Amyloid-beta protein 40
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 homooligomer Homooligomer Protein × 172 PDB declaration: 172-meric（172） Consistent with protein copy count | Chain 0； UniProt 672–711 Chain 1； UniProt 672–711 Chain 2； UniProt 672–711 Chain 3； UniProt 672–711 Chain 4； UniProt 672–711 Chain 5； UniProt 672–711 Chain 6； UniProt 672–711 Chain 7； UniProt 672–711 Chain 8； UniProt 672–711 Chain 9； UniProt 672–711 Chain A； UniProt 672–711 Chain A0； UniProt 672–711 Chain A1； UniProt 672–711 Chain A2； UniProt 672–711 Chain A3； UniProt 672–711 Chain A4； UniProt 672–711 Chain A5； UniProt 672–711 Chain A6； UniProt 672–711 Chain A7； UniProt 672–711 Chain A8； UniProt 672–711 Chain A9； UniProt 672–711 Chain AA； UniProt 672–711 Chain AB； UniProt 672–711 Chain AC； UniProt 672–711 Chain AD； UniProt 672–711 Chain AE； UniProt 672–711 Chain AF； UniProt 672–711 Chain AG； UniProt 672–711 Chain AH； UniProt 672–711 Chain AI； UniProt 672–711 Chain AJ； UniProt 672–711 Chain AK； UniProt 672–711 Chain AL； UniProt 672–711 Chain AM； UniProt 672–711 Chain AN； UniProt 672–711 Chain AO； UniProt 672–711 Chain AP； UniProt 672–711 Chain AQ； UniProt 672–711 Chain AR； UniProt 672–711 Chain AS； UniProt 672–711 Chain AT； UniProt 672–711 Chain AU； UniProt 672–711 Chain AV； UniProt 672–711 Chain AW； UniProt 672–711 Chain AX； UniProt 672–711 Chain AY； UniProt 672–711 Chain AZ； UniProt 672–711 Chain Aa； UniProt 672–711 Chain Ab； UniProt 672–711 Chain Ac； UniProt 672–711 Chain Ad； UniProt 672–711 Chain Ae； UniProt 672–711 Chain Af； UniProt 672–711 Chain Ag； UniProt 672–711 Chain Ah； UniProt 672–711 Chain Ai； UniProt 672–711 Chain Aj； UniProt 672–711 Chain Ak； UniProt 672–711 Chain Al； UniProt 672–711 Chain Am； UniProt 672–711 Chain An； UniProt 672–711 Chain Ao； UniProt 672–711 Chain Ap； UniProt 672–711 Chain Aq； UniProt 672–711 Chain Ar； UniProt 672–711 Chain As； UniProt 672–711 Chain At； UniProt 672–711 Chain Au； UniProt 672–711 Chain Av； UniProt 672–711 Chain Aw； UniProt 672–711 Chain Ax； UniProt 672–711 Chain Ay； UniProt 672–711 Chain Az； UniProt 672–711 Chain B； UniProt 672–711 Chain BA； UniProt 672–711 Chain BB； UniProt 672–711 Chain BC； UniProt 672–711 Chain BD； UniProt 672–711 Chain BE； UniProt 672–711 Chain BF； UniProt 672–711 Chain BG； UniProt 672–711 Chain BH； UniProt 672–711 Chain BI； UniProt 672–711 Chain BJ； UniProt 672–711 Chain BK； UniProt 672–711 Chain BL； UniProt 672–711 Chain BM； UniProt 672–711 Chain BN； UniProt 672–711 Chain BO； UniProt 672–711 Chain BP； UniProt 672–711 Chain BQ； UniProt 672–711 Chain BR； UniProt 672–711 Chain BS； UniProt 672–711 Chain BT； UniProt 672–711 Chain BU； UniProt 672–711 Chain BV； UniProt 672–711 Chain BW； UniProt 672–711 Chain BX； UniProt 672–711 Chain BY； UniProt 672–711 Chain BZ； UniProt 672–711 Chain Ba； UniProt 672–711 Chain Bb； UniProt 672–711 Chain Bc； UniProt 672–711 Chain Bd； UniProt 672–711 Chain Be； UniProt 672–711 Chain Bf； UniProt 672–711 Chain Bg； UniProt 672–711 Chain Bh； UniProt 672–711 Chain Bi； UniProt 672–711 Chain Bj； UniProt 672–711 Chain Bk； UniProt 672–711 Chain Bl； UniProt 672–711 Chain Bm； UniProt 672–711 Chain Bn； UniProt 672–711 Chain Bo； UniProt 672–711 Chain Bp； UniProt 672–711 Chain Bq； UniProt 672–711 Chain Br； UniProt 672–711 Chain Bs； UniProt 672–711 Chain Bt； UniProt 672–711 Chain Bu； UniProt 672–711 Chain Bv； UniProt 672–711 Chain C； UniProt 672–711 Chain D； UniProt 672–711 Chain E； UniProt 672–711 Chain F； UniProt 672–711 Chain G； UniProt 672–711 Chain H； UniProt 672–711 Chain I； UniProt 672–711 Chain J； UniProt 672–711 Chain K； UniProt 672–711 Chain L； UniProt 672–711 Chain M； UniProt 672–711 Chain N； UniProt 672–711 Chain O； UniProt 672–711 Chain P； UniProt 672–711 Chain Q； UniProt 672–711 Chain R； UniProt 672–711 Chain S； UniProt 672–711 Chain T； UniProt 672–711 Chain U； UniProt 672–711 Chain V； UniProt 672–711 Chain W； UniProt 672–711 Chain X； UniProt 672–711 Chain Y； UniProt 672–711 Chain Z； UniProt 672–711 Chain a； UniProt 672–711 Chain b； UniProt 672–711 Chain c； UniProt 672–711 Chain d； UniProt 672–711 Chain e； UniProt 672–711 Chain f； UniProt 672–711 Chain g； UniProt 672–711 Chain h； UniProt 672–711 Chain i； UniProt 672–711 Chain j； UniProt 672–711 Chain k； UniProt 672–711 Chain l； UniProt 672–711 Chain m； UniProt 672–711 Chain n； UniProt 672–711 Chain o； UniProt 672–711 Chain p； UniProt 672–711 Chain q； UniProt 672–711 Chain r； UniProt 672–711 Chain s； UniProt 672–711 Chain t； UniProt 672–711 Chain u； UniProt 672–711 Chain v； UniProt 672–711 Chain w； UniProt 672–711 Chain x； UniProt 672–711 Chain y； UniProt 672–711 Chain z； UniProt 672–711 | Not recorded | No other associated polymer | ELECTRON MICROSCOPY cryo-EM buffer：pH 8 cryo-EM vitrification conditions：Cryogen ETHANE | Resolution 3.60 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 9M5R | Assembly / Oligomeric State | Construct | Mutations and Modifications | Ligands, Ions and Non-polymers | Method and Experimental Conditions | Structure Quality |
|---|---|---|---|---|---|---|---|
| 11EN Structure of Rapidly twisting Amyloid-beta 40 fibril , RT-Ab40(2_1) Deposited 2026-02-19 | Different construct Different mutation/modification Different oligomeric state Different experimental conditions Different structure-quality metrics | Assembly 1 Protein homooligomer Homooligomer；Protein × 6 PDB declaration: hexameric |
Chain A
672–711（40 aa）
Chain B
672–711（40 aa）
Chain C
672–711（40 aa）
Chain D
672–711（40 aa）
Chain E
672–711（40 aa）
Chain F
672–711（40 aa）
|
Not recorded | No recorded non-water small molecule |
ELECTRON MICROSCOPY
cryo-EM buffer
pH 7.4
cryo-EM vitrification conditions
Cryogen ETHANE
|
Resolution 2.50 Å |
| 11EO Structure of Rapidly twisting Amyloid-beta 40 fibril , RT-Ab40(C2) Deposited 2026-02-19 | Different construct Different mutation/modification Different oligomeric state Different experimental conditions Different structure-quality metrics | Assembly 1 Protein homooligomer Homooligomer；Protein × 6 PDB declaration: hexameric |
Chain A
672–711（40 aa）
Chain B
672–711（40 aa）
Chain C
672–711（40 aa）
Chain D
672–711（40 aa）
Chain E
672–711（40 aa）
Chain F
672–711（40 aa）
|
Not recorded | No recorded non-water small molecule |
ELECTRON MICROSCOPY
cryo-EM buffer
pH 7.4
cryo-EM vitrification conditions
Cryogen ETHANE
|
Resolution 2.73 Å |
| 11EP Structure of Rapidly twisting Amyloid-beta 40 fibril , RT-Ab40(C1) Deposited 2026-02-19 | Different construct Different mutation/modification Different oligomeric state Different experimental conditions Different structure-quality metrics | Assembly 1 Protein homooligomer Homooligomer；Protein × 6 PDB declaration: hexameric |
Chain A
672–711（40 aa）
Chain B
672–711（40 aa）
Chain C
672–711（40 aa）
Chain D
672–711（40 aa）
Chain E
672–711（40 aa）
Chain F
672–711（40 aa）
|
Not recorded | No recorded non-water small molecule |
ELECTRON MICROSCOPY
cryo-EM buffer
pH 7.4
cryo-EM vitrification conditions
Cryogen ETHANE
|
Resolution 2.75 Å |
| 12GB High Resolution Structure of Monomorphic AB1-40 Fibrils Deposited 2026-04-03 | Different construct Different mutation/modification Different oligomeric state Different 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 experimental conditions Different structure-quality metrics | Assembly 1 Protein homooligomer Homooligomer；Protein × 12 PDB declaration: dodecameric |
Chain A
672–713（42 aa）
Chain B
672–713（42 aa）
Chain C
672–713（42 aa）
Chain D
672–713（42 aa）
Chain E
672–713（42 aa）
Chain F
672–713（42 aa）
Chain G
672–713（42 aa）
Chain H
672–713（42 aa）
Chain I
672–713（42 aa）
Chain J
672–713（42 aa）
Chain K
672–713（42 aa）
Chain L
672–713（42 aa）
|
Not recorded | No recorded non-water small molecule |
ELECTRON MICROSCOPY
cryo-EM buffer
pH 7.4
cryo-EM vitrification conditions
Cryogen ETHANE
|
Resolution 3.40 Å |
| 2BEG 3D Structure of Alzheimer's Abeta(1-42) fibrils Deposited 2005-10-24 | Different construct Different mutation/modification Different oligomeric state Different 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 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
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 experimental conditions Different structure-quality metrics | Assembly 1 Other combination Heteromer；Protein × 5 PDB declaration: pentameric |
Chain E
688–770（83 aa）
Fragment：C83
|
Mutation：V8C | NAG 2-acetamido-2-deoxy-beta-D-glucopyranose × 6 PC1 1,2-DIACYL-SN-GLYCERO-3-PHOSPHOCHOLINE × 2 CLR CHOLESTEROL × 3 |
ELECTRON MICROSCOPY
cryo-EM buffer
pH 7.4
cryo-EM vitrification conditions
Cryogen ETHANE
|
Resolution 2.60 Å |
| 6NB9 Amyloid-Beta (20-34) with L-isoaspartate 23 Deposited 2018-12-06 | Different construct Different mutation/modification Different oligomeric state Different 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 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 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 Different structure-quality metrics | Assembly 1 Protein homooligomer Homooligomer；Protein × 10 PDB declaration: decameric |
Chain A
672–713（42 aa）
Chain B
672–713（42 aa）
Chain C
672–713（42 aa）
Chain D
672–713（42 aa）
Chain E
672–713（42 aa）
Chain F
672–713（42 aa）
Chain G
672–713（42 aa）
Chain H
672–713（42 aa）
Chain I
672–713（42 aa）
Chain J
672–713（42 aa）
|
Not recorded | UNX UNKNOWN LIGAND × 10 |
ELECTRON MICROSCOPY
cryo-EM buffer
pH 7.5
cryo-EM vitrification conditions
Cryogen ETHANE
|
Resolution 2.80 Å |
| 7RTZ X-ray crystallographic structure of a beta-hairpin peptide derived from amyloid beta 14-40 Deposited 2021-08-16 | Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental 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 Different structure-quality metrics | Assembly 1 Protein homooligomer Homooligomer；Protein × 6 PDB declaration: hexameric |
Chain A
672–713（42 aa）
Chain B
672–713（42 aa）
|
Not recorded | No recorded non-water small molecule |
ELECTRON MICROSCOPY
cryo-EM buffer
pH 7.5
cryo-EM vitrification conditions
Cryogen ETHANE
|
Resolution 2.80 Å |
| 8BG0 Amyloid-beta tetrameric filaments with the Arctic mutation (E22G) from Alzheimer's disease brains | ABeta40 Deposited 2022-10-27 | Different construct Different mutation/modification Different oligomeric state Different 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 experimental conditions Different structure-quality metrics | Assembly 1 Protein homooligomer Homooligomer；Protein × 10 PDB declaration: decameric |
Chain A
653–692（40 aa）
Fragment：UNP residues 653-692
Chain B
653–692（40 aa）
Fragment：UNP residues 653-692
Chain C
653–692（40 aa）
Fragment：UNP residues 653-692
Chain D
653–692（40 aa）
Fragment：UNP residues 653-692
Chain E
653–692（40 aa）
Fragment：UNP residues 653-692
Chain F
653–692（40 aa）
Fragment：UNP residues 653-692
Chain G
653–692（40 aa）
Fragment：UNP residues 653-692
Chain I
653–692（40 aa）
Fragment：UNP residues 653-692
Chain J
653–692（40 aa）
Fragment：UNP residues 653-692
Chain K
653–692（40 aa）
Fragment：UNP residues 653-692
|
Not recorded | No recorded non-water small molecule |
ELECTRON MICROSCOPY
cryo-EM buffer
pH 7.4
cryo-EM vitrification conditions
Cryogen ETHANE
|
Resolution 2.87 Å |
| 8FF3 Amyloid-beta (1-40) fibrils derived from familial Dutch-type CAA patient (population B) Deposited 2022-12-07 | Different construct Different mutation/modification Different oligomeric state Different experimental conditions Different structure-quality metrics | Assembly 1 Protein homooligomer Homooligomer；Protein × 6 PDB declaration: hexameric |
Chain A
653–692（40 aa）
Fragment：UNP residues 653-692
Chain B
653–692（40 aa）
Fragment：UNP residues 653-692
Chain C
653–692（40 aa）
Fragment：UNP residues 653-692
Chain a
653–692（40 aa）
Fragment：UNP residues 653-692
Chain b
653–692（40 aa）
Fragment：UNP residues 653-692
Chain c
653–692（40 aa）
Fragment：UNP residues 653-692
|
Not recorded | No recorded non-water small molecule |
ELECTRON MICROSCOPY
cryo-EM buffer
pH 7.4
cryo-EM vitrification conditions
Cryogen ETHANE
|
Resolution 3.09 Å |
| 8KEW The cryo-EM structure of type1 amyloid beta 42 fibril. Deposited 2023-08-13 | Different construct Different mutation/modification Different oligomeric state Different 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 mutation/modification 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 mutation/modification 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 experimental conditions Different structure-quality metrics | Assembly 1 Protein homooligomer Homooligomer；Protein × 10 PDB declaration: decameric |
Chain A
672–713（42 aa）
Chain B
672–713（42 aa）
Chain C
672–713（42 aa）
Chain D
672–713（42 aa）
Chain E
672–713（42 aa）
Chain F
672–713（42 aa）
Chain G
672–713（42 aa）
Chain H
672–713（42 aa）
Chain I
672–713（42 aa）
Chain J
672–713（42 aa）
|
Not recorded | No recorded non-water small molecule |
ELECTRON MICROSCOPY
cryo-EM buffer
pH 7.4
cryo-EM vitrification conditions
Cryogen ETHANE
|
Resolution 3.00 Å |
| 8OL3 Murine type III Abeta fibril from APP/PS1 mouse Deposited 2023-03-30 | Different construct Different mutation/modification Different oligomeric state Different experimental conditions Different structure-quality metrics | Assembly 1 Protein homooligomer Homooligomer；Protein × 10 PDB declaration: decameric |
Chain A
672–713（42 aa）
Chain B
672–713（42 aa）
Chain C
672–713（42 aa）
Chain D
672–713（42 aa）
Chain E
672–713（42 aa）
Chain F
672–713（42 aa）
Chain G
672–713（42 aa）
Chain H
672–713（42 aa）
Chain I
672–713（42 aa）
Chain J
672–713（42 aa）
|
Not recorded | No recorded non-water small molecule |
ELECTRON MICROSCOPY
cryo-EM buffer
pH 7.4
cryo-EM vitrification conditions
Cryogen ETHANE
|
Resolution 3.50 Å |
| 8OL5 Murine type II Abeta fibril from ARTE10 mouse Deposited 2023-03-30 | Different construct Different mutation/modification Different oligomeric state Different experimental conditions Different structure-quality metrics | Assembly 1 Protein homooligomer Homooligomer；Protein × 10 PDB declaration: decameric |
Chain A
672–713（42 aa）
Chain B
672–713（42 aa）
Chain C
672–713（42 aa）
Chain D
672–713（42 aa）
Chain E
672–713（42 aa）
Chain F
672–713（42 aa）
Chain G
672–713（42 aa）
Chain H
672–713（42 aa）
Chain I
672–713（42 aa）
Chain J
672–713（42 aa）
|
Not recorded | No recorded non-water small molecule |
ELECTRON MICROSCOPY
cryo-EM buffer
pH 7.4
cryo-EM vitrification conditions
Cryogen ETHANE
|
Resolution 3.40 Å |
| 8OL6 Murine type II Abeta fibril from tgAPPSwe mouse Deposited 2023-03-30 | Different construct Different mutation/modification Different oligomeric state Different experimental conditions Different structure-quality metrics | Assembly 1 Protein homooligomer Homooligomer；Protein × 10 PDB declaration: decameric |
Chain A
672–713（42 aa）
Chain B
672–713（42 aa）
Chain C
672–713（42 aa）
Chain D
672–713（42 aa）
Chain E
672–713（42 aa）
Chain F
672–713（42 aa）
Chain G
672–713（42 aa）
Chain H
672–713（42 aa）
Chain I
672–713（42 aa）
Chain J
672–713（42 aa）
|
Not recorded | No recorded non-water small molecule |
ELECTRON MICROSCOPY
cryo-EM buffer
pH 7.4
cryo-EM vitrification conditions
Cryogen ETHANE
|
Resolution 3.80 Å |
| 8OL7 MurineArc type I Abeta fibril from tg-APPArcSwe mouse Deposited 2023-03-30 | Different construct Different mutation/modification Different oligomeric state Different experimental conditions Different structure-quality metrics | Assembly 1 Protein homooligomer Homooligomer；Protein × 10 PDB declaration: decameric |
Chain A
672–713（42 aa）
Chain B
672–713（42 aa）
Chain C
672–713（42 aa）
Chain D
672–713（42 aa）
Chain E
672–713（42 aa）
Chain F
672–713（42 aa）
Chain G
672–713（42 aa）
Chain H
672–713（42 aa）
Chain I
672–713（42 aa）
Chain J
672–713（42 aa）
|
Not recorded | No recorded non-water small molecule |
ELECTRON MICROSCOPY
cryo-EM buffer
pH 7.4
cryo-EM vitrification conditions
Cryogen ETHANE
|
Resolution 3.00 Å |
| 8OLG DI2 Abeta fibril from tg-SwDI mouse Deposited 2023-03-30 | Different construct Different mutation/modification Different oligomeric state Different experimental conditions Different structure-quality metrics | Assembly 1 Protein homooligomer Homooligomer；Protein × 5 PDB declaration: pentameric |
Chain A
672–713（42 aa）
Chain B
672–713（42 aa）
Chain C
672–713（42 aa）
Chain D
672–713（42 aa）
Chain E
672–713（42 aa）
|
Not recorded | No recorded non-water small molecule |
ELECTRON MICROSCOPY
cryo-EM buffer
pH 7.4
cryo-EM vitrification conditions
Cryogen ETHANE
|
Resolution 4.20 Å |
| 8OLN DI1 Abeta fibril from tg-SwDI mouse Deposited 2023-03-30 | Different construct Different mutation/modification Different oligomeric state Different experimental conditions Different structure-quality metrics | Assembly 1 Protein homooligomer Homooligomer；Protein × 10 PDB declaration: decameric |
Chain A
672–713（42 aa）
Chain B
672–713（42 aa）
Chain C
672–713（42 aa）
Chain D
672–713（42 aa）
Chain E
672–713（42 aa）
Chain F
672–713（42 aa）
Chain G
672–713（42 aa）
Chain H
672–713（42 aa）
Chain I
672–713（42 aa）
Chain J
672–713（42 aa）
|
Not recorded | No recorded non-water small molecule |
ELECTRON MICROSCOPY
cryo-EM buffer
pH 7.4
cryo-EM vitrification conditions
Cryogen ETHANE
|
Resolution 3.30 Å |
| 8OLO Murine type III Abeta fibril from ARTE10 mouse Deposited 2023-03-30 | Different construct Different mutation/modification Different oligomeric state Different experimental conditions Different structure-quality metrics | Assembly 1 Protein homooligomer Homooligomer；Protein × 10 PDB declaration: decameric |
Chain A
672–713（42 aa）
Chain B
672–713（42 aa）
Chain C
672–713（42 aa）
Chain D
672–713（42 aa）
Chain E
672–713（42 aa）
Chain F
672–713（42 aa）
Chain G
672–713（42 aa）
Chain H
672–713（42 aa）
Chain I
672–713（42 aa）
Chain J
672–713（42 aa）
|
Not recorded | No recorded non-water small molecule |
ELECTRON MICROSCOPY
cryo-EM buffer
pH 7.4
cryo-EM vitrification conditions
Cryogen ETHANE
|
Resolution 3.50 Å |
| 8OLQ DI3 Abeta fibril from tg-SwDI mouse Deposited 2023-03-30 | Different construct Different mutation/modification Different oligomeric state Different experimental conditions Different structure-quality metrics | Assembly 1 Protein homooligomer Homooligomer；Protein × 5 PDB declaration: pentameric |
Chain A
672–713（42 aa）
Chain B
672–713（42 aa）
Chain C
672–713（42 aa）
Chain D
672–713（42 aa）
Chain E
672–713（42 aa）
|
Not recorded | No recorded non-water small molecule |
ELECTRON MICROSCOPY
cryo-EM buffer
pH 7.4
cryo-EM vitrification conditions
Cryogen ETHANE
|
Resolution 4.00 Å |
| 8OTF Ab typeII filament from Guam ALS/PDC Deposited 2023-04-20 | Different construct Different mutation/modification Different oligomeric state Different experimental conditions Different structure-quality metrics | Assembly 1 Protein homooligomer Homooligomer；Protein × 6 PDB declaration: hexameric |
Chain A
1–770（770 aa）
Chain B
1–770（770 aa）
Chain C
1–770（770 aa）
Chain D
1–770（770 aa）
Chain E
1–770（770 aa）
Chain F
1–770（770 aa）
|
Not recorded | No recorded non-water small molecule |
ELECTRON MICROSCOPY
cryo-EM buffer
pH 7.4
cryo-EM vitrification conditions
Cryogen ETHANE
|
Resolution 3.30 Å |
| 8SEJ Type I beta-amyloid 42 Filaments from Down syndrome Deposited 2023-04-10 | Different construct Different mutation/modification Different oligomeric state Different 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 experimental conditions Different structure-quality metrics | Assembly 1 Protein homooligomer Homooligomer；Protein × 10 PDB declaration: decameric |
Chain A
672–711（40 aa）
Chain B
672–711（40 aa）
Chain C
672–711（40 aa）
Chain D
672–711（40 aa）
Chain E
672–711（40 aa）
Chain F
672–711（40 aa）
Chain G
672–711（40 aa）
Chain H
672–711（40 aa）
Chain I
672–711（40 aa）
Chain J
672–711（40 aa）
|
Not recorded | No recorded non-water small molecule |
ELECTRON MICROSCOPY
cryo-EM buffer
pH 7.4
cryo-EM vitrification conditions
Cryogen ETHANE
|
Resolution 3.50 Å |
| 8SEL Type IIIb beta-amyloid 40 Filaments from Down Syndrome Deposited 2023-04-10 | Different construct Different mutation/modification Different oligomeric state Different experimental conditions Different structure-quality metrics | Assembly 1 Protein homooligomer Homooligomer；Protein × 20 PDB declaration: eicosameric |
Chain A
672–711（40 aa）
Chain B
672–711（40 aa）
Chain C
672–711（40 aa）
Chain D
672–711（40 aa）
Chain E
672–711（40 aa）
Chain F
672–711（40 aa）
Chain G
672–711（40 aa）
Chain H
672–711（40 aa）
Chain I
672–711（40 aa）
Chain J
672–711（40 aa）
Chain K
672–711（40 aa）
Chain L
672–711（40 aa）
Chain M
672–711（40 aa）
Chain N
672–711（40 aa）
Chain O
672–711（40 aa）
Chain P
672–711（40 aa）
Chain Q
672–711（40 aa）
Chain R
672–711（40 aa）
Chain S
672–711（40 aa）
Chain T
672–711（40 aa）
|
Not recorded | No recorded non-water small molecule |
ELECTRON MICROSCOPY
cryo-EM buffer
pH 7.4
cryo-EM vitrification conditions
Cryogen ETHANE
|
Resolution 3.80 Å |
| 8X52 Cryo-EM structure of human gamma-secretase in complex with Abeta49 Deposited 2023-11-16 | Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental conditions Different structure-quality metrics | Assembly 1 Other combination Heteromer；Protein × 5 PDB declaration: pentameric |
Chain E
540–639（100 aa）
|
Not recorded | NAG 2-acetamido-2-deoxy-beta-D-glucopyranose × 6 PC1 1,2-DIACYL-SN-GLYCERO-3-PHOSPHOCHOLINE × 2 CLR CHOLESTEROL × 2 |
ELECTRON MICROSCOPY
cryo-EM buffer
pH 7.4
cryo-EM vitrification conditions
Cryogen ETHANE
|
Resolution 2.90 Å |
| 8X53 Cryo-EM structure of human gamma-secretase in complex with Abeta46 Deposited 2023-11-16 | Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental conditions Different structure-quality metrics | Assembly 1 Other combination Heteromer；Protein × 5 PDB declaration: pentameric |
Chain E
541–586（46 aa）
|
Not recorded | NAG 2-acetamido-2-deoxy-beta-D-glucopyranose × 6 PC1 1,2-DIACYL-SN-GLYCERO-3-PHOSPHOCHOLINE × 3 CLR CHOLESTEROL × 2 |
ELECTRON MICROSCOPY
cryo-EM buffer
pH 7.4
cryo-EM vitrification conditions
Cryogen ETHANE
|
Resolution 3.00 Å |
| 8X54 Cryo-EM structure of human gamma-secretase in complex with APP-C99 Deposited 2023-11-16 | Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental conditions Different structure-quality metrics | Assembly 1 Other combination Heteromer；Protein × 5 PDB declaration: pentameric |
Chain E
540–639（100 aa）
|
Not recorded | NAG 2-acetamido-2-deoxy-beta-D-glucopyranose × 6 PC1 1,2-DIACYL-SN-GLYCERO-3-PHOSPHOCHOLINE × 3 CLR CHOLESTEROL × 3 |
ELECTRON MICROSCOPY
cryo-EM buffer
pH 7.4
cryo-EM vitrification conditions
Cryogen ETHANE
|
Resolution 2.90 Å |
| 8Z9V Amyloid beta and TTR Deposited 2024-04-23 | Different construct Different 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 Different structure-quality metrics | Assembly 1 Protein homooligomer Homooligomer；Protein × 10 PDB declaration: decameric |
Chain A
672–713（42 aa）
Fragment：UNP residues 672-713
Chain B
672–713（42 aa）
Fragment：UNP residues 672-713
Chain C
672–713（42 aa）
Fragment：UNP residues 672-713
Chain D
672–713（42 aa）
Fragment：UNP residues 672-713
Chain E
672–713（42 aa）
Fragment：UNP residues 672-713
Chain F
672–713（42 aa）
Fragment：UNP residues 672-713
Chain G
672–713（42 aa）
Fragment：UNP residues 672-713
Chain H
672–713（42 aa）
Fragment：UNP residues 672-713
Chain I
672–713（42 aa）
Fragment：UNP residues 672-713
Chain J
672–713（42 aa）
Fragment：UNP residues 672-713
|
Not recorded | No recorded non-water small molecule |
ELECTRON MICROSCOPY
cryo-EM buffer
pH 7.4
cryo-EM vitrification conditions
Cryogen NITROGEN
|
Resolution 2.80 Å |
| 9CZN Type Ic amyloid-beta 42 filaments in dominantly inherited Alzheimer disease with cotton wool plaques Deposited 2024-08-05 | Different construct Different mutation/modification Different oligomeric state Different experimental conditions Different structure-quality metrics | Assembly 1 Protein homooligomer Homooligomer；Protein × 20 PDB declaration: eicosameric |
Chain A
680–713（34 aa）
Fragment：UNP residues 680-713
Chain B
680–713（34 aa）
Fragment：UNP residues 680-713
Chain C
680–713（34 aa）
Fragment：UNP residues 680-713
Chain D
680–713（34 aa）
Fragment：UNP residues 680-713
Chain E
680–713（34 aa）
Fragment：UNP residues 680-713
Chain F
680–713（34 aa）
Fragment：UNP residues 680-713
Chain G
680–713（34 aa）
Fragment：UNP residues 680-713
Chain H
680–713（34 aa）
Fragment：UNP residues 680-713
Chain I
680–713（34 aa）
Fragment：UNP residues 680-713
Chain J
680–713（34 aa）
Fragment：UNP residues 680-713
Chain K
680–713（34 aa）
Fragment：UNP residues 680-713
Chain L
680–713（34 aa）
Fragment：UNP residues 680-713
Chain M
680–713（34 aa）
Fragment：UNP residues 680-713
Chain N
680–713（34 aa）
Fragment：UNP residues 680-713
Chain O
680–713（34 aa）
Fragment：UNP residues 680-713
Chain P
680–713（34 aa）
Fragment：UNP residues 680-713
Chain Q
680–713（34 aa）
Fragment：UNP residues 680-713
Chain R
680–713（34 aa）
Fragment：UNP residues 680-713
Chain S
680–713（34 aa）
Fragment：UNP residues 680-713
Chain T
680–713（34 aa）
Fragment：UNP residues 680-713
|
Not recorded | No recorded non-water small molecule |
ELECTRON MICROSCOPY
cryo-EM buffer
pH 7.4
cryo-EM vitrification conditions
Cryogen ETHANE
|
Resolution 2.60 Å |
| 9CZP Type Id amyloid-beta 42 filaments in dominantly inherited Alzheimer disease with cotton wool plaques Deposited 2024-08-05 | Different construct Different mutation/modification Different oligomeric state Different experimental conditions Different structure-quality metrics | Assembly 1 Protein homooligomer Homooligomer；Protein × 20 PDB declaration: eicosameric |
Chain A
680–713（34 aa）
Fragment：UNP residues 680-713
Chain B
680–713（34 aa）
Fragment：UNP residues 680-713
Chain C
680–713（34 aa）
Fragment：UNP residues 680-713
Chain D
680–713（34 aa）
Fragment：UNP residues 680-713
Chain E
680–713（34 aa）
Fragment：UNP residues 680-713
Chain F
680–713（34 aa）
Fragment：UNP residues 680-713
Chain G
680–713（34 aa）
Fragment：UNP residues 680-713
Chain H
680–713（34 aa）
Fragment：UNP residues 680-713
Chain I
680–713（34 aa）
Fragment：UNP residues 680-713
Chain J
680–713（34 aa）
Fragment：UNP residues 680-713
Chain K
680–713（34 aa）
Fragment：UNP residues 680-713
Chain L
680–713（34 aa）
Fragment：UNP residues 680-713
Chain M
680–713（34 aa）
Fragment：UNP residues 680-713
Chain N
680–713（34 aa）
Fragment：UNP residues 680-713
Chain O
680–713（34 aa）
Fragment：UNP residues 680-713
Chain P
680–713（34 aa）
Fragment：UNP residues 680-713
Chain Q
680–713（34 aa）
Fragment：UNP residues 680-713
Chain R
680–713（34 aa）
Fragment：UNP residues 680-713
Chain S
680–713（34 aa）
Fragment：UNP residues 680-713
Chain T
680–713（34 aa）
Fragment：UNP residues 680-713
|
Not recorded | No recorded non-water small molecule |
ELECTRON MICROSCOPY
cryo-EM buffer
pH 7.4
cryo-EM vitrification conditions
Cryogen ETHANE
|
Resolution 3.30 Å |
| 9FH2 Cryo-EM Structure of Amyloid-beta Fibrils Carrying the Uppsala AbetaUpp(1-42)delta(19-24) Mutation - Polymorph 1 Deposited 2024-05-26 | Different construct Different mutation/modification Different oligomeric state Different 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 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 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 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 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 structure-quality metrics | Assembly 1 Protein homooligomer Homooligomer；Protein × 15 PDB declaration: pentadecameric |
Chain A
672–713（42 aa）
Chain B
672–713（42 aa）
Chain BA
672–713（42 aa）
Chain BB
672–713（42 aa）
Chain BC
672–713（42 aa）
Chain BD
672–713（42 aa）
Chain BE
672–713（42 aa）
Chain C
672–713（42 aa）
Chain CA
672–713（42 aa）
Chain CB
672–713（42 aa）
Chain CC
672–713（42 aa）
Chain CD
672–713（42 aa）
Chain CE
672–713（42 aa）
Chain D
672–713（42 aa）
Chain E
672–713（42 aa）
|
Non-standard monomer：Yes (specific site not provided by mmCIF) Non-standard monomer：Yes (specific site not provided by mmCIF) Non-standard monomer：Yes (specific site not provided by mmCIF) Non-standard monomer：Yes (specific site not provided by mmCIF) Non-standard monomer：Yes (specific site not provided by mmCIF) Non-standard monomer：Yes (specific site not provided by mmCIF) Non-standard monomer：Yes (specific site not provided by mmCIF) Non-standard monomer：Yes (specific site not provided by mmCIF) Non-standard monomer：Yes (specific site not provided by mmCIF) Non-standard monomer：Yes (specific site not provided by mmCIF) Non-standard monomer：Yes (specific site not provided by mmCIF) Non-standard monomer：Yes (specific site not provided by mmCIF) Non-standard monomer：Yes (specific site not provided by mmCIF) Non-standard monomer：Yes (specific site not provided by mmCIF) Non-standard monomer：Yes (specific site not provided by mmCIF) | No recorded non-water small molecule |
ELECTRON MICROSCOPY
cryo-EM buffer
pH 8
cryo-EM vitrification conditions
Cryogen ETHANE
|
Resolution 2.90 Å |
| 9K0D Cryo-EM structure of Amyloid-beta42-4b polymorph 1 Deposited 2024-10-15 | Different construct Different mutation/modification Different oligomeric state Different experimental conditions Different structure-quality metrics | Assembly 1 Protein heterocomplex Heteromer；Protein × 18 PDB declaration: 18-meric |
Chain B
680–692（13 aa）
Chain F
680–692（13 aa）
Chain K
680–692（13 aa）
Chain L
680–692（13 aa）
Chain S
680–692（13 aa）
Chain T
680–692（13 aa）
|
Not recorded | No recorded non-water small molecule |
ELECTRON MICROSCOPY
cryo-EM buffer
pH 7.4
cryo-EM vitrification conditions
Cryogen ETHANE
|
Resolution 2.60 Å |
| 9K0E Cryo-EM structure of Amyloid-beta42-4b polymorph 2 Deposited 2024-10-15 | Different construct Different mutation/modification Different oligomeric state Different experimental conditions Different structure-quality metrics | Assembly 1 Protein heterocomplex Heteromer；Protein × 12 PDB declaration: 12-meric |
Chain A
680–692（13 aa）
Chain D
680–692（13 aa）
Chain E
680–692（13 aa）
Chain F
680–692（13 aa）
Chain L
680–692（13 aa）
Chain M
680–692（13 aa）
|
Not recorded | No recorded non-water small molecule |
ELECTRON MICROSCOPY
cryo-EM buffer
pH 7.4
cryo-EM vitrification conditions
Cryogen ETHANE
|
Resolution 2.80 Å |
| 9K0F Cryo-EM structure of Amyloid-beta42-4b polymorph 3 Deposited 2024-10-15 | Different construct Different mutation/modification Different oligomeric state Different experimental conditions Different structure-quality metrics | Assembly 1 Protein heterocomplex Heteromer；Protein × 12 PDB declaration: 12-meric |
Chain K
680–692（13 aa）
Chain N
680–692（13 aa）
Chain O
680–692（13 aa）
|
Not recorded | No recorded non-water small molecule |
ELECTRON MICROSCOPY
cryo-EM buffer
pH 7.4
cryo-EM vitrification conditions
Cryogen ETHANE
|
Resolution 2.80 Å |
| 9LLM Structure of C-Terminal of AB40 Peptide containing GXXXG Motif in SDS Micelles Deposited 2025-01-17 | Different construct Different 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 mutation/modification Different oligomeric state 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 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 |
| 9OBK A-beta42-Met-R-SO amyloidal fibril 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 × 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 experimental conditions Different structure-quality metrics | Assembly 1 Protein homooligomer Homooligomer；Protein × 10 PDB declaration: decameric |
Chain A
688–713（26 aa）
Chain B
688–713（26 aa）
Chain C
688–713（26 aa）
Chain D
688–713（26 aa）
Chain E
688–713（26 aa）
Chain F
688–713（26 aa）
Chain G
688–713（26 aa）
Chain H
688–713（26 aa）
Chain I
688–713（26 aa）
Chain J
688–713（26 aa）
|
Non-standard monomer：Yes (specific site not provided by mmCIF) Non-standard monomer：Yes (specific site not provided by mmCIF) Non-standard monomer：Yes (specific site not provided by mmCIF) Non-standard monomer：Yes (specific site not provided by mmCIF) Non-standard monomer：Yes (specific site not provided by mmCIF) Non-standard monomer：Yes (specific site not provided by mmCIF) Non-standard monomer：Yes (specific site not provided by mmCIF) Non-standard monomer：Yes (specific site not provided by mmCIF) Non-standard monomer：Yes (specific site not provided by mmCIF) Non-standard monomer：Yes (specific site not provided by mmCIF) | No recorded non-water small molecule |
ELECTRON MICROSCOPY
cryo-EM buffer
pH 7.4
cryo-EM vitrification conditions
Cryogen ETHANE
|
Resolution 3.64 Å |
| 9RIV Population B fibril generated from the Heterotypic interaction of Abeta40 and Medin. Deposited 2025-06-11 | Different construct Different mutation/modification Different oligomeric state Different 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 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 experimental conditions Different structure-quality metrics | Assembly 1 Protein homooligomer Homooligomer；Protein × 12 PDB declaration: dodecameric |
Chain A
672–713（42 aa）
Chain B
672–713（42 aa）
Chain C
672–713（42 aa）
Chain D
672–713（42 aa）
Chain E
672–713（42 aa）
Chain F
672–713（42 aa）
Chain G
672–713（42 aa）
Chain H
672–713（42 aa）
Chain I
672–713（42 aa）
Chain J
672–713（42 aa）
Chain K
672–713（42 aa）
Chain L
672–713（42 aa）
|
Not recorded | No recorded non-water small molecule |
ELECTRON MICROSCOPY
cryo-EM buffer
pH 7.4
cryo-EM vitrification conditions
Cryogen ETHANE
|
Resolution 3.50 Å |
| 9WAP Structure of Type II Abeta fibrils from AppNL-FPsen1P117L mice Deposited 2025-08-12 | Different construct Different mutation/modification Different oligomeric state Different experimental conditions Different structure-quality metrics | Assembly 1 Protein homooligomer Homooligomer；Protein × 12 PDB declaration: dodecameric |
Chain A
672–713（42 aa）
Chain B
672–713（42 aa）
Chain C
672–713（42 aa）
Chain D
672–713（42 aa）
Chain E
672–713（42 aa）
Chain F
672–713（42 aa）
Chain G
672–713（42 aa）
Chain H
672–713（42 aa）
Chain I
672–713（42 aa）
Chain J
672–713（42 aa）
Chain K
672–713（42 aa）
Chain L
672–713（42 aa）
|
Not recorded | No recorded non-water small molecule |
ELECTRON MICROSCOPY
cryo-EM buffer
pH 7.4
cryo-EM vitrification conditions
Cryogen ETHANE
|
Resolution 3.22 Å |
211 other PDB entries and 282 assemblies. Open the comparison page and filter oligomeric states
View Construct and Data Evidence
| UniProt name | A4_HUMAN |
| Isoform | — |
| PDB entities | 1 |
| Chains and sequence ranges | Author chain 0； PDBConstruct 1–40； UniProt 672–711 Author chain 1； PDBConstruct 1–40； UniProt 672–711 Author chain 2； PDBConstruct 1–40； UniProt 672–711 Author chain 3； PDBConstruct 1–40； UniProt 672–711 Author chain 4； PDBConstruct 1–40； UniProt 672–711 Author chain 5； PDBConstruct 1–40； UniProt 672–711 Author chain 6； PDBConstruct 1–40； UniProt 672–711 Author chain 7； PDBConstruct 1–40； UniProt 672–711 Author chain 8； PDBConstruct 1–40； UniProt 672–711 Author chain 9； PDBConstruct 1–40； UniProt 672–711 Author chain A； PDBConstruct 1–40； UniProt 672–711 Author chain A0； PDBConstruct 1–40； UniProt 672–711 Author chain A1； PDBConstruct 1–40； UniProt 672–711 Author chain A2； PDBConstruct 1–40； UniProt 672–711 Author chain A3； PDBConstruct 1–40； UniProt 672–711 Author chain A4； PDBConstruct 1–40； UniProt 672–711 Author chain A5； PDBConstruct 1–40； UniProt 672–711 Author chain A6； PDBConstruct 1–40； UniProt 672–711 Author chain A7； PDBConstruct 1–40； UniProt 672–711 Author chain A8； PDBConstruct 1–40； UniProt 672–711 Author chain A9； PDBConstruct 1–40； UniProt 672–711 Author chain AA； PDBConstruct 1–40； UniProt 672–711 Author chain AB； PDBConstruct 1–40； UniProt 672–711 Author chain AC； PDBConstruct 1–40； UniProt 672–711 Author chain AD； PDBConstruct 1–40； UniProt 672–711 Author chain AE； PDBConstruct 1–40； UniProt 672–711 Author chain AF； PDBConstruct 1–40； UniProt 672–711 Author chain AG； PDBConstruct 1–40； UniProt 672–711 Author chain AH； PDBConstruct 1–40； UniProt 672–711 Author chain AI； PDBConstruct 1–40； UniProt 672–711 Author chain AJ； PDBConstruct 1–40； UniProt 672–711 Author chain AK； PDBConstruct 1–40； UniProt 672–711 Author chain AL； PDBConstruct 1–40； UniProt 672–711 Author chain AM； PDBConstruct 1–40； UniProt 672–711 Author chain AN； PDBConstruct 1–40； UniProt 672–711 Author chain AO； PDBConstruct 1–40； UniProt 672–711 Author chain AP； PDBConstruct 1–40； UniProt 672–711 Author chain AQ； PDBConstruct 1–40； UniProt 672–711 Author chain AR； PDBConstruct 1–40； UniProt 672–711 Author chain AS； PDBConstruct 1–40； UniProt 672–711 Author chain AT； PDBConstruct 1–40； UniProt 672–711 Author chain AU； PDBConstruct 1–40； UniProt 672–711 Author chain AV； PDBConstruct 1–40； UniProt 672–711 Author chain AW； PDBConstruct 1–40； UniProt 672–711 Author chain AX； PDBConstruct 1–40； UniProt 672–711 Author chain AY； PDBConstruct 1–40； UniProt 672–711 Author chain AZ； PDBConstruct 1–40； UniProt 672–711 Author chain Aa； PDBConstruct 1–40； UniProt 672–711 Author chain Ab； PDBConstruct 1–40； UniProt 672–711 Author chain Ac； PDBConstruct 1–40； UniProt 672–711 Author chain Ad； PDBConstruct 1–40； UniProt 672–711 Author chain Ae； PDBConstruct 1–40； UniProt 672–711 Author chain Af； PDBConstruct 1–40； UniProt 672–711 Author chain Ag； PDBConstruct 1–40； UniProt 672–711 Author chain Ah； PDBConstruct 1–40； UniProt 672–711 Author chain Ai； PDBConstruct 1–40； UniProt 672–711 Author chain Aj； PDBConstruct 1–40； UniProt 672–711 Author chain Ak； PDBConstruct 1–40； UniProt 672–711 Author chain Al； PDBConstruct 1–40； UniProt 672–711 Author chain Am； PDBConstruct 1–40； UniProt 672–711 Author chain An； PDBConstruct 1–40； UniProt 672–711 Author chain Ao； PDBConstruct 1–40； UniProt 672–711 Author chain Ap； PDBConstruct 1–40； UniProt 672–711 Author chain Aq； PDBConstruct 1–40； UniProt 672–711 Author chain Ar； PDBConstruct 1–40； UniProt 672–711 Author chain As； PDBConstruct 1–40； UniProt 672–711 Author chain At； PDBConstruct 1–40； UniProt 672–711 Author chain Au； PDBConstruct 1–40； UniProt 672–711 Author chain Av； PDBConstruct 1–40； UniProt 672–711 Author chain Aw； PDBConstruct 1–40； UniProt 672–711 Author chain Ax； PDBConstruct 1–40； UniProt 672–711 Author chain Ay； PDBConstruct 1–40； UniProt 672–711 Author chain Az； PDBConstruct 1–40； UniProt 672–711 Author chain B； PDBConstruct 1–40； UniProt 672–711 Author chain BA； PDBConstruct 1–40； UniProt 672–711 Author chain BB； PDBConstruct 1–40； UniProt 672–711 Author chain BC； PDBConstruct 1–40； UniProt 672–711 Author chain BD； PDBConstruct 1–40； UniProt 672–711 Author chain BE； PDBConstruct 1–40； UniProt 672–711 Author chain BF； PDBConstruct 1–40； UniProt 672–711 Author chain BG； PDBConstruct 1–40； UniProt 672–711 Author chain BH； PDBConstruct 1–40； UniProt 672–711 Author chain BI； PDBConstruct 1–40； UniProt 672–711 Author chain BJ； PDBConstruct 1–40； UniProt 672–711 Author chain BK； PDBConstruct 1–40； UniProt 672–711 Author chain BL； PDBConstruct 1–40； UniProt 672–711 Author chain BM； PDBConstruct 1–40； UniProt 672–711 Author chain BN； PDBConstruct 1–40； UniProt 672–711 Author chain BO； PDBConstruct 1–40； UniProt 672–711 Author chain BP； PDBConstruct 1–40； UniProt 672–711 Author chain BQ； PDBConstruct 1–40； UniProt 672–711 Author chain BR； PDBConstruct 1–40； UniProt 672–711 Author chain BS； PDBConstruct 1–40； UniProt 672–711 Author chain BT； PDBConstruct 1–40； UniProt 672–711 Author chain BU； PDBConstruct 1–40； UniProt 672–711 Author chain BV； PDBConstruct 1–40； UniProt 672–711 Author chain BW； PDBConstruct 1–40； UniProt 672–711 Author chain BX； PDBConstruct 1–40； UniProt 672–711 Author chain BY； PDBConstruct 1–40； UniProt 672–711 Author chain BZ； PDBConstruct 1–40； UniProt 672–711 Author chain Ba； PDBConstruct 1–40； UniProt 672–711 Author chain Bb； PDBConstruct 1–40； UniProt 672–711 Author chain Bc； PDBConstruct 1–40； UniProt 672–711 Author chain Bd； PDBConstruct 1–40； UniProt 672–711 Author chain Be； PDBConstruct 1–40； UniProt 672–711 Author chain Bf； PDBConstruct 1–40； UniProt 672–711 Author chain Bg； PDBConstruct 1–40； UniProt 672–711 Author chain Bh； PDBConstruct 1–40； UniProt 672–711 Author chain Bi； PDBConstruct 1–40； UniProt 672–711 Author chain Bj； PDBConstruct 1–40； UniProt 672–711 Author chain Bk； PDBConstruct 1–40； UniProt 672–711 Author chain Bl； PDBConstruct 1–40； UniProt 672–711 Author chain Bm； PDBConstruct 1–40； UniProt 672–711 Author chain Bn； PDBConstruct 1–40； UniProt 672–711 Author chain Bo； PDBConstruct 1–40； UniProt 672–711 Author chain Bp； PDBConstruct 1–40； UniProt 672–711 Author chain Bq； PDBConstruct 1–40； UniProt 672–711 Author chain Br； PDBConstruct 1–40； UniProt 672–711 Author chain Bs； PDBConstruct 1–40； UniProt 672–711 Author chain Bt； PDBConstruct 1–40； UniProt 672–711 Author chain Bu； PDBConstruct 1–40； UniProt 672–711 Author chain Bv； PDBConstruct 1–40； UniProt 672–711 Author chain C； PDBConstruct 1–40； UniProt 672–711 Author chain D； PDBConstruct 1–40； UniProt 672–711 Author chain E； PDBConstruct 1–40； UniProt 672–711 Author chain F； PDBConstruct 1–40； UniProt 672–711 Author chain G； PDBConstruct 1–40； UniProt 672–711 Author chain H； PDBConstruct 1–40； UniProt 672–711 Author chain I； PDBConstruct 1–40； UniProt 672–711 Author chain J； PDBConstruct 1–40； UniProt 672–711 Author chain K； PDBConstruct 1–40； UniProt 672–711 Author chain L； PDBConstruct 1–40； UniProt 672–711 Author chain M； PDBConstruct 1–40； UniProt 672–711 Author chain N； PDBConstruct 1–40； UniProt 672–711 Author chain O； PDBConstruct 1–40； UniProt 672–711 Author chain P； PDBConstruct 1–40； UniProt 672–711 Author chain Q； PDBConstruct 1–40； UniProt 672–711 Author chain R； PDBConstruct 1–40； UniProt 672–711 Author chain S； PDBConstruct 1–40； UniProt 672–711 Author chain T； PDBConstruct 1–40； UniProt 672–711 Author chain U； PDBConstruct 1–40； UniProt 672–711 Author chain V； PDBConstruct 1–40； UniProt 672–711 Author chain W； PDBConstruct 1–40； UniProt 672–711 Author chain X； PDBConstruct 1–40； UniProt 672–711 Author chain Y； PDBConstruct 1–40； UniProt 672–711 Author chain Z； PDBConstruct 1–40； UniProt 672–711 Author chain a； PDBConstruct 1–40； UniProt 672–711 Author chain b； PDBConstruct 1–40； UniProt 672–711 Author chain c； PDBConstruct 1–40； UniProt 672–711 Author chain d； PDBConstruct 1–40； UniProt 672–711 Author chain e； PDBConstruct 1–40； UniProt 672–711 Author chain f； PDBConstruct 1–40； UniProt 672–711 Author chain g； PDBConstruct 1–40； UniProt 672–711 Author chain h； PDBConstruct 1–40； UniProt 672–711 Author chain i； PDBConstruct 1–40； UniProt 672–711 Author chain j； PDBConstruct 1–40； UniProt 672–711 Author chain k； PDBConstruct 1–40； UniProt 672–711 Author chain l； PDBConstruct 1–40； UniProt 672–711 Author chain m； PDBConstruct 1–40； UniProt 672–711 Author chain n； PDBConstruct 1–40； UniProt 672–711 Author chain o； PDBConstruct 1–40； UniProt 672–711 Author chain p； PDBConstruct 1–40； UniProt 672–711 Author chain q； PDBConstruct 1–40； UniProt 672–711 Author chain r； PDBConstruct 1–40； UniProt 672–711 Author chain s； PDBConstruct 1–40； UniProt 672–711 Author chain t； PDBConstruct 1–40； UniProt 672–711 Author chain u； PDBConstruct 1–40； UniProt 672–711 Author chain v； PDBConstruct 1–40； UniProt 672–711 Author chain w； PDBConstruct 1–40； UniProt 672–711 Author chain x； PDBConstruct 1–40； UniProt 672–711 Author chain y； PDBConstruct 1–40； UniProt 672–711 Author chain z； PDBConstruct 1–40； UniProt 672–711 |
