9k0e

Cryo-EM structure of Amyloid-beta42-4b polymorph 2

Method: ELECTRON MICROSCOPY D_max: 95.7 Å Quality: GOOD

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1. Protein Identity and Related Structures Protein Identity & Related Structures

Amyloid-beta A4 protein

OrganismNot specified

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 × 12 PDB declaration: 12-meric（12） Consistent with protein copy count	Chain B； UniProt 524–565 Chain G； UniProt 524–565 Chain H； UniProt 524–565 Chain I； UniProt 524–565 Chain N； UniProt 524–565 Chain O； UniProt 524–565	Not recorded	Amyloid-beta protein 40 × 6 （P05067）	ELECTRON MICROSCOPY cryo-EM buffer：pH 7.4 cryo-EM vitrification conditions：Cryogen ETHANE	Resolution 2.80 Å

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 9K0E	Assembly / Oligomeric State	Construct	Mutations and Modifications	Ligands, Ions and Non-polymers	Method and Experimental Conditions	Structure Quality
7WVY Cryo-EM structure of the human formyl peptide receptor 2 in complex with Abeta42 and Gi2 Deposited 2022-02-11	Different construct Different mutation/modification Different oligomeric state Different experimental conditions Different structure-quality metrics	Assembly 1 Insufficient information Heteromer；Protein × 5 PDB declaration: pentameric	Chain L 524–565（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 3.00 Å
9K0D Cryo-EM structure of Amyloid-beta42-4b polymorph 1 Deposited 2024-10-15	Different construct Different mutation/modification Different oligomeric state Different structure-quality metrics	Assembly 1 Protein heterocomplex Heteromer；Protein × 18 PDB declaration: 18-meric	Chain C 524–565（42 aa） Chain D 524–565（42 aa） Chain G 524–565（42 aa） Chain H 524–565（42 aa） Chain M 524–565（42 aa） Chain N 524–565（42 aa） Chain O 524–565（42 aa） Chain P 524–565（42 aa） Chain U 524–565（42 aa） Chain V 524–565（42 aa） Chain W 524–565（42 aa） Chain X 524–565（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 2.60 Å
9K0F Cryo-EM structure of Amyloid-beta42-4b polymorph 3 Deposited 2024-10-15	Different construct Different mutation/modification	Assembly 1 Protein heterocomplex Heteromer；Protein × 12 PDB declaration: 12-meric	Chain D 524–565（42 aa） Chain E 524–565（42 aa） Chain F 524–565（42 aa） Chain G 524–565（42 aa） Chain H 524–565（42 aa） Chain I 524–565（42 aa） Chain J 524–565（42 aa） Chain L 524–565（42 aa） Chain M 524–565（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 2.80 Å

3 other PDB entries and 3 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence

UniProt name	B4DMD5_HUMAN
Isoform	—
PDB entities	1
Chains and sequence ranges	Author chain B； PDBConstruct 1–42； UniProt 524–565 Author chain G； PDBConstruct 1–42； UniProt 524–565 Author chain H； PDBConstruct 1–42； UniProt 524–565 Author chain I； PDBConstruct 1–42； UniProt 524–565 Author chain N； PDBConstruct 1–42； UniProt 524–565 Author chain O； PDBConstruct 1–42； UniProt 524–565

Amyloid-beta protein 40

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 × 12 PDB declaration: 12-meric（12） Consistent with protein copy count	Chain A； UniProt 680–692 Chain D； UniProt 680–692 Chain E； UniProt 680–692 Chain F； UniProt 680–692 Chain L； UniProt 680–692 Chain M； UniProt 680–692	Not recorded	Amyloid-beta A4 protein × 6 （B4DMD5）	ELECTRON MICROSCOPY cryo-EM buffer：pH 7.4 cryo-EM vitrification conditions：Cryogen ETHANE	Resolution 2.80 Å

Other States of the Same Protein in the Database

Other PDB	Difference from Current Entry 9K0E	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 oligomeric state 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 oligomeric state 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 oligomeric state 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 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 experimental method 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 mutation/modification Different oligomeric state 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 mutation/modification Different oligomeric state 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 mutation/modification Different oligomeric state 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 mutation/modification Different oligomeric state 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 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 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 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 mutation/modification Different oligomeric state Different experimental method 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 mutation/modification Different oligomeric state Different experimental method 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 mutation/modification Different oligomeric state Different experimental method 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 mutation/modification Different oligomeric state 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 mutation/modification Different oligomeric state 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 mutation/modification Different oligomeric state Different experimental method 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 mutation/modification Different oligomeric state 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 mutation/modification Different oligomeric state 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 mutation/modification Different oligomeric state 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 mutation/modification Different oligomeric state 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 mutation/modification Different oligomeric state 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 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 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 mutation/modification Different oligomeric state 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 experimental method 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 experimental method 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 experimental method 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 mutation/modification Different oligomeric state 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 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 mutation/modification Different oligomeric state Different experimental method 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 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 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 mutation/modification Different oligomeric state 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 mutation/modification Different oligomeric state Different experimental method 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 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 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 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 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 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 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 mutation/modification Different oligomeric state Different ligand/ion Different experimental method 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 mutation/modification Different oligomeric state Different ligand/ion Different experimental method 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 mutation/modification Different oligomeric state Different ligand/ion Different experimental method 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 mutation/modification Different oligomeric state Different ligand/ion Different experimental method 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 mutation/modification Different oligomeric state Different ligand/ion Different experimental method 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 mutation/modification Different oligomeric state Different experimental method 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 mutation/modification Different oligomeric state Different ligand/ion Different experimental method 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 mutation/modification Different oligomeric state 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：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 mutation/modification Different oligomeric state Different experimental method 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 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 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 mutation/modification Different oligomeric state 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 mutation/modification Different oligomeric state 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 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 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 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 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 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 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 mutation/modification Different oligomeric state 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 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 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 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 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：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 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：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 mutation/modification Different oligomeric state 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 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 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 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 oligomeric state 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 mutation/modification Different oligomeric state 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 mutation/modification 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 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 mutation/modification Different oligomeric state Different ligand/ion Different experimental method 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 mutation/modification Different oligomeric state Different ligand/ion Different experimental method 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 mutation/modification Different oligomeric state Different experimental method 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 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 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 experimental method 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 experimental method 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 experimental method 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 experimental method 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 experimental method 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 experimental method 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 experimental method 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 mutation/modification Different oligomeric state Different ligand/ion Different experimental method 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 mutation/modification Different oligomeric state Different experimental method 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 mutation/modification Different oligomeric state Different experimental method 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 oligomeric state Different experimental method 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 oligomeric state Different experimental method 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 oligomeric state Different experimental method 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 oligomeric state Different experimental method 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 mutation/modification Different oligomeric state Different ligand/ion Different experimental method 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 mutation/modification Different oligomeric state Different experimental method 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 mutation/modification Different oligomeric state Different experimental method 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 mutation/modification Different oligomeric state Different experimental method 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 mutation/modification Different oligomeric state Different experimental method 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 mutation/modification Different oligomeric state Different experimental method 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 mutation/modification Different oligomeric state Different experimental method 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 mutation/modification Different oligomeric state Different experimental method 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 mutation/modification Different oligomeric state Different experimental method 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 mutation/modification Different oligomeric state Different ligand/ion Different experimental method 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 method 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 mutation/modification Different oligomeric state Different ligand/ion Different experimental method 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 mutation/modification Different oligomeric state Different ligand/ion Different experimental method 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 mutation/modification Different oligomeric state Different ligand/ion Different experimental method 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 method 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 method 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 method 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 mutation/modification Different oligomeric state Different ligand/ion Different experimental method 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 mutation/modification Different oligomeric state Different ligand/ion Different experimental method 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 mutation/modification Different oligomeric state Different ligand/ion Different experimental method 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 mutation/modification Different oligomeric state Different ligand/ion Different experimental method 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 mutation/modification Different oligomeric state Different ligand/ion Different experimental method 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 mutation/modification Different oligomeric state Different ligand/ion Different experimental method 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 mutation/modification Different oligomeric state Different ligand/ion Different experimental method 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 mutation/modification Different oligomeric state Different ligand/ion Different experimental method 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 mutation/modification Different oligomeric state Different ligand/ion Different experimental method 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
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) Deposited 2009-12-29	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 × 2 PDB declaration: dimeric	Chain B 761–767（7 aa） Fragment：C-terminus, residues 761-767	Not recorded	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
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 experimental method 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 mutation/modification Different oligomeric state Different experimental method 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 mutation/modification Different oligomeric state Different experimental method 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 mutation/modification Different oligomeric state Different experimental method 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 experimental method 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 method 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 method 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 experimental method 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 experimental method 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 mutation/modification Different oligomeric state Different experimental method 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 mutation/modification Different oligomeric state Different experimental method 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 mutation/modification Different oligomeric state Different experimental method 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 mutation/modification Different oligomeric state Different experimental method 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 mutation/modification Different oligomeric state Different experimental method 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 mutation/modification Different oligomeric state Different experimental method 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 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 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 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 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 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 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 mutation/modification Different oligomeric state Different experimental method 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 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 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 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 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 mutation/modification Different oligomeric state Different ligand/ion Different experimental method 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 mutation/modification Different oligomeric state Different experimental method 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 mutation/modification Different oligomeric state Different experimental method 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 oligomeric state Different experimental method 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 mutation/modification Different oligomeric state Different experimental method 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 mutation/modification Different oligomeric state Different experimental method 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 mutation/modification Different oligomeric state Different experimental method 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 mutation/modification Different oligomeric state Different experimental method 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 mutation/modification 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 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 mutation/modification Different oligomeric state Different ligand/ion Different experimental method 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 mutation/modification Different oligomeric state Different experimental method 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 mutation/modification Different oligomeric state Different experimental method 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 mutation/modification 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 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 mutation/modification Different oligomeric state Different experimental method 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 mutation/modification Different oligomeric state Different experimental method 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 mutation/modification Different oligomeric state Different experimental method 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 mutation/modification Different oligomeric state Different experimental method 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 mutation/modification Different oligomeric state Different experimental method 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 mutation/modification Different oligomeric state Different ligand/ion Different experimental method 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 mutation/modification Different oligomeric state Different ligand/ion Different experimental method 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 mutation/modification Different oligomeric state Different ligand/ion Different experimental method 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 mutation/modification Different oligomeric state Different ligand/ion Different experimental method 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 mutation/modification Different oligomeric state Different ligand/ion Different experimental method 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 mutation/modification Different oligomeric state Different ligand/ion Different experimental method 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 method 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 oligomeric state Different experimental method 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 oligomeric state Different experimental method 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 mutation/modification 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 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 mutation/modification Different oligomeric state Different ligand/ion Different experimental method 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 experimental method 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 experimental method 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 method 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 method 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 method 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 method 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 experimental method 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 experimental method 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 method 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 method 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 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 method 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 experimental method 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 experimental method 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 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 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 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 mutation/modification Different oligomeric state Different experimental method 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 method 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 mutation/modification Different oligomeric state Different ligand/ion Different experimental method 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 mutation/modification Different oligomeric state Different experimental method 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 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 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 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 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 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 mutation/modification Different oligomeric state 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 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 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 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 oligomeric state 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 method 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 method 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 method 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 experimental method 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 mutation/modification Different oligomeric state 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 mutation/modification Different oligomeric state 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 mutation/modification Different oligomeric state 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 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 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 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 mutation/modification Different oligomeric state 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 oligomeric state 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 method 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 experimental method 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 experimental method 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 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 method 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 method 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 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 conditions	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 method 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 experimental method 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 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 mutation/modification Different oligomeric state 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 mutation/modification Different oligomeric state 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 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 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 experimental conditions	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 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 oligomeric state Different ligand/ion Different experimental method 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 oligomeric state Different ligand/ion Different experimental method 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 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 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 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 oligomeric state 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 oligomeric state 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 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 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 oligomeric state 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 oligomeric state 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 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 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 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 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 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 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 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 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 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 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 oligomeric state 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 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 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 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 mutation/modification Different oligomeric state Different ligand/ion 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 mutation/modification Different oligomeric state Different ligand/ion 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 mutation/modification Different oligomeric state Different ligand/ion 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 mutation/modification Different oligomeric state 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 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 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 experimental conditions	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 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 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 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 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 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 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 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 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 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 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 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 oligomeric state 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
9K0F Cryo-EM structure of Amyloid-beta42-4b polymorph 3 Deposited 2024-10-15	Different construct Different mutation/modification	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 mutation/modification Different oligomeric state 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 oligomeric state 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 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 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 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 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 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 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 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 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 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 A； PDBConstruct 1–13； UniProt 680–692 Author chain D； PDBConstruct 1–13； UniProt 680–692 Author chain E； PDBConstruct 1–13； UniProt 680–692 Author chain F； PDBConstruct 1–13； UniProt 680–692 Author chain L； PDBConstruct 1–13； UniProt 680–692 Author chain M； PDBConstruct 1–13； UniProt 680–692

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

P(r) Distance Distribution P(r) Distribution

Download Download SAXS (.dat) P(r) (.pr.out) CIF

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2. Structure Basics 2. Structure Basics

Entry ID entry_id	9k0e
Deposition date deposition_date	2024-10-15
最后修订 last_revision	2025-08-06
Structure title title	Cryo-EM structure of Amyloid-beta42-4b polymorph 2
Keywords keywords	helical fibril, amyloid-beta, PROTEIN FIBRIL, MEMBRANE PROTEIN; MEMBRANE PROTEIN
Experimental Method method	ELECTRON MICROSCOPY

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3. SAXS Parameters (CRYSOL theoretical calculation) 3. SAXS Parameters (CRYSOL)

Radius of gyration Rg (Guinier) rg_guinier	27.90 Å
Radius of gyration Rg (electron density) rg_electron	27.90 Å
Forward intensity I(0) i0	10920000.00
Molecular weight molecular_weight	26623.0 kDa
Excluded volume excluded_volume	34062 Å³
Envelope volume envelope_volume	43825 Å³
Hydration-shell volume shell_volume	15471 Å³
Envelope diameter envelope_diameter	93.1 Å
Shell Rg shell_rg	30.38 Å
Envelope Rg envelope_rg	27.83 Å
Shape Rg shape_rg	28.00 Å
Total Rg total_rg	27.88 Å
Total atoms total_atoms	1884
Residues n_residues	246
Spherical-harmonic order n_harmonics	20
q range q_range	— – 0.5000 Å⁻¹
Data points n_points	101
Shell type shell_type	directional
Solvent electron density solvent_density	0.3340 e/Å³
Shell contrast contrast_shell	0.0300 e/Å³
CRYSOL version crysol_version	4.1.3

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4. P(r) Distance Distribution (GNOM inversion) 4. P(r) Analysis (GNOM)

Maximum dimension Dmax dmax	95.7 Å
Rg (real space) rg_real	28.42 Å
Rg uncertainty (real space) rg_real_error	1.15 Å
I(0) (real space) i0_real	1.0920e+07
I(0) uncertainty (real space) i0_real_error	1.8940e+05
Rg (reciprocal space) rg_reciprocal	28.26 Å
I(0) (reciprocal space) i0_reciprocal	10920000.0000
Solution quality estimate total_estimate	0.7635
Solution quality rating solution_quality	GOOD a GOOD solution
P(r) peaks n_peaks	4
Primary peak position r_peak_primary	31.9 Å
Skewness Skewness skewness	0.519
Kurtosis Kurtosis kurtosis	-0.493
Angular range angular_range	— – 0.2850 Å⁻¹
Current regularization parameter α current_alpha	0.0000
Highest regularization parameter α highest_alpha	331300.0000
Real-space data points n_real_points	58
GNOM version gnom_version	4.1.3
Quality Criteria quality_criteria	AN1: 0.000; Oscil: 0.550; Stabil: 0.999; Sysdev: 1.000; Positv: 1.000; Valcen: 0.316; Smooth: 0.957

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5. Crystallography and Experiment 5. Crystallography & Experiment

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6. Entities and Polymers Entities & Polymers (3)

Entity 1 Entity 1 polymer

Description description	Amyloid-beta A4 protein
Molecular weight formula_weight	4520.1 kDa
Source method src_method	syn
Copy count entity_count	6

Polymer Polymer

Polymer type type	polypeptide(L)
Chain IDs strand_id	G,B,N,H,O,I
Atom count atom_count	1890

DAEFRHDSGYEVHHQKLVFFAEDVGSNKGAIIGLMVGGVVIA

Entity 2 Entity 2 polymer

Description description	Amyloid-beta protein 40
Molecular weight formula_weight	1577.8 kDa
Source method src_method	syn
Copy count entity_count	6

Polymer Polymer

Polymer type type	polypeptide(L)
Chain IDs strand_id	F,A,L,D,M,E

GYEVHHQKLVFFA

Entity 3 Entity 3 water

Description description	water
Molecular weight formula_weight	18.0 kDa
Source method src_method	nat
Copy count entity_count	6

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8. Citations (1)

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Unit-cell length a length_a	1.000 Å
Unit-cell length b length_b	1.000 Å
Unit-cell length c length_c	1.000 Å
Unit-cell angle α angle_alpha	90.00 °
Unit-cell angle β angle_beta	90.00 °
Unit-cell angle γ angle_gamma	90.00 °
Molecules per unit cell Z z_pdb	—

Space group space_group	P 1
Space-group number int_tables_number	1
Crystal system crystal_system	—

Resolution resolution	2.80 Å
Resolution测定方法 resolution_method	—
颗粒数 num_particles	62839

fit	/app/data/saxs_computation/k0/9k0e/9k0e.fit
pddf	/app/data/pr_computation/k0/9k0e/9k0e.pr.out
profile	/app/data/saxs_computation/k0/9k0e/9k0e.dat

Cryo-EM structure of Amyloid-beta42-4b polymorph 2

1. Protein Identity and Related Structures Protein Identity & Related Structures

Amyloid-beta A4 protein

State in the Current Structure

Other States of the Same Protein in the Database

Amyloid-beta protein 40

State in the Current Structure

Other States of the Same Protein in the Database

SAXS scattering curve SAXS Profile

P(r) Distance Distribution P(r) Distribution

2. Structure Basics 2. Structure Basics

3. SAXS Parameters (CRYSOL theoretical calculation) 3. SAXS Parameters (CRYSOL)

4. P(r) Distance Distribution (GNOM inversion) 4. P(r) Analysis (GNOM)

5. Crystallography and Experiment 5. Crystallography & Experiment

Unit cell Unit Cell

Symmetry Symmetry

冷冻电镜 EM 3D

6. Entities and Polymers Entities & Polymers (3)

Entity 1 Entity 1 polymer

Polymer Polymer

Entity 2 Entity 2 polymer

Polymer Polymer

Entity 3 Entity 3 water

8. Citations (1)

9. Files and Curves (10)

Files (7)

Curves (3)