality metrics Assembly 1 Protein heterocomplex Heteromer；Protein × 3 PDB declaration: trimeric
Chain P 672–711（40 aa） Fragment：residues 672-711
Not recorded No recorded non-water small molecule X-RAY DIFFRACTION
X-ray crystallization conditions VAPOR DIFFUSION, SITTING DROP；pH 7.5；295 K；Protein: 5.3 mg/ml, 10 mM Hepes, pH 7.5, 75 mM NaCl. Protein:peptide molar ratio: 1:4.5. Reservoir: 0.2M NaCl, 25% Peg 4K, 0.1M Hepes pH 7.5, VAPOR DIFFUSION, SITTING DROP, temperature 295K
Resolution 1.50 Å R-free 0.212
3IFO X-ray structure of amyloid beta peptide:antibody (Abeta1-7:10D5) complex Deposited 2009-07-24 Different construct Different oligomeric state Different ligand/ion Different experimental conditions Different structure-quality metrics Assembly 1 Protein heterocomplex Heteromer；Protein × 3 PDB declaration: trimeric
Chain P 672–678（7 aa） Fragment：residues 672-678
Not recorded No recorded non-water small molecule X-RAY DIFFRACTION
X-ray crystallization conditions VAPOR DIFFUSION, SITTING DROP；pH 7.5；295 K；Protein: 15 mg/ml, 10 mM Hepes pH 7.5, 75 mM NaCl. Protein:peptide molar ratio: 1:2. Reservoir: 30% PEG4K, VAPOR DIFFUSION, SITTING DROP, temperature 295K
Resolution 2.15 Å R-free 0.218
3IFO X-ray structure of amyloid beta peptide:antibody (Abeta1-7:10D5) complex Deposited 2009-07-24 Different construct Different oligomeric state Different ligand/ion Different experimental conditions Different structure-quality metrics Assembly 2 Protein heterocomplex Heteromer；Protein × 3 PDB declaration: trimeric
Chain Q 672–678（7 aa） Fragment：residues 672-678
Not recorded No recorded non-water small molecule X-RAY DIFFRACTION
X-ray crystallization conditions VAPOR DIFFUSION, SITTING DROP；pH 7.5；295 K；Protein: 15 mg/ml, 10 mM Hepes pH 7.5, 75 mM NaCl. Protein:peptide molar ratio: 1:2. Reservoir: 30% PEG4K, VAPOR DIFFUSION, SITTING DROP, temperature 295K
Resolution 2.15 Å R-free 0.218
3IFP X-ray structure of amyloid beta peptide:antibody (Abeta1-7:12B4) complex Deposited 2009-07-24 Different construct Different oligomeric state Different ligand/ion Different experimental conditions Different structure-quality metrics Assembly 1 Protein heterocomplex Heteromer；Protein × 3 PDB declaration: trimeric
Chain P 672–678（7 aa） Fragment：residues 672-678
Not recorded No recorded non-water small molecule X-RAY DIFFRACTION
X-ray crystallization conditions VAPOR DIFFUSION, HANGING DROP；pH 7；295 K；Protein: 4.1 mg/ml, 10 mM Hepes pH 7.5, 75 mM NaCl. Protein:peptide molar ratio: 1:1.8. Reservoir: 30%PEG8K, 0.1M Hepes pH 7.0, 0.2M (NH4)2SO4, VAPOR DIFFUSION, HANGING DROP, temperature 295K
Resolution 2.95 Å R-free 0.269
3IFP X-ray structure of amyloid beta peptide:antibody (Abeta1-7:12B4) complex Deposited 2009-07-24 Different construct Different oligomeric state Different ligand/ion Different experimental conditions Different structure-quality metrics Assembly 2 Protein heterocomplex Heteromer；Protein × 3 PDB declaration: trimeric
Chain Q 672–678（7 aa） Fragment：residues 672-678
Not recorded No recorded non-water small molecule X-RAY DIFFRACTION
X-ray crystallization conditions VAPOR DIFFUSION, HANGING DROP；pH 7；295 K；Protein: 4.1 mg/ml, 10 mM Hepes pH 7.5, 75 mM NaCl. Protein:peptide molar ratio: 1:1.8. Reservoir: 30%PEG8K, 0.1M Hepes pH 7.0, 0.2M (NH4)2SO4, VAPOR DIFFUSION, HANGING DROP, temperature 295K
Resolution 2.95 Å R-free 0.269
3IFP X-ray structure of amyloid beta peptide:antibody (Abeta1-7:12B4) complex Deposited 2009-07-24 Different construct Different oligomeric state Different ligand/ion Different experimental conditions Different structure-quality metrics Assembly 3 Protein heterocomplex Heteromer；Protein × 3 PDB declaration: trimeric
Chain R 672–678（7 aa） Fragment：residues 672-678
Not recorded No recorded non-water small molecule X-RAY DIFFRACTION
X-ray crystallization conditions VAPOR DIFFUSION, HANGING DROP；pH 7；295 K；Protein: 4.1 mg/ml, 10 mM Hepes pH 7.5, 75 mM NaCl. Protein:peptide molar ratio: 1:1.8. Reservoir: 30%PEG8K, 0.1M Hepes pH 7.0, 0.2M (NH4)2SO4, VAPOR DIFFUSION, HANGING DROP, temperature 295K
Resolution 2.95 Å R-free 0.269
3IFP X-ray structure of amyloid beta peptide:antibody (Abeta1-7:12B4) complex Deposited 2009-07-24 Different construct Different oligomeric state Different ligand/ion Different experimental conditions Different structure-quality metrics Assembly 4 Protein heterocomplex Heteromer；Protein × 3 PDB declaration: trimeric
Chain S 672–678（7 aa） Fragment：residues 672-678
Not recorded No recorded non-water small molecule X-RAY DIFFRACTION
X-ray crystallization conditions VAPOR DIFFUSION, HANGING DROP；pH 7；295 K；Protein: 4.1 mg/ml, 10 mM Hepes pH 7.5, 75 mM NaCl. Protein:peptide molar ratio: 1:1.8. Reservoir: 30%PEG8K, 0.1M Hepes pH 7.0, 0.2M (NH4)2SO4, VAPOR DIFFUSION, HANGING DROP, temperature 295K
Resolution 2.95 Å R-free 0.269
3JTI Crystal structure of the complex formed between Phospholipase A2 with beta-amyloid fragment, Lys-Gly-Ala-Ile-Ile-Gly-Leu-Met at 1.8 A resolution Deposited 2009-09-12 Different construct Different ligand/ion Different experimental conditions Different structure-quality metrics Assembly 1 Protein heterocomplex Heteromer；Protein × 2 PDB declaration: dimeric
Chain B 699–706（8 aa） Fragment：UNP residues 699-706
Not recorded CA CALCIUM ION × 1 X-RAY DIFFRACTION
X-ray crystallization conditions VAPOR DIFFUSION, HANGING DROP；pH 6；290 K；10MM SODIUM PHOSPHATE, 1mM CACL2, pH 6.0, VAPOR DIFFUSION, HANGING DROP, temperature 290K
Resolution 1.80 Å R-free 0.210
3KTM Structure of the Heparin-induced E1-Dimer of the Amyloid Precursor Protein (APP) Deposited 2009-11-25 Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental conditions Different structure-quality metrics Assembly 1 Protein homooligomer Homooligomer；Protein × 2 PDB declaration: dimeric
Chain A 18–190（173 aa） Fragment：UNP residues 18-190
Chain C 18–190（173 aa） Fragment：UNP residues 18-190
Not recorded BU4 (3R)-butane-1,3-diol × 2 SO4 SULFATE ION × 1 ACT ACETATE ION × 1 X-RAY DIFFRACTION
X-ray crystallization conditions VAPOR DIFFUSION, SITTING DROP；pH 5；293 K；pH 5.0, VAPOR DIFFUSION, SITTING DROP, temperature 293K
Resolution 2.70 Å R-free 0.250
3KTM Structure of the Heparin-induced E1-Dimer of the Amyloid Precursor Protein (APP) Deposited 2009-11-25 Different construct Different oligomeric state Different ligand/ion Different experimental conditions Different structure-quality metrics Assembly 10 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric
Chain F 18–190（173 aa） Fragment：UNP residues 18-190
Not recorded BU4 (3R)-butane-1,3-diol × 1 X-RAY DIFFRACTION
X-ray crystallization conditions VAPOR DIFFUSION, SITTING DROP；pH 5；293 K；pH 5.0, VAPOR DIFFUSION, SITTING DROP, temperature 293K
Resolution 2.70 Å R-free 0.250
3KTM Structure of the Heparin-induced E1-Dimer of the Amyloid Precursor Protein (APP) Deposited 2009-11-25 Different construct Different oligomeric state Different ligand/ion Different experimental conditions Different structure-quality metrics Assembly 11 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric
Chain G 18–190（173 aa） Fragment：UNP residues 18-190
Not recorded BU4 (3R)-butane-1,3-diol × 1 X-RAY DIFFRACTION
X-ray crystallization conditions VAPOR DIFFUSION, SITTING DROP；pH 5；293 K；pH 5.0, VAPOR DIFFUSION, SITTING DROP, temperature 293K
Resolution 2.70 Å R-free 0.250
3KTM Structure of the Heparin-induced E1-Dimer of the Amyloid Precursor Protein (APP) Deposited 2009-11-25 Different construct Different oligomeric state Different ligand/ion Different experimental conditions Different structure-quality metrics Assembly 12 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric
Chain H 18–190（173 aa） Fragment：UNP residues 18-190
Not recorded BU4 (3R)-butane-1,3-diol × 1 SO4 SULFATE ION × 1 ACT ACETATE ION × 1 X-RAY DIFFRACTION
X-ray crystallization conditions VAPOR DIFFUSION, SITTING DROP；pH 5；293 K；pH 5.0, VAPOR DIFFUSION, SITTING DROP, temperature 293K
Resolution 2.70 Å R-free 0.250
3KTM Structure of the Heparin-induced E1-Dimer of the Amyloid Precursor Protein (APP) Deposited 2009-11-25 Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental conditions Different structure-quality metrics Assembly 2 Protein homooligomer Homooligomer；Protein × 2 PDB declaration: dimeric
Chain B 18–190（173 aa） Fragment：UNP residues 18-190
Chain D 18–190（173 aa） Fragment：UNP residues 18-190
Not recorded BU4 (3R)-butane-1,3-diol × 2 SO4 SULFATE ION × 2 ACT ACETATE ION × 1 X-RAY DIFFRACTION
X-ray crystallization conditions VAPOR DIFFUSION, SITTING DROP；pH 5；293 K；pH 5.0, VAPOR DIFFUSION, SITTING DROP, temperature 293K
Resolution 2.70 Å R-free 0.250
3KTM Structure of the Heparin-induced E1-Dimer of the Amyloid Precursor Protein (APP) Deposited 2009-11-25 Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental conditions Different structure-quality metrics Assembly 3 Protein homooligomer Homooligomer；Protein × 2 PDB declaration: dimeric
Chain F 18–190（173 aa） Fragment：UNP residues 18-190
Chain H 18–190（173 aa） Fragment：UNP residues 18-190
Not recorded BU4 (3R)-butane-1,3-diol × 2 SO4 SULFATE ION × 1 ACT ACETATE ION × 1 X-RAY DIFFRACTION
X-ray crystallization conditions VAPOR DIFFUSION, SITTING DROP；pH 5；293 K；pH 5.0, VAPOR DIFFUSION, SITTING DROP, temperature 293K
Resolution 2.70 Å R-free 0.250
3KTM Structure of the Heparin-induced E1-Dimer of the Amyloid Precursor Protein (APP) Deposited 2009-11-25 Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental conditions Different structure-quality metrics Assembly 4 Protein homooligomer Homooligomer；Protein × 2 PDB declaration: dimeric
Chain E 18–190（173 aa） Fragment：UNP residues 18-190
Chain G 18–190（173 aa） Fragment：UNP residues 18-190
Not recorded BU4 (3R)-butane-1,3-diol × 2 SO4 SULFATE ION × 1 ACT ACETATE ION × 1 X-RAY DIFFRACTION
X-ray crystallization conditions VAPOR DIFFUSION, SITTING DROP；pH 5；293 K；pH 5.0, VAPOR DIFFUSION, SITTING DROP, temperature 293K
Resolution 2.70 Å R-free 0.250
3KTM Structure of the Heparin-induced E1-Dimer of the Amyloid Precursor Protein (APP) Deposited 2009-11-25 Different construct Different oligomeric state Different ligand/ion Different experimental conditions Different structure-quality metrics Assembly 5 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric
Chain A 18–190（173 aa） Fragment：UNP residues 18-190
Not recorded BU4 (3R)-butane-1,3-diol × 1 X-RAY DIFFRACTION
X-ray crystallization conditions VAPOR DIFFUSION, SITTING DROP；pH 5；293 K；pH 5.0, VAPOR DIFFUSION, SITTING DROP, temperature 293K
Resolution 2.70 Å R-free 0.250
3KTM Structure of the Heparin-induced E1-Dimer of the Amyloid Precursor Protein (APP) Deposited 2009-11-25 Different construct Different oligomeric state Different ligand/ion Different experimental conditions Different structure-quality metrics Assembly 6 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric
Chain B 18–190（173 aa） Fragment：UNP residues 18-190
Not recorded BU4 (3R)-butane-1,3-diol × 1 SO4 SULFATE ION × 1 ACT ACETATE ION × 1 X-RAY DIFFRACTION
X-ray crystallization conditions VAPOR DIFFUSION, SITTING DROP；pH 5；293 K；pH 5.0, VAPOR DIFFUSION, SITTING DROP, temperature 293K
Resolution 2.70 Å R-free 0.250
3KTM Structure of the Heparin-induced E1-Dimer of the Amyloid Precursor Protein (APP) Deposited 2009-11-25 Different construct Different oligomeric state Different ligand/ion Different experimental conditions Different structure-quality metrics Assembly 7 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric
Chain C 18–190（173 aa） Fragment：UNP residues 18-190
Not recorded BU4 (3R)-butane-1,3-diol × 1 SO4 SULFATE ION × 1 ACT ACETATE ION × 1 X-RAY DIFFRACTION
X-ray crystallization conditions VAPOR DIFFUSION, SITTING DROP；pH 5；293 K；pH 5.0, VAPOR DIFFUSION, SITTING DROP, temperature 293K
Resolution 2.70 Å R-free 0.250
3KTM Structure of the Heparin-induced E1-Dimer of the Amyloid Precursor Protein (APP) Deposited 2009-11-25 Different construct Different oligomeric state Different ligand/ion Different experimental conditions Different structure-quality metrics Assembly 8 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric
Chain D 18–190（173 aa） Fragment：UNP residues 18-190
Not recorded BU4 (3R)-butane-1,3-diol × 1 SO4 SULFATE ION × 1 X-RAY DIFFRACTION
X-ray crystallization conditions VAPOR DIFFUSION, SITTING DROP；pH 5；293 K；pH 5.0, VAPOR DIFFUSION, SITTING DROP, temperature 293K
Resolution 2.70 Å R-free 0.250
3KTM Structure of the Heparin-induced E1-Dimer of the Amyloid Precursor Protein (APP) Deposited 2009-11-25 Different construct Different oligomeric state Different ligand/ion Different experimental conditions Different structure-quality metrics Assembly 9 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric
Chain E 18–190（173 aa） Fragment：UNP residues 18-190
Not recorded BU4 (3R)-butane-1,3-diol × 1 SO4 SULFATE ION × 1 ACT ACETATE ION × 1 X-RAY DIFFRACTION
X-ray crystallization conditions VAPOR DIFFUSION, SITTING DROP；pH 5；293 K；pH 5.0, VAPOR DIFFUSION, SITTING DROP, temperature 293K
Resolution 2.70 Å R-free 0.250
3L33 Human mesotrypsin complexed with amyloid precursor protein inhibitor(APPI) Deposited 2009-12-16 Different construct Different ligand/ion Different experimental conditions Different structure-quality metrics Assembly 1 Protein heterocomplex Heteromer；Protein × 2 PDB declaration: dimeric
Chain E 290–341（52 aa） Fragment：UNP residues 290-341
Not recorded FMT FORMIC ACID × 9 CA CALCIUM ION × 1 X-RAY DIFFRACTION
X-ray crystallization conditions VAPOR DIFFUSION, HANGING DROP；298 K；4M sodium formate solution, VAPOR DIFFUSION, HANGING DROP, temperature 298.0K
Resolution 2.48 Å R-free 0.256
3L33 Human mesotrypsin complexed with amyloid precursor protein inhibitor(APPI) Deposited 2009-12-16 Different construct Different ligand/ion Different experimental conditions Different structure-quality metrics Assembly 2 Protein heterocomplex Heteromer；Protein × 2 PDB declaration: dimeric
Chain F 290–341（52 aa） Fragment：UNP residues 290-341
Not recorded FMT FORMIC ACID × 6 CA CALCIUM ION × 1 X-RAY DIFFRACTION
X-ray crystallization conditions VAPOR DIFFUSION, HANGING DROP；298 K；4M sodium formate solution, VAPOR DIFFUSION, HANGING DROP, temperature 298.0K
Resolution 2.48 Å R-free 0.256
3L33 Human mesotrypsin complexed with amyloid precursor protein inhibitor(APPI) Deposited 2009-12-16 Different construct Different ligand/ion Different experimental conditions Different structure-quality metrics Assembly 3 Protein heterocomplex Heteromer；Protein × 2 PDB declaration: dimeric
Chain G 290–341（52 aa） Fragment：UNP residues 290-341
Not recorded FMT FORMIC ACID × 3 CA CALCIUM ION × 1 X-RAY DIFFRACTION
X-ray crystallization conditions VAPOR DIFFUSION, HANGING DROP；298 K；4M sodium formate solution, VAPOR DIFFUSION, HANGING DROP, temperature 298.0K
Resolution 2.48 Å R-free 0.256
3L33 Human mesotrypsin complexed with amyloid precursor protein inhibitor(APPI) Deposited 2009-12-16 Different construct Different ligand/ion Different experimental conditions Different structure-quality metrics Assembly 4 Protein heterocomplex Heteromer；Protein × 2 PDB declaration: dimeric
Chain H 290–341（52 aa） Fragment：UNP residues 290-341
Not recorded FMT FORMIC ACID × 1 CA CALCIUM ION × 1 X-RAY DIFFRACTION
X-ray crystallization conditions VAPOR DIFFUSION, HANGING DROP；298 K；4M sodium formate solution, VAPOR DIFFUSION, HANGING DROP, temperature 298.0K
Resolution 2.48 Å R-free 0.256
3MOQ Amyloid beta(18-41) peptide fusion with new antigen receptor variable domain from sharks Deposited 2010-04-23 Different construct Different oligomeric state Different ligand/ion Different experimental conditions Different structure-quality metrics Assembly 1 Insufficient information Monomer；Protein × 1 PDB declaration: monomeric
Chain A 689–712（24 aa）
Not recorded No recorded non-water small molecule X-RAY DIFFRACTION
X-ray crystallization conditions VAPOR DIFFUSION, HANGING DROP；pH 6；298 K；20% PEG 6000, 0.2M AMMONIUM CHLORIDE, 0.1M MES, pH 6.0, VAPOR DIFFUSION, HANGING DROP, temperature 298.0K
Resolution 2.05 Å R-free 0.249
3MOQ Amyloid beta(18-41) peptide fusion with new antigen receptor variable domain from sharks Deposited 2010-04-23 Different construct Different oligomeric state Different ligand/ion Different experimental conditions Different structure-quality metrics Assembly 2 Insufficient information Monomer；Protein × 1 PDB declaration: monomeric
Chain B 689–712（24 aa）
Not recorded No recorded non-water small molecule X-RAY DIFFRACTION
X-ray crystallization conditions VAPOR DIFFUSION, HANGING DROP；pH 6；298 K；20% PEG 6000, 0.2M AMMONIUM CHLORIDE, 0.1M MES, pH 6.0, VAPOR DIFFUSION, HANGING DROP, temperature 298.0K
Resolution 2.05 Å R-free 0.249
3MOQ Amyloid beta(18-41) peptide fusion with new antigen receptor variable domain from sharks Deposited 2010-04-23 Different construct Different oligomeric state Different ligand/ion Different experimental conditions Different structure-quality metrics Assembly 3 Insufficient information Monomer；Protein × 1 PDB declaration: monomeric
Chain C 689–712（24 aa）
Not recorded No recorded non-water small molecule X-RAY DIFFRACTION
X-ray crystallization conditions VAPOR DIFFUSION, HANGING DROP；pH 6；298 K；20% PEG 6000, 0.2M AMMONIUM CHLORIDE, 0.1M MES, pH 6.0, VAPOR DIFFUSION, HANGING DROP, temperature 298.0K
Resolution 2.05 Å R-free 0.249
3MOQ Amyloid beta(18-41) peptide fusion with new antigen receptor variable domain from sharks Deposited 2010-04-23 Different construct Different oligomeric state Different ligand/ion Different experimental conditions Different structure-quality metrics Assembly 4 Insufficient information Monomer；Protein × 1 PDB declaration: monomeric
Chain D 689–712（24 aa）
Not recorded No recorded non-water small molecule X-RAY DIFFRACTION
X-ray crystallization conditions VAPOR DIFFUSION, HANGING DROP；pH 6；298 K；20% PEG 6000, 0.2M AMMONIUM CHLORIDE, 0.1M MES, pH 6.0, VAPOR DIFFUSION, HANGING DROP, temperature 298.0K
Resolution 2.05 Å R-free 0.249
3MOQ Amyloid beta(18-41) peptide fusion with new antigen receptor variable domain from sharks Deposited 2010-04-23 Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental conditions Different structure-quality metrics Assembly 5 Insufficient information Homooligomer；Protein × 4 PDB declaration: tetrameric
Chain A 689–712（24 aa）
Chain B 689–712（24 aa）
Chain C 689–712（24 aa）
Chain D 689–712（24 aa）
Not recorded No recorded non-water small molecule X-RAY DIFFRACTION
X-ray crystallization conditions VAPOR DIFFUSION, HANGING DROP；pH 6；298 K；20% PEG 6000, 0.2M AMMONIUM CHLORIDE, 0.1M MES, pH 6.0, VAPOR DIFFUSION, HANGING DROP, temperature 298.0K
Resolution 2.05 Å R-free 0.249
3NYJ Crystal Structure Analysis of APP E2 domain Deposited 2010-07-15 Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental conditions Different structure-quality metrics Assembly 1 Protein homooligomer Homooligomer；Protein × 2 PDB declaration: dimeric
Chain A 365–567（203 aa）
Non-standard monomer：Yes (specific site not provided by mmCIF) OS OSMIUM ION × 2 X-RAY DIFFRACTION
X-ray crystallization conditions VAPOR DIFFUSION；pH 5.6；298 K；20% PEG 4000, 20% isopropanol, 0.1M Na Citrate, pH 5.6, vapor diffusion, temperature 298K
Resolution 3.20 Å R-free 0.380
3OVJ Structure of an amyloid forming peptide KLVFFA from amyloid beta in complex with orange G Deposited 2010-09-16 Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental conditions Different structure-quality metrics Assembly 1 Protein homooligomer Homooligomer；Protein × 4 PDB declaration: tetrameric
Chain A 687–692（6 aa） Fragment：KLVFFA (UNP residues 687-692)
Chain B 687–692（6 aa） Fragment：KLVFFA (UNP residues 687-692)
Chain C 687–692（6 aa） Fragment：KLVFFA (UNP residues 687-692)
Chain D 687–692（6 aa） Fragment：KLVFFA (UNP residues 687-692)
Not recorded ORA 7-hydroxy-8-[(E)-phenyldiazenyl]naphthalene-1,3-disulfonic acid × 2 X-RAY DIFFRACTION
X-ray crystallization conditions VAPOR DIFFUSION, HANGING DROP；291 K；reservoir contained 30% w/v Polyethylene glycol 1,500, 20% v/v Glycerol, vapor diffusion, hanging drop, temperature 291K
X-ray crystallization conditions VAPOR DIFFUSION, HANGING DROP；291 K；reservoir contained 10% w/v Polyethylene glycol 1,500, 30% v/v Glycerol, vapor diffusion, hanging drop, temperature 291K
Resolution 1.80 Å R-free 0.220
3OW9 Structure of an amyloid forming peptide KLVFFA from amyloid beta, alternate polymorph II Deposited 2010-09-17 Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental conditions Different structure-quality metrics Assembly 1 Protein homooligomer Homooligomer；Protein × 12 PDB declaration: dodecameric
Chain A 687–692（6 aa） Fragment：KLVFFA (UNP residues 687-692)
Chain B 687–692（6 aa） Fragment：KLVFFA (UNP residues 687-692)
Not recorded No recorded non-water small molecule X-RAY DIFFRACTION
X-ray crystallization conditions VAPOR DIFFUSION, HANGING DROP；291 K；reservoir contained 30% (v/v) Jeffamine M-600, 0.1M Mes pH 6.5 ; 0.05M CsCl, 1mM FDDNP, vapor diffusion, hanging drop, temperature 291K
Resolution 1.80 Å R-free 0.258
3PZZ Structure of an amyloid forming peptide GAIIGL (29-34) from amyloid beta Deposited 2010-12-14 Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental conditions Different structure-quality metrics Assembly 1 Protein homooligomer Homooligomer；Protein × 12 PDB declaration: dodecameric
Chain A 700–705（6 aa） Fragment：GAIIGL hexapeptide segment (UNP residues 700-705)
Chain B 700–705（6 aa） Fragment：GAIIGL hexapeptide segment (UNP residues 700-705)
Not recorded No recorded non-water small molecule X-RAY DIFFRACTION
X-ray crystallization conditions VAPOR DIFFUSION, HANGING DROP；291 K；reservoir contained 14.4% PEG 8000, 0.08 M Na Cacodylate pH 6.5, 0.16 M Calcium Acetate, 20% v/v Glycerol, vapor diffusion, hanging drop, temperature 291K
Resolution 1.29 Å R-free 0.196
3Q2X Structure of an amyloid forming peptide NKGAII (residues 27-32) from amyloid beta Deposited 2010-12-20 Different construct Different oligomeric state Different ligand/ion Different experimental conditions Different structure-quality metrics Assembly 1 Protein homooligomer Homooligomer；Protein × 6 PDB declaration: hexameric
Chain A 698–703（6 aa） Fragment：NKGAII hexapeptide segment (UNP residues 698-703)
Not recorded No recorded non-water small molecule X-RAY DIFFRACTION
X-ray crystallization conditions VAPOR DIFFUSION, HANGING DROP；291 K；reservoir contained 2.4M Sodium Malonate, 15% v/v Glycerol, vapor diffusion, hanging drop, temperature 291K
Resolution 1.45 Å R-free 0.259
3SV1 Crystal structure of APP peptide bound rat Mint2 PARM Deposited 2011-07-12 Different construct Different ligand/ion Different experimental conditions Different structure-quality metrics Assembly 1 Protein heterocomplex Heteromer；Protein × 2 PDB declaration: dimeric
Chain D 754–767（14 aa） Fragment：C-terminal peptide, residues 754-767
Not recorded No recorded non-water small molecule X-RAY DIFFRACTION
X-ray crystallization conditions VAPOR DIFFUSION, SITTING DROP；pH 7.5；293 K；0.1M HEPES, 36% PEG200, pH 7.5, VAPOR DIFFUSION, SITTING DROP, temperature 293K
Resolution 3.30 Å R-free 0.301
3SV1 Crystal structure of APP peptide bound rat Mint2 PARM Deposited 2011-07-12 Different construct Different ligand/ion Different experimental conditions Different structure-quality metrics Assembly 2 Protein heterocomplex Heteromer；Protein × 2 PDB declaration: dimeric
Chain E 754–767（14 aa） Fragment：C-terminal peptide, residues 754-767
Not recorded No recorded non-water small molecule X-RAY DIFFRACTION
X-ray crystallization conditions VAPOR DIFFUSION, SITTING DROP；pH 7.5；293 K；0.1M HEPES, 36% PEG200, pH 7.5, VAPOR DIFFUSION, SITTING DROP, temperature 293K
Resolution 3.30 Å R-free 0.301
3SV1 Crystal structure of APP peptide bound rat Mint2 PARM Deposited 2011-07-12 Different construct Different ligand/ion Different experimental conditions Different structure-quality metrics Assembly 3 Protein heterocomplex Heteromer；Protein × 2 PDB declaration: dimeric
Chain F 754–767（14 aa） Fragment：C-terminal peptide, residues 754-767
Not recorded No recorded non-water small molecule X-RAY DIFFRACTION
X-ray crystallization conditions VAPOR DIFFUSION, SITTING DROP；pH 7.5；293 K；0.1M HEPES, 36% PEG200, pH 7.5, VAPOR DIFFUSION, SITTING DROP, temperature 293K
Resolution 3.30 Å R-free 0.301
3U0T Fab-antibody complex Deposited 2011-09-29 Different construct Different oligomeric state Different ligand/ion Different experimental conditions Different structure-quality metrics Assembly 1 Protein heterocomplex Heteromer；Protein × 3 PDB declaration: trimeric
Chain E 701–711（11 aa） Fragment：UNP residues 701-711
Not recorded No recorded non-water small molecule X-RAY DIFFRACTION mmCIF provides none of the parsed conditions Resolution 2.50 Å R-free 0.268
3U0T Fab-antibody complex Deposited 2011-09-29 Different construct Different oligomeric state Different ligand/ion Different experimental conditions Different structure-quality metrics Assembly 2 Protein heterocomplex Heteromer；Protein × 3 PDB declaration: trimeric
Chain F 701–711（11 aa） Fragment：UNP residues 701-711
Not recorded No recorded non-water small molecule X-RAY DIFFRACTION mmCIF provides none of the parsed conditions Resolution 2.50 Å R-free 0.268
3UMH X-ray structure of the E2 domain of the human amyloid precursor protein (APP) in complex with cadmium Deposited 2011-11-13 Different construct Different oligomeric state Different ligand/ion Different experimental conditions Different structure-quality metrics Assembly 1 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric
Chain A 370–575（206 aa） Fragment：HUMAN AMYLOID PRECURSOR PROTEIN E2 DOMAIN
Not recorded ACT ACETATE ION × 2 CD CADMIUM ION × 9 X-RAY DIFFRACTION
X-ray crystallization conditions VAPOR DIFFUSION, SITTING DROP；pH 6.4；293 K；0.1 mM HEPES, 1 M sodium acetate, 10 mM MgCl2, 50 mM CdSO4, pH 6.4, VAPOR DIFFUSION, SITTING DROP, temperature 293K
Resolution 2.00 Å R-free 0.240
3UMI X-ray structure of the E2 domain of the human amyloid precursor protein (APP) in complex with zinc Deposited 2011-11-13 Different construct Different oligomeric state Different ligand/ion Different experimental conditions Different structure-quality metrics Assembly 1 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric
Chain A 370–575（206 aa） Fragment：HUMAN AMYLOID PRECURSOR PROTEIN E2 DOMAIN
Not recorded ACT ACETATE ION × 1 ZN ZINC ION × 1 CD CADMIUM ION × 8 X-RAY DIFFRACTION
X-ray crystallization conditions VAPOR DIFFUSION, SITTING DROP；pH 6.4；293 K；0.1 mM HEPES, 1 M sodium acetate, 10 mM MgCl2, 50 mM CdSO4, pH 6.4, VAPOR DIFFUSION, SITTING DROP, temperature 293K
Resolution 2.40 Å R-free 0.245
3UMK X-ray structure of the E2 domain of the human amyloid precursor protein (APP) in complex with copper Deposited 2011-11-13 Different construct Different oligomeric state Different ligand/ion Different experimental conditions Different structure-quality metrics Assembly 1 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric
Chain A 370–575（206 aa） Fragment：HUMAN AMYLOID PRECURSOR PROTEIN E2 DOMAIN
Not recorded ACT ACETATE ION × 1 CU COPPER (II) ION × 2 CD CADMIUM ION × 7 X-RAY DIFFRACTION
X-ray crystallization conditions VAPOR DIFFUSION, SITTING DROP；pH 6.4；293 K；0.1 mM HEPES, 1 M sodium acetate, 10 mM MgCl2, 50 mM CdSO4, pH 6.4, VAPOR DIFFUSION, SITTING DROP, temperature 293K
Resolution 2.60 Å R-free 0.239
4HIX Crystal structure of a humanised 3D6 Fab bound to amyloid beta peptide Deposited 2012-10-12 Different construct Different oligomeric state Different ligand/ion Different experimental conditions Different structure-quality metrics Assembly 1 Protein heterocomplex Heteromer；Protein × 3 PDB declaration: trimeric
Chain A 672–699（28 aa）
Not recorded No recorded non-water small molecule X-RAY DIFFRACTION
X-ray crystallization conditions VAPOR DIFFUSION, HANGING DROP；295 K；sodium formate, PEG 3350, VAPOR DIFFUSION, HANGING DROP, temperature 295K
Resolution 2.20 Å R-free 0.220
4JFN Crystal structure of the N-terminal, growth factor-like domain of the amyloid precursor protein bound to copper Deposited 2013-02-28 Different construct Different oligomeric state Different ligand/ion Different experimental conditions Different structure-quality metrics Assembly 1 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric
Chain A 23–185（163 aa） Fragment：growth factor-like domain (GFLD), UNP residues 23-185
Not recorded CU COPPER (II) ION × 1 GOL GLYCEROL × 1 X-RAY DIFFRACTION
X-ray crystallization conditions VAPOR DIFFUSION, HANGING DROP；pH 7.5；291 K；6% (w/v) PEG 3350, 0.1 M Hepes, pH 7.5, VAPOR DIFFUSION, HANGING DROP, temperature 291K
Resolution 1.75 Å R-free 0.230
4M1C Crystal Structure Analysis of Fab-Bound Human Insulin Degrading Enzyme (IDE) in Complex with Amyloid-Beta (1-40) Deposited 2013-08-02 Different construct Different oligomeric state Different ligand/ion Different experimental conditions Different structure-quality metrics Assembly 1 Protein heterocomplex Heteromer；Protein × 4 PDB declaration: tetrameric
Chain G 672–711（40 aa）
Not recorded ZN ZINC ION × 1 X-RAY DIFFRACTION
X-ray crystallization conditions VAPOR DIFFUSION, HANGING DROP；pH 6.5；291.15 K；0.1M Sodium cacodylate, pH6.5, 0.2M MgCl2, 10% PEG-3000, VAPOR DIFFUSION, HANGING DROP, temperature 291.15K
Resolution 3.50 Å R-free 0.270
4M1C Crystal Structure Analysis of Fab-Bound Human Insulin Degrading Enzyme (IDE) in Complex with Amyloid-Beta (1-40) Deposited 2013-08-02 Different construct Different oligomeric state Different ligand/ion Different experimental conditions Different structure-quality metrics Assembly 2 Protein heterocomplex Heteromer；Protein × 4 PDB declaration: tetrameric
Chain H 672–711（40 aa）
Not recorded ZN ZINC ION × 1 X-RAY DIFFRACTION
X-ray crystallization conditions VAPOR DIFFUSION, HANGING DROP；pH 6.5；291.15 K；0.1M Sodium cacodylate, pH6.5, 0.2M MgCl2, 10% PEG-3000, VAPOR DIFFUSION, HANGING DROP, temperature 291.15K
Resolution 3.50 Å R-free 0.270
4MDR Crystal structure of adaptor protein complex 4 (AP-4) mu4 subunit C-terminal domain D190A mutant, in complex with a sorting peptide from the amyloid precursor protein (APP) Deposited 2013-08-23 Different construct Different ligand/ion Different experimental conditions Different structure-quality metrics Assembly 1 Protein heterocomplex Heteromer；Protein × 2 PDB declaration: dimeric
Chain B 758–767（10 aa） Fragment：C-terminus, residues 761-767
Not recorded No recorded non-water small molecule X-RAY DIFFRACTION
X-ray crystallization conditions VAPOR DIFFUSION, HANGING DROP；pH 7；295 K；15% PEG 6000, 3% trimethylamine N-oxide dihydrate, 0.1M HEPES, pH 7.0, VAPOR DIFFUSION, HANGING DROP, temperature 295.0K
Resolution 1.85 Å R-free 0.260
4MVI Crystal structure of an engineered lipocalin (Anticalin US7) in complex with the Alzheimer amyloid peptide Abeta(1-40) Deposited 2013-09-24 Different construct Different ligand/ion Different experimental conditions Different structure-quality metrics Assembly 1 Protein heterocomplex Heteromer；Protein × 2 PDB declaration: dimeric
Chain B 672–711（40 aa） Fragment：UNP residues 672-711
Not recorded No recorded non-water small molecule X-RAY DIFFRACTION
X-ray crystallization conditions VAPOR DIFFUSION, HANGING DROP；pH 5.25；293 K；30 % (w/v) PEG 4000, 100 mM sodium acetate, pH 5.25, VAPOR DIFFUSION, HANGING DROP, temperature 293K
Resolution 1.70 Å R-free 0.212
4MVK Crystal structure of an engineered lipocalin (Anticalin US7) in complex with the Alzheimer amyloid peptide fragment VFFAED Deposited 2013-09-24 Different construct Different mutation/modification Different ligand/ion Different experimental conditions Different structure-quality metrics Assembly 1 Protein heterocomplex Heteromer；Protein × 2 PDB declaration: dimeric
Chain B 689–694（6 aa） Fragment：UNP residues 689-694
Non-standard monomer：Yes (specific site not provided by mmCIF) No recorded non-water small molecule X-RAY DIFFRACTION
X-ray crystallization conditions VAPOR DIFFUSION, HANGING DROP；pH 6.5；293 K；27 % (w/v) PEG 8000, 100 mM MES, pH 6.5, vapor diffusion, hanging drop, temperature 293K
Resolution 1.50 Å R-free 0.186
4MVL Crystal structure of an engineered lipocalin (Anticalin H1GA) in complex with the Alzheimer amyloid peptide Abeta1-40 Deposited 2013-09-24 Different construct Different ligand/ion Different experimental conditions Different structure-quality metrics Assembly 1 Protein heterocomplex Heteromer；Protein × 2 PDB declaration: dimeric
Chain E 672–711（40 aa） Fragment：UNP residues 672-711
Not recorded No recorded non-water small molecule X-RAY DIFFRACTION
X-ray crystallization conditions VAPOR DIFFUSION, HANGING DROP；pH 8；293 K；24 % (w/v) PEG 3350, pH 8.0, VAPOR DIFFUSION, HANGING DROP, temperature 293K
Resolution 2.30 Å R-free 0.279
4MVL Crystal structure of an engineered lipocalin (Anticalin H1GA) in complex with the Alzheimer amyloid peptide Abeta1-40 Deposited 2013-09-24 Different construct Different ligand/ion Different experimental conditions Different structure-quality metrics Assembly 2 Protein heterocomplex Heteromer；Protein × 2 PDB declaration: dimeric
Chain F 672–711（40 aa） Fragment：UNP residues 672-711
Not recorded No recorded non-water small molecule X-RAY DIFFRACTION
X-ray crystallization conditions VAPOR DIFFUSION, HANGING DROP；pH 8；293 K；24 % (w/v) PEG 3350, pH 8.0, VAPOR DIFFUSION, HANGING DROP, temperature 293K
Resolution 2.30 Å R-free 0.279
4MVL Crystal structure of an engineered lipocalin (Anticalin H1GA) in complex with the Alzheimer amyloid peptide Abeta1-40 Deposited 2013-09-24 Different construct Different ligand/ion Different experimental conditions Different structure-quality metrics Assembly 3 Protein heterocomplex Heteromer；Protein × 2 PDB declaration: dimeric
Chain G 672–711（40 aa） Fragment：UNP residues 672-711
Not recorded No recorded non-water small molecule X-RAY DIFFRACTION
X-ray crystallization conditions VAPOR DIFFUSION, HANGING DROP；pH 8；293 K；24 % (w/v) PEG 3350, pH 8.0, VAPOR DIFFUSION, HANGING DROP, temperature 293K
Resolution 2.30 Å R-free 0.279
4MVL Crystal structure of an engineered lipocalin (Anticalin H1GA) in complex with the Alzheimer amyloid peptide Abeta1-40 Deposited 2013-09-24 Different construct Different ligand/ion Different experimental conditions Different structure-quality metrics Assembly 4 Protein heterocomplex Heteromer；Protein × 2 PDB declaration: dimeric
Chain H 672–711（40 aa） Fragment：UNP residues 672-711
Not recorded No recorded non-water small molecule X-RAY DIFFRACTION
X-ray crystallization conditions VAPOR DIFFUSION, HANGING DROP；pH 8；293 K；24 % (w/v) PEG 3350, pH 8.0, VAPOR DIFFUSION, HANGING DROP, temperature 293K
Resolution 2.30 Å R-free 0.279
4NGE Crystal Structure of Human Presequence Protease in Complex with Amyloid-beta (1-40) Deposited 2013-11-01 Different construct Different oligomeric state Different ligand/ion Different experimental conditions Different structure-quality metrics Assembly 1 Protein heterocomplex Heteromer；Protein × 3 PDB declaration: trimeric
Chain B 672–711（40 aa） Fragment：UNP residues 572-711
Not recorded ZN ZINC ION × 1 GOL GLYCEROL × 1 ACT ACETATE ION × 2 X-RAY DIFFRACTION
X-ray crystallization conditions VAPOR DIFFUSION, HANGING DROP；pH 6.5；291.15 K；15.2% w/v PEG8000, 15 mM TCEP, 80 mM sodium cacodylate, pH 6.5, 160 mM calcium acetate, 20% v/v glycerol, VAPOR DIFFUSION, HANGING DROP, temperature 291.15K
Resolution 2.70 Å R-free 0.232
4NGE Crystal Structure of Human Presequence Protease in Complex with Amyloid-beta (1-40) Deposited 2013-11-01 Different construct Different oligomeric state Different ligand/ion Different experimental conditions Different structure-quality metrics Assembly 2 Protein heterocomplex Heteromer；Protein × 3 PDB declaration: trimeric
Chain E 672–711（40 aa） Fragment：UNP residues 572-711
Not recorded ZN ZINC ION × 1 GOL GLYCEROL × 2 X-RAY DIFFRACTION
X-ray crystallization conditions VAPOR DIFFUSION, HANGING DROP；pH 6.5；291.15 K；15.2% w/v PEG8000, 15 mM TCEP, 80 mM sodium cacodylate, pH 6.5, 160 mM calcium acetate, 20% v/v glycerol, VAPOR DIFFUSION, HANGING DROP, temperature 291.15K
Resolution 2.70 Å R-free 0.232
4OJF Humanised 3D6 Fab complexed to amyloid beta 1-8 Deposited 2014-01-21 Different construct Different oligomeric state Different ligand/ion Different experimental conditions Different structure-quality metrics Assembly 1 Protein heterocomplex Heteromer；Protein × 3 PDB declaration: trimeric
Chain A 672–679（8 aa） Fragment：UNP residues 672-679
Not recorded No recorded non-water small molecule X-RAY DIFFRACTION
X-ray crystallization conditions VAPOR DIFFUSION, HANGING DROP；pH 7.5；293 K；0.1M HEPES, 25%(w/v) PEG 6000, pH 7.5, VAPOR DIFFUSION, HANGING DROP, temperature 293K
Resolution 2.00 Å R-free 0.215
4ONF Fab fragment of 3D6 in complex with amyloid beta 1-7 Deposited 2014-01-28 Different construct Different oligomeric state Different ligand/ion Different experimental conditions Different structure-quality metrics Assembly 1 Protein heterocomplex Heteromer；Protein × 3 PDB declaration: trimeric
Chain P 672–678（7 aa） Fragment：unp residues 672-678
Not recorded No recorded non-water small molecule X-RAY DIFFRACTION
X-ray crystallization conditions VAPOR DIFFUSION, HANGING DROP；pH 9；295 K；30% Peg400, 0.1 M Tris, pH 9.0, VAPOR DIFFUSION, HANGING DROP, temperature 295K
Resolution 2.00 Å R-free 0.203
4ONG Fab fragment of 3D6 in complex with amyloid beta 1-40 Deposited 2014-01-28 Different construct Different oligomeric state Different ligand/ion Different experimental conditions Different structure-quality metrics Assembly 1 Protein heterocomplex Heteromer；Protein × 3 PDB declaration: trimeric
Chain P 672–711（40 aa） Fragment：unp residues 672-711
Not recorded ZN ZINC ION × 27 IMD IMIDAZOLE × 3 CL CHLORIDE ION × 11 X-RAY DIFFRACTION
X-ray crystallization conditions VAPOR DIFFUSION, SITTING DROP；pH 8；295 K；2.5 M NaCl, 0.1 Imidazole pH 8.0, 0.2 ZnAc2., VAPOR DIFFUSION, SITTING DROP, temperature 295K
Resolution 2.20 Å R-free 0.227
4PQD The longer crystal structure of the grow factor like domain from Beta amypoid precusor protein (APP22-126) Deposited 2014-03-02 Different construct Different oligomeric state Different ligand/ion Different experimental conditions Different structure-quality metrics Assembly 1 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric
Chain A 22–126（105 aa） Fragment：the N-terminal GFLD doamin of APP, UNP residues 22-126
Not recorded No recorded non-water small molecule X-RAY DIFFRACTION
X-ray crystallization conditions VAPOR DIFFUSION, HANGING DROP；pH 7；288 K；60% v/v TacsimateTM pH 7.0, VAPOR DIFFUSION, HANGING DROP, temperature 288K
Resolution 1.33 Å R-free 0.186
4PWQ HIGH-RESOLUTION CRYSTAL STRUCTURE OF THE E1-DOMAIN of THE AMYLOID PRECURSOR PROTEIN Deposited 2014-03-21 Different construct Different oligomeric state Different ligand/ion Different experimental conditions Different structure-quality metrics Assembly 1 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric
Chain A 18–190（173 aa） Fragment：E1 domain
Not recorded No recorded non-water small molecule X-RAY DIFFRACTION
X-ray crystallization conditions VAPOR DIFFUSION, SITTING DROP；pH 5.6；283 K；0.1M Na-citrate, 20% PEG4000, 11% 2-propanole, 10mM sarcosine, pH 5.6, VAPOR DIFFUSION, SITTING DROP, temperature 283K
Resolution 1.40 Å R-free 0.185
4PWQ HIGH-RESOLUTION CRYSTAL STRUCTURE OF THE E1-DOMAIN of THE AMYLOID PRECURSOR PROTEIN Deposited 2014-03-21 Different construct Different oligomeric state Different ligand/ion Different experimental conditions Different structure-quality metrics Assembly 2 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric
Chain B 18–190（173 aa） Fragment：E1 domain
Not recorded No recorded non-water small molecule X-RAY DIFFRACTION
X-ray crystallization conditions VAPOR DIFFUSION, SITTING DROP；pH 5.6；283 K；0.1M Na-citrate, 20% PEG4000, 11% 2-propanole, 10mM sarcosine, pH 5.6, VAPOR DIFFUSION, SITTING DROP, temperature 283K
Resolution 1.40 Å R-free 0.185
4XXD Crystal Structure of mid-region amyloid beta capture by solanezumab Deposited 2015-01-30 Different construct Different oligomeric state Different ligand/ion Different experimental conditions Different structure-quality metrics Assembly 1 Protein heterocomplex Heteromer；Protein × 3 PDB declaration: trimeric
Chain C 683–699（17 aa） Fragment：UNP residues 683-699
Not recorded No recorded non-water small molecule X-RAY DIFFRACTION
X-ray crystallization conditions VAPOR DIFFUSION, HANGING DROP；pH 4；292 K；PEG 3350, sodium citrate
Resolution 2.41 Å R-free 0.290
4XXD Crystal Structure of mid-region amyloid beta capture by solanezumab Deposited 2015-01-30 Different construct Different oligomeric state Different ligand/ion Different experimental conditions Different structure-quality metrics Assembly 2 Protein heterocomplex Heteromer；Protein × 3 PDB declaration: trimeric
Chain F 683–699（17 aa） Fragment：UNP residues 683-699
Not recorded No recorded non-water small molecule X-RAY DIFFRACTION
X-ray crystallization conditions VAPOR DIFFUSION, HANGING DROP；pH 4；292 K；PEG 3350, sodium citrate
Resolution 2.41 Å R-free 0.290
5AM8 Crystal structure of the Angiotensin-1 converting enzyme N-domain in complex with amyloid-beta 4-10 Deposited 2015-03-10 Different construct Different oligomeric state Different ligand/ion Different experimental conditions Different structure-quality metrics Assembly 1 Other combination Heteromer；Protein × 2 PDB declaration: dimeric
Chain R 675–681（7 aa） Fragment：FRAGMENT 4-10, UNP RESIDUES 675-681
Not recorded ZN ZINC ION × 1 CL CHLORIDE ION × 1 SO4 SULFATE ION × 1 PEG DI(HYDROXYETHYL)ETHER × 4 X-RAY DIFFRACTION
X-ray crystallization conditions pH 8.5；0.06 M DIVALENT CATIONS, 0.1 M TRIS/BICINE PH 8.5, 30 % PEG550MME/PEG20000
Resolution 1.90 Å R-free 0.224
5AM8 Crystal structure of the Angiotensin-1 converting enzyme N-domain in complex with amyloid-beta 4-10 Deposited 2015-03-10 Different construct Different oligomeric state Different ligand/ion Different experimental conditions Different structure-quality metrics Assembly 2 Other combination Heteromer；Protein × 2 PDB declaration: dimeric
Chain P 675–681（7 aa） Fragment：FRAGMENT 4-10, UNP RESIDUES 675-681
Not recorded ZN ZINC ION × 1 CL CHLORIDE ION × 1 SO4 SULFATE ION × 1 NAG 2-acetamido-2-deoxy-beta-D-glucopyranose × 1 PEG DI(HYDROXYETHYL)ETHER × 4 P6G HEXAETHYLENE GLYCOL × 1 X-RAY DIFFRACTION
X-ray crystallization conditions pH 8.5；0.06 M DIVALENT CATIONS, 0.1 M TRIS/BICINE PH 8.5, 30 % PEG550MME/PEG20000
Resolution 1.90 Å R-free 0.224
5AM8 Crystal structure of the Angiotensin-1 converting enzyme N-domain in complex with amyloid-beta 4-10 Deposited 2015-03-10 Different construct Different oligomeric state Different ligand/ion Different experimental conditions Different structure-quality metrics Assembly 3 Other combination Heteromer；Protein × 2 PDB declaration: dimeric
Chain S 675–681（7 aa） Fragment：FRAGMENT 4-10, UNP RESIDUES 675-681
Not recorded ZN ZINC ION × 1 CL CHLORIDE ION × 1 SO4 SULFATE ION × 1 NAG 2-acetamido-2-deoxy-beta-D-glucopyranose × 2 PEG DI(HYDROXYETHYL)ETHER × 5 P6G HEXAETHYLENE GLYCOL × 1 X-RAY DIFFRACTION
X-ray crystallization conditions pH 8.5；0.06 M DIVALENT CATIONS, 0.1 M TRIS/BICINE PH 8.5, 30 % PEG550MME/PEG20000
Resolution 1.90 Å R-free 0.224
5AM8 Crystal structure of the Angiotensin-1 converting enzyme N-domain in complex with amyloid-beta 4-10 Deposited 2015-03-10 Different construct Different oligomeric state Different ligand/ion Different experimental conditions Different structure-quality metrics Assembly 4 Other combination Heteromer；Protein × 2 PDB declaration: dimeric
Chain Q 675–681（7 aa） Fragment：FRAGMENT 4-10, UNP RESIDUES 675-681
Not recorded ZN ZINC ION × 1 CL CHLORIDE ION × 1 SO4 SULFATE ION × 1 PEG DI(HYDROXYETHYL)ETHER × 5 P6G HEXAETHYLENE GLYCOL × 1 X-RAY DIFFRACTION
X-ray crystallization conditions pH 8.5；0.06 M DIVALENT CATIONS, 0.1 M TRIS/BICINE PH 8.5, 30 % PEG550MME/PEG20000
Resolution 1.90 Å R-free 0.224
5AMB Crystal structure of the Angiotensin-1 converting enzyme N-domain in complex with amyloid-beta 35-42 Deposited 2015-03-10 Different construct Different oligomeric state Different ligand/ion Different experimental conditions Different structure-quality metrics Assembly 1 Other combination Heteromer；Protein × 2 PDB declaration: dimeric
Chain P 706–713（8 aa） Fragment：UNP RESIDUES 706-713
Not recorded ZN ZINC ION × 1 CL CHLORIDE ION × 1 PEG DI(HYDROXYETHYL)ETHER × 3 P6G HEXAETHYLENE GLYCOL × 1 X-RAY DIFFRACTION
X-ray crystallization conditions pH 8.5；0.06 M DIVALENT CATIONS, 0.1 M TRIS/ BICINE PH 8.5, 30 % PEG550MME/PEG20000
Resolution 1.55 Å R-free 0.181
5AMB Crystal structure of the Angiotensin-1 converting enzyme N-domain in complex with amyloid-beta 35-42 Deposited 2015-03-10 Different construct Different oligomeric state Different ligand/ion Different experimental conditions Different structure-quality metrics Assembly 2 Other combination Heteromer；Protein × 2 PDB declaration: dimeric
Chain Q 706–713（8 aa） Fragment：UNP RESIDUES 706-713
Not recorded ZN ZINC ION × 1 CL CHLORIDE ION × 1 PEG DI(HYDROXYETHYL)ETHER × 1 P6G HEXAETHYLENE GLYCOL × 2 PG4 TETRAETHYLENE GLYCOL × 1 X-RAY DIFFRACTION
X-ray crystallization conditions pH 8.5；0.06 M DIVALENT CATIONS, 0.1 M TRIS/ BICINE PH 8.5, 30 % PEG550MME/PEG20000
Resolution 1.55 Å R-free 0.181
5BUO A receptor molecule Deposited 2015-06-04 Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental conditions Different structure-quality metrics Assembly 1 Other combination Homooligomer；Protein × 2 PDB declaration: dimeric
Chain A 351–691（341 aa） Fragment：UNP Residues 351-691
Chain B 351–691（341 aa） Fragment：UNP Residues 351-691
Not recorded ZN ZINC ION × 6 CA CALCIUM ION × 1 GOL GLYCEROL × 3 ACT ACETATE ION × 1 SCN THIOCYANATE ION × 3 SO4 SULFATE ION × 1 MG MAGNESIUM ION × 1 X-RAY DIFFRACTION
X-ray crystallization conditions VAPOR DIFFUSION, SITTING DROP；293 K；PEG3350, ammonium acetate, bis-tris, zinc, thiocyanate
Resolution 2.31 Å R-free 0.241
5C67 Human Mesotrypsin in complex with amyloid precursor protein inhibitor variant APPI-M17G/I18F/F34V Deposited 2015-06-22 Different construct Different mutation/modification Different ligand/ion Different experimental conditions Different structure-quality metrics Assembly 1 Protein heterocomplex Heteromer；Protein × 2 PDB declaration: dimeric
Chain E 294–346（53 aa）
Mutation：M15G, I16F, F32V No recorded non-water small molecule X-RAY DIFFRACTION
X-ray crystallization conditions VAPOR DIFFUSION, HANGING DROP；pH 7.5；298 K；0.1 M ammonium sulfate, 0.1 M Tris pH 7.5, and 20% PEG-1000
Resolution 1.83 Å R-free 0.267
5C67 Human Mesotrypsin in complex with amyloid precursor protein inhibitor variant APPI-M17G/I18F/F34V Deposited 2015-06-22 Different construct Different mutation/modification Different ligand/ion Different experimental conditions Different structure-quality metrics Assembly 2 Protein heterocomplex Heteromer；Protein × 2 PDB declaration: dimeric
Chain C 294–346（53 aa）
Mutation：M15G, I16F, F32V No recorded non-water small molecule X-RAY DIFFRACTION
X-ray crystallization conditions VAPOR DIFFUSION, HANGING DROP；pH 7.5；298 K；0.1 M ammonium sulfate, 0.1 M Tris pH 7.5, and 20% PEG-1000
Resolution 1.83 Å R-free 0.267
5CSZ CRYSTAL STRUCTURE OF GANTENERUMAB FAB FRAGMENT IN COMPLEX WITH ABETA 1-11 Deposited 2015-07-23 Different construct Different oligomeric state Different ligand/ion Different experimental conditions Different structure-quality metrics Assembly 1 Protein heterocomplex Heteromer；Protein × 3 PDB declaration: trimeric
Chain D 672–682（11 aa） Fragment：UNP residues 672-682
Not recorded NAG 2-acetamido-2-deoxy-beta-D-glucopyranose × 1 SO4 SULFATE ION × 1 X-RAY DIFFRACTION
X-ray crystallization conditions VAPOR DIFFUSION, SITTING DROP；293 K；25 % PEG 3350, 0.1M Bis-Tris 6.5, 0.2 M ammonium sulfate
Resolution 1.80 Å R-free 0.230
5CSZ CRYSTAL STRUCTURE OF GANTENERUMAB FAB FRAGMENT IN COMPLEX WITH ABETA 1-11 Deposited 2015-07-23 Different construct Different oligomeric state Different ligand/ion Different experimental conditions Different structure-quality metrics Assembly 2 Protein heterocomplex Heteromer；Protein × 3 PDB declaration: trimeric
Chain E 672–682（11 aa） Fragment：UNP residues 672-682
Not recorded NAG 2-acetamido-2-deoxy-beta-D-glucopyranose × 1 SO4 SULFATE ION × 1 X-RAY DIFFRACTION
X-ray crystallization conditions VAPOR DIFFUSION, SITTING DROP；293 K；25 % PEG 3350, 0.1M Bis-Tris 6.5, 0.2 M ammonium sulfate
Resolution 1.80 Å R-free 0.230
5HOX X-ray crystallographic structure of an A-beta 17_36 beta-hairpin. Synchrotron data set. (LVFFAEDCGSNKCAII(SAR)LMV). Deposited 2016-01-19 Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental conditions Different structure-quality metrics Assembly 1 Protein homooligomer Homooligomer；Protein × 3 PDB declaration: trimeric
Chain A 687–707（21 aa） Fragment：UNP residues 687-707
Chain B 687–707（21 aa） Fragment：UNP residues 687-707
Chain C 687–707（21 aa） Fragment：UNP residues 687-707
Mutation：V24C, G29C, G33Sar Non-standard monomer：Yes (specific site not provided by mmCIF) Mutation：V24C, G29C, G33Sar Non-standard monomer：Yes (specific site not provided by mmCIF) Mutation：V24C, G29C, G33Sar Non-standard monomer：Yes (specific site not provided by mmCIF) No recorded non-water small molecule X-RAY DIFFRACTION
X-ray crystallization conditions VAPOR DIFFUSION, HANGING DROP；pH 7.1；296 K；0.1 M HEPES Buffer, 29% (v/v) Jeffamine M-600
Resolution 1.90 Å R-free 0.250
5HOX X-ray crystallographic structure of an A-beta 17_36 beta-hairpin. Synchrotron data set. (LVFFAEDCGSNKCAII(SAR)LMV). Deposited 2016-01-19 Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental conditions Different structure-quality metrics Assembly 2 Protein homooligomer Homooligomer；Protein × 6 PDB declaration: hexameric
Chain A 687–707（21 aa） Fragment：UNP residues 687-707
Chain B 687–707（21 aa） Fragment：UNP residues 687-707
Chain C 687–707（21 aa） Fragment：UNP residues 687-707
Mutation：V24C, G29C, G33Sar Non-standard monomer：Yes (specific site not provided by mmCIF) Mutation：V24C, G29C, G33Sar Non-standard monomer：Yes (specific site not provided by mmCIF) Mutation：V24C, G29C, G33Sar Non-standard monomer：Yes (specific site not provided by mmCIF) No recorded non-water small molecule X-RAY DIFFRACTION
X-ray crystallization conditions VAPOR DIFFUSION, HANGING DROP；pH 7.1；296 K；0.1 M HEPES Buffer, 29% (v/v) Jeffamine M-600
Resolution 1.90 Å R-free 0.250
5HOX X-ray crystallographic structure of an A-beta 17_36 beta-hairpin. Synchrotron data set. (LVFFAEDCGSNKCAII(SAR)LMV). Deposited 2016-01-19 Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental conditions Different structure-quality metrics Assembly 3 Protein homooligomer Homooligomer；Protein × 3 PDB declaration: trimeric
Chain D 687–707（21 aa） Fragment：UNP residues 687-707
Chain E 687–707（21 aa） Fragment：UNP residues 687-707
Chain F 687–707（21 aa） Fragment：UNP residues 687-707
Mutation：V24C, G29C, G33Sar Non-standard monomer：Yes (specific site not provided by mmCIF) Mutation：V24C, G29C, G33Sar Non-standard monomer：Yes (specific site not provided by mmCIF) Mutation：V24C, G29C, G33Sar Non-standard monomer：Yes (specific site not provided by mmCIF) JEF O-(O-(2-AMINOPROPYL)-O'-(2-METHOXYETHYL)POLYPROPYLENE GLYCOL 500) × 1 X-RAY DIFFRACTION
X-ray crystallization conditions VAPOR DIFFUSION, HANGING DROP；pH 7.1；296 K；0.1 M HEPES Buffer, 29% (v/v) Jeffamine M-600
Resolution 1.90 Å R-free 0.250
5HOX X-ray crystallographic structure of an A-beta 17_36 beta-hairpin. Synchrotron data set. (LVFFAEDCGSNKCAII(SAR)LMV). Deposited 2016-01-19 Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental conditions Different structure-quality metrics Assembly 4 Protein homooligomer Homooligomer；Protein × 6 PDB declaration: hexameric
Chain D 687–707（21 aa） Fragment：UNP residues 687-707
Chain E 687–707（21 aa） Fragment：UNP residues 687-707
Chain F 687–707（21 aa） Fragment：UNP residues 687-707
Mutation：V24C, G29C, G33Sar Non-standard monomer：Yes (specific site not provided by mmCIF) Mutation：V24C, G29C, G33Sar Non-standard monomer：Yes (specific site not provided by mmCIF) Mutation：V24C, G29C, G33Sar Non-standard monomer：Yes (specific site not provided by mmCIF) JEF O-(O-(2-AMINOPROPYL)-O'-(2-METHOXYETHYL)POLYPROPYLENE GLYCOL 500) × 2 X-RAY DIFFRACTION
X-ray crystallization conditions VAPOR DIFFUSION, HANGING DROP；pH 7.1；296 K；0.1 M HEPES Buffer, 29% (v/v) Jeffamine M-600
Resolution 1.90 Å R-free 0.250
5HOX X-ray crystallographic structure of an A-beta 17_36 beta-hairpin. Synchrotron data set. (LVFFAEDCGSNKCAII(SAR)LMV). Deposited 2016-01-19 Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental conditions Different structure-quality metrics Assembly 5 Protein homooligomer Homooligomer；Protein × 12 PDB declaration: dodecameric
Chain A 687–707（21 aa） Fragment：UNP residues 687-707
Chain B 687–707（21 aa） Fragment：UNP residues 687-707
Chain C 687–707（21 aa） Fragment：UNP residues 687-707
Chain D 687–707（21 aa） Fragment：UNP residues 687-707
Chain E 687–707（21 aa） Fragment：UNP residues 687-707
Chain F 687–707（21 aa） Fragment：UNP residues 687-707
Mutation：V24C, G29C, G33Sar Non-standard monomer：Yes (specific site not provided by mmCIF) Mutation：V24C, G29C, G33Sar Non-standard monomer：Yes (specific site not provided by mmCIF) Mutation：V24C, G29C, G33Sar Non-standard monomer：Yes (specific site not provided by mmCIF) Mutation：V24C, G29C, G33Sar Non-standard monomer：Yes (specific site not provided by mmCIF) Mutation：V24C, G29C, G33Sar Non-standard monomer：Yes (specific site not provided by mmCIF) Mutation：V24C, G29C, G33Sar Non-standard monomer：Yes (specific site not provided by mmCIF) JEF O-(O-(2-AMINOPROPYL)-O'-(2-METHOXYETHYL)POLYPROPYLENE GLYCOL 500) × 2 X-RAY DIFFRACTION
X-ray crystallization conditions VAPOR DIFFUSION, HANGING DROP；pH 7.1；296 K；0.1 M HEPES Buffer, 29% (v/v) Jeffamine M-600
Resolution 1.90 Å R-free 0.250
5HOY X-ray crystallographic structure of an A-beta 17_36 beta-hairpin. X-ray diffractometer data set. (LVFFAEDCGSNKCAII(SAR)LMV). Deposited 2016-01-19 Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental conditions Different structure-quality metrics Assembly 1 Protein homooligomer Homooligomer；Protein × 12 PDB declaration: dodecameric
Chain A 687–707（21 aa） Fragment：UNP residues 687-707
Chain B 687–707（21 aa） Fragment：UNP residues 687-707
Chain C 687–707（21 aa） Fragment：UNP residues 687-707
Chain D 687–707（21 aa） Fragment：UNP residues 687-707
Chain E 687–707（21 aa） Fragment：UNP residues 687-707
Chain F 687–707（21 aa） Fragment：UNP residues 687-707
Mutation：V24C, G29C, G33SAR Non-standard monomer：Yes (specific site not provided by mmCIF) Mutation：V24C, G29C, G33SAR Non-standard monomer：Yes (specific site not provided by mmCIF) Mutation：V24C, G29C, G33SAR Non-standard monomer：Yes (specific site not provided by mmCIF) Mutation：V24C, G29C, G33SAR Non-standard monomer：Yes (specific site not provided by mmCIF) Mutation：V24C, G29C, G33SAR Non-standard monomer：Yes (specific site not provided by mmCIF) Mutation：V24C, G29C, G33SAR Non-standard monomer：Yes (specific site not provided by mmCIF) JEF O-(O-(2-AMINOPROPYL)-O'-(2-METHOXYETHYL)POLYPROPYLENE GLYCOL 500) × 2 X-RAY DIFFRACTION
X-ray crystallization conditions VAPOR DIFFUSION, HANGING DROP；pH 6.9；296 K；0.1 M HEPES Buffer, 27% (v/v) Jeffamine M-600
Resolution 2.29 Å R-free 0.276
5HOY X-ray crystallographic structure of an A-beta 17_36 beta-hairpin. X-ray diffractometer data set. (LVFFAEDCGSNKCAII(SAR)LMV). Deposited 2016-01-19 Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental conditions Different structure-quality metrics Assembly 2 Protein homooligomer Homooligomer；Protein × 3 PDB declaration: trimeric
Chain A 687–707（21 aa） Fragment：UNP residues 687-707
Chain B 687–707（21 aa） Fragment：UNP residues 687-707
Chain C 687–707（21 aa） Fragment：UNP residues 687-707
Mutation：V24C, G29C, G33SAR Non-standard monomer：Yes (specific site not provided by mmCIF) Mutation：V24C, G29C, G33SAR Non-standard monomer：Yes (specific site not provided by mmCIF) Mutation：V24C, G29C, G33SAR Non-standard monomer：Yes (specific site not provided by mmCIF) No recorded non-water small molecule X-RAY DIFFRACTION
X-ray crystallization conditions VAPOR DIFFUSION, HANGING DROP；pH 6.9；296 K；0.1 M HEPES Buffer, 27% (v/v) Jeffamine M-600
Resolution 2.29 Å R-free 0.276
5HOY X-ray crystallographic structure of an A-beta 17_36 beta-hairpin. X-ray diffractometer data set. (LVFFAEDCGSNKCAII(SAR)LMV). Deposited 2016-01-19 Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental conditions Different structure-quality metrics Assembly 3 Protein homooligomer Homooligomer；Protein × 6 PDB declaration: hexameric
Chain A 687–707（21 aa） Fragment：UNP residues 687-707
Chain B 687–707（21 aa） Fragment：UNP residues 687-707
Chain C 687–707（21 aa） Fragment：UNP residues 687-707
Mutation：V24C, G29C, G33SAR Non-standard monomer：Yes (specific site not provided by mmCIF) Mutation：V24C, G29C, G33SAR Non-standard monomer：Yes (specific site not provided by mmCIF) Mutation：V24C, G29C, G33SAR Non-standard monomer：Yes (specific site not provided by mmCIF) No recorded non-water small molecule X-RAY DIFFRACTION
X-ray crystallization conditions VAPOR DIFFUSION, HANGING DROP；pH 6.9；296 K；0.1 M HEPES Buffer, 27% (v/v) Jeffamine M-600
Resolution 2.29 Å R-free 0.276
5HOY X-ray crystallographic structure of an A-beta 17_36 beta-hairpin. X-ray diffractometer data set. (LVFFAEDCGSNKCAII(SAR)LMV). Deposited 2016-01-19 Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental conditions Different structure-quality metrics Assembly 4 Protein homooligomer Homooligomer；Protein × 3 PDB declaration: trimeric
Chain D 687–707（21 aa） Fragment：UNP residues 687-707
Chain E 687–707（21 aa） Fragment：UNP residues 687-707
Chain F 687–707（21 aa） Fragment：UNP residues 687-707
Mutation：V24C, G29C, G33SAR Non-standard monomer：Yes (specific site not provided by mmCIF) Mutation：V24C, G29C, G33SAR Non-standard monomer：Yes (specific site not provided by mmCIF) Mutation：V24C, G29C, G33SAR Non-standard monomer：Yes (specific site not provided by mmCIF) JEF O-(O-(2-AMINOPROPYL)-O'-(2-METHOXYETHYL)POLYPROPYLENE GLYCOL 500) × 1 X-RAY DIFFRACTION
X-ray crystallization conditions VAPOR DIFFUSION, HANGING DROP；pH 6.9；296 K；0.1 M HEPES Buffer, 27% (v/v) Jeffamine M-600
Resolution 2.29 Å R-free 0.276
5HOY X-ray crystallographic structure of an A-beta 17_36 beta-hairpin. X-ray diffractometer data set. (LVFFAEDCGSNKCAII(SAR)LMV). Deposited 2016-01-19 Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental conditions Different structure-quality metrics Assembly 5 Protein homooligomer Homooligomer；Protein × 6 PDB declaration: hexameric
Chain D 687–707（21 aa） Fragment：UNP residues 687-707
Chain E 687–707（21 aa） Fragment：UNP residues 687-707
Chain F 687–707（21 aa） Fragment：UNP residues 687-707
Mutation：V24C, G29C, G33SAR Non-standard monomer：Yes (specific site not provided by mmCIF) Mutation：V24C, G29C, G33SAR Non-standard monomer：Yes (specific site not provided by mmCIF) Mutation：V24C, G29C, G33SAR Non-standard monomer：Yes (specific site not provided by mmCIF) JEF O-(O-(2-AMINOPROPYL)-O'-(2-METHOXYETHYL)POLYPROPYLENE GLYCOL 500) × 2 X-RAY DIFFRACTION
X-ray crystallization conditions VAPOR DIFFUSION, HANGING DROP；pH 6.9；296 K；0.1 M HEPES Buffer, 27% (v/v) Jeffamine M-600
Resolution 2.29 Å R-free 0.276
5KK3 Atomic Resolution Structure of Monomorphic AB42 Amyloid Fibrils Deposited 2016-06-20 Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental method Different experimental conditions Different structure-quality metrics Assembly 1 Protein homooligomer Homooligomer；Protein × 18 PDB declaration: octadecameric
Chain A 672–713（42 aa） Fragment：residues 672-713
Chain B 672–713（42 aa） Fragment：residues 672-713
Chain C 672–713（42 aa） Fragment：residues 672-713
Chain D 672–713（42 aa） Fragment：residues 672-713
Chain E 672–713（42 aa） Fragment：residues 672-713
Chain F 672–713（42 aa） Fragment：residues 672-713
Chain G 672–713（42 aa） Fragment：residues 672-713
Chain H 672–713（42 aa） Fragment：residues 672-713
Chain I 672–713（42 aa） Fragment：residues 672-713
Chain J 672–713（42 aa） Fragment：residues 672-713
Chain K 672–713（42 aa） Fragment：residues 672-713
Chain L 672–713（42 aa） Fragment：residues 672-713
Chain M 672–713（42 aa） Fragment：residues 672-713
Chain N 672–713（42 aa） Fragment：residues 672-713
Chain O 672–713（42 aa） Fragment：residues 672-713
Chain P 672–713（42 aa） Fragment：residues 672-713
Chain Q 672–713（42 aa） Fragment：residues 672-713
Chain R 672–713（42 aa） Fragment：residues 672-713
Not recorded No recorded non-water small molecule SOLID-STATE NMR
NMR measurement conditions pH 8；277 K；Ionic strength (raw mmCIF value) 1；Pressure 1
NMR sample composition 1 mg/uL [U-100% 13C; U-100% 15N] AB42-M01-42, 20 mM sodium phosphate, 0.2 mM EDTA, 0.02 % sodium azide, 100% H2O | 100% H2O
NMR sample composition 1 mg/uL [U-30% 13C; U-30% 15N] AB42-M01-42, 20 mM sodium phosphate, 0.2 mM EDTA, 0.02 % sodium azide, 100% H2O | 100% H2O
NMR sample composition 1 mg/uL [1,6-13C-glucose, U-100% 15N] AB42-M01-42, 20 mM sodium phosphate, 0.2 mM EDTA, 0.02 % sodium azide, 100% H2O | 100% H2O
NMR sample composition 1 mg/uL [2-13C-glycerol, U-100% 15N] AB42-M01-42, 20 mM sodium phosphate, 0.2 mM EDTA, 0.02 % sodium azide, 100% H2O | 100% H2O
Resolution not provided
5MYO Structure of Pyroglutamate-Abeta-specific Fab c#6 in complex with human Abeta-pE3-12-PEGb Deposited 2017-01-27 Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental conditions Different structure-quality metrics Assembly 1 Protein heterocomplex Heteromer；Protein × 3 PDB declaration: trimeric
Chain E 674–683（10 aa） Fragment：UNP residues 674-683
Non-standard monomer：Yes (specific site not provided by mmCIF) SO4 SULFATE ION × 1 GOL GLYCEROL × 2 X-RAY DIFFRACTION
X-ray crystallization conditions VAPOR DIFFUSION, HANGING DROP；286 K；25.5% w/v PEG 4000 15% glycerol 170 mM ammonium sulfate
Resolution 1.59 Å R-free 0.215
5NX1 Combinatorial Engineering of Proteolytically Resistant APPI Variants that Selectively Inhibit Human Kallikrein 6 for Cancer Therapy Deposited 2017-05-09 Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental conditions Different structure-quality metrics Assembly 1 Protein heterocomplex Heteromer；Protein × 4 PDB declaration: tetrameric
Chain B 289–301（13 aa） Fragment：UNP residues 289-301
Chain C 289–346（58 aa） Fragment：UNP residues 289-346
Chain D 302–346（45 aa） Fragment：UNP residues 302-346
Not recorded No recorded non-water small molecule X-RAY DIFFRACTION
X-ray crystallization conditions VAPOR DIFFUSION；293 K；0.2M Ammonium Sulfate, 0.1M Bis-Tris pH 5.5, 25% Polyethylene Glycol 3350
Resolution 1.85 Å R-free 0.226
5NX3 Combinatorial Engineering of Proteolytically Resistant APPI Variants that Selectively Inhibit Human Kallikrein 6 for Cancer Therapy Deposited 2017-05-09 Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental conditions Different structure-quality metrics Assembly 1 Protein heterocomplex Heteromer；Protein × 4 PDB declaration: tetrameric
Chain B 289–301（13 aa） Fragment：Inhibitor domain, UNP Residues 294-346
Chain C 289–346（58 aa） Fragment：Inhibitor domain, UNP Residues 289-346
Chain D 306–346（41 aa） Fragment：Inhibitor domain, UNP Residues 306-346
Not recorded No recorded non-water small molecule X-RAY DIFFRACTION
X-ray crystallization conditions VAPOR DIFFUSION, SITTING DROP；293 K；0.1M tri-Na Citrate pH 5.6, 20% 2-propanol , 20% Polyethylene Glycol 4000
Resolution 2.30 Å R-free 0.226
5OQV Near-atomic resolution fibril structure of complete amyloid-beta(1-42) by cryo-EM Deposited 2017-08-14 Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental method Different experimental conditions Different structure-quality metrics Assembly 1 Protein homooligomer Homooligomer；Protein × 9 PDB declaration: nonameric
Chain A 672–713（42 aa）
Chain B 672–713（42 aa）
Chain C 672–713（42 aa）
Chain D 672–713（42 aa）
Chain E 672–713（42 aa）
Chain F 672–713（42 aa）
Chain G 672–713（42 aa）
Chain H 672–713（42 aa）
Chain I 672–713（42 aa）
Not recorded No recorded non-water small molecule ELECTRON MICROSCOPY
cryo-EM buffer pH 2；in water
cryo-EM vitrification conditions Cryogen ETHANE；2.5 microL sample was applied to the grid, blotted for 2.5 s before plunging.
Resolution 4.00 Å
5TXD Structure of amyloid-beta derived peptide - NKGAIF Deposited 2016-11-16 Different construct Different oligomeric state Different ligand/ion Different experimental conditions Different structure-quality metrics Assembly 1 Protein homooligomer Homooligomer；Protein × 8 PDB declaration: octameric
Chain Z 698–703（6 aa） Fragment：unp residues 698-703
Not recorded PO4 PHOSPHATE ION × 8 X-RAY DIFFRACTION
X-ray crystallization conditions VAPOR DIFFUSION, HANGING DROP；pH 5；298 K；reservoir contained 20% PEG 3350, 0.2M Potassium Phosphate dibasic
Resolution 1.45 Å R-free 0.191
5VZY Crystal structure of crenezumab Fab in complex with Abeta Deposited 2017-05-29 Different construct Different oligomeric state Different ligand/ion Different experimental conditions Different structure-quality metrics Assembly 1 Protein heterocomplex Heteromer；Protein × 3 PDB declaration: trimeric
Chain A 682–696（15 aa） Fragment：UNP residues 682-696
Not recorded No recorded non-water small molecule X-RAY DIFFRACTION
X-ray crystallization conditions VAPOR DIFFUSION, SITTING DROP；277 K；0.2 M magnesium chloride hexahydrate, 0.1 M Tris hydrochloride pH 8.5, 30% w/v polyethylene glycol 4000
Resolution 2.32 Å R-free 0.249
5W3P ANTIBODY C706 IN COMPLEX WTH BETA-AMYLOID PEPTIDE 1-16 Deposited 2017-06-08 Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental conditions Different structure-quality metrics Assembly 1 Protein heterocomplex Heteromer；Protein × 3 PDB declaration: trimeric
Chain P 671–688（18 aa） Fragment：RESIDUES 1-16
Non-standard monomer：Yes (specific site not provided by mmCIF) SO4 SULFATE ION × 4 GOL GLYCEROL × 3 X-RAY DIFFRACTION
X-ray crystallization conditions VAPOR DIFFUSION, SITTING DROP；pH 4.5；293 K；2.0 M AMMONIUM SULFATE, 0.1 M SODIUM ACETATE, PH 4.5
Resolution 1.92 Å R-free 0.236
6GFI Structure of Human Mesotrypsin in complex with APPI variant T11V/M17R/I18F/F34V Deposited 2018-04-30 Different construct Different ligand/ion Different experimental conditions Different structure-quality metrics Assembly 1 Protein heterocomplex Heteromer；Protein × 2 PDB declaration: dimeric
Chain E 294–346（53 aa）
Not recorded EDO 1,2-ETHANEDIOL × 1 X-RAY DIFFRACTION
X-ray crystallization conditions VAPOR DIFFUSION, SITTING DROP；293 K；0.1M Sodium Chloride, 0.1M Bis-Tris pH 6.8 , 1.42M Ammonium Sulfate
Resolution 2.30 Å R-free 0.301
6GFI Structure of Human Mesotrypsin in complex with APPI variant T11V/M17R/I18F/F34V Deposited 2018-04-30 Different construct Different ligand/ion Different experimental conditions Different structure-quality metrics Assembly 2 Protein heterocomplex Heteromer；Protein × 2 PDB declaration: dimeric
Chain C 294–346（53 aa）
Not recorded No recorded non-water small molecule X-RAY DIFFRACTION
X-ray crystallization conditions VAPOR DIFFUSION, SITTING DROP；293 K；0.1M Sodium Chloride, 0.1M Bis-Tris pH 6.8 , 1.42M Ammonium Sulfate
Resolution 2.30 Å R-free 0.301
6IYC Recognition of the Amyloid Precursor Protein by Human gamma-secretase Deposited 2018-12-14 Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental method Different experimental conditions Different structure-quality metrics Assembly 1 Other combination Heteromer；Protein × 5 PDB declaration: pentameric
Chain E 688–770（83 aa） Fragment：C83
Mutation：V8C NAG 2-acetamido-2-deoxy-beta-D-glucopyranose × 6 PC1 1,2-DIACYL-SN-GLYCERO-3-PHOSPHOCHOLINE × 2 CLR CHOLESTEROL × 3 ELECTRON MICROSCOPY
cryo-EM buffer pH 7.4
cryo-EM vitrification conditions Cryogen ETHANE
Resolution 2.60 Å
6NB9 Amyloid-Beta (20-34) with L-isoaspartate 23 Deposited 2018-12-06 Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental method Different experimental conditions Different structure-quality metrics Assembly 1 Protein homooligomer Homooligomer；Protein × 10 PDB declaration: decameric
Chain A 691–705（15 aa） Fragment：residues 20-34
Mutation：L-isoaspartate 23 Non-standard monomer：Yes (specific site not provided by mmCIF) No recorded non-water small molecule ELECTRON CRYSTALLOGRAPHY
cryo-EM buffer pH 7.6
cryo-EM vitrification conditions Cryogen ETHANE
X-ray crystallization conditions BATCH；pH 7.6；310 K；0.05M Tris-HCl, 0.15M NaCl, 1% DMSO
Resolution 1.05 Å R-free 0.246
6O4J Amyloid Beta KLVFFAENVGS 16-26 D23N Iowa mutation Deposited 2019-02-28 Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental method Different experimental conditions Different structure-quality metrics Assembly 1 Protein homooligomer Homooligomer；Protein × 12 PDB declaration: dodecameric
Chain A 687–697（11 aa） Fragment：UNP residues 687-697
Chain B 687–697（11 aa） Fragment：UNP residues 687-697
Mutation：D23N Non-standard monomer：Yes (specific site not provided by mmCIF) Mutation：D23N Non-standard monomer：Yes (specific site not provided by mmCIF) No recorded non-water small molecule ELECTRON CRYSTALLOGRAPHY
cryo-EM buffer pH 8
cryo-EM vitrification conditions Cryogen ETHANE
X-ray crystallization conditions UNSPECIFIED
Resolution 1.40 Å R-free 0.283
6OC9 S8 phosphorylated beta amyloid 40 fibrils Deposited 2019-03-22 Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental method Different experimental conditions Different structure-quality metrics Assembly 1 Protein homooligomer Homooligomer；Protein × 10 PDB declaration: decameric
Chain A 653–692（40 aa） Fragment：residues 616-655
Chain B 653–692（40 aa） Fragment：residues 616-655
Chain C 653–692（40 aa） Fragment：residues 616-655
Chain D 653–692（40 aa） Fragment：residues 616-655
Chain E 653–692（40 aa） Fragment：residues 616-655
Chain F 653–692（40 aa） Fragment：residues 616-655
Chain G 653–692（40 aa） Fragment：residues 616-655
Chain H 653–692（40 aa） Fragment：residues 616-655
Chain I 653–692（40 aa） Fragment：residues 616-655
Chain J 653–692（40 aa） Fragment：residues 616-655
Not recorded 2PO PHOSPHONATE × 10 SOLID-STATE NMR
NMR measurement conditions pH 7.4；280 K；Ionic strength (raw mmCIF value) 10；Pressure 1
NMR sample composition 50 uM 13C, 15N-uniformly labeled E3, G9, V18, F20, D23, S26, K28 beta amyloid peptide, 50 uM 13C, 15N-uniformly labeled A2, F4, D7, Y10, V24, G25 beta amyloid peptide, 50 uM 13C, 15N-uniformly labeled Q15, F19, A21, I31, L34, V36, G37 beta amyloid peptide, 50 uM 13C, 15N-uniformly labeled V12, E22, G29, A30, M35 beta amyloid peptide, 50 uM 13C, 15N-uniformly labeled E11, L17, N27, I32, G33, G38, V39 beta amyloid peptide, 50 uM 13C, 15N-uniformly labeled F19, L34 beta amyloid peptide, 50 uM 13C, 15N-uniformly labeled E3, F4, V24, G25, S26 beta amyloid peptide, 50 uM 13C, 15N-uniformly labeled V12, F20, E22 beta amyloid peptide, 50 uM 13C, 15N-uniformly labeled I31, G33, V39 beta amyloid peptide, water | water
NMR sample composition 50 uM 2H labeled L17, 2H-CD3 beta amyloid peptide, 50 uM 2H labeled F19, 2H-ring-D5 beta amyloid peptide, 50 2H labeled uM L34, 2H-CD3 beta amyloid peptide, 50 uM 2H labeled M35, 2H-CD3 beta amyloid peptide, 50 uM 2H labeled V36, 2H-CD3 beta amyloid peptide, water | water
NMR sample composition 50 uM 13C selective labeled A2-CH3, V12-CO beta amyloid peptide, 50 uM 13C selective labeled V18-CO, A21-CH3 beta amyloid peptide, 50 uM 13C selective labeled V24-CO, A30-CH3 beta amyloid peptide, 50 uM 13C selective labeled G33-CO, V39-Ca beta amyloid peptide, 50 uM 13C selective labeled V36-Ca, G38-CO beta amyloid peptide, 50 uM 13C selective labeled G9-CO beta amyloid peptide, water | water
Resolution not provided
6RHY Structure of pore-forming amyloid-beta tetramers Deposited 2019-04-23 Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental method Different experimental conditions Different structure-quality metrics Assembly 1 Protein homooligomer Homooligomer；Protein × 4 PDB declaration: tetrameric
Chain A 672–713（42 aa）
Chain B 672–713（42 aa）
Chain C 672–713（42 aa）
Chain D 672–713（42 aa）
Not recorded No recorded non-water small molecule SOLUTION NMR
NMR measurement conditions pH 8.5；310.15 K；Pressure 1
NMR measurement conditions pH 9.5；310.15 K；Pressure 1
NMR sample composition 1 mM [U-15N] Amyloid-beta A4 protein, 10 mM [U-2H] TRIS-d11, 28.5 mM [U-2H] DPC-d38, 90% H2O/10% D2O | 90% H2O/10% D2O
NMR sample composition 1 mM [U-13C; U-15N; U-2H] Amyloid-beta A4 protein, 10 mM [U-2H] TRIS-d11, 28.5 mM [U-2H] DPC-d38, 90% H2O/10% D2O | 90% H2O/10% D2O
NMR sample composition 1 mM [U-2H,13C,15N]-Ile-[13CH3]d1, Ala-[13CH3], Leu/Val-[13CH3]proR Amyloid-beta A4 protein, 10 mM [U-2H] TRIS-d11, 28.5 mM [U-2H] DPC-d38, 90% H2O/10% D2O | 90% H2O/10% D2O
NMR sample composition 1 mM [U-2H,15N]-Ile-[13CH3]d1, Ala-[13CH3], Leu/Val-[13CH3]proR Amyloid-beta A4 protein, 10 mM [U-2H] TRIS-d11, 28.5 mM [U-2H] DPC-d38, 90% H2O/10% D2O | 90% H2O/10% D2O
Resolution not provided
6SHS Abeta fibril (Morphology I) Deposited 2019-08-08 Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental method Different experimental conditions Different structure-quality metrics Assembly 1 Protein homooligomer Homooligomer；Protein × 12 PDB declaration: dodecameric
Chain A 616–655（40 aa）
Chain B 616–655（40 aa）
Chain C 616–655（40 aa）
Chain D 616–655（40 aa）
Chain E 616–655（40 aa）
Chain F 616–655（40 aa）
Chain G 616–655（40 aa）
Chain H 616–655（40 aa）
Chain I 616–655（40 aa）
Chain J 616–655（40 aa）
Chain K 616–655（40 aa）
Chain L 616–655（40 aa）
Not recorded No recorded non-water small molecule ELECTRON MICROSCOPY
cryo-EM buffer pH 7
cryo-EM vitrification conditions Cryogen ETHANE
Resolution 4.40 Å
6SZF Solution structure of the amyloid beta-peptide (1-42) Deposited 2019-10-02 Different construct Different oligomeric state Different ligand/ion Different experimental method Different experimental conditions Different structure-quality metrics Assembly 1 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric
Chain A 672–713（42 aa）
Not recorded No recorded non-water small molecule SOLUTION NMR
NMR measurement conditions pH 5.4；300 K；Ionic strength (raw mmCIF value) 0；Pressure ambient
NMR sample composition 0.5 mM Amyloid beta-peptide (1-42), 50% H2O/50% HFIP | 50% H2O/50% HFIP
Resolution not provided
6TI5 A New Structural Model of Abeta(1-40) Fibrils Deposited 2019-11-21 Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental method Different experimental conditions Different structure-quality metrics Assembly 1 Protein homooligomer Homooligomer；Protein × 16 PDB declaration: hexadecameric
Chain A 616–655（40 aa）
Chain B 616–655（40 aa）
Chain C 616–655（40 aa）
Chain D 616–655（40 aa）
Chain E 616–655（40 aa）
Chain F 616–655（40 aa）
Chain G 616–655（40 aa）
Chain H 616–655（40 aa）
Chain I 616–655（40 aa）
Chain J 616–655（40 aa）
Chain K 616–655（40 aa）
Chain L 616–655（40 aa）
Chain M 616–655（40 aa）
Chain N 616–655（40 aa）
Chain O 616–655（40 aa）
Chain P 616–655（40 aa）
Not recorded No recorded non-water small molecule SOLID-STATE NMR
NMR measurement conditions pH 8.5；283 K；Ionic strength (raw mmCIF value) 0；Pressure 1
NMR sample composition 100 uM [U-100% 13C; U-100% 15N] Amyloid beta peptide 1-40, 50 mM ammonium acetate, H2O | H2O
Resolution not provided
6TI6 Mixing Abeta(1-40) and Abeta(1-42) peptides generates unique amyloid fibrils Deposited 2019-11-21 Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental method Different experimental conditions Different structure-quality metrics Assembly 1 Protein homooligomer Homooligomer；Protein × 16 PDB declaration: hexadecameric
Chain A 616–655（40 aa）
Chain B 598–639（42 aa）
Chain C 616–655（40 aa）
Chain D 598–639（42 aa）
Chain E 616–655（40 aa）
Chain F 598–639（42 aa）
Chain G 616–655（40 aa）
Chain H 598–639（42 aa）
Chain I 616–655（40 aa）
Chain J 598–639（42 aa）
Chain K 616–655（40 aa）
Chain L 598–639（42 aa）
Chain M 616–655（40 aa）
Chain N 598–639（42 aa）
Chain O 616–655（40 aa）
Chain P 598–639（42 aa）
Not recorded No recorded non-water small molecule SOLID-STATE NMR
NMR measurement conditions pH 8.5；283 K；Ionic strength (raw mmCIF value) 0；Pressure 1
NMR sample composition 50 uM [U-100% 13C; U-100% 15N] Amyloid-beta peptide 1-40, 50 uM Amyloid-beta peptide 1-42, 50 mM ammonium acetate, H2O | H2O
NMR sample composition 70 uM [U-100% 13C; U-100% 15N] Amyloid-beta peptide 1-40, 30 uM Amyloid-beta peptide 1-42, 50 mM ammonium acetate, H2O | H2O
NMR sample composition 50 uM Amyloid-beta peptide 1-40, 50 uM [U-100% 13C; U-100% 15N] Amyloid-beta peptide 1-42, 50 mM ammonium acetate, H2O | H2O
NMR sample composition 50 uM [U-100% 13C] Amyloid-beta peptide 1-40, 50 uM [U-100% 15N] Amyloid-beta peptide 1-42, 50 mM ammonium acetate, H2O | H2O
Resolution not provided
6TI7 Mixing Abeta(1-40) and Abeta(1-42) peptides generates unique amyloid fibrils Deposited 2019-11-21 Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental method Different experimental conditions Different structure-quality metrics Assembly 1 Protein homooligomer Homooligomer；Protein × 16 PDB declaration: hexadecameric
Chain A 616–655（40 aa）
Chain B 598–639（42 aa）
Chain C 616–655（40 aa）
Chain D 598–639（42 aa）
Chain E 616–655（40 aa）
Chain F 598–639（42 aa）
Chain G 616–655（40 aa）
Chain H 598–639（42 aa）
Chain I 598–639（42 aa）
Chain J 616–655（40 aa）
Chain K 598–639（42 aa）
Chain L 616–655（40 aa）
Chain M 598–639（42 aa）
Chain N 616–655（40 aa）
Chain O 598–639（42 aa）
Chain P 616–655（40 aa）
Not recorded No recorded non-water small molecule SOLID-STATE NMR
NMR measurement conditions pH 8.5；283 K；Ionic strength (raw mmCIF value) 0；Pressure 1
NMR sample composition 50 uM [U-100% 13C; U-100% 15N] Amyloid-beta peptide 1-40, 50 uM Amyloid-beta peptide 1-42, 50 mM ammonium acetate, H2O | H2O
NMR sample composition 70 uM [U-100% 13C; U-100% 15N] Amyloid-beta peptide 1-40, 30 uM Amyloid-beta peptide 1-42, 50 mM ammonium acetate, H2O | H2O
NMR sample composition 50 uM Amyloid-beta peptide 1-40, 50 uM [U-100% 13C; U-100% 15N] Amyloid-beta peptide 1-42, 50 mM ammonium acetate, H2O | H2O
NMR sample composition 50 uM [U-100% 13C] Amyloid-beta peptide 1-40, 50 uM [U-100% 15N] Amyloid-beta peptide 1-42, 50 mM ammonium acetate, H2O | H2O
Resolution not provided
6W0O Amyloid-beta(1-40) fibril derived from Alzheimer's disease cortical tissue Deposited 2020-03-02 Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental method Different experimental conditions Different structure-quality metrics Assembly 1 Protein homooligomer Homooligomer；Protein × 6 PDB declaration: hexameric
Chain 1 653–692（40 aa） Fragment：UNP residues 653-692
Chain 2 653–692（40 aa） Fragment：UNP residues 653-692
Chain 3 653–692（40 aa） Fragment：UNP residues 653-692
Chain 4 653–692（40 aa） Fragment：UNP residues 653-692
Chain 5 653–692（40 aa） Fragment：UNP residues 653-692
Chain 6 653–692（40 aa） Fragment：UNP residues 653-692
Not recorded No recorded non-water small molecule Experimental method not declared
cryo-EM buffer pH 7.4；10 mM phosphate buffer with 0.01% NaN3 to avoid microbial contamination. Buffers were filtered to avoid contamination.
cryo-EM vitrification conditions Cryogen ETHANE；The grids were preblotted for 10 seconds and blotted for 6 seconds before plunging.
NMR measurement conditions pH 7.4；297 K；Ionic strength (raw mmCIF value) 10；Pressure 1
NMR sample composition 100 uM U-15N,13C amyloid-beta(1-40), phosphate buffer | phosphate buffer
Resolution 2.77 Å
6WXM X-ray crystallographic structure of a beta-hairpin peptide derived from amyloid beta 16-36 Deposited 2020-05-11 Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental conditions Different structure-quality metrics Assembly 1 Protein homooligomer Homooligomer；Protein × 8 PDB declaration: octameric
Chain A 685–706（22 aa）
Chain B 685–706（22 aa）
Chain C 685–706（22 aa）
Chain D 685–706（22 aa）
Chain E 685–706（22 aa）
Chain F 685–706（22 aa）
Chain G 685–706（22 aa）
Chain H 685–706（22 aa）
Non-standard monomer：Yes (specific site not provided by mmCIF) Non-standard monomer：Yes (specific site not provided by mmCIF) Non-standard monomer：Yes (specific site not provided by mmCIF) Non-standard monomer：Yes (specific site not provided by mmCIF) Non-standard monomer：Yes (specific site not provided by mmCIF) Non-standard monomer：Yes (specific site not provided by mmCIF) Non-standard monomer：Yes (specific site not provided by mmCIF) Non-standard monomer：Yes (specific site not provided by mmCIF) HEZ HEXANE-1,6-DIOL × 7 X-RAY DIFFRACTION
X-ray crystallization conditions VAPOR DIFFUSION, HANGING DROP；pH 5；296.15 K；0.1 M sodium acetate (pH 5.0), 0.1 M CoCl2, 1.1 M 1,6-hexanediol
Resolution 2.30 Å R-free 0.218
6WXM X-ray crystallographic structure of a beta-hairpin peptide derived from amyloid beta 16-36 Deposited 2020-05-11 Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental conditions Different structure-quality metrics Assembly 2 Protein homooligomer Homooligomer；Protein × 4 PDB declaration: tetrameric
Chain I 685–706（22 aa）
Chain J 685–706（22 aa）
Non-standard monomer：Yes (specific site not provided by mmCIF) Non-standard monomer：Yes (specific site not provided by mmCIF) HEZ HEXANE-1,6-DIOL × 6 X-RAY DIFFRACTION
X-ray crystallization conditions VAPOR DIFFUSION, HANGING DROP；pH 5；296.15 K；0.1 M sodium acetate (pH 5.0), 0.1 M CoCl2, 1.1 M 1,6-hexanediol
Resolution 2.30 Å R-free 0.218
6WXM X-ray crystallographic structure of a beta-hairpin peptide derived from amyloid beta 16-36 Deposited 2020-05-11 Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental conditions Different structure-quality metrics Assembly 3 Protein homooligomer Homooligomer；Protein × 4 PDB declaration: tetrameric
Chain I 685–706（22 aa）
Chain J 685–706（22 aa）
Non-standard monomer：Yes (specific site not provided by mmCIF) Non-standard monomer：Yes (specific site not provided by mmCIF) HEZ HEXANE-1,6-DIOL × 6 X-RAY DIFFRACTION
X-ray crystallization conditions VAPOR DIFFUSION, HANGING DROP；pH 5；296.15 K；0.1 M sodium acetate (pH 5.0), 0.1 M CoCl2, 1.1 M 1,6-hexanediol
Resolution 2.30 Å R-free 0.218
6WXM X-ray crystallographic structure of a beta-hairpin peptide derived from amyloid beta 16-36 Deposited 2020-05-11 Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental conditions Different structure-quality metrics Assembly 4 Protein homooligomer Homooligomer；Protein × 2 PDB declaration: dimeric
Chain K 685–706（22 aa）
Non-standard monomer：Yes (specific site not provided by mmCIF) No recorded non-water small molecule X-RAY DIFFRACTION
X-ray crystallization conditions VAPOR DIFFUSION, HANGING DROP；pH 5；296.15 K；0.1 M sodium acetate (pH 5.0), 0.1 M CoCl2, 1.1 M 1,6-hexanediol
Resolution 2.30 Å R-free 0.218
6XOV CryoEM structure of human presequence protease in partial closed state 1 Deposited 2020-07-07 Different construct Different oligomeric state Different ligand/ion Different experimental method Different experimental conditions Different structure-quality metrics Assembly 1 Protein heterocomplex Heteromer；Protein × 3 PDB declaration: trimeric
Chain B 653–692（40 aa） Fragment：UNP residues 653-692
Not recorded No recorded non-water small molecule ELECTRON MICROSCOPY
cryo-EM buffer pH 7.7；20 mM Tris, pH 7.7, 150 mM NaCl, 10mM KCl, 20 mM EDTA and 1 mM 2-mercaptoethanol
cryo-EM vitrification conditions Cryogen ETHANE
Resolution 3.30 Å
6YHF Solution NMR Structure of APP TMD Deposited 2020-03-29 Different construct Different oligomeric state Different ligand/ion Different experimental method Different experimental conditions Different structure-quality metrics Assembly 1 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric
Chain A 697–726（30 aa） Fragment：Amyloid precursor protein transmembrane domain
Not recorded No recorded non-water small molecule SOLUTION NMR
NMR measurement conditions pH 7；298 K；Ionic strength (raw mmCIF value) 0；Pressure ambient
NMR sample composition 500 uM APP WT, 80% TFE-d2, 20% H2O | 80% TFE-d2, 20% H2O
Resolution not provided
6YHI Solution NMR Structure of APP G38L mutant TMD Deposited 2020-03-30 Different construct Different oligomeric state Different ligand/ion Different experimental method Different experimental conditions Different structure-quality metrics Assembly 1 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric
Chain A 697–726（30 aa） Fragment：Amyloid precursor protein transmembrane domain
Not recorded No recorded non-water small molecule SOLUTION NMR
NMR measurement conditions pH 7；298 K；Ionic strength (raw mmCIF value) 0；Pressure ambient
NMR sample composition 500 uM APP G38L, 80% TFE-d2, 20% H2O | 80% TFE-d2, 20% H2O
Resolution not provided
6YHO Solution NMR Structure of APP G38P mutant TM Deposited 2020-03-30 Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental method Different experimental conditions Different structure-quality metrics Assembly 1 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric
Chain A 697–726（30 aa） Fragment：Amyloid precursor protein transmembrane domain
Mutation：G38P No recorded non-water small molecule SOLUTION NMR
NMR measurement conditions pH 7；298 K；Ionic strength (raw mmCIF value) 0；Pressure ambient
NMR sample composition 500 uM APP G38P, 80% TFE-d2, 20% H2O | 80% TFE-d2, 20% H2O
Resolution not provided
6YHP Solution NMR Structure of APP V44M mutant TMD Deposited 2020-03-30 Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental method Different experimental conditions Different structure-quality metrics Assembly 1 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric
Chain A 697–726（30 aa） Fragment：Amyloid precursor protein transmembrane domain
Mutation：V44M No recorded non-water small molecule SOLUTION NMR
NMR measurement conditions pH 7；298 K；Ionic strength (raw mmCIF value) 0；Pressure ambient
NMR sample composition 500 uM APP V44M, 80% TFE-d2, 20% H2O | 80% TFE-d2, 20% H2O
Resolution not provided
6YHX Solution NMR Structure of APP I45T mutant TMD Deposited 2020-03-31 Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental method Different experimental conditions Different structure-quality metrics Assembly 1 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric
Chain A 697–726（30 aa） Fragment：Amyloid precursor protein transmembrane domain
Mutation：I45T No recorded non-water small molecule SOLUTION NMR
NMR measurement conditions pH 7；298 K；Ionic strength (raw mmCIF value) 0；Pressure ambient
NMR sample composition 500 uM APP I45T, 80% TFE-d2, 20% H2O | 80% TFE-d2, 20% H2O
Resolution not provided
7B3J Dynamic complex between all-D-enantiomeric peptide D3 with wild-type amyloid precursor protein 672-726 fragment (amyloid beta 1-55) Deposited 2020-12-01 Different construct Different ligand/ion Different experimental method Different experimental conditions Different structure-quality metrics Assembly 1 Protein heterocomplex Heteromer；Protein × 2 PDB declaration: dimeric
Chain A 579–633（55 aa）
Not recorded No recorded non-water small molecule SOLUTION NMR
NMR measurement conditions pH 6.9；303 K；Ionic strength (raw mmCIF value) 20；Pressure 1
NMR sample composition 0.2 mM [U-13C; U-15N] APP672-726, 90% H2O/10% D2O | 90% H2O/10% D2O
NMR sample composition 0.2 mM [U-13C; U-15N] APP672-726, 0.2 mM D3cys(MTSL), 90% H2O/10% D2O | 90% H2O/10% D2O
NMR sample composition 0.2 mM [U-13C; U-15N] APP672-726, 0.2 mM (MTSL)cysD3, 90% H2O/10% D2O | 90% H2O/10% D2O
Resolution not provided
7B3K Dynamic complex between all-D-enantiomeric peptide D3 with L723P mutant of amyloid precursor protein (APP) 672-726 fragment (amyloid beta 1-55) Deposited 2020-12-01 Different construct Different mutation/modification Different ligand/ion Different experimental method Different experimental conditions Different structure-quality metrics Assembly 1 Protein heterocomplex Heteromer；Protein × 2 PDB declaration: dimeric
Chain A 579–633（55 aa）
Mutation：V52P No recorded non-water small molecule SOLUTION NMR
NMR measurement conditions pH 6.9；303 K；Ionic strength (raw mmCIF value) 20；Pressure 1
NMR sample composition 0.2 mM [U-13C; U-15N] APP_L723P_672-726, 90% H2O/10% D2O | 90% H2O/10% D2O
NMR sample composition 0.2 mM [U-13C; U-15N] APP_L723P_672-726, 0.2 mM D3cys(MTSL), 90% H2O/10% D2O | 90% H2O/10% D2O
Resolution not provided
7JXN Beta hairpin derived from Abeta17-36 with an F20Cha mutation Deposited 2020-08-27 Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental conditions Different structure-quality metrics Assembly 1 Protein homooligomer Homooligomer；Protein × 2 PDB declaration: dimeric
Chain A 686–706（21 aa）
Chain D 686–706（21 aa）
Non-standard monomer：Yes (specific site not provided by mmCIF) Non-standard monomer：Yes (specific site not provided by mmCIF) CL CHLORIDE ION × 2 NA SODIUM ION × 1 X-RAY DIFFRACTION
X-ray crystallization conditions VAPOR DIFFUSION, HANGING DROP；297.15 K；Bis-Tris buffer, ammonium acetate, and methyl-2,4-pentanediol
Resolution 2.00 Å R-free 0.301
7JXN Beta hairpin derived from Abeta17-36 with an F20Cha mutation Deposited 2020-08-27 Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental conditions Different structure-quality metrics Assembly 2 Protein homooligomer Homooligomer；Protein × 2 PDB declaration: dimeric
Chain B 686–706（21 aa）
Chain C 686–706（21 aa）
Non-standard monomer：Yes (specific site not provided by mmCIF) Non-standard monomer：Yes (specific site not provided by mmCIF) No recorded non-water small molecule X-RAY DIFFRACTION
X-ray crystallization conditions VAPOR DIFFUSION, HANGING DROP；297.15 K；Bis-Tris buffer, ammonium acetate, and methyl-2,4-pentanediol
Resolution 2.00 Å R-free 0.301
7JXO Triangular trimer of beta-hairpins derived from Abeta17-36 with an F20Cha mutation Deposited 2020-08-27 Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental conditions Different structure-quality metrics Assembly 1 Protein homooligomer Homooligomer；Protein × 12 PDB declaration: dodecameric
Chain A 686–706（21 aa）
Chain B 686–706（21 aa）
Chain C 686–706（21 aa）
Non-standard monomer：Yes (specific site not provided by mmCIF) Non-standard monomer：Yes (specific site not provided by mmCIF) Non-standard monomer：Yes (specific site not provided by mmCIF) No recorded non-water small molecule X-RAY DIFFRACTION
X-ray crystallization conditions VAPOR DIFFUSION, HANGING DROP；297.15 K；Tris buffer, MgCl2, and 1,6-hexanediol
Resolution 2.81 Å R-free 0.320
7O1Q Amyloid beta oligomer displayed on the alpha hemolysin scaffold Deposited 2021-03-30 Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental method Different experimental conditions Different structure-quality metrics Assembly 1 Insufficient information Homooligomer；Protein × 7 PDB declaration: heptameric
Chain A 672–713（42 aa）
Chain B 672–713（42 aa）
Chain C 672–713（42 aa）
Chain D 672–713（42 aa）
Chain E 672–713（42 aa）
Chain F 672–713（42 aa）
Chain G 672–713（42 aa）
Not recorded No recorded non-water small molecule ELECTRON MICROSCOPY
cryo-EM buffer pH 8；50 mM Tris-HCl, pH 8.0, 500 mM NaCl, 250 mM imidazole and 0.38 mM DDM
cryo-EM vitrification conditions Cryogen ETHANE
Resolution 3.40 Å
7OW1 Crystal Structure of TAP01 in complex with amyloid beta peptide Deposited 2021-06-16 Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental conditions Different structure-quality metrics Assembly 1 Protein heterocomplex Heteromer；Protein × 3 PDB declaration: trimeric
Chain A 674–685（12 aa） Fragment：UNP residues 674-683
Non-standard monomer：Yes (specific site not provided by mmCIF) FLC CITRATE ANION × 1 X-RAY DIFFRACTION
X-ray crystallization conditions VAPOR DIFFUSION, HANGING DROP；292 K；20% PEG3350 0.2 M ammonium citrate
Resolution 1.40 Å R-free 0.200
7OXN Crystal Structure of TAP01 in complex with cyclised amyloid beta peptide Deposited 2021-06-22 Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental conditions Different structure-quality metrics Assembly 1 Protein heterocomplex Heteromer；Protein × 3 PDB declaration: trimeric
Chain A 672–685（14 aa）
Non-standard monomer：Yes (specific site not provided by mmCIF) EDO 1,2-ETHANEDIOL × 1 ZN ZINC ION × 1 X-RAY DIFFRACTION
X-ray crystallization conditions VAPOR DIFFUSION, HANGING DROP；pH 7；292 K；20% PEG 6K 0.1 M HEPES, pH 7.0 0.01 M zinc chloride
Resolution 2.50 Å R-free 0.265
7Q4B Type I beta-amyloid 42 Filaments from Human Brain Deposited 2021-10-30 Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental method Different experimental conditions Different structure-quality metrics Assembly 1 Protein homooligomer Homooligomer；Protein × 10 PDB declaration: decameric
Chain A 672–713（42 aa）
Chain B 672–713（42 aa）
Chain C 672–713（42 aa）
Chain D 672–713（42 aa）
Chain E 672–713（42 aa）
Chain F 672–713（42 aa）
Chain G 672–713（42 aa）
Chain H 672–713（42 aa）
Chain I 672–713（42 aa）
Chain R 672–713（42 aa）
Not recorded UNX UNKNOWN LIGAND × 10 ELECTRON MICROSCOPY
cryo-EM buffer pH 7.5
cryo-EM vitrification conditions Cryogen ETHANE
Resolution 2.50 Å
7Q4M Type II beta-amyloid 42 Filaments from Human Brain Deposited 2021-11-01 Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental method Different experimental conditions Different structure-quality metrics Assembly 1 Protein homooligomer Homooligomer；Protein × 10 PDB declaration: decameric
Chain A 672–713（42 aa）
Chain B 672–713（42 aa）
Chain C 672–713（42 aa）
Chain D 672–713（42 aa）
Chain E 672–713（42 aa）
Chain F 672–713（42 aa）
Chain G 672–713（42 aa）
Chain H 672–713（42 aa）
Chain I 672–713（42 aa）
Chain J 672–713（42 aa）
Not recorded UNX UNKNOWN LIGAND × 10 ELECTRON MICROSCOPY
cryo-EM buffer pH 7.5
cryo-EM vitrification conditions Cryogen ETHANE
Resolution 2.80 Å
7RTZ X-ray crystallographic structure of a beta-hairpin peptide derived from amyloid beta 14-40 Deposited 2021-08-16 Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental conditions Different structure-quality metrics Assembly 1 Protein homooligomer Homooligomer；Protein × 2 PDB declaration: dimeric
Chain A 682–711（30 aa）
Chain B 682–711（30 aa）
Non-standard monomer：Yes (specific site not provided by mmCIF) Non-standard monomer：Yes (specific site not provided by mmCIF) CL CHLORIDE ION × 1 X-RAY DIFFRACTION
X-ray crystallization conditions VAPOR DIFFUSION, HANGING DROP；296.15 K；0.2 M magnesium acetate tetrahydrate, 0.1 M sodium cacodylate trihydrate pH 6.5, and 30% (v/v) 2-methyl-2,4-pentanediol
Resolution 2.10 Å R-free 0.293
7U4P Covalently stabilized triangular trimer composed of Abeta17-36 beta-hairpins Deposited 2022-02-28 Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental conditions Different structure-quality metrics Assembly 1 Protein homooligomer Homooligomer；Protein × 12 PDB declaration: dodecameric
Chain A 687–707（21 aa）
Chain B 687–707（21 aa）
Chain C 687–707（21 aa）
Non-standard monomer：Yes (specific site not provided by mmCIF) Non-standard monomer：Yes (specific site not provided by mmCIF) Non-standard monomer：Yes (specific site not provided by mmCIF) No recorded non-water small molecule X-RAY DIFFRACTION
X-ray crystallization conditions VAPOR DIFFUSION, HANGING DROP；298.15 K；0.1 M Tris at pH 8.3, 0.2 M MgCl2, 2.8 M 1,6-hexanediol
Resolution 1.80 Å R-free 0.247
7Y8Q Amyloid-beta assemblage on GM1-containing membranes Deposited 2022-06-24 Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental method Different experimental conditions Different structure-quality metrics Assembly 1 Protein homooligomer Homooligomer；Protein × 8 PDB declaration: octameric
Chain A 672–711（40 aa）
Chain B 672–711（40 aa）
Chain C 672–711（40 aa）
Chain D 672–711（40 aa）
Chain E 672–711（40 aa）
Chain F 672–711（40 aa）
Chain G 672–711（40 aa）
Chain H 672–711（40 aa）
Not recorded No recorded non-water small molecule SOLID-STATE NMR
NMR measurement conditions pH 7.4；288 K；Ionic strength (raw mmCIF value) 5；Pressure 1
NMR sample composition 1 mM [U-13C; U-15N] Amyloid beta(1-40), 8 mM GM1, 2 mM DMPC, none | none
Resolution not provided
8AZS Type I amyloid-beta 42 filaments from high-spin supernatants of aqueous extracts from Alzheimer's disease brains | ABeta42 Deposited 2022-09-06 Different construct Different oligomeric state Different ligand/ion Different experimental method Different experimental conditions Different structure-quality metrics Assembly 1 Protein homooligomer Homooligomer；Protein × 6 PDB declaration: hexameric
Chain H 672–713（42 aa）
Not recorded No recorded non-water small molecule ELECTRON MICROSCOPY
cryo-EM buffer pH 7.5
cryo-EM vitrification conditions Cryogen ETHANE
Resolution 2.90 Å
8AZT Type II amyloid-beta 42 filaments from high-spin supernatants of aqueous extracts from Alzheimer's disease brains | ABeta42 Deposited 2022-09-06 Different construct Different oligomeric state Different ligand/ion Different experimental method Different experimental conditions Different structure-quality metrics Assembly 1 Protein homooligomer Homooligomer；Protein × 6 PDB declaration: hexameric
Chain B 672–713（42 aa）
Not recorded No recorded non-water small molecule ELECTRON MICROSCOPY
cryo-EM buffer pH 7.5
cryo-EM vitrification conditions Cryogen ETHANE
Resolution 3.70 Å
8BFA Sarkosyl-extracted AppNL-G-F Abeta42 fibril structure Deposited 2022-10-24 Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental method Different experimental conditions Different structure-quality metrics Assembly 1 Protein homooligomer Homooligomer；Protein × 10 PDB declaration: decameric
Chain A 672–713（42 aa）
Chain B 672–713（42 aa）
Chain C 672–713（42 aa）
Chain D 672–713（42 aa）
Chain E 672–713（42 aa）
Chain F 672–713（42 aa）
Chain G 672–713（42 aa）
Chain H 672–713（42 aa）
Chain I 672–713（42 aa）
Chain J 672–713（42 aa）
Not recorded No recorded non-water small molecule ELECTRON MICROSCOPY
cryo-EM buffer pH 7.4
cryo-EM vitrification conditions Cryogen ETHANE；6s blot
Resolution 3.00 Å
8BFB Sarkosyl-extracted AppNL-G-F Abeta42 fibril structure (Methoxy-X04-labelled mice) Deposited 2022-10-24 Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental method Different experimental conditions Different structure-quality metrics Assembly 1 Protein homooligomer Homooligomer；Protein × 10 PDB declaration: decameric
Chain A 672–713（42 aa）
Chain B 672–713（42 aa）
Chain C 672–713（42 aa）
Chain D 672–713（42 aa）
Chain E 672–713（42 aa）
Chain F 672–713（42 aa）
Chain G 672–713（42 aa）
Chain H 672–713（42 aa）
Chain I 672–713（42 aa）
Chain J 672–713（42 aa）
Not recorded No recorded non-water small molecule ELECTRON MICROSCOPY
cryo-EM buffer pH 7.4
cryo-EM vitrification conditions Cryogen ETHANE；6s blot
Resolution 3.20 Å
8BFZ Amyloid-beta 42 filaments extracted from the human brain with Arctic mutation (E22G) of Alzheimer's disease | ABeta42 Deposited 2022-10-27 Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental method Different experimental conditions Different structure-quality metrics Assembly 1 Protein homooligomer Homooligomer；Protein × 6 PDB declaration: hexameric
Chain A 672–713（42 aa）
Chain B 672–713（42 aa）
Not recorded No recorded non-water small molecule ELECTRON MICROSCOPY
cryo-EM buffer pH 7.5
cryo-EM vitrification conditions Cryogen ETHANE
Resolution 2.80 Å
8BG0 Amyloid-beta tetrameric filaments with the Arctic mutation (E22G) from Alzheimer's disease brains | ABeta40 Deposited 2022-10-27 Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental method Different experimental conditions Different structure-quality metrics Assembly 1 Protein homooligomer Homooligomer；Protein × 12 PDB declaration: dodecameric
Chain A 616–655（40 aa）
Chain B 616–655（40 aa）
Chain C 616–655（40 aa）
Chain D 616–655（40 aa）
Not recorded No recorded non-water small molecule ELECTRON MICROSCOPY
cryo-EM buffer pH 7.5
cryo-EM vitrification conditions Cryogen ETHANE
Resolution 1.99 Å
8C3H Cereblon isoform 4 from Magnetospirillum gryphiswaldense in complex a long aspartimide degron peptide Deposited 2022-12-23 Different construct Different mutation/modification Different ligand/ion Different experimental conditions Different structure-quality metrics Assembly 1 Protein heterocomplex Heteromer；Protein × 2 PDB declaration: dimeric
Chain D 763–770（8 aa）
Non-standard monomer：Yes (specific site not provided by mmCIF) ZN ZINC ION × 1 X-RAY DIFFRACTION
X-ray crystallization conditions VAPOR DIFFUSION；274 K；0.5 M (NH4)H2PO4
Resolution 1.71 Å R-free 0.210
8C3H Cereblon isoform 4 from Magnetospirillum gryphiswaldense in complex a long aspartimide degron peptide Deposited 2022-12-23 Different construct Different mutation/modification Different ligand/ion Different experimental conditions Different structure-quality metrics Assembly 2 Protein heterocomplex Heteromer；Protein × 2 PDB declaration: dimeric
Chain E 763–770（8 aa）
Non-standard monomer：Yes (specific site not provided by mmCIF) ZN ZINC ION × 1 X-RAY DIFFRACTION
X-ray crystallization conditions VAPOR DIFFUSION；274 K；0.5 M (NH4)H2PO4
Resolution 1.71 Å R-free 0.210
8EZD Brain-derived 42-residue amyloid-beta fibril type A Deposited 2022-10-31 Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental method Different experimental conditions Different structure-quality metrics Assembly 1 Protein homooligomer Homooligomer；Protein × 8 PDB declaration: octameric
Chain A 672–713（42 aa） Fragment：residues 672-713
Chain B 672–713（42 aa） Fragment：residues 672-713
Chain C 672–713（42 aa） Fragment：residues 672-713
Chain D 672–713（42 aa） Fragment：residues 672-713
Chain E 672–713（42 aa） Fragment：residues 672-713
Chain F 672–713（42 aa） Fragment：residues 672-713
Chain G 672–713（42 aa） Fragment：residues 672-713
Chain H 672–713（42 aa） Fragment：residues 672-713
Not recorded No recorded non-water small molecule ELECTRON MICROSCOPY
cryo-EM buffer pH 7.4；10mM Na-phosphate, 0.1% sodium azide
cryo-EM vitrification conditions Cryogen ETHANE；Preblot for 12-13 seconds and blot for 2.5-3.0 seconds before plunging
Resolution 2.83 Å
8EZE Brain-derived 42-residue amyloid-beta fibril type B Deposited 2022-10-31 Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental method Different experimental conditions Different structure-quality metrics Assembly 1 Protein homooligomer Homooligomer；Protein × 8 PDB declaration: octameric
Chain A 672–713（42 aa） Fragment：residues 672-713
Chain B 672–713（42 aa） Fragment：residues 672-713
Chain C 672–713（42 aa） Fragment：residues 672-713
Chain D 672–713（42 aa） Fragment：residues 672-713
Chain E 672–713（42 aa） Fragment：residues 672-713
Chain F 672–713（42 aa） Fragment：residues 672-713
Chain G 672–713（42 aa） Fragment：residues 672-713
Chain H 672–713（42 aa） Fragment：residues 672-713
Not recorded No recorded non-water small molecule ELECTRON MICROSCOPY
cryo-EM buffer pH 7.4；10mM Na-phosphate, 0.1% sodium azide
cryo-EM vitrification conditions Cryogen ETHANE；Preblot for 12-13 seconds and blot for 2.5-3.0 seconds before plunging
Resolution 2.76 Å
8FF2 Amyloid-beta (1-40) fibrils derived from a CAA patient Deposited 2022-12-07 Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental method Different experimental conditions Different structure-quality metrics Assembly 1 Protein homooligomer Homooligomer；Protein × 10 PDB declaration: decameric
Chain A 653–692（40 aa） Fragment：UNP residues 653-692
Chain B 653–692（40 aa） Fragment：UNP residues 653-692
Chain C 653–692（40 aa） Fragment：UNP residues 653-692
Chain D 653–692（40 aa） Fragment：UNP residues 653-692
Chain E 653–692（40 aa） Fragment：UNP residues 653-692
Chain F 653–692（40 aa） Fragment：UNP residues 653-692
Chain G 653–692（40 aa） Fragment：UNP residues 653-692
Chain I 653–692（40 aa） Fragment：UNP residues 653-692
Chain J 653–692（40 aa） Fragment：UNP residues 653-692
Chain K 653–692（40 aa） Fragment：UNP residues 653-692
Not recorded No recorded non-water small molecule ELECTRON MICROSCOPY
cryo-EM buffer pH 7.4
cryo-EM vitrification conditions Cryogen ETHANE
Resolution 2.87 Å
8FF3 Amyloid-beta (1-40) fibrils derived from familial Dutch-type CAA patient (population B) Deposited 2022-12-07 Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental method Different experimental conditions Different structure-quality metrics Assembly 1 Protein homooligomer Homooligomer；Protein × 6 PDB declaration: hexameric
Chain A 653–692（40 aa） Fragment：UNP residues 653-692
Chain B 653–692（40 aa） Fragment：UNP residues 653-692
Chain C 653–692（40 aa） Fragment：UNP residues 653-692
Chain a 653–692（40 aa） Fragment：UNP residues 653-692
Chain b 653–692（40 aa） Fragment：UNP residues 653-692
Chain c 653–692（40 aa） Fragment：UNP residues 653-692
Not recorded No recorded non-water small molecule ELECTRON MICROSCOPY
cryo-EM buffer pH 7.4
cryo-EM vitrification conditions Cryogen ETHANE
Resolution 3.09 Å
8KEW The cryo-EM structure of type1 amyloid beta 42 fibril. Deposited 2023-08-13 Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental method Different experimental conditions Different structure-quality metrics Assembly 1 Protein homooligomer Homooligomer；Protein × 6 PDB declaration: hexameric
Chain A 1–770（770 aa）
Chain B 1–770（770 aa）
Chain C 1–770（770 aa）
Chain D 1–770（770 aa）
Chain F 1–770（770 aa）
Chain G 1–770（770 aa）
Not recorded No recorded non-water small molecule ELECTRON MICROSCOPY
cryo-EM buffer pH 7.5
cryo-EM vitrification conditions Cryogen ETHANE
Resolution 3.30 Å
8KF1 The cryo-EM structure of AV-45 bound type1 amyloid beta 42 fibril. Deposited 2023-08-15 Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental method Different experimental conditions Different structure-quality metrics Assembly 1 Protein homooligomer Homooligomer；Protein × 12 PDB declaration: 12-meric
Chain A 1–770（770 aa）
Chain B 1–770（770 aa）
Chain C 1–770（770 aa）
Chain D 1–770（770 aa）
Chain E 1–770（770 aa）
Chain F 1–770（770 aa）
Chain G 1–770（770 aa）
Chain H 1–770（770 aa）
Chain I 1–770（770 aa）
Chain J 1–770（770 aa）
Chain K 1–770（770 aa）
Chain L 1–770（770 aa）
Not recorded VW6 4-[2-[6-[2-[2-(2-fluoranylethoxy)ethoxy]ethoxy]pyridin-3-yl]ethyl]-~{N}-methyl-aniline × 2 ELECTRON MICROSCOPY
cryo-EM buffer pH 7.5
cryo-EM vitrification conditions Cryogen ETHANE
Resolution 3.30 Å
8KF3 The cryo-EM structure of type3 amyloid beta 42 fibril. Deposited 2023-08-15 Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental method Different experimental conditions Different structure-quality metrics Assembly 1 Protein homooligomer Homooligomer；Protein × 9 PDB declaration: nonameric
Chain A 1–770（770 aa）
Chain B 1–770（770 aa）
Chain C 1–770（770 aa）
Chain D 1–770（770 aa）
Chain E 1–770（770 aa）
Chain F 1–770（770 aa）
Chain G 1–770（770 aa）
Chain H 1–770（770 aa）
Chain I 1–770（770 aa）
Not recorded No recorded non-water small molecule ELECTRON MICROSCOPY
cryo-EM buffer pH 7.5
cryo-EM vitrification conditions Cryogen ETHANE
Resolution 3.50 Å
8KF4 The cryo-EM structure of type1 amyloid beta 42 fibril in AD2 patient. Deposited 2023-08-15 Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental method Different experimental conditions Different structure-quality metrics Assembly 1 Protein homooligomer Homooligomer；Protein × 6 PDB declaration: hexameric
Chain A 1–770（770 aa）
Chain B 1–770（770 aa）
Chain C 1–770（770 aa）
Chain D 1–770（770 aa）
Chain E 1–770（770 aa）
Chain F 1–770（770 aa）
Not recorded No recorded non-water small molecule ELECTRON MICROSCOPY
cryo-EM buffer pH 7.5
cryo-EM vitrification conditions Cryogen ETHANE
Resolution 3.00 Å
8KF5 The cryo-EM structure of type1 amyloid beta 42 fibril in AD3. Deposited 2023-08-15 Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental method Different experimental conditions Different structure-quality metrics Assembly 1 Protein homooligomer Homooligomer；Protein × 6 PDB declaration: hexameric
Chain A 1–770（770 aa）
Chain B 1–770（770 aa）
Chain C 1–770（770 aa）
Chain D 1–770（770 aa）
Chain E 1–770（770 aa）
Chain F 1–770（770 aa）
Not recorded No recorded non-water small molecule ELECTRON MICROSCOPY
cryo-EM buffer pH 7.5
cryo-EM vitrification conditions Cryogen ETHANE
Resolution 3.40 Å
8KF6 The cryo-EM structure of AV-45 bound type3 amyloid beta 42 fibril. Deposited 2023-08-15 Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental method Different experimental conditions Different structure-quality metrics Assembly 1 Protein homooligomer Homooligomer；Protein × 9 PDB declaration: nonameric
Chain A 1–770（770 aa）
Chain B 1–770（770 aa）
Chain C 1–770（770 aa）
Chain D 1–770（770 aa）
Chain E 1–770（770 aa）
Chain F 1–770（770 aa）
Chain G 1–770（770 aa）
Chain H 1–770（770 aa）
Chain I 1–770（770 aa）
Not recorded No recorded non-water small molecule ELECTRON MICROSCOPY
cryo-EM buffer pH 7.5
cryo-EM vitrification conditions Cryogen ETHANE
Resolution 3.70 Å
8OL2 Murine type II Abeta fibril from APP23 mouse Deposited 2023-03-30 Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental method Different experimental conditions Different structure-quality metrics Assembly 1 Protein homooligomer Homooligomer；Protein × 10 PDB declaration: decameric
Chain A 672–713（42 aa）
Chain B 672–713（42 aa）
Chain C 672–713（42 aa）
Chain D 672–713（42 aa）
Chain E 672–713（42 aa）
Chain F 672–713（42 aa）
Chain G 672–713（42 aa）
Chain H 672–713（42 aa）
Chain I 672–713（42 aa）
Chain J 672–713（42 aa）
Not recorded No recorded non-water small molecule ELECTRON MICROSCOPY
cryo-EM buffer pH 7.4
cryo-EM vitrification conditions Cryogen ETHANE
Resolution 3.00 Å
8OL3 Murine type III Abeta fibril from APP/PS1 mouse Deposited 2023-03-30 Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental method Different experimental conditions Different structure-quality metrics Assembly 1 Protein homooligomer Homooligomer；Protein × 10 PDB declaration: decameric
Chain A 672–713（42 aa）
Chain B 672–713（42 aa）
Chain C 672–713（42 aa）
Chain D 672–713（42 aa）
Chain E 672–713（42 aa）
Chain F 672–713（42 aa）
Chain G 672–713（42 aa）
Chain H 672–713（42 aa）
Chain I 672–713（42 aa）
Chain J 672–713（42 aa）
Not recorded No recorded non-water small molecule ELECTRON MICROSCOPY
cryo-EM buffer pH 7.4
cryo-EM vitrification conditions Cryogen ETHANE
Resolution 3.50 Å
8OL5 Murine type II Abeta fibril from ARTE10 mouse Deposited 2023-03-30 Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental method Different experimental conditions Different structure-quality metrics Assembly 1 Protein homooligomer Homooligomer；Protein × 10 PDB declaration: decameric
Chain A 672–713（42 aa）
Chain B 672–713（42 aa）
Chain C 672–713（42 aa）
Chain D 672–713（42 aa）
Chain E 672–713（42 aa）
Chain F 672–713（42 aa）
Chain G 672–713（42 aa）
Chain H 672–713（42 aa）
Chain I 672–713（42 aa）
Chain J 672–713（42 aa）
Not recorded No recorded non-water small molecule ELECTRON MICROSCOPY
cryo-EM buffer pH 7.4
cryo-EM vitrification conditions Cryogen ETHANE
Resolution 3.40 Å
8OL6 Murine type II Abeta fibril from tgAPPSwe mouse Deposited 2023-03-30 Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental method Different experimental conditions Different structure-quality metrics Assembly 1 Protein homooligomer Homooligomer；Protein × 10 PDB declaration: decameric
Chain A 672–713（42 aa）
Chain B 672–713（42 aa）
Chain C 672–713（42 aa）
Chain D 672–713（42 aa）
Chain E 672–713（42 aa）
Chain F 672–713（42 aa）
Chain G 672–713（42 aa）
Chain H 672–713（42 aa）
Chain I 672–713（42 aa）
Chain J 672–713（42 aa）
Not recorded No recorded non-water small molecule ELECTRON MICROSCOPY
cryo-EM buffer pH 7.4
cryo-EM vitrification conditions Cryogen ETHANE
Resolution 3.80 Å
8OL7 MurineArc type I Abeta fibril from tg-APPArcSwe mouse Deposited 2023-03-30 Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental method Different experimental conditions Different structure-quality metrics Assembly 1 Protein homooligomer Homooligomer；Protein × 10 PDB declaration: decameric
Chain A 672–713（42 aa）
Chain B 672–713（42 aa）
Chain C 672–713（42 aa）
Chain D 672–713（42 aa）
Chain E 672–713（42 aa）
Chain F 672–713（42 aa）
Chain G 672–713（42 aa）
Chain H 672–713（42 aa）
Chain I 672–713（42 aa）
Chain J 672–713（42 aa）
Not recorded No recorded non-water small molecule ELECTRON MICROSCOPY
cryo-EM buffer pH 7.4
cryo-EM vitrification conditions Cryogen ETHANE
Resolution 3.00 Å
8OLG DI2 Abeta fibril from tg-SwDI mouse Deposited 2023-03-30 Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental method Different experimental conditions Different structure-quality metrics Assembly 1 Protein homooligomer Homooligomer；Protein × 5 PDB declaration: pentameric
Chain A 672–713（42 aa）
Chain B 672–713（42 aa）
Chain C 672–713（42 aa）
Chain D 672–713（42 aa）
Chain E 672–713（42 aa）
Not recorded No recorded non-water small molecule ELECTRON MICROSCOPY
cryo-EM buffer pH 7.4
cryo-EM vitrification conditions Cryogen ETHANE
Resolution 4.20 Å
8OLN DI1 Abeta fibril from tg-SwDI mouse Deposited 2023-03-30 Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental method Different experimental conditions Different structure-quality metrics Assembly 1 Protein homooligomer Homooligomer；Protein × 10 PDB declaration: decameric
Chain A 672–713（42 aa）
Chain B 672–713（42 aa）
Chain C 672–713（42 aa）
Chain D 672–713（42 aa）
Chain E 672–713（42 aa）
Chain F 672–713（42 aa）
Chain G 672–713（42 aa）
Chain H 672–713（42 aa）
Chain I 672–713（42 aa）
Chain J 672–713（42 aa）
Not recorded No recorded non-water small molecule ELECTRON MICROSCOPY
cryo-EM buffer pH 7.4
cryo-EM vitrification conditions Cryogen ETHANE
Resolution 3.30 Å
8OLO Murine type III Abeta fibril from ARTE10 mouse Deposited 2023-03-30 Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental method Different experimental conditions Different structure-quality metrics Assembly 1 Protein homooligomer Homooligomer；Protein × 10 PDB declaration: decameric
Chain A 672–713（42 aa）
Chain B 672–713（42 aa）
Chain C 672–713（42 aa）
Chain D 672–713（42 aa）
Chain E 672–713（42 aa）
Chain F 672–713（42 aa）
Chain G 672–713（42 aa）
Chain H 672–713（42 aa）
Chain I 672–713（42 aa）
Chain J 672–713（42 aa）
Not recorded No recorded non-water small molecule ELECTRON MICROSCOPY
cryo-EM buffer pH 7.4
cryo-EM vitrification conditions Cryogen ETHANE
Resolution 3.50 Å
8OLQ DI3 Abeta fibril from tg-SwDI mouse Deposited 2023-03-30 Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental method Different experimental conditions Different structure-quality metrics Assembly 1 Protein homooligomer Homooligomer；Protein × 5 PDB declaration: pentameric
Chain A 672–713（42 aa）
Chain B 672–713（42 aa）
Chain C 672–713（42 aa）
Chain D 672–713（42 aa）
Chain E 672–713（42 aa）
Not recorded No recorded non-water small molecule ELECTRON MICROSCOPY
cryo-EM buffer pH 7.4
cryo-EM vitrification conditions Cryogen ETHANE
Resolution 4.00 Å
8OTF Ab typeII filament from Guam ALS/PDC Deposited 2023-04-20 Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental method Different experimental conditions Different structure-quality metrics Assembly 1 Protein homooligomer Homooligomer；Protein × 6 PDB declaration: hexameric
Chain A 1–770（770 aa）
Chain B 1–770（770 aa）
Chain C 1–770（770 aa）
Chain D 1–770（770 aa）
Chain E 1–770（770 aa）
Chain F 1–770（770 aa）
Not recorded No recorded non-water small molecule ELECTRON MICROSCOPY
cryo-EM buffer pH 7.4
cryo-EM vitrification conditions Cryogen ETHANE
Resolution 3.30 Å
8SEJ Type I beta-amyloid 42 Filaments from Down syndrome Deposited 2023-04-10 Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental method Different experimental conditions Different structure-quality metrics Assembly 1 Protein homooligomer Homooligomer；Protein × 10 PDB declaration: decameric
Chain A 680–713（34 aa）
Chain B 680–713（34 aa）
Chain C 680–713（34 aa）
Chain D 680–713（34 aa）
Chain E 680–713（34 aa）
Chain F 680–713（34 aa）
Chain G 680–713（34 aa）
Chain H 680–713（34 aa）
Chain I 680–713（34 aa）
Chain J 680–713（34 aa）
Not recorded No recorded non-water small molecule ELECTRON MICROSCOPY
cryo-EM buffer pH 7.2
cryo-EM vitrification conditions Cryogen ETHANE
Resolution 3.17 Å
8SEK Type IIIa beta-amyloid 40 Filaments from Down syndrome Deposited 2023-04-10 Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental method Different experimental conditions Different structure-quality metrics Assembly 1 Protein homooligomer Homooligomer；Protein × 10 PDB declaration: decameric
Chain A 672–711（40 aa）
Chain B 672–711（40 aa）
Chain C 672–711（40 aa）
Chain D 672–711（40 aa）
Chain E 672–711（40 aa）
Chain F 672–711（40 aa）
Chain G 672–711（40 aa）
Chain H 672–711（40 aa）
Chain I 672–711（40 aa）
Chain J 672–711（40 aa）
Not recorded No recorded non-water small molecule ELECTRON MICROSCOPY
cryo-EM buffer pH 7.4
cryo-EM vitrification conditions Cryogen ETHANE
Resolution 3.50 Å
8SEL Type IIIb beta-amyloid 40 Filaments from Down Syndrome Deposited 2023-04-10 Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental method Different experimental conditions Different structure-quality metrics Assembly 1 Protein homooligomer Homooligomer；Protein × 20 PDB declaration: eicosameric
Chain A 672–711（40 aa）
Chain B 672–711（40 aa）
Chain C 672–711（40 aa）
Chain D 672–711（40 aa）
Chain E 672–711（40 aa）
Chain F 672–711（40 aa）
Chain G 672–711（40 aa）
Chain H 672–711（40 aa）
Chain I 672–711（40 aa）
Chain J 672–711（40 aa）
Chain K 672–711（40 aa）
Chain L 672–711（40 aa）
Chain M 672–711（40 aa）
Chain N 672–711（40 aa）
Chain O 672–711（40 aa）
Chain P 672–711（40 aa）
Chain Q 672–711（40 aa）
Chain R 672–711（40 aa）
Chain S 672–711（40 aa）
Chain T 672–711（40 aa）
Not recorded No recorded non-water small molecule ELECTRON MICROSCOPY
cryo-EM buffer pH 7.4
cryo-EM vitrification conditions Cryogen ETHANE
Resolution 3.80 Å
8X52 Cryo-EM structure of human gamma-secretase in complex with Abeta49 Deposited 2023-11-16 Different construct Different oligomeric state Different ligand/ion Different experimental method Different experimental conditions Different structure-quality metrics Assembly 1 Other combination Heteromer；Protein × 5 PDB declaration: pentameric
Chain E 540–639（100 aa）
Not recorded NAG 2-acetamido-2-deoxy-beta-D-glucopyranose × 6 PC1 1,2-DIACYL-SN-GLYCERO-3-PHOSPHOCHOLINE × 2 CLR CHOLESTEROL × 2 ELECTRON MICROSCOPY
cryo-EM buffer pH 7.4
cryo-EM vitrification conditions Cryogen ETHANE
Resolution 2.90 Å
8X53 Cryo-EM structure of human gamma-secretase in complex with Abeta46 Deposited 2023-11-16 Different construct Different oligomeric state Different ligand/ion Different experimental method Different experimental conditions Different structure-quality metrics Assembly 1 Other combination Heteromer；Protein × 5 PDB declaration: pentameric
Chain E 541–586（46 aa）
Not recorded NAG 2-acetamido-2-deoxy-beta-D-glucopyranose × 6 PC1 1,2-DIACYL-SN-GLYCERO-3-PHOSPHOCHOLINE × 3 CLR CHOLESTEROL × 2 ELECTRON MICROSCOPY
cryo-EM buffer pH 7.4
cryo-EM vitrification conditions Cryogen ETHANE
Resolution 3.00 Å
8X54 Cryo-EM structure of human gamma-secretase in complex with APP-C99 Deposited 2023-11-16 Different construct Different oligomeric state Different ligand/ion Different experimental method Different experimental conditions Different structure-quality metrics Assembly 1 Other combination Heteromer；Protein × 5 PDB declaration: pentameric
Chain E 540–639（100 aa）
Not recorded NAG 2-acetamido-2-deoxy-beta-D-glucopyranose × 6 PC1 1,2-DIACYL-SN-GLYCERO-3-PHOSPHOCHOLINE × 3 CLR CHOLESTEROL × 3 ELECTRON MICROSCOPY
cryo-EM buffer pH 7.4
cryo-EM vitrification conditions Cryogen ETHANE
Resolution 2.90 Å
8Z9V Amyloid beta and TTR Deposited 2024-04-23 Different construct Different oligomeric state Different ligand/ion Different experimental method Different experimental conditions Different structure-quality metrics Assembly 1 Protein heterocomplex Heteromer；Protein × 3 PDB declaration: trimeric
Chain e 678–713（36 aa）
Not recorded No recorded non-water small molecule ELECTRON MICROSCOPY
cryo-EM buffer pH 7.82
cryo-EM vitrification conditions Cryogen NITROGEN
Resolution 7.84 Å
9CK6 Cryo-EM structure of sarkosyl insoluble amyloid-beta 42 filaments extracted from human brain tissue Deposited 2024-07-08 Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental method Different experimental conditions Different structure-quality metrics Assembly 1 Protein homooligomer Homooligomer；Protein × 10 PDB declaration: decameric
Chain A 672–713（42 aa） Fragment：UNP residues 672-713
Chain B 672–713（42 aa） Fragment：UNP residues 672-713
Chain C 672–713（42 aa） Fragment：UNP residues 672-713
Chain D 672–713（42 aa） Fragment：UNP residues 672-713
Chain E 672–713（42 aa） Fragment：UNP residues 672-713
Chain F 672–713（42 aa） Fragment：UNP residues 672-713
Chain G 672–713（42 aa） Fragment：UNP residues 672-713
Chain H 672–713（42 aa） Fragment：UNP residues 672-713
Chain I 672–713（42 aa） Fragment：UNP residues 672-713
Chain R 672–713（42 aa） Fragment：UNP residues 672-713
Not recorded No recorded non-water small molecule ELECTRON MICROSCOPY
cryo-EM buffer pH 7.4
cryo-EM vitrification conditions Cryogen NITROGEN
Resolution 3.00 Å
9CKI Cryo-EM structure of the poly(4-styrenesulfonic acid-co-maleic acid) [PSCMA]-extractable amyloid-beta 42 oligomer from human brain tissue (Conformation 2) Deposited 2024-07-09 Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental method Different experimental conditions Different structure-quality metrics Assembly 1 Protein homooligomer Homooligomer；Protein × 10 PDB declaration: decameric
Chain A 672–713（42 aa） Fragment：UNP residues 672-713
Chain B 672–713（42 aa） Fragment：UNP residues 672-713
Chain C 672–713（42 aa） Fragment：UNP residues 672-713
Chain D 672–713（42 aa） Fragment：UNP residues 672-713
Chain E 672–713（42 aa） Fragment：UNP residues 672-713
Chain F 672–713（42 aa） Fragment：UNP residues 672-713
Chain G 672–713（42 aa） Fragment：UNP residues 672-713
Chain H 672–713（42 aa） Fragment：UNP residues 672-713
Chain I 672–713（42 aa） Fragment：UNP residues 672-713
Chain J 672–713（42 aa） Fragment：UNP residues 672-713
Not recorded No recorded non-water small molecule ELECTRON MICROSCOPY
cryo-EM buffer pH 7.4
cryo-EM vitrification conditions Cryogen NITROGEN
Resolution 3.10 Å
9CO4 Cryo-EM structure of the receptor-bound amyloid-beta 42 oligomer from human brain tissue (Conformation 1) Deposited 2024-07-16 Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental method Different experimental conditions Different structure-quality metrics Assembly 1 Protein homooligomer Homooligomer；Protein × 10 PDB declaration: decameric
Chain A 672–713（42 aa） Fragment：UNP residues 672-713
Chain B 672–713（42 aa） Fragment：UNP residues 672-713
Chain C 672–713（42 aa） Fragment：UNP residues 672-713
Chain D 672–713（42 aa） Fragment：UNP residues 672-713
Chain E 672–713（42 aa） Fragment：UNP residues 672-713
Chain F 672–713（42 aa） Fragment：UNP residues 672-713
Chain G 672–713（42 aa） Fragment：UNP residues 672-713
Chain H 672–713（42 aa） Fragment：UNP residues 672-713
Chain I 672–713（42 aa） Fragment：UNP residues 672-713
Chain J 672–713（42 aa） Fragment：UNP residues 672-713
Not recorded No recorded non-water small molecule ELECTRON MICROSCOPY
cryo-EM buffer pH 7.4
cryo-EM vitrification conditions Cryogen NITROGEN
Resolution 2.80 Å
9CZN Type Ic amyloid-beta 42 filaments in dominantly inherited Alzheimer disease with cotton wool plaques Deposited 2024-08-05 Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental method Different experimental conditions Different structure-quality metrics Assembly 1 Protein homooligomer Homooligomer；Protein × 20 PDB declaration: eicosameric
Chain A 680–713（34 aa） Fragment：UNP residues 680-713
Chain B 680–713（34 aa） Fragment：UNP residues 680-713
Chain C 680–713（34 aa） Fragment：UNP residues 680-713
Chain D 680–713（34 aa） Fragment：UNP residues 680-713
Chain E 680–713（34 aa） Fragment：UNP residues 680-713
Chain F 680–713（34 aa） Fragment：UNP residues 680-713
Chain G 680–713（34 aa） Fragment：UNP residues 680-713
Chain H 680–713（34 aa） Fragment：UNP residues 680-713
Chain I 680–713（34 aa） Fragment：UNP residues 680-713
Chain J 680–713（34 aa） Fragment：UNP residues 680-713
Chain K 680–713（34 aa） Fragment：UNP residues 680-713
Chain L 680–713（34 aa） Fragment：UNP residues 680-713
Chain M 680–713（34 aa） Fragment：UNP residues 680-713
Chain N 680–713（34 aa） Fragment：UNP residues 680-713
Chain O 680–713（34 aa） Fragment：UNP residues 680-713
Chain P 680–713（34 aa） Fragment：UNP residues 680-713
Chain Q 680–713（34 aa） Fragment：UNP residues 680-713
Chain R 680–713（34 aa） Fragment：UNP residues 680-713
Chain S 680–713（34 aa） Fragment：UNP residues 680-713
Chain T 680–713（34 aa） Fragment：UNP residues 680-713
Not recorded No recorded non-water small molecule ELECTRON MICROSCOPY
cryo-EM buffer pH 7.4
cryo-EM vitrification conditions Cryogen ETHANE
Resolution 2.60 Å
9CZP Type Id amyloid-beta 42 filaments in dominantly inherited Alzheimer disease with cotton wool plaques Deposited 2024-08-05 Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental method Different experimental conditions Different structure-quality metrics Assembly 1 Protein homooligomer Homooligomer；Protein × 20 PDB declaration: eicosameric
Chain A 680–713（34 aa） Fragment：UNP residues 680-713
Chain B 680–713（34 aa） Fragment：UNP residues 680-713
Chain C 680–713（34 aa） Fragment：UNP residues 680-713
Chain D 680–713（34 aa） Fragment：UNP residues 680-713
Chain E 680–713（34 aa） Fragment：UNP residues 680-713
Chain F 680–713（34 aa） Fragment：UNP residues 680-713
Chain G 680–713（34 aa） Fragment：UNP residues 680-713
Chain H 680–713（34 aa） Fragment：UNP residues 680-713
Chain I 680–713（34 aa） Fragment：UNP residues 680-713
Chain J 680–713（34 aa） Fragment：UNP residues 680-713
Chain K 680–713（34 aa） Fragment：UNP residues 680-713
Chain L 680–713（34 aa） Fragment：UNP residues 680-713
Chain M 680–713（34 aa） Fragment：UNP residues 680-713
Chain N 680–713（34 aa） Fragment：UNP residues 680-713
Chain O 680–713（34 aa） Fragment：UNP residues 680-713
Chain P 680–713（34 aa） Fragment：UNP residues 680-713
Chain Q 680–713（34 aa） Fragment：UNP residues 680-713
Chain R 680–713（34 aa） Fragment：UNP residues 680-713
Chain S 680–713（34 aa） Fragment：UNP residues 680-713
Chain T 680–713（34 aa） Fragment：UNP residues 680-713
Not recorded No recorded non-water small molecule ELECTRON MICROSCOPY
cryo-EM buffer pH 7.4
cryo-EM vitrification conditions Cryogen ETHANE
Resolution 3.30 Å
9FH2 Cryo-EM Structure of Amyloid-beta Fibrils Carrying the Uppsala AbetaUpp(1-42)delta(19-24) Mutation - Polymorph 1 Deposited 2024-05-26 Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental method Different experimental conditions Different structure-quality metrics Assembly 1 Protein homooligomer Homooligomer；Protein × 10 PDB declaration: decameric
Chain A 672–713（42 aa）
Chain B 672–713（42 aa）
Chain C 672–713（42 aa）
Chain D 672–713（42 aa）
Chain E 672–713（42 aa）
Chain F 672–713（42 aa）
Chain G 672–713（42 aa）
Chain H 672–713（42 aa）
Chain I 672–713（42 aa）
Chain J 672–713（42 aa）
Not recorded No recorded non-water small molecule ELECTRON MICROSCOPY
cryo-EM buffer pH 2；30% (v/v) acetonitrile (AcN), 0.1% (v/v) trifluoroacetic acid (TFA) at pH 2 (~300 uM monomer concentration)
cryo-EM vitrification conditions Cryogen ETHANE
Resolution 3.70 Å
9FH3 Cryo-EM Structure of Amyloid-beta Fibrils Carrying the Uppsala AbetaUpp(1-42)delta(19-24) Mutation - Polymorph 2 Deposited 2024-05-26 Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental method Different experimental conditions Different structure-quality metrics Assembly 1 Protein homooligomer Homooligomer；Protein × 10 PDB declaration: decameric
Chain A 672–713（42 aa）
Chain B 672–713（42 aa）
Chain C 672–713（42 aa）
Chain D 672–713（42 aa）
Chain E 672–713（42 aa）
Chain F 672–713（42 aa）
Chain G 672–713（42 aa）
Chain H 672–713（42 aa）
Chain I 672–713（42 aa）
Chain J 672–713（42 aa）
Not recorded No recorded non-water small molecule ELECTRON MICROSCOPY
cryo-EM buffer pH 2；30% (v/v) acetonitrile (AcN), 0.1% (v/v) trifluoroacetic acid (TFA) at pH 2 (~300 uM monomer concentration)
cryo-EM vitrification conditions Cryogen ETHANE
Resolution 3.90 Å
9FH4 Cryo-EM Structure of Amyloid-beta Fibrils Carrying the Uppsala AbetaUpp(1-42)delta(19-24) Mutation - Polymorph 3 Deposited 2024-05-26 Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental method Different experimental conditions Different structure-quality metrics Assembly 1 Protein homooligomer Homooligomer；Protein × 10 PDB declaration: decameric
Chain A 672–713（42 aa）
Chain B 672–713（42 aa）
Chain C 672–713（42 aa）
Chain D 672–713（42 aa）
Chain E 672–713（42 aa）
Chain F 672–713（42 aa）
Chain G 672–713（42 aa）
Chain H 672–713（42 aa）
Chain I 672–713（42 aa）
Chain J 672–713（42 aa）
Not recorded No recorded non-water small molecule ELECTRON MICROSCOPY
cryo-EM buffer pH 2；30% (v/v) acetonitrile (AcN), 0.1% (v/v) trifluoroacetic acid (TFA) at pH 2 (~300 uM monomer concentration)
cryo-EM vitrification conditions Cryogen ETHANE
Resolution 4.00 Å
9FH5 Cryo-EM Structure of Amyloid-beta Fibrils Carrying the Uppsala AbetaUpp(1-42)delta(19-24) Mutation - Polymorph 4 Deposited 2024-05-26 Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental method Different experimental conditions Different structure-quality metrics Assembly 1 Protein homooligomer Homooligomer；Protein × 20 PDB declaration: 20-meric
Chain A 672–713（42 aa）
Chain B 672–713（42 aa）
Chain C 672–713（42 aa）
Chain D 672–713（42 aa）
Chain E 672–713（42 aa）
Chain F 672–713（42 aa）
Chain G 672–713（42 aa）
Chain H 672–713（42 aa）
Chain I 672–713（42 aa）
Chain J 672–713（42 aa）
Chain K 672–713（42 aa）
Chain L 672–713（42 aa）
Chain M 672–713（42 aa）
Chain N 672–713（42 aa）
Chain O 672–713（42 aa）
Chain P 672–713（42 aa）
Chain Q 672–713（42 aa）
Chain R 672–713（42 aa）
Chain S 672–713（42 aa）
Chain T 672–713（42 aa）
Not recorded No recorded non-water small molecule ELECTRON MICROSCOPY
cryo-EM buffer pH 2；30% (v/v) acetonitrile (AcN), 0.1% (v/v) trifluoroacetic acid (TFA) at pH 2 (~300 uM monomer concentration)
cryo-EM vitrification conditions Cryogen ETHANE
Resolution 3.80 Å
9IIO J-shaped conformer of amyloid beta (1-40) Deposited 2024-06-21 Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental method Different experimental conditions Different structure-quality metrics Assembly 1 Protein homooligomer Homooligomer；Protein × 40 PDB declaration: 40-meric
Chain 2 672–711（40 aa）
Chain 3 672–711（40 aa）
Chain 4 672–711（40 aa）
Chain 5 672–711（40 aa）
Chain 6 672–711（40 aa）
Chain A 672–711（40 aa）
Chain B 672–711（40 aa）
Chain C 672–711（40 aa）
Chain D 672–711（40 aa）
Chain E 672–711（40 aa）
Chain F 672–711（40 aa）
Chain G 672–711（40 aa）
Chain H 672–711（40 aa）
Chain I 672–711（40 aa）
Chain J 672–711（40 aa）
Chain K 672–711（40 aa）
Chain L 672–711（40 aa）
Chain M 672–711（40 aa）
Chain N 672–711（40 aa）
Chain O 672–711（40 aa）
Chain P 672–711（40 aa）
Chain Q 672–711（40 aa）
Chain R 672–711（40 aa）
Chain S 672–711（40 aa）
Chain T 672–711（40 aa）
Chain U 672–711（40 aa）
Chain V 672–711（40 aa）
Chain W 672–711（40 aa）
Chain X 672–711（40 aa）
Chain Y 672–711（40 aa）
Chain Z 672–711（40 aa）
Chain a 672–711（40 aa）
Chain b 672–711（40 aa）
Chain c 672–711（40 aa）
Chain d 672–711（40 aa）
Chain e 672–711（40 aa）
Chain f 672–711（40 aa）
Chain g 672–711（40 aa）
Chain h 672–711（40 aa）
Chain i 672–711（40 aa）
Not recorded No recorded non-water small molecule ELECTRON MICROSCOPY
cryo-EM buffer pH 8
cryo-EM vitrification conditions Cryogen ETHANE
Resolution 3.30 Å
9JAZ Cryo-EM structure of the class I amyloid-beta 42 fibril containing a D-Asp at position 23 Deposited 2024-08-26 Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental method Different experimental conditions Different structure-quality metrics Assembly 1 Protein homooligomer Homooligomer；Protein × 12 PDB declaration: dodecameric
Chain A 672–713（42 aa）
Chain AA 672–713（42 aa）
Chain B 672–713（42 aa）
Chain BB 672–713（42 aa）
Chain C 672–713（42 aa）
Chain CC 672–713（42 aa）
Chain D 672–713（42 aa）
Chain DD 672–713（42 aa）
Chain E 672–713（42 aa）
Chain EE 672–713（42 aa）
Chain F 672–713（42 aa）
Chain FF 672–713（42 aa）
Non-standard monomer：Yes (specific site not provided by mmCIF) Non-standard monomer：Yes (specific site not provided by mmCIF) Non-standard monomer：Yes (specific site not provided by mmCIF) Non-standard monomer：Yes (specific site not provided by mmCIF) Non-standard monomer：Yes (specific site not provided by mmCIF) Non-standard monomer：Yes (specific site not provided by mmCIF) Non-standard monomer：Yes (specific site not provided by mmCIF) Non-standard monomer：Yes (specific site not provided by mmCIF) Non-standard monomer：Yes (specific site not provided by mmCIF) Non-standard monomer：Yes (specific site not provided by mmCIF) Non-standard monomer：Yes (specific site not provided by mmCIF) Non-standard monomer：Yes (specific site not provided by mmCIF) No recorded non-water small molecule ELECTRON MICROSCOPY
cryo-EM buffer pH 8
cryo-EM vitrification conditions Cryogen ETHANE
Resolution 3.00 Å
9JB0 Cryo-EM structure of the class II amyloid-beta 42 fibril containing a D-Asp at position 23 Deposited 2024-08-26 Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental method Different experimental conditions Different structure-quality metrics Assembly 1 Protein homooligomer Homooligomer；Protein × 12 PDB declaration: dodecameric
Chain A 672–713（42 aa）
Chain AA 672–713（42 aa）
Chain B 672–713（42 aa）
Chain BB 672–713（42 aa）
Chain C 672–713（42 aa）
Chain CC 672–713（42 aa）
Chain D 672–713（42 aa）
Chain DD 672–713（42 aa）
Chain E 672–713（42 aa）
Chain EE 672–713（42 aa）
Chain F 672–713（42 aa）
Chain FF 672–713（42 aa）
Non-standard monomer：Yes (specific site not provided by mmCIF) Non-standard monomer：Yes (specific site not provided by mmCIF) Non-standard monomer：Yes (specific site not provided by mmCIF) Non-standard monomer：Yes (specific site not provided by mmCIF) Non-standard monomer：Yes (specific site not provided by mmCIF) Non-standard monomer：Yes (specific site not provided by mmCIF) Non-standard monomer：Yes (specific site not provided by mmCIF) Non-standard monomer：Yes (specific site not provided by mmCIF) Non-standard monomer：Yes (specific site not provided by mmCIF) Non-standard monomer：Yes (specific site not provided by mmCIF) Non-standard monomer：Yes (specific site not provided by mmCIF) Non-standard monomer：Yes (specific site not provided by mmCIF) No recorded non-water small molecule ELECTRON MICROSCOPY
cryo-EM buffer pH 8
cryo-EM vitrification conditions Cryogen ETHANE
Resolution 2.90 Å
9JB1 Cryo-EM structure of the type I amyloid-beta 42 fibril containing a D-Asp at positions 7 and 23 Deposited 2024-08-26 Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental method Different experimental conditions Different structure-quality metrics Assembly 1 Protein homooligomer Homooligomer；Protein × 12 PDB declaration: dodecameric
Chain FF 672–713（42 aa）
Chain FG 672–713（42 aa）
Chain FH 672–713（42 aa）
Chain FI 672–713（42 aa）
Chain FJ 672–713（42 aa）
Chain FK 672–713（42 aa）
Chain FL 672–713（42 aa）
Chain FM 672–713（42 aa）
Chain FN 672–713（42 aa）
Chain FO 672–713（42 aa）
Chain FP 672–713（42 aa）
Chain FQ 672–713（42 aa）
Non-standard monomer：Yes (specific site not provided by mmCIF) Non-standard monomer：Yes (specific site not provided by mmCIF) Non-standard monomer：Yes (specific site not provided by mmCIF) Non-standard monomer：Yes (specific site not provided by mmCIF) Non-standard monomer：Yes (specific site not provided by mmCIF) Non-standard monomer：Yes (specific site not provided by mmCIF) Non-standard monomer：Yes (specific site not provided by mmCIF) Non-standard monomer：Yes (specific site not provided by mmCIF) Non-standard monomer：Yes (specific site not provided by mmCIF) Non-standard monomer：Yes (specific site not provided by mmCIF) Non-standard monomer：Yes (specific site not provided by mmCIF) Non-standard monomer：Yes (specific site not provided by mmCIF) No recorded non-water small molecule ELECTRON MICROSCOPY
cryo-EM buffer pH 8
cryo-EM vitrification conditions Cryogen ETHANE
Resolution 2.50 Å
9JB2 Cryo-EM structure of the type II amyloid-beta 42 fibril containing a D-Asp at positions 7 and 23 Deposited 2024-08-26 Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental method Different experimental conditions Different structure-quality metrics Assembly 1 Protein homooligomer Homooligomer；Protein × 15 PDB declaration: pentadecameric
Chain A 672–713（42 aa）
Chain B 672–713（42 aa）
Chain BA 672–713（42 aa）
Chain BB 672–713（42 aa）
Chain BC 672–713（42 aa）
Chain BD 672–713（42 aa）
Chain BE 672–713（42 aa）
Chain C 672–713（42 aa）
Chain CA 672–713（42 aa）
Chain CB 672–713（42 aa）
Chain CC 672–713（42 aa）
Chain CD 672–713（42 aa）
Chain CE 672–713（42 aa）
Chain D 672–713（42 aa）
Chain E 672–713（42 aa）
Non-standard monomer：Yes (specific site not provided by mmCIF) Non-standard monomer：Yes (specific site not provided by mmCIF) Non-standard monomer：Yes (specific site not provided by mmCIF) Non-standard monomer：Yes (specific site not provided by mmCIF) Non-standard monomer：Yes (specific site not provided by mmCIF) Non-standard monomer：Yes (specific site not provided by mmCIF) Non-standard monomer：Yes (specific site not provided by mmCIF) Non-standard monomer：Yes (specific site not provided by mmCIF) Non-standard monomer：Yes (specific site not provided by mmCIF) Non-standard monomer：Yes (specific site not provided by mmCIF) Non-standard monomer：Yes (specific site not provided by mmCIF) Non-standard monomer：Yes (specific site not provided by mmCIF) Non-standard monomer：Yes (specific site not provided by mmCIF) Non-standard monomer：Yes (specific site not provided by mmCIF) Non-standard monomer：Yes (specific site not provided by mmCIF) No recorded non-water small molecule ELECTRON MICROSCOPY
cryo-EM buffer pH 8
cryo-EM vitrification conditions Cryogen ETHANE
Resolution 2.90 Å
9K0D Cryo-EM structure of Amyloid-beta42-4b polymorph 1 Deposited 2024-10-15 Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental method Different experimental conditions Different structure-quality metrics Assembly 1 Protein heterocomplex Heteromer；Protein × 18 PDB declaration: 18-meric
Chain B 680–692（13 aa）
Chain F 680–692（13 aa）
Chain K 680–692（13 aa）
Chain L 680–692（13 aa）
Chain S 680–692（13 aa）
Chain T 680–692（13 aa）
Not recorded No recorded non-water small molecule ELECTRON MICROSCOPY
cryo-EM buffer pH 7.4
cryo-EM vitrification conditions Cryogen ETHANE
Resolution 2.60 Å
9K0E Cryo-EM structure of Amyloid-beta42-4b polymorph 2 Deposited 2024-10-15 Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental method Different experimental conditions Different structure-quality metrics Assembly 1 Protein heterocomplex Heteromer；Protein × 12 PDB declaration: 12-meric
Chain A 680–692（13 aa）
Chain D 680–692（13 aa）
Chain E 680–692（13 aa）
Chain F 680–692（13 aa）
Chain L 680–692（13 aa）
Chain M 680–692（13 aa）
Not recorded No recorded non-water small molecule ELECTRON MICROSCOPY
cryo-EM buffer pH 7.4
cryo-EM vitrification conditions Cryogen ETHANE
Resolution 2.80 Å
9K0F Cryo-EM structure of Amyloid-beta42-4b polymorph 3 Deposited 2024-10-15 Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental method Different experimental conditions Different structure-quality metrics Assembly 1 Protein heterocomplex Heteromer；Protein × 12 PDB declaration: 12-meric
Chain K 680–692（13 aa）
Chain N 680–692（13 aa）
Chain O 680–692（13 aa）
Not recorded No recorded non-water small molecule ELECTRON MICROSCOPY
cryo-EM buffer pH 7.4
cryo-EM vitrification conditions Cryogen ETHANE
Resolution 2.80 Å
9LLM Structure of C-Terminal of AB40 Peptide containing GXXXG Motif in SDS Micelles Deposited 2025-01-17 Different construct Different oligomeric state Different ligand/ion Different experimental method Different experimental conditions Different structure-quality metrics Assembly 1 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric
Chain A 692–711（20 aa）
Not recorded No recorded non-water small molecule SOLUTION NMR
NMR measurement conditions pH 5.2；298 K；Ionic strength (raw mmCIF value) 20；Pressure 1
NMR sample composition 1 mM AV20, 0.1 mM SDS, 90% H2O/10% D2O | 90% H2O/10% D2O
Resolution not provided
9M5P I-type amyloid fibril (40) of Tottori (D7N) mutant Deposited 2025-03-06 Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental method Different experimental conditions Different structure-quality metrics Assembly 1 Protein homooligomer Homooligomer；Protein × 6 PDB declaration: hexameric
Chain 1 672–711（40 aa）
Chain 2 672–711（40 aa）
Chain 3 672–711（40 aa）
Chain 4 672–711（40 aa）
Chain 5 672–711（40 aa）
Chain 6 672–711（40 aa）
Not recorded No recorded non-water small molecule ELECTRON MICROSCOPY
cryo-EM buffer pH 8
cryo-EM vitrification conditions Cryogen ETHANE
Resolution 3.30 Å
9M5Q V-type (V1-type) amyloid fibril (40) of Tottori (D7N) mutant Deposited 2025-03-06 Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental method Different experimental conditions Different structure-quality metrics Assembly 1 Protein homooligomer Homooligomer；Protein × 21 PDB declaration: 21-meric
Chain AL 672–711（40 aa）
Chain AM 672–711（40 aa）
Chain AN 672–711（40 aa）
Chain AO 672–711（40 aa）
Chain AP 672–711（40 aa）
Chain AQ 672–711（40 aa）
Chain AR 672–711（40 aa）
Chain AS 672–711（40 aa）
Chain AT 672–711（40 aa）
Chain AU 672–711（40 aa）
Chain AV 672–711（40 aa）
Chain AW 672–711（40 aa）
Chain AX 672–711（40 aa）
Chain AY 672–711（40 aa）
Chain AZ 672–711（40 aa）
Chain Aa 672–711（40 aa）
Chain Ab 672–711（40 aa）
Chain Ac 672–711（40 aa）
Chain Ad 672–711（40 aa）
Chain Ae 672–711（40 aa）
Chain Af 672–711（40 aa）
Not recorded No recorded non-water small molecule ELECTRON MICROSCOPY
cryo-EM buffer pH 8
cryo-EM vitrification conditions Cryogen ETHANE
Resolution 3.30 Å
9M5R ES-type (short pitch) amyloid fibril (40) of Tottori (D7N) mutant Deposited 2025-03-06 Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental method Different experimental conditions Different structure-quality metrics Assembly 1 Protein homooligomer Homooligomer；Protein × 172 PDB declaration: 172-meric
Chain 0 672–711（40 aa）
Chain 1 672–711（40 aa）
Chain 2 672–711（40 aa）
Chain 3 672–711（40 aa）
Chain 4 672–711（40 aa）
Chain 5 672–711（40 aa）
Chain 6 672–711（40 aa）
Chain 7 672–711（40 aa）
Chain 8 672–711（40 aa）
Chain 9 672–711（40 aa）
Chain A 672–711（40 aa）
Chain A0 672–711（40 aa）
Chain A1 672–711（40 aa）
Chain A2 672–711（40 aa）
Chain A3 672–711（40 aa）
Chain A4 672–711（40 aa）
Chain A5 672–711（40 aa）
Chain A6 672–711（40 aa）
Chain A7 672–711（40 aa）
Chain A8 672–711（40 aa）
Chain A9 672–711（40 aa）
Chain AA 672–711（40 aa）
Chain AB 672–711（40 aa）
Chain AC 672–711（40 aa）
Chain AD 672–711（40 aa）
Chain AE 672–711（40 aa）
Chain AF 672–711（40 aa）
Chain AG 672–711（40 aa）
Chain AH 672–711（40 aa）
Chain AI 672–711（40 aa）
Chain AJ 672–711（40 aa）
Chain AK 672–711（40 aa）
Chain AL 672–711（40 aa）
Chain AM 672–711（40 aa）
Chain AN 672–711（40 aa）
Chain AO 672–711（40 aa）
Chain AP 672–711（40 aa）
Chain AQ 672–711（40 aa）
Chain AR 672–711（40 aa）
Chain AS 672–711（40 aa）
Chain AT 672–711（40 aa）
Chain AU 672–711（40 aa）
Chain AV 672–711（40 aa）
Chain AW 672–711（40 aa）
Chain AX 672–711（40 aa）
Chain AY 672–711（40 aa）
Chain AZ 672–711（40 aa）
Chain Aa 672–711（40 aa）
Chain Ab 672–711（40 aa）
Chain Ac 672–711（40 aa）
Chain Ad 672–711（40 aa）
Chain Ae 672–711（40 aa）
Chain Af 672–711（40 aa）
Chain Ag 672–711（40 aa）
Chain Ah 672–711（40 aa）
Chain Ai 672–711（40 aa）
Chain Aj 672–711（40 aa）
Chain Ak 672–711（40 aa）
Chain Al 672–711（40 aa）
Chain Am 672–711（40 aa）
Chain An 672–711（40 aa）
Chain Ao 672–711（40 aa）
Chain Ap 672–711（40 aa）
Chain Aq 672–711（40 aa）
Chain Ar 672–711（40 aa）
Chain As 672–711（40 aa）
Chain At 672–711（40 aa）
Chain Au 672–711（40 aa）
Chain Av 672–711（40 aa）
Chain Aw 672–711（40 aa）
Chain Ax 672–711（40 aa）
Chain Ay 672–711（40 aa）
Chain Az 672–711（40 aa）
Chain B 672–711（40 aa）
Chain BA 672–711（40 aa）
Chain BB 672–711（40 aa）
Chain BC 672–711（40 aa）
Chain BD 672–711（40 aa）
Chain BE 672–711（40 aa）
Chain BF 672–711（40 aa）
Chain BG 672–711（40 aa）
Chain BH 672–711（40 aa）
Chain BI 672–711（40 aa）
Chain BJ 672–711（40 aa）
Chain BK 672–711（40 aa）
Chain BL 672–711（40 aa）
Chain BM 672–711（40 aa）
Chain BN 672–711（40 aa）
Chain BO 672–711（40 aa）
Chain BP 672–711（40 aa）
Chain BQ 672–711（40 aa）
Chain BR 672–711（40 aa）
Chain BS 672–711（40 aa）
Chain BT 672–711（40 aa）
Chain BU 672–711（40 aa）
Chain BV 672–711（40 aa）
Chain BW 672–711（40 aa）
Chain BX 672–711（40 aa）
Chain BY 672–711（40 aa）
Chain BZ 672–711（40 aa）
Chain Ba 672–711（40 aa）
Chain Bb 672–711（40 aa）
Chain Bc 672–711（40 aa）
Chain Bd 672–711（40 aa）
Chain Be 672–711（40 aa）
Chain Bf 672–711（40 aa）
Chain Bg 672–711（40 aa）
Chain Bh 672–711（40 aa）
Chain Bi 672–711（40 aa）
Chain Bj 672–711（40 aa）
Chain Bk 672–711（40 aa）
Chain Bl 672–711（40 aa）
Chain Bm 672–711（40 aa）
Chain Bn 672–711（40 aa）
Chain Bo 672–711（40 aa）
Chain Bp 672–711（40 aa）
Chain Bq 672–711（40 aa）
Chain Br 672–711（40 aa）
Chain Bs 672–711（40 aa）
Chain Bt 672–711（40 aa）
Chain Bu 672–711（40 aa）
Chain Bv 672–711（40 aa）
Chain C 672–711（40 aa）
Chain D 672–711（40 aa）
Chain E 672–711（40 aa）
Chain F 672–711（40 aa）
Chain G 672–711（40 aa）
Chain H 672–711（40 aa）
Chain I 672–711（40 aa）
Chain J 672–711（40 aa）
Chain K 672–711（40 aa）
Chain L 672–711（40 aa）
Chain M 672–711（40 aa）
Chain N 672–711（40 aa）
Chain O 672–711（40 aa）
Chain P 672–711（40 aa）
Chain Q 672–711（40 aa）
Chain R 672–711（40 aa）
Chain S 672–711（40 aa）
Chain T 672–711（40 aa）
Chain U 672–711（40 aa）
Chain V 672–711（40 aa）
Chain W 672–711（40 aa）
Chain X 672–711（40 aa）
Chain Y 672–711（40 aa）
Chain Z 672–711（40 aa）
Chain a 672–711（40 aa）
Chain b 672–711（40 aa）
Chain c 672–711（40 aa）
Chain d 672–711（40 aa）
Chain e 672–711（40 aa）
Chain f 672–711（40 aa）
Chain g 672–711（40 aa）
Chain h 672–711（40 aa）
Chain i 672–711（40 aa）
Chain j 672–711（40 aa）
Chain k 672–711（40 aa）
Chain l 672–711（40 aa）
Chain m 672–711（40 aa）
Chain n 672–711（40 aa）
Chain o 672–711（40 aa）
Chain p 672–711（40 aa）
Chain q 672–711（40 aa）
Chain r 672–711（40 aa）
Chain s 672–711（40 aa）
Chain t 672–711（40 aa）
Chain u 672–711（40 aa）
Chain v 672–711（40 aa）
Chain w 672–711（40 aa）
Chain x 672–711（40 aa）
Chain y 672–711（40 aa）
Chain z 672–711（40 aa）
Not recorded No recorded non-water small molecule ELECTRON MICROSCOPY
cryo-EM buffer pH 8
cryo-EM vitrification conditions Cryogen ETHANE
Resolution 3.60 Å
9OBK A-beta42-Met-R-SO amyloidal fibril Deposited 2025-04-22 Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental method Different experimental conditions Different structure-quality metrics Assembly 1 Protein homooligomer Homooligomer；Protein × 10 PDB declaration: decameric
Chain A 685–712（28 aa）
Chain B 685–712（28 aa）
Chain C 685–712（28 aa）
Chain D 685–712（28 aa）
Chain E 685–712（28 aa）
Chain F 685–712（28 aa）
Chain G 685–712（28 aa）
Chain H 685–712（28 aa）
Chain I 685–712（28 aa）
Chain J 685–712（28 aa）
Non-standard monomer：Yes (specific site not provided by mmCIF) Non-standard monomer：Yes (specific site not provided by mmCIF) Non-standard monomer：Yes (specific site not provided by mmCIF) Non-standard monomer：Yes (specific site not provided by mmCIF) Non-standard monomer：Yes (specific site not provided by mmCIF) Non-standard monomer：Yes (specific site not provided by mmCIF) Non-standard monomer：Yes (specific site not provided by mmCIF) Non-standard monomer：Yes (specific site not provided by mmCIF) Non-standard monomer：Yes (specific site not provided by mmCIF) Non-standard monomer：Yes (specific site not provided by mmCIF) No recorded non-water small molecule ELECTRON MICROSCOPY
cryo-EM buffer pH 7.4
cryo-EM vitrification conditions Cryogen ETHANE
Resolution 3.01 Å
9ONC A-beta42-Met-R-SO amyloidal fibril - class3 Deposited 2025-05-14 Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental method Different experimental conditions Different structure-quality metrics Assembly 1 Protein homooligomer Homooligomer；Protein × 10 PDB declaration: decameric
Chain A 688–713（26 aa）
Chain B 688–713（26 aa）
Chain C 688–713（26 aa）
Chain D 688–713（26 aa）
Chain E 688–713（26 aa）
Chain F 688–713（26 aa）
Chain G 688–713（26 aa）
Chain H 688–713（26 aa）
Chain I 688–713（26 aa）
Chain J 688–713（26 aa）
Non-standard monomer：Yes (specific site not provided by mmCIF) Non-standard monomer：Yes (specific site not provided by mmCIF) Non-standard monomer：Yes (specific site not provided by mmCIF) Non-standard monomer：Yes (specific site not provided by mmCIF) Non-standard monomer：Yes (specific site not provided by mmCIF) Non-standard monomer：Yes (specific site not provided by mmCIF) Non-standard monomer：Yes (specific site not provided by mmCIF) Non-standard monomer：Yes (specific site not provided by mmCIF) Non-standard monomer：Yes (specific site not provided by mmCIF) Non-standard monomer：Yes (specific site not provided by mmCIF) No recorded non-water small molecule ELECTRON MICROSCOPY
cryo-EM buffer pH 7.4
cryo-EM vitrification conditions Cryogen ETHANE
Resolution 3.64 Å
9RIV Population B fibril generated from the Heterotypic interaction of Abeta40 and Medin. Deposited 2025-06-11 Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental method Different experimental conditions Different structure-quality metrics Assembly 1 Protein homooligomer Homooligomer；Protein × 10 PDB declaration: decameric
Chain A 672–711（40 aa）
Chain B 672–711（40 aa）
Chain C 672–711（40 aa）
Chain D 672–711（40 aa）
Chain E 672–711（40 aa）
Chain F 672–711（40 aa）
Chain G 672–711（40 aa）
Chain H 672–711（40 aa）
Chain I 672–711（40 aa）
Chain J 672–711（40 aa）
Not recorded No recorded non-water small molecule ELECTRON MICROSCOPY
cryo-EM buffer pH 7.5
cryo-EM vitrification conditions Cryogen ETHANE
Resolution 2.63 Å
9RIW Population A fibril generated from the Heterotypic interaction of Abeta40 and Medin. Deposited 2025-06-11 Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental method Different experimental conditions Different structure-quality metrics Assembly 1 Protein homooligomer Homooligomer；Protein × 8 PDB declaration: octameric
Chain A 672–711（40 aa）
Chain B 672–711（40 aa）
Chain C 672–711（40 aa）
Chain D 672–711（40 aa）
Chain E 672–711（40 aa）
Chain F 672–711（40 aa）
Chain G 672–711（40 aa）
Chain H 672–711（40 aa）
Not recorded No recorded non-water small molecule ELECTRON MICROSCOPY
cryo-EM buffer pH 7.5
cryo-EM vitrification conditions Cryogen ETHANE
Resolution 3.10 Å
9UMH V-type (V2-type) amyloid fibril (40) of Tottori (D7N) mutant Deposited 2025-04-22 Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental method Different experimental conditions Different structure-quality metrics Assembly 1 Protein homooligomer Homooligomer；Protein × 21 PDB declaration: 21-meric
Chain AL 672–711（40 aa）
Chain AM 672–711（40 aa）
Chain AN 672–711（40 aa）
Chain AO 672–711（40 aa）
Chain AP 672–711（40 aa）
Chain AQ 672–711（40 aa）
Chain AR 672–711（40 aa）
Chain AS 672–711（40 aa）
Chain AT 672–711（40 aa）
Chain AU 672–711（40 aa）
Chain AV 672–711（40 aa）
Chain AW 672–711（40 aa）
Chain AX 672–711（40 aa）
Chain AY 672–711（40 aa）
Chain AZ 672–711（40 aa）
Chain Aa 672–711（40 aa）
Chain Ab 672–711（40 aa）
Chain Ac 672–711（40 aa）
Chain Ad 672–711（40 aa）
Chain Ae 672–711（40 aa）
Chain Af 672–711（40 aa）
Not recorded No recorded non-water small molecule ELECTRON MICROSCOPY
cryo-EM buffer pH 8
cryo-EM vitrification conditions Cryogen ETHANE
Resolution 3.10 Å
9WAO Structure of type II Abeta fibrils from 5xFAD mice Deposited 2025-08-12 Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental method Different experimental conditions Different structure-quality metrics Assembly 1 Protein homooligomer Homooligomer；Protein × 12 PDB declaration: dodecameric
Chain A 672–713（42 aa）
Chain B 672–713（42 aa）
Chain C 672–713（42 aa）
Chain D 672–713（42 aa）
Chain E 672–713（42 aa）
Chain F 672–713（42 aa）
Chain G 672–713（42 aa）
Chain H 672–713（42 aa）
Chain I 672–713（42 aa）
Chain J 672–713（42 aa）
Chain K 672–713（42 aa）
Chain L 672–713（42 aa）
Not recorded No recorded non-water small molecule ELECTRON MICROSCOPY
cryo-EM buffer pH 7.4
cryo-EM vitrification conditions Cryogen ETHANE
Resolution 3.50 Å
9WAP Structure of Type II Abeta fibrils from AppNL-FPsen1P117L mice Deposited 2025-08-12 Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental method Different experimental conditions Different structure-quality metrics Assembly 1 Protein homooligomer Homooligomer；Protein × 12 PDB declaration: dodecameric
Chain A 672–713（42 aa）
Chain B 672–713（42 aa）
Chain C 672–713（42 aa）
Chain D 672–713（42 aa）
Chain E 672–713（42 aa）
Chain F 672–713（42 aa）
Chain G 672–713（42 aa）
Chain H 672–713（42 aa）
Chain I 672–713（42 aa）
Chain J 672–713（42 aa）
Chain K 672–713（42 aa）
Chain L 672–713（42 aa）
Not recorded No recorded non-water small molecule ELECTRON MICROSCOPY
cryo-EM buffer pH 7.4
cryo-EM vitrification conditions Cryogen ETHANE
Resolution 3.22 Å

211 other PDB entries and 282 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name A4_HUMAN
Isoform —
PDB entities 2
Chains and sequence ranges Author chain B； PDBConstruct 1–7； UniProt 761–767

The page prioritizes protein identity, the current assembly, associated components, oligomeric state and cross-PDB links. Chain mapping and sequence ranges are retained as data evidence. Internal IDs, import timestamps and assembly operation expressions are maintenance fields and are not shown here.

SAXS scattering curve SAXS Profile

SAXS profile for 3l81

P(r) Distance Distribution P(r) Distribution

P(r) distribution for 3l81
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2. Structure Basics 2. Structure Basics

Entry ID entry_id3l81
Deposition date deposition_date2009-12-29
Structure title titleCrystal structure of adaptor protein complex 4 (AP-4) mu4 subunit C-terminal domain, in complex with a sorting peptide from the amyloid precursor protein (APP)
Keywords keywords;immunoglobulin-like beta-sandwich, Coated pit, Golgi apparatus, Membrane, Phosphoprotein, Protein transport, Transport, Alzheimer disease, Amyloid, Amyloidosis, TRANSPORT PROTEIN ;; TRANSPORT PROTEIN
Experimental Method methodX-RAY DIFFRACTION
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3. SAXS Parameters (CRYSOL theoretical calculation) 3. SAXS Parameters (CRYSOL)

Radius of gyration Rg (Guinier) rg_guinier23.27 Å
Radius of gyration Rg (electron density) rg_electron22.52 Å
Forward intensity I(0) i014517800.00
Molecular weight molecular_weight29136.0 kDa
Excluded volume excluded_volume36726 ų
Envelope volume envelope_volume46143 ų
Hydration-shell volume shell_volume18353 ų
Envelope diameter envelope_diameter81.6 Å
Shell Rg shell_rg27.77 Å
Envelope Rg envelope_rg22.93 Å
Shape Rg shape_rg22.52 Å
Total Rg total_rg23.23 Å
Total atoms total_atoms2056
Residues n_residues257
Spherical-harmonic order n_harmonics20
q range q_range— – 0.5000 Å−1
Data points n_points101
Shell type shell_typedirectional
Solvent electron density solvent_density0.3340 e/ų
Shell contrast contrast_shell0.0300 e/ų
CRYSOL version crysol_version4.1.3
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4. P(r) Distance Distribution (GNOM inversion) 4. P(r) Analysis (GNOM)

Maximum dimension Dmax dmax80.2 Å
Rg (real space) rg_real23.45 Å
Rg uncertainty (real space) rg_real_error0.59 Å
I(0) (real space) i0_real1.4520e+07
I(0) uncertainty (real space) i0_real_error1.8140e+05
Rg (reciprocal space) rg_reciprocal23.41 Å
I(0) (reciprocal space) i0_reciprocal14520000.0000
Solution quality estimate total_estimate0.8386
Solution quality rating solution_quality GOOD a GOOD solution
P(r) peaks n_peaks2
Primary peak position r_peak_primary22.2 Å
Skewness Skewness skewness0.528
Kurtosis Kurtosis kurtosis-0.272
Angular range angular_range— – 0.3400 Å−1
Current regularization parameter α current_alpha0.0000
Highest regularization parameter α highest_alpha4435000.0000
Real-space data points n_real_points66
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.713; Stabil: 1.000; Sysdev: 1.000; Positv: 1.000; Valcen: 0.796; Smooth: 0.963
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5. Crystallography and Experiment 5. Crystallography & Experiment

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6. Entities and Polymers Entities & Polymers (4)

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7. Fold Classification (SCOP + CATH) 3 domains

SCOP 2.08 (1 domains)

Domain ID domain_idd3l81a_
Class classb — All beta proteins
Fold Fold foldb.2 — Common fold of diphtheria toxin/transcription factors/cytochrome f
Superfamily Superfamily superfamilyb.2.7 — Second domain of Mu2 adaptin subunit (ap50) of ap2 adaptor
Family Family familyb.2.7.0 — automated matches

CATH v4.4 (2 domains)

Domain ID domain_id3l81A01
Class class2 — Mainly Beta
Architecture architecture60 — Sandwich
Topology topology40 — Immunoglobulin-like
Homologous superfamily homologous superfamily1170 — Mu homology domain, subdomain B
Domain ID domain_id3l81A02
Class class2 — Mainly Beta
Architecture architecture60 — Sandwich
Topology topology40 — Immunoglobulin-like
Homologous superfamily homologous superfamily1170 — Mu homology domain, subdomain B
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8. Citations (1)

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9. Files and Curves (10)