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APR Prediction Models
GAP (Generalized Aggregation Proneness)
ANuPP (Prediciton of Nucleating APRs)
V
L
AmY-Pred (Predicting antibody light chain aggregation)
Aggregation Kinetics Prediction Models
AggreRATE-Disc (Classifying Aggregating Point Mutation)
AggreRATE-Pred (Predicting Aggregation Rate for Point Mutation)
AbsoluRATE (Predicting Absolute aggregation rate)
Amylo-Pipe (Comprehensive aggregation prediction)
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APR Prediction Models:
GAP (Generalized Aggregation Proneness)
ANuPP (Prediciton of Nucleating APRs)
V
L
AmY-Pred (Predicting antibody light chain aggregation)
Aggregation Kinetics Prediction Models:
AggreRATE-Disc (Classifying Aggregating Point Mutation)
AggreRATE-Pred (Predicting Aggregation Rate for Point Mutation)
AbsoluRATE (Predicting Absolute aggregation rate)
Amylo-Pipe (Comprehensive aggregation prediction)
Structure database of aggregation related proteins and peptides
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Protein Name
Peptide Sequence
Entry ID
PDB ID
Method
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Aggregating complex
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Displaying 541 to 565 records out of 565 records fetched.
Entry
PDB ID
Protein
Name
Species
Length
Mutation(s)
Class
Type
Method
Resolution (
Å
)
PMID
S-0541
6FHC
Psm alpha-3
Staphylococcus aureus
6
No
Non-amyloid
Fibril
X-RAY DIFFRACTION
1.51
30158633
S-0542
6FHD
Psm alpha-3
Staphylococcus aureus
6
No
Non-amyloid
Fibril
X-RAY DIFFRACTION
1.85
30158633
S-0543
6FK0
Cystatin-M
Homo sapiens
131
No
Amyloid
Protein
X-RAY DIFFRACTION
2.9
29967063
S-0544
6H6B
Alpha-synuclein
Homo sapiens
121
No
Amyloid
Fibril
ELECTRON MICROSCOPY
3.42
29969391
S-0545
6G8C
Major curlin subunit
Escherichia coli
6
No
Amyloid
Fibril
X-RAY DIFFRACTION
1.65
S-0546
6G8D
Major curlin subunit
Escherichia coli
6
No
Amyloid
Fibril
X-RAY DIFFRACTION
1.85
S-0547
6G8E
Major curlin subunit
Escherichia coli
6
No
Amyloid
Fibril
X-RAY DIFFRACTION
1.7
S-0548
6G9G
Major curlin subunit
Escherichia coli
6
Amyloid
Fibril
X-RAY DIFFRACTION
1.6
S-0549
6GHX
Thermolysin
Geobacillus stearothermophilus
316
No
Non-amyloid
Inhibitor complex
X-RAY DIFFRACTION
1.16
30403288
S-0550
6GK3
Beta-2-microglobulin
Homo sapiens
64
No
Amyloid
Fibril
ELECTRON MICROSCOPY
3.97
30375379
S-0551
6GX5
Microtubule-associated protein tau
Homo sapiens
94
No
Non-amyloid
Fibril
ELECTRON MICROSCOPY
3.2
30158706
S-0552
6HRE
Microtubule-associated protein tau
Homo sapiens
441
No
Amyloid
Fibril
ELECTRON MICROSCOPY
3.2
30276465
S-0553
6HRF
Microtubule-associated protein tau
Homo sapiens
441
No
Amyloid
Fibril
ELECTRON MICROSCOPY
3.3
30276465
S-0554
6HUD
Immunoglobulin Light-Chain
Homo sapiens
136
No
Amyloid
Fibril
ELECTRON MICROSCOPY
4.0
30894521
S-0555
6IC3
Immunoglobulin lambda 1 light chain
Homo sapiens
116
No
Amyloid
Fibril
ELECTRON MICROSCOPY
3.3
30894526
S-0556
6IMX
Transthyretin
Homo sapiens
159
V30M
Non-amyloid
Inhibitor complex
X-RAY DIFFRACTION
1.6
30688456
S-0557
6IMY
Transthyretin
Homo sapiens
159
V30M
Non-amyloid
Inhibitor complex
X-RAY DIFFRACTION
1.5
30688456
S-0558
6J60
hnRNP A1
Homo sapiens
9
No
Amyloid
Peptide
ELECTRON CRYSTALLOGRAPHY
0.96
S-0559
6M7M
InaZ protein
Pseudomonas syringae
6
No
Amyloid
Fibril
X-RAY DIFFRACTION
1.1
30867917
S-0560
6M9I
Ice nucleation protein
Pseudomonas syringae
6
No
Amyloid
Fibril
ELECTRON CRYSTALLOGRAPHY
0.9
30867917
S-0561
6M9J
Ice nucleation protein
Pseudomonas syringae
6
No
Amyloid
Fibril
ELECTRON CRYSTALLOGRAPHY
0.9
30867917
S-0562
6MST
Serum amyloid A-1 protein
Homo sapiens
66
No
Amyloid
Fibril
ELECTRON MICROSCOPY
2.7
S-0563
6NWP
Microtubule-associated protein tau
Homo sapiens
441
No
Amyloid
Fibril
ELECTRON MICROSCOPY
2.3
30894745
S-0564
6NWQ
Microtubule-associated protein tau
Homo sapiens
441
No
Amyloid
Fibril
ELECTRON MICROSCOPY
3.4
30894745
S-0565
6O3N
alphaAmA
synthetic construct
27
No
Amyloid
Fibril
X-RAY DIFFRACTION
3.7
30061717
Entry:S-0541
PDB ID: 6FHC
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Protein Contacts Atlas
Sequence & Sec. Str.
Chain 1
1
L
F
K
F
F
K
6
Helix: Magenta; Strand: Yellow; Coil & Turn: White.
Charged residues and Proline are highlighed in blue.
Description
Crystal Structure of the Amyloid-like hexametric polymorph of the LFKFFK segment from the S. aureus PSMalpha3
They show that PSMAlpha1 and PSMAlpha4, involved in biofilm structuring, form canonical cross-Beta amyloid fibrils wherein Beta-sheets tightly mate through steric zipper interfaces, conferring high stability. Contrastingly, a truncated PSMAlpha3 has antibacterial activity, forms reversible fibrils, and reveals two polymorphic and atypical Beta-rich fibril architectures. These architectures are radically different from both the cross-Alpha fibrils formed by full-length PSMAlpha3, and from the canonical cross-Beta fibrils.
Literature
PMID:
30158633
Author(s):
Salinas, N., Colletier, J.P., Moshe, A., Landau, M.
Reference:
Nat Commun. 2018 Aug 29;9(1):3512.
Download
Entry:
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JSON
Structure:
PDB
CIF
FASTA
Contact Network:
CSV
JSON
Protein Information
Protein Name:
Psm alpha-3
Alternative Name:
Gene Name:
Sequence Length:
6
Species:
Staphylococcus aureus
Mutation(s):
No
E.C. Number:
UniProt ID:
H9BRQ7
Keyword(s):
Psm alpha-3
Structure Information
PDB ID:
6FHC
Amyloid Category:
Non-amyloid
Type:
Fibril
Global Stoichiometry:
Homo 54-mer - A54
PDB Classification:
PROTEIN FIBRIL
Method:
X-RAY DIFFRACTION
Resolution (
Å
):
1.51
R free:
0.162
Ligand Information
Ligand ID
Chain ID
Ligand Formula
Ligand MW
Ligand Name
Ligand SMILES
InChI Key
CL
A
Cl -1
35.45
CHLORIDE ION
[Cl-]
VEXZGXHMUGYJMC-UHFFFAOYSA-M
CO3
A
C O3 -2
60.01
CARBONATE ION
C(=O)([O-])[O-]
BVKZGUZCCUSVTD-UHFFFAOYSA-L
PG4
A
C8 H18 O5
194.23
TETRAETHYLENE GLYCOL
C(COCCOCCOCCO)O
UWHCKJMYHZGTIT-UHFFFAOYSA-N
SCN
A
C N S -1
58.08
THIOCYANATE ION
C(#N)[S-]
ZMZDMBWJUHKJPS-UHFFFAOYSA-M
Entry:S-0542
PDB ID: 6FHD
CSV
JSON
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Structure
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Protein Contacts Atlas
Sequence & Sec. Str.
Chain 1
1
L
F
K
F
F
K
6
Chain 2
1
L
F
K
F
F
K
6
Helix: Magenta; Strand: Yellow; Coil & Turn: White.
Charged residues and Proline are highlighed in blue.
Description
Crystal Structure of the Amyloid-like, out-of-register beta-sheets, polymorph of the LFKFFK segment from the S. aureus PSMalpha3
They show that PSMAlpha1 and PSMAlpha4, involved in biofilm structuring, form canonical cross-Beta amyloid fibrils wherein Beta-sheets tightly mate through steric zipper interfaces, conferring high stability. Contrastingly, a truncated PSMAlpha3 has antibacterial activity, forms reversible fibrils, and reveals two polymorphic and atypical Beta-rich fibril architectures. These architectures are radically different from both the cross-Alpha fibrils formed by full-length PSMAlpha3, and from the canonical cross-Beta fibrils.
Literature
PMID:
30158633
Author(s):
Salinas, N., Colletier, J.P., Moshe, A., Landau, M.
Reference:
Nat Commun. 2018 Aug 29;9(1):3512.
Download
Entry:
CSV
JSON
Structure:
PDB
CIF
FASTA
Contact Network:
CSV
JSON
Protein Information
Protein Name:
Psm alpha-3
Alternative Name:
Gene Name:
Sequence Length:
6
Species:
Staphylococcus aureus
Mutation(s):
No
E.C. Number:
UniProt ID:
H9BRQ7
Keyword(s):
Psm alpha-3
Structure Information
PDB ID:
6FHD
Amyloid Category:
Non-amyloid
Type:
Fibril
Global Stoichiometry:
Homo 36-mer - A36
PDB Classification:
PROTEIN FIBRIL
Method:
X-RAY DIFFRACTION
Resolution (
Å
):
1.85
R free:
0.187
Ligand Information
Ligand ID
Chain ID
Ligand Formula
Ligand MW
Ligand Name
Ligand SMILES
InChI Key
SO4
A
O4 S -2
96.06
SULFATE ION
[O-]S(=O)(=O)[O-]
QAOWNCQODCNURD-UHFFFAOYSA-L
nan
B
Na 1
22.99
SODIUM ION
[Na+]
FKNQFGJONOIPTF-UHFFFAOYSA-N
SO4
B
O4 S -2
96.06
SULFATE ION
[O-]S(=O)(=O)[O-]
QAOWNCQODCNURD-UHFFFAOYSA-L
Entry:S-0543
PDB ID: 6FK0
CSV
JSON
Close ×
Structure
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View interactive contact network
Protein Contacts Atlas
Sequence & Sec. Str.
Chain 1
1
M
D
R
P
Q
E
R
M
V
G
E
L
R
D
L
S
P
D
D
P
Q
V
Q
K
A
25
26
A
Q
A
A
V
A
S
Y
N
M
G
S
N
S
I
Y
Y
F
R
D
T
H
I
I
K
50
51
A
Q
S
Q
L
V
A
G
I
K
Y
F
L
T
M
E
M
G
S
T
D
C
R
K
T
75
76
R
V
T
G
D
H
V
D
L
T
T
C
P
L
A
A
G
A
Q
Q
E
K
L
R
C
100
101
D
F
E
V
L
V
V
P
W
Q
N
S
S
Q
L
L
K
H
N
C
V
Q
M
L
E
125
126
H
H
H
H
H
H
131
Chain 2
1
M
D
R
P
Q
E
R
M
V
G
E
L
R
D
L
S
P
D
D
P
Q
V
Q
K
A
25
26
A
Q
A
A
V
A
S
Y
N
M
G
S
N
S
I
Y
Y
F
R
D
T
H
I
I
K
50
51
A
Q
S
Q
L
V
A
G
I
K
Y
F
L
T
M
E
M
G
S
T
D
C
R
K
T
75
76
R
V
T
G
D
H
V
D
L
T
T
C
P
L
A
A
G
A
Q
Q
E
K
L
R
C
100
101
D
F
E
V
L
V
V
P
W
Q
N
S
S
Q
L
L
K
H
N
C
V
Q
M
L
E
125
126
H
H
H
H
H
H
131
Helix: Magenta; Strand: Yellow; Coil & Turn: White.
Charged residues and Proline are highlighed in blue.
Description
Xray structure of domain-swapped cystatin E dimer
Conformational destabilization of cystatin E leads to the formation of a domain-swapped dimer with increased conformational stability. This dimer was active as a legumain inhibitor by forming a trimeric complex. By contrast, the binding sites toward papain-like proteases were buried within the cystatin E dimer. They also showed that the dimers could further convert to amyloid fibrils. Cystatin E amyloid fibrils contained functional protein, which inhibited both legumain and papain-like enzymes. Fibril formation was further regulated by glycosylation.
Literature
PMID:
29967063
Author(s):
Dall, E., Hollerweger, J.C., Dahms, S.O., Cui, H., Haussermann, K., Brandstetter, H.
Reference:
J Biol Chem. 2018 Aug 24;293(34):13151-13165.
Download
Entry:
CSV
JSON
Structure:
PDB
CIF
FASTA
Contact Network:
CSV
JSON
Protein Information
Protein Name:
Cystatin-M
Alternative Name:
Cystatin-6, Cystatin-E
Gene Name:
CST6
Sequence Length:
131
Species:
Homo sapiens
Mutation(s):
No
E.C. Number:
UniProt ID:
Q15828
Keyword(s):
Cystatin-M
Structure Information
PDB ID:
6FK0
Amyloid Category:
Amyloid
Type:
Protein
Global Stoichiometry:
Homo 2-mer - A2
PDB Classification:
hydrolase inhibitor
Method:
X-RAY DIFFRACTION
Resolution (
Å
):
2.9
R free:
0.273
Entry:S-0544
PDB ID: 6H6B
CSV
JSON
Close ×
Structure
Press 'p' to pause
View interactive contact network
Sequence & Sec. Str.
Chain 1
1
M
D
V
F
M
K
G
L
S
K
A
K
E
G
V
V
A
A
A
E
K
T
K
Q
G
25
26
V
A
E
A
A
G
K
T
K
E
G
V
L
Y
V
G
S
K
T
K
E
G
V
V
H
50
51
G
V
A
T
V
A
E
K
T
K
E
Q
V
T
N
V
G
G
A
V
V
T
G
V
T
75
76
A
V
A
Q
K
T
V
E
G
A
G
S
I
A
A
A
T
G
F
V
K
K
D
Q
L
100
101
G
K
N
E
E
G
A
P
Q
E
G
I
L
E
D
M
P
V
D
P
D
121
Chain 2
1
M
D
V
F
M
K
G
L
S
K
A
K
E
G
V
V
A
A
A
E
K
T
K
Q
G
25
26
V
A
E
A
A
G
K
T
K
E
G
V
L
Y
V
G
S
K
T
K
E
G
V
V
H
50
51
G
V
A
T
V
A
E
K
T
K
E
Q
V
T
N
V
G
G
A
V
V
T
G
V
T
75
76
A
V
A
Q
K
T
V
E
G
A
G
S
I
A
A
A
T
G
F
V
K
K
D
Q
L
100
101
G
K
N
E
E
G
A
P
Q
E
G
I
L
E
D
M
P
V
D
P
D
121
Chain 3
1
M
D
V
F
M
K
G
L
S
K
A
K
E
G
V
V
A
A
A
E
K
T
K
Q
G
25
26
V
A
E
A
A
G
K
T
K
E
G
V
L
Y
V
G
S
K
T
K
E
G
V
V
H
50
51
G
V
A
T
V
A
E
K
T
K
E
Q
V
T
N
V
G
G
A
V
V
T
G
V
T
75
76
A
V
A
Q
K
T
V
E
G
A
G
S
I
A
A
A
T
G
F
V
K
K
D
Q
L
100
101
G
K
N
E
E
G
A
P
Q
E
G
I
L
E
D
M
P
V
D
P
D
121
Chain 4
1
M
D
V
F
M
K
G
L
S
K
A
K
E
G
V
V
A
A
A
E
K
T
K
Q
G
25
26
V
A
E
A
A
G
K
T
K
E
G
V
L
Y
V
G
S
K
T
K
E
G
V
V
H
50
51
G
V
A
T
V
A
E
K
T
K
E
Q
V
T
N
V
G
G
A
V
V
T
G
V
T
75
76
A
V
A
Q
K
T
V
E
G
A
G
S
I
A
A
A
T
G
F
V
K
K
D
Q
L
100
101
G
K
N
E
E
G
A
P
Q
E
G
I
L
E
D
M
P
V
D
P
D
121
Chain 5
1
M
D
V
F
M
K
G
L
S
K
A
K
E
G
V
V
A
A
A
E
K
T
K
Q
G
25
26
V
A
E
A
A
G
K
T
K
E
G
V
L
Y
V
G
S
K
T
K
E
G
V
V
H
50
51
G
V
A
T
V
A
E
K
T
K
E
Q
V
T
N
V
G
G
A
V
V
T
G
V
T
75
76
A
V
A
Q
K
T
V
E
G
A
G
S
I
A
A
A
T
G
F
V
K
K
D
Q
L
100
101
G
K
N
E
E
G
A
P
Q
E
G
I
L
E
D
M
P
V
D
P
D
121
Chain 6
1
M
D
V
F
M
K
G
L
S
K
A
K
E
G
V
V
A
A
A
E
K
T
K
Q
G
25
26
V
A
E
A
A
G
K
T
K
E
G
V
L
Y
V
G
S
K
T
K
E
G
V
V
H
50
51
G
V
A
T
V
A
E
K
T
K
E
Q
V
T
N
V
G
G
A
V
V
T
G
V
T
75
76
A
V
A
Q
K
T
V
E
G
A
G
S
I
A
A
A
T
G
F
V
K
K
D
Q
L
100
101
G
K
N
E
E
G
A
P
Q
E
G
I
L
E
D
M
P
V
D
P
D
121
Chain 7
1
M
D
V
F
M
K
G
L
S
K
A
K
E
G
V
V
A
A
A
E
K
T
K
Q
G
25
26
V
A
E
A
A
G
K
T
K
E
G
V
L
Y
V
G
S
K
T
K
E
G
V
V
H
50
51
G
V
A
T
V
A
E
K
T
K
E
Q
V
T
N
V
G
G
A
V
V
T
G
V
T
75
76
A
V
A
Q
K
T
V
E
G
A
G
S
I
A
A
A
T
G
F
V
K
K
D
Q
L
100
101
G
K
N
E
E
G
A
P
Q
E
G
I
L
E
D
M
P
V
D
P
D
121
Chain 8
1
M
D
V
F
M
K
G
L
S
K
A
K
E
G
V
V
A
A
A
E
K
T
K
Q
G
25
26
V
A
E
A
A
G
K
T
K
E
G
V
L
Y
V
G
S
K
T
K
E
G
V
V
H
50
51
G
V
A
T
V
A
E
K
T
K
E
Q
V
T
N
V
G
G
A
V
V
T
G
V
T
75
76
A
V
A
Q
K
T
V
E
G
A
G
S
I
A
A
A
T
G
F
V
K
K
D
Q
L
100
101
G
K
N
E
E
G
A
P
Q
E
G
I
L
E
D
M
P
V
D
P
D
121
Chain 9
1
M
D
V
F
M
K
G
L
S
K
A
K
E
G
V
V
A
A
A
E
K
T
K
Q
G
25
26
V
A
E
A
A
G
K
T
K
E
G
V
L
Y
V
G
S
K
T
K
E
G
V
V
H
50
51
G
V
A
T
V
A
E
K
T
K
E
Q
V
T
N
V
G
G
A
V
V
T
G
V
T
75
76
A
V
A
Q
K
T
V
E
G
A
G
S
I
A
A
A
T
G
F
V
K
K
D
Q
L
100
101
G
K
N
E
E
G
A
P
Q
E
G
I
L
E
D
M
P
V
D
P
D
121
Chain 10
1
M
D
V
F
M
K
G
L
S
K
A
K
E
G
V
V
A
A
A
E
K
T
K
Q
G
25
26
V
A
E
A
A
G
K
T
K
E
G
V
L
Y
V
G
S
K
T
K
E
G
V
V
H
50
51
G
V
A
T
V
A
E
K
T
K
E
Q
V
T
N
V
G
G
A
V
V
T
G
V
T
75
76
A
V
A
Q
K
T
V
E
G
A
G
S
I
A
A
A
T
G
F
V
K
K
D
Q
L
100
101
G
K
N
E
E
G
A
P
Q
E
G
I
L
E
D
M
P
V
D
P
D
121
Helix: Magenta; Strand: Yellow; Coil & Turn: White.
Charged residues and Proline are highlighed in blue.
Description
Structure of alpha-synuclein fibrils
The structure of cytotoxic alpha-synuclein fibrils (residues 1-121). Two protofilaments form a polar fibril composed of staggered Beta-strands. The backbone of residues 38 to 95, including the fibril core and the non-amyloid component region.
Literature
PMID:
29969391
Author(s):
Guerrero-Ferreira, R., Taylor, N.M.I., Mona, D., Ringler, P., Lauer, M.E., Riek, R., Britschgi, M., Stahlberg, H.
Reference:
Elife. 2018 Jul 3;7. pii: e36402.
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Protein Information
Protein Name:
Alpha-synuclein
Alternative Name:
Non-A beta component of AD amyloid, Non-A4 component of amyloid precursor
Gene Name:
SNCA, NACP, PARK1
Sequence Length:
121
Species:
Homo sapiens
Mutation(s):
No
E.C. Number:
UniProt ID:
P37840
Keyword(s):
Alpha-synuclein
Structure Information
PDB ID:
6H6B
Amyloid Category:
Amyloid
Type:
Fibril
Global Stoichiometry:
Homo 10-mer - A10
PDB Classification:
PROTEIN FIBRIL
Method:
ELECTRON MICROSCOPY
Resolution (
Å
):
3.42
R free:
Entry:S-0545
PDB ID: 6G8C
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Sequence & Sec. Str.
Chain 1
1
I
Y
Q
Y
G
G
6
Helix: Magenta; Strand: Yellow; Coil & Turn: White.
Charged residues and Proline are highlighed in blue.
Description
Crystal Structure of the Amyloid-like IYQYGG segment from the R1 repeat of the E. coli Biofilm-associated CsgA Curli protein
Crystal Structure of the Amyloid-like IYQYGG segment from the R1 repeat of the E. coli Biofilm-associated CsgA Curli protein
Literature
PMID:
Author(s):
Perov, S., Salinas, N., Lidor, O., Golan, N., Tayeb-Fligelman, E., Willbold, D., Landau, M.
Reference:
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Structure:
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Contact Network:
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Protein Information
Protein Name:
Major curlin subunit
Alternative Name:
Gene Name:
Sequence Length:
6
Species:
Escherichia coli
Mutation(s):
No
E.C. Number:
UniProt ID:
P28307
Keyword(s):
Major curlin subunit
Structure Information
PDB ID:
6G8C
Amyloid Category:
Amyloid
Type:
Fibril
Global Stoichiometry:
Homo 18-mer - A18
PDB Classification:
PROTEIN FIBRIL
Method:
X-RAY DIFFRACTION
Resolution (
Å
):
1.65
R free:
0.17800000
Entry:S-0546
PDB ID: 6G8D
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Sequence & Sec. Str.
Chain 1
1
L
N
I
Y
Q
Y
6
Helix: Magenta; Strand: Yellow; Coil & Turn: White.
Charged residues and Proline are highlighed in blue.
Description
Crystal Structure of the Amyloid-like LNIYQY segment from the R1 repeat of the E. coli Biofilm-associated CsgA Curli protein
Crystal Structure of the Amyloid-like LNIYQY segment from the R1 repeat of the E. coli Biofilm-associated CsgA Curli protein
Literature
PMID:
Author(s):
Perov, S., Salinas, N., Lidor, O., Golan, N., Tayeb-Fligelman, E., Willbold, D., Landau, M.
Reference:
Download
Entry:
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Structure:
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Contact Network:
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Protein Information
Protein Name:
Major curlin subunit
Alternative Name:
Gene Name:
Sequence Length:
6
Species:
Escherichia coli
Mutation(s):
No
E.C. Number:
UniProt ID:
P28307
Keyword(s):
Major curlin subunit
Structure Information
PDB ID:
6G8D
Amyloid Category:
Amyloid
Type:
Fibril
Global Stoichiometry:
Homo 18-mer - A18
PDB Classification:
PROTEIN FIBRIL
Method:
X-RAY DIFFRACTION
Resolution (
Å
):
1.85
R free:
0.191
Entry:S-0547
PDB ID: 6G8E
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Sequence & Sec. Str.
Chain 1
1
V
T
Q
V
G
F
6
Chain 2
1
V
T
Q
V
G
F
6
Helix: Magenta; Strand: Yellow; Coil & Turn: White.
Charged residues and Proline are highlighed in blue.
Description
Crystal Structure of the Amyloid-like VTQVGF segment from the R5 repeat of the E. coli Biofilm-associated CsgA Curli protein
Crystal Structure of the Amyloid-like VTQVGF segment from the R5 repeat of the E. coli Biofilm-associated CsgA Curli protein
Literature
PMID:
Author(s):
Perov, S., Salinas, N., Lidor, O., Golan, N., Tayeb-Fligelman, E., Willbold, D., Landau, M.
Reference:
Download
Entry:
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Structure:
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FASTA
Contact Network:
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Protein Information
Protein Name:
Major curlin subunit
Alternative Name:
Gene Name:
Sequence Length:
6
Species:
Escherichia coli
Mutation(s):
No
E.C. Number:
UniProt ID:
P28307
Keyword(s):
Major curlin subunit
Structure Information
PDB ID:
6G8E
Amyloid Category:
Amyloid
Type:
Fibril
Global Stoichiometry:
Homo 18-mer - A18
PDB Classification:
PROTEIN FIBRIL
Method:
X-RAY DIFFRACTION
Resolution (
Å
):
1.7
R free:
0.132
Entry:S-0548
PDB ID: 6G9G
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Sequence & Sec. Str.
Chain 1
1
T
A
S
N
S
S
6
Helix: Magenta; Strand: Yellow; Coil & Turn: White.
Charged residues and Proline are highlighed in blue.
Description
Crystal Structure of the TASNSS segment from the R4-R5 loop of the E. coli Biofilm-associated CsgA Curli protein
Literature
PMID:
Author(s):
Perov, S., Salinas, N., Lidor, O., Golan, N., Tayeb-Fligelman, E., Willbold, D., Landau, M.
Reference:
Download
Entry:
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Structure:
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FASTA
Contact Network:
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JSON
Protein Information
Protein Name:
Major curlin subunit
Alternative Name:
Gene Name:
Sequence Length:
6
Species:
Escherichia coli
Mutation(s):
E.C. Number:
UniProt ID:
P28307
Keyword(s):
Major curlin subunit
Structure Information
PDB ID:
6G9G
Amyloid Category:
Amyloid
Type:
Fibril
Global Stoichiometry:
PDB Classification:
PROTEIN FIBRIL
Method:
X-RAY DIFFRACTION
Resolution (
Å
):
1.6
R free:
0.135
Entry:S-0549
PDB ID: 6GHX
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Sequence & Sec. Str.
Chain 1
1
I
T
G
T
S
T
V
G
V
G
R
G
V
L
G
D
Q
K
N
I
N
T
T
Y
S
25
26
T
Y
Y
Y
L
Q
D
N
T
R
G
N
G
I
F
T
Y
D
A
K
Y
R
T
T
L
50
51
P
G
S
L
W
A
D
A
D
N
Q
F
F
A
S
Y
D
A
P
A
V
D
A
H
Y
75
76
Y
A
G
V
T
Y
D
Y
Y
K
N
V
H
N
R
L
S
Y
D
G
N
N
A
A
I
100
101
R
S
S
V
H
Y
S
Q
G
Y
N
N
A
F
W
N
G
S
Q
M
V
Y
G
D
G
125
126
D
G
Q
T
F
I
P
L
S
G
G
I
D
V
V
A
H
E
L
T
H
A
V
T
D
150
151
Y
T
A
G
L
I
Y
Q
N
E
S
G
A
I
N
E
A
I
S
D
I
F
G
T
L
175
176
V
E
F
Y
A
N
K
N
P
D
W
E
I
G
E
D
V
Y
T
P
G
I
S
G
D
200
201
S
L
R
S
M
S
D
P
A
K
Y
G
D
P
D
H
Y
S
K
R
Y
T
G
T
Q
225
226
D
N
G
G
V
H
I
N
S
G
I
I
N
K
A
A
Y
L
I
S
Q
G
G
T
H
250
251
Y
G
V
S
V
V
G
I
G
R
D
K
L
G
K
I
F
Y
R
A
L
T
Q
Y
L
275
276
T
P
T
S
N
F
S
Q
L
R
A
A
A
V
Q
S
A
T
D
L
Y
G
S
T
S
300
301
Q
E
V
A
S
V
K
Q
A
F
D
A
V
G
V
K
316
Helix: Magenta; Strand: Yellow; Coil & Turn: White.
Charged residues and Proline are highlighed in blue.
Description
Alzheimer's Amyloid-Beta Peptide Fragment 31-35 in Complex with Cd-substituted Thermolysin
The interaction of the amyloid-Beta peptide (ABeta) with thermolysin (TLN) was investigated by X-ray crystallography. Structural models of the complexes of TLN with several ABeta fragments show that, despite the numerous possible cleavage sites of the ABeta sequence, the C-terminal product of Ala30-Ile31 cleavage does not dissociate, thus inhibiting the enzyme. The high similarity between the TLN structural motif and neprilysin (NEP), the most extensively studied peptidase associated with ABeta clearance, suggests that NEP should be more efficient against ABeta polymorphs where Ala30-Ile31 is inaccessible.
Literature
PMID:
30403288
Author(s):
Leite, J.P., Gales, L.
Reference:
FEBS Lett. 2019 Jan;593(1):128-137.
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Protein Information
Protein Name:
Thermolysin
Alternative Name:
Neutral protease
Gene Name:
nprS, nprM
Sequence Length:
316
Species:
Geobacillus stearothermophilus
Mutation(s):
No
E.C. Number:
3.4.24.27
UniProt ID:
P43133
Keyword(s):
Thermolysin
Structure Information
PDB ID:
6GHX
Amyloid Category:
Non-amyloid
Type:
Inhibitor complex
Global Stoichiometry:
Monomer - A
PDB Classification:
HYDROLASE
Method:
X-RAY DIFFRACTION
Resolution (
Å
):
1.16
R free:
0.22
Ligand Information
Ligand ID
Chain ID
Ligand Formula
Ligand MW
Ligand Name
Ligand SMILES
InChI Key
CA
A
Ca 2
40.08
CALCIUM ION
[Ca+2]
BHPQYMZQTOCNFJ-UHFFFAOYSA-N
CD
A
Cd 2
112.41
CADMIUM ION
[Cd+2]
WLZRMCYVCSSEQC-UHFFFAOYSA-N
DMS
A
C2 H6 O S
78.13
DIMETHYL SULFOXIDE
CS(=O)C
IAZDPXIOMUYVGZ-UHFFFAOYSA-N
ILE
A
C6 H13 N O2
131.17
ISOLEUCINE
CC[C@H](C)[C@@H](C(=O)O)N
AGPKZVBTJJNPAG-WHFBIAKZSA-N
Entry:S-0550
PDB ID: 6GK3
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Sequence & Sec. Str.
Chain 1
1
F
L
N
C
Y
V
S
G
F
H
P
S
D
I
E
V
D
L
L
K
N
G
E
R
I
25
26
E
K
V
E
H
S
D
L
S
F
S
K
D
W
S
F
Y
L
L
Y
Y
T
E
F
T
50
51
P
T
E
K
D
E
Y
A
C
R
V
N
H
V
64
Chain 2
1
F
L
N
C
Y
V
S
G
F
H
P
S
D
I
E
V
D
L
L
K
N
G
E
R
I
25
26
E
K
V
E
H
S
D
L
S
F
S
K
D
W
S
F
Y
L
L
Y
Y
T
E
F
T
50
51
P
T
E
K
D
E
Y
A
C
R
V
N
H
V
64
Chain 3
1
F
L
N
C
Y
V
S
G
F
H
P
S
D
I
E
V
D
L
L
K
N
G
E
R
I
25
26
E
K
V
E
H
S
D
L
S
F
S
K
D
W
S
F
Y
L
L
Y
Y
T
E
F
T
50
51
P
T
E
K
D
E
Y
A
C
R
V
N
H
V
64
Chain 4
1
F
L
N
C
Y
V
S
G
F
H
P
S
D
I
E
V
D
L
L
K
N
G
E
R
I
25
26
E
K
V
E
H
S
D
L
S
F
S
K
D
W
S
F
Y
L
L
Y
Y
T
E
F
T
50
51
P
T
E
K
D
E
Y
A
C
R
V
N
H
V
64
Chain 5
1
F
L
N
C
Y
V
S
G
F
H
P
S
D
I
E
V
D
L
L
K
N
G
E
R
I
25
26
E
K
V
E
H
S
D
L
S
F
S
K
D
W
S
F
Y
L
L
Y
Y
T
E
F
T
50
51
P
T
E
K
D
E
Y
A
C
R
V
N
H
V
64
Chain 6
1
F
L
N
C
Y
V
S
G
F
H
P
S
D
I
E
V
D
L
L
K
N
G
E
R
I
25
26
E
K
V
E
H
S
D
L
S
F
S
K
D
W
S
F
Y
L
L
Y
Y
T
E
F
T
50
51
P
T
E
K
D
E
Y
A
C
R
V
N
H
V
64
Chain 7
1
F
L
N
C
Y
V
S
G
F
H
P
S
D
I
E
V
D
L
L
K
N
G
E
R
I
25
26
E
K
V
E
H
S
D
L
S
F
S
K
D
W
S
F
Y
L
L
Y
Y
T
E
F
T
50
51
P
T
E
K
D
E
Y
A
C
R
V
N
H
V
64
Chain 8
1
F
L
N
C
Y
V
S
G
F
H
P
S
D
I
E
V
D
L
L
K
N
G
E
R
I
25
26
E
K
V
E
H
S
D
L
S
F
S
K
D
W
S
F
Y
L
L
Y
Y
T
E
F
T
50
51
P
T
E
K
D
E
Y
A
C
R
V
N
H
V
64
Helix: Magenta; Strand: Yellow; Coil & Turn: White.
Charged residues and Proline are highlighed in blue.
Description
Two protofilament beta-2-microglobulin amyloid fibril
The structure of an amyloid fibril formed in vitro from Beta 2 -microglobulin (Beta 2 m), the culprit protein of dialysis-related amyloidosis. The fibril is composed of two identical protofilaments assembled from subunits that do not share Beta 2 m's native tertiary fold, but are formed from similar Beta-strands. The fibrils share motifs with other amyloid fibrils, but also contain unique features including ?-stacking interactions perpendicular to the fibril axis and an intramolecular disulfide that stabilises the subunit fold.
Literature
PMID:
30375379
Author(s):
Iadanza, M.G., Silvers, R., Boardman, J., Smith, H.I., Karamanos, T.K., Debelouchina, G.T., Su, Y., Griffin, R.G., Ranson, N.A., Radford, S.E.
Reference:
Nat Commun. 2018 Oct 30;9(1):4517.
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Protein Information
Protein Name:
Beta-2-microglobulin
Alternative Name:
Gene Name:
B2M, CDABP0092, HDCMA22P
Sequence Length:
64
Species:
Homo sapiens
Mutation(s):
No
E.C. Number:
UniProt ID:
P61769
Keyword(s):
Beta-2-microglobulin
Structure Information
PDB ID:
6GK3
Amyloid Category:
Amyloid
Type:
Fibril
Global Stoichiometry:
Homo 8-mer - A8
PDB Classification:
PROTEIN FIBRIL
Method:
ELECTRON MICROSCOPY
Resolution (
Å
):
3.97
R free:
Entry:S-0551
PDB ID: 6GX5
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Sequence & Sec. Str.
Chain 1
1
K
N
V
K
S
K
I
G
S
T
E
N
L
K
H
Q
P
G
G
G
K
V
Q
I
V
25
26
Y
K
P
V
D
L
S
K
V
T
S
K
C
G
S
L
G
N
I
H
H
K
P
G
G
50
51
G
Q
V
E
V
K
S
E
K
L
D
F
K
D
R
V
Q
S
K
I
G
S
L
D
N
75
76
I
T
H
V
P
G
G
G
N
K
K
I
E
T
H
K
L
T
F
94
Chain 2
1
K
N
V
K
S
K
I
G
S
T
E
N
L
K
H
Q
P
G
G
G
K
V
Q
I
V
25
26
Y
K
P
V
D
L
S
K
V
T
S
K
C
G
S
L
G
N
I
H
H
K
P
G
G
50
51
G
Q
V
E
V
K
S
E
K
L
D
F
K
D
R
V
Q
S
K
I
G
S
L
D
N
75
76
I
T
H
V
P
G
G
G
N
K
K
I
E
T
H
K
L
T
F
94
Chain 3
1
K
N
V
K
S
K
I
G
S
T
E
N
L
K
H
Q
P
G
G
G
K
V
Q
I
V
25
26
Y
K
P
V
D
L
S
K
V
T
S
K
C
G
S
L
G
N
I
H
H
K
P
G
G
50
51
G
Q
V
E
V
K
S
E
K
L
D
F
K
D
R
V
Q
S
K
I
G
S
L
D
N
75
76
I
T
H
V
P
G
G
G
N
K
K
I
E
T
H
K
L
T
F
94
Helix: Magenta; Strand: Yellow; Coil & Turn: White.
Charged residues and Proline are highlighed in blue.
Description
Narrow Pick Filament from Pick's disease brain
The structures of tau filaments from patients with Pick's disease, a neurodegenerative disorder characterized by frontotemporal dementia. The filaments consist of residues Lys254-Phe378 of 3R tau, which are folded differently from the tau filaments in Alzheimer's disease, establishing the existence of conformers of assembled tau.
Literature
PMID:
30158706
Author(s):
Falcon, B., Zhang, W., Murzin, A.G., Murshudov, G., Garringer, H.J., Vidal, R., Crowther, R.A., Ghetti, B., Scheres, S.H.W., Goedert, M.
Reference:
Nature. 2018 Sep;561(7721):137-140.
Download
Entry:
CSV
JSON
Structure:
PDB
CIF
FASTA
Contact Network:
CSV
JSON
Protein Information
Protein Name:
Microtubule-associated protein tau
Alternative Name:
Neurofibrillary tangle protein, Paired helical filament-tau
Gene Name:
MAPT, MAPTL, MTBT1, TAU
Sequence Length:
94
Species:
Homo sapiens
Mutation(s):
No
E.C. Number:
UniProt ID:
P10636
Keyword(s):
Microtubule-associated protein tau
Structure Information
PDB ID:
6GX5
Amyloid Category:
Non-amyloid
Type:
Fibril
Global Stoichiometry:
Homo 3-mer - A3
PDB Classification:
PROTEIN FIBRIL
Method:
ELECTRON MICROSCOPY
Resolution (
Å
):
3.2
R free:
Entry:S-0552
PDB ID: 6HRE
CSV
JSON
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Structure
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Sequence & Sec. Str.
Chain 1
1
M
A
E
P
R
Q
E
F
E
V
M
E
D
H
A
G
T
Y
G
L
G
D
R
K
D
25
26
Q
G
G
Y
T
M
H
Q
D
Q
E
G
D
T
D
A
G
L
K
E
S
P
L
Q
T
50
51
P
T
E
D
G
S
E
E
P
G
S
E
T
S
D
A
K
S
T
P
T
A
E
D
V
75
76
T
A
P
L
V
D
E
G
A
P
G
K
Q
A
A
A
Q
P
H
T
E
I
P
E
G
100
101
T
T
A
E
E
A
G
I
G
D
T
P
S
L
E
D
E
A
A
G
H
V
T
Q
A
125
126
R
M
V
S
K
S
K
D
G
T
G
S
D
D
K
K
A
K
G
A
D
G
K
T
K
150
151
I
A
T
P
R
G
A
A
P
P
G
Q
K
G
Q
A
N
A
T
R
I
P
A
K
T
175
176
P
P
A
P
K
T
P
P
S
S
G
E
P
P
K
S
G
D
R
S
G
Y
S
S
P
200
201
G
S
P
G
T
P
G
S
R
S
R
T
P
S
L
P
T
P
P
T
R
E
P
K
K
225
226
V
A
V
V
R
T
P
P
K
S
P
S
S
A
K
S
R
L
Q
T
A
P
V
P
M
250
251
P
D
L
K
N
V
K
S
K
I
G
S
T
E
N
L
K
H
Q
P
G
G
G
K
V
275
276
Q
I
I
N
K
K
L
D
L
S
N
V
Q
S
K
C
G
S
K
D
N
I
K
H
V
300
301
P
G
G
G
S
V
Q
I
V
Y
K
P
V
D
L
S
K
V
T
S
K
C
G
S
L
325
326
G
N
I
H
H
K
P
G
G
G
Q
V
E
V
K
S
E
K
L
D
F
K
D
R
V
350
351
Q
S
K
I
G
S
L
D
N
I
T
H
V
P
G
G
G
N
K
K
I
E
T
H
K
375
376
L
T
F
R
E
N
A
K
A
K
T
D
H
G
A
E
I
V
Y
K
S
P
V
V
S
400
401
G
D
T
S
P
R
H
L
S
N
V
S
S
T
G
S
I
D
M
V
D
S
P
Q
L
425
426
A
T
L
A
D
E
V
S
A
S
L
A
K
Q
G
L
441
Chain 2
1
M
A
E
P
R
Q
E
F
E
V
M
E
D
H
A
G
T
Y
G
L
G
D
R
K
D
25
26
Q
G
G
Y
T
M
H
Q
D
Q
E
G
D
T
D
A
G
L
K
E
S
P
L
Q
T
50
51
P
T
E
D
G
S
E
E
P
G
S
E
T
S
D
A
K
S
T
P
T
A
E
D
V
75
76
T
A
P
L
V
D
E
G
A
P
G
K
Q
A
A
A
Q
P
H
T
E
I
P
E
G
100
101
T
T
A
E
E
A
G
I
G
D
T
P
S
L
E
D
E
A
A
G
H
V
T
Q
A
125
126
R
M
V
S
K
S
K
D
G
T
G
S
D
D
K
K
A
K
G
A
D
G
K
T
K
150
151
I
A
T
P
R
G
A
A
P
P
G
Q
K
G
Q
A
N
A
T
R
I
P
A
K
T
175
176
P
P
A
P
K
T
P
P
S
S
G
E
P
P
K
S
G
D
R
S
G
Y
S
S
P
200
201
G
S
P
G
T
P
G
S
R
S
R
T
P
S
L
P
T
P
P
T
R
E
P
K
K
225
226
V
A
V
V
R
T
P
P
K
S
P
S
S
A
K
S
R
L
Q
T
A
P
V
P
M
250
251
P
D
L
K
N
V
K
S
K
I
G
S
T
E
N
L
K
H
Q
P
G
G
G
K
V
275
276
Q
I
I
N
K
K
L
D
L
S
N
V
Q
S
K
C
G
S
K
D
N
I
K
H
V
300
301
P
G
G
G
S
V
Q
I
V
Y
K
P
V
D
L
S
K
V
T
S
K
C
G
S
L
325
326
G
N
I
H
H
K
P
G
G
G
Q
V
E
V
K
S
E
K
L
D
F
K
D
R
V
350
351
Q
S
K
I
G
S
L
D
N
I
T
H
V
P
G
G
G
N
K
K
I
E
T
H
K
375
376
L
T
F
R
E
N
A
K
A
K
T
D
H
G
A
E
I
V
Y
K
S
P
V
V
S
400
401
G
D
T
S
P
R
H
L
S
N
V
S
S
T
G
S
I
D
M
V
D
S
P
Q
L
425
426
A
T
L
A
D
E
V
S
A
S
L
A
K
Q
G
L
441
Chain 3
1
M
A
E
P
R
Q
E
F
E
V
M
E
D
H
A
G
T
Y
G
L
G
D
R
K
D
25
26
Q
G
G
Y
T
M
H
Q
D
Q
E
G
D
T
D
A
G
L
K
E
S
P
L
Q
T
50
51
P
T
E
D
G
S
E
E
P
G
S
E
T
S
D
A
K
S
T
P
T
A
E
D
V
75
76
T
A
P
L
V
D
E
G
A
P
G
K
Q
A
A
A
Q
P
H
T
E
I
P
E
G
100
101
T
T
A
E
E
A
G
I
G
D
T
P
S
L
E
D
E
A
A
G
H
V
T
Q
A
125
126
R
M
V
S
K
S
K
D
G
T
G
S
D
D
K
K
A
K
G
A
D
G
K
T
K
150
151
I
A
T
P
R
G
A
A
P
P
G
Q
K
G
Q
A
N
A
T
R
I
P
A
K
T
175
176
P
P
A
P
K
T
P
P
S
S
G
E
P
P
K
S
G
D
R
S
G
Y
S
S
P
200
201
G
S
P
G
T
P
G
S
R
S
R
T
P
S
L
P
T
P
P
T
R
E
P
K
K
225
226
V
A
V
V
R
T
P
P
K
S
P
S
S
A
K
S
R
L
Q
T
A
P
V
P
M
250
251
P
D
L
K
N
V
K
S
K
I
G
S
T
E
N
L
K
H
Q
P
G
G
G
K
V
275
276
Q
I
I
N
K
K
L
D
L
S
N
V
Q
S
K
C
G
S
K
D
N
I
K
H
V
300
301
P
G
G
G
S
V
Q
I
V
Y
K
P
V
D
L
S
K
V
T
S
K
C
G
S
L
325
326
G
N
I
H
H
K
P
G
G
G
Q
V
E
V
K
S
E
K
L
D
F
K
D
R
V
350
351
Q
S
K
I
G
S
L
D
N
I
T
H
V
P
G
G
G
N
K
K
I
E
T
H
K
375
376
L
T
F
R
E
N
A
K
A
K
T
D
H
G
A
E
I
V
Y
K
S
P
V
V
S
400
401
G
D
T
S
P
R
H
L
S
N
V
S
S
T
G
S
I
D
M
V
D
S
P
Q
L
425
426
A
T
L
A
D
E
V
S
A
S
L
A
K
Q
G
L
441
Chain 4
1
M
A
E
P
R
Q
E
F
E
V
M
E
D
H
A
G
T
Y
G
L
G
D
R
K
D
25
26
Q
G
G
Y
T
M
H
Q
D
Q
E
G
D
T
D
A
G
L
K
E
S
P
L
Q
T
50
51
P
T
E
D
G
S
E
E
P
G
S
E
T
S
D
A
K
S
T
P
T
A
E
D
V
75
76
T
A
P
L
V
D
E
G
A
P
G
K
Q
A
A
A
Q
P
H
T
E
I
P
E
G
100
101
T
T
A
E
E
A
G
I
G
D
T
P
S
L
E
D
E
A
A
G
H
V
T
Q
A
125
126
R
M
V
S
K
S
K
D
G
T
G
S
D
D
K
K
A
K
G
A
D
G
K
T
K
150
151
I
A
T
P
R
G
A
A
P
P
G
Q
K
G
Q
A
N
A
T
R
I
P
A
K
T
175
176
P
P
A
P
K
T
P
P
S
S
G
E
P
P
K
S
G
D
R
S
G
Y
S
S
P
200
201
G
S
P
G
T
P
G
S
R
S
R
T
P
S
L
P
T
P
P
T
R
E
P
K
K
225
226
V
A
V
V
R
T
P
P
K
S
P
S
S
A
K
S
R
L
Q
T
A
P
V
P
M
250
251
P
D
L
K
N
V
K
S
K
I
G
S
T
E
N
L
K
H
Q
P
G
G
G
K
V
275
276
Q
I
I
N
K
K
L
D
L
S
N
V
Q
S
K
C
G
S
K
D
N
I
K
H
V
300
301
P
G
G
G
S
V
Q
I
V
Y
K
P
V
D
L
S
K
V
T
S
K
C
G
S
L
325
326
G
N
I
H
H
K
P
G
G
G
Q
V
E
V
K
S
E
K
L
D
F
K
D
R
V
350
351
Q
S
K
I
G
S
L
D
N
I
T
H
V
P
G
G
G
N
K
K
I
E
T
H
K
375
376
L
T
F
R
E
N
A
K
A
K
T
D
H
G
A
E
I
V
Y
K
S
P
V
V
S
400
401
G
D
T
S
P
R
H
L
S
N
V
S
S
T
G
S
I
D
M
V
D
S
P
Q
L
425
426
A
T
L
A
D
E
V
S
A
S
L
A
K
Q
G
L
441
Chain 5
1
M
A
E
P
R
Q
E
F
E
V
M
E
D
H
A
G
T
Y
G
L
G
D
R
K
D
25
26
Q
G
G
Y
T
M
H
Q
D
Q
E
G
D
T
D
A
G
L
K
E
S
P
L
Q
T
50
51
P
T
E
D
G
S
E
E
P
G
S
E
T
S
D
A
K
S
T
P
T
A
E
D
V
75
76
T
A
P
L
V
D
E
G
A
P
G
K
Q
A
A
A
Q
P
H
T
E
I
P
E
G
100
101
T
T
A
E
E
A
G
I
G
D
T
P
S
L
E
D
E
A
A
G
H
V
T
Q
A
125
126
R
M
V
S
K
S
K
D
G
T
G
S
D
D
K
K
A
K
G
A
D
G
K
T
K
150
151
I
A
T
P
R
G
A
A
P
P
G
Q
K
G
Q
A
N
A
T
R
I
P
A
K
T
175
176
P
P
A
P
K
T
P
P
S
S
G
E
P
P
K
S
G
D
R
S
G
Y
S
S
P
200
201
G
S
P
G
T
P
G
S
R
S
R
T
P
S
L
P
T
P
P
T
R
E
P
K
K
225
226
V
A
V
V
R
T
P
P
K
S
P
S
S
A
K
S
R
L
Q
T
A
P
V
P
M
250
251
P
D
L
K
N
V
K
S
K
I
G
S
T
E
N
L
K
H
Q
P
G
G
G
K
V
275
276
Q
I
I
N
K
K
L
D
L
S
N
V
Q
S
K
C
G
S
K
D
N
I
K
H
V
300
301
P
G
G
G
S
V
Q
I
V
Y
K
P
V
D
L
S
K
V
T
S
K
C
G
S
L
325
326
G
N
I
H
H
K
P
G
G
G
Q
V
E
V
K
S
E
K
L
D
F
K
D
R
V
350
351
Q
S
K
I
G
S
L
D
N
I
T
H
V
P
G
G
G
N
K
K
I
E
T
H
K
375
376
L
T
F
R
E
N
A
K
A
K
T
D
H
G
A
E
I
V
Y
K
S
P
V
V
S
400
401
G
D
T
S
P
R
H
L
S
N
V
S
S
T
G
S
I
D
M
V
D
S
P
Q
L
425
426
A
T
L
A
D
E
V
S
A
S
L
A
K
Q
G
L
441
Chain 6
1
M
A
E
P
R
Q
E
F
E
V
M
E
D
H
A
G
T
Y
G
L
G
D
R
K
D
25
26
Q
G
G
Y
T
M
H
Q
D
Q
E
G
D
T
D
A
G
L
K
E
S
P
L
Q
T
50
51
P
T
E
D
G
S
E
E
P
G
S
E
T
S
D
A
K
S
T
P
T
A
E
D
V
75
76
T
A
P
L
V
D
E
G
A
P
G
K
Q
A
A
A
Q
P
H
T
E
I
P
E
G
100
101
T
T
A
E
E
A
G
I
G
D
T
P
S
L
E
D
E
A
A
G
H
V
T
Q
A
125
126
R
M
V
S
K
S
K
D
G
T
G
S
D
D
K
K
A
K
G
A
D
G
K
T
K
150
151
I
A
T
P
R
G
A
A
P
P
G
Q
K
G
Q
A
N
A
T
R
I
P
A
K
T
175
176
P
P
A
P
K
T
P
P
S
S
G
E
P
P
K
S
G
D
R
S
G
Y
S
S
P
200
201
G
S
P
G
T
P
G
S
R
S
R
T
P
S
L
P
T
P
P
T
R
E
P
K
K
225
226
V
A
V
V
R
T
P
P
K
S
P
S
S
A
K
S
R
L
Q
T
A
P
V
P
M
250
251
P
D
L
K
N
V
K
S
K
I
G
S
T
E
N
L
K
H
Q
P
G
G
G
K
V
275
276
Q
I
I
N
K
K
L
D
L
S
N
V
Q
S
K
C
G
S
K
D
N
I
K
H
V
300
301
P
G
G
G
S
V
Q
I
V
Y
K
P
V
D
L
S
K
V
T
S
K
C
G
S
L
325
326
G
N
I
H
H
K
P
G
G
G
Q
V
E
V
K
S
E
K
L
D
F
K
D
R
V
350
351
Q
S
K
I
G
S
L
D
N
I
T
H
V
P
G
G
G
N
K
K
I
E
T
H
K
375
376
L
T
F
R
E
N
A
K
A
K
T
D
H
G
A
E
I
V
Y
K
S
P
V
V
S
400
401
G
D
T
S
P
R
H
L
S
N
V
S
S
T
G
S
I
D
M
V
D
S
P
Q
L
425
426
A
T
L
A
D
E
V
S
A
S
L
A
K
Q
G
L
441
Helix: Magenta; Strand: Yellow; Coil & Turn: White.
Charged residues and Proline are highlighed in blue.
Description
Paired helical filament from sporadic Alzheimer's disease brain
The high-resolution structures of PHFs and SFs from the frontal cortex of 3 cases of AD, 2 sporadic and 1 inherited, were determined by cryo-EM. PHFs and SFs were made of two C-shaped protofilaments with a combined cross-Beta/Beta-helix structure. The higher resolution structures obtained here showed two additional amino acids at each end of the protofilament. The immuno-EM findings, which indicated the presence of repeats 3 and 4, but not of the N-terminal regions of repeats 1 and 2, of tau in the filament cores of all AD cases, were consistent with the cryo-EM results.
Literature
PMID:
30276465
Author(s):
Falcon, B., Zhang, W., Schweighauser, M., Murzin, A.G., Vidal, R., Garringer, H.J., Ghetti, B., Scheres, S.H.W., Goedert, M.
Reference:
Acta Neuropathol. 2018 Nov;136(5):699-708.
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Entry:
CSV
JSON
Structure:
PDB
CIF
FASTA
Contact Network:
CSV
JSON
Protein Information
Protein Name:
Microtubule-associated protein tau
Alternative Name:
Neurofibrillary tangle protein, Paired helical filament-tau
Gene Name:
MAPT, MAPTL, MTBT1, TAU
Sequence Length:
441
Species:
Homo sapiens
Mutation(s):
No
E.C. Number:
UniProt ID:
P10636
Keyword(s):
Microtubule-associated protein tau
Structure Information
PDB ID:
6HRE
Amyloid Category:
Amyloid
Type:
Fibril
Global Stoichiometry:
Homo 6-mer - A6
PDB Classification:
PROTEIN FIBRIL
Method:
ELECTRON MICROSCOPY
Resolution (
Å
):
3.2
R free:
Entry:S-0553
PDB ID: 6HRF
CSV
JSON
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Structure
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Sequence & Sec. Str.
Chain 1
1
M
A
E
P
R
Q
E
F
E
V
M
E
D
H
A
G
T
Y
G
L
G
D
R
K
D
25
26
Q
G
G
Y
T
M
H
Q
D
Q
E
G
D
T
D
A
G
L
K
E
S
P
L
Q
T
50
51
P
T
E
D
G
S
E
E
P
G
S
E
T
S
D
A
K
S
T
P
T
A
E
D
V
75
76
T
A
P
L
V
D
E
G
A
P
G
K
Q
A
A
A
Q
P
H
T
E
I
P
E
G
100
101
T
T
A
E
E
A
G
I
G
D
T
P
S
L
E
D
E
A
A
G
H
V
T
Q
A
125
126
R
M
V
S
K
S
K
D
G
T
G
S
D
D
K
K
A
K
G
A
D
G
K
T
K
150
151
I
A
T
P
R
G
A
A
P
P
G
Q
K
G
Q
A
N
A
T
R
I
P
A
K
T
175
176
P
P
A
P
K
T
P
P
S
S
G
E
P
P
K
S
G
D
R
S
G
Y
S
S
P
200
201
G
S
P
G
T
P
G
S
R
S
R
T
P
S
L
P
T
P
P
T
R
E
P
K
K
225
226
V
A
V
V
R
T
P
P
K
S
P
S
S
A
K
S
R
L
Q
T
A
P
V
P
M
250
251
P
D
L
K
N
V
K
S
K
I
G
S
T
E
N
L
K
H
Q
P
G
G
G
K
V
275
276
Q
I
I
N
K
K
L
D
L
S
N
V
Q
S
K
C
G
S
K
D
N
I
K
H
V
300
301
P
G
G
G
S
V
Q
I
V
Y
K
P
V
D
L
S
K
V
T
S
K
C
G
S
L
325
326
G
N
I
H
H
K
P
G
G
G
Q
V
E
V
K
S
E
K
L
D
F
K
D
R
V
350
351
Q
S
K
I
G
S
L
D
N
I
T
H
V
P
G
G
G
N
K
K
I
E
T
H
K
375
376
L
T
F
R
E
N
A
K
A
K
T
D
H
G
A
E
I
V
Y
K
S
P
V
V
S
400
401
G
D
T
S
P
R
H
L
S
N
V
S
S
T
G
S
I
D
M
V
D
S
P
Q
L
425
426
A
T
L
A
D
E
V
S
A
S
L
A
K
Q
G
L
441
Chain 2
1
M
A
E
P
R
Q
E
F
E
V
M
E
D
H
A
G
T
Y
G
L
G
D
R
K
D
25
26
Q
G
G
Y
T
M
H
Q
D
Q
E
G
D
T
D
A
G
L
K
E
S
P
L
Q
T
50
51
P
T
E
D
G
S
E
E
P
G
S
E
T
S
D
A
K
S
T
P
T
A
E
D
V
75
76
T
A
P
L
V
D
E
G
A
P
G
K
Q
A
A
A
Q
P
H
T
E
I
P
E
G
100
101
T
T
A
E
E
A
G
I
G
D
T
P
S
L
E
D
E
A
A
G
H
V
T
Q
A
125
126
R
M
V
S
K
S
K
D
G
T
G
S
D
D
K
K
A
K
G
A
D
G
K
T
K
150
151
I
A
T
P
R
G
A
A
P
P
G
Q
K
G
Q
A
N
A
T
R
I
P
A
K
T
175
176
P
P
A
P
K
T
P
P
S
S
G
E
P
P
K
S
G
D
R
S
G
Y
S
S
P
200
201
G
S
P
G
T
P
G
S
R
S
R
T
P
S
L
P
T
P
P
T
R
E
P
K
K
225
226
V
A
V
V
R
T
P
P
K
S
P
S
S
A
K
S
R
L
Q
T
A
P
V
P
M
250
251
P
D
L
K
N
V
K
S
K
I
G
S
T
E
N
L
K
H
Q
P
G
G
G
K
V
275
276
Q
I
I
N
K
K
L
D
L
S
N
V
Q
S
K
C
G
S
K
D
N
I
K
H
V
300
301
P
G
G
G
S
V
Q
I
V
Y
K
P
V
D
L
S
K
V
T
S
K
C
G
S
L
325
326
G
N
I
H
H
K
P
G
G
G
Q
V
E
V
K
S
E
K
L
D
F
K
D
R
V
350
351
Q
S
K
I
G
S
L
D
N
I
T
H
V
P
G
G
G
N
K
K
I
E
T
H
K
375
376
L
T
F
R
E
N
A
K
A
K
T
D
H
G
A
E
I
V
Y
K
S
P
V
V
S
400
401
G
D
T
S
P
R
H
L
S
N
V
S
S
T
G
S
I
D
M
V
D
S
P
Q
L
425
426
A
T
L
A
D
E
V
S
A
S
L
A
K
Q
G
L
441
Chain 3
1
M
A
E
P
R
Q
E
F
E
V
M
E
D
H
A
G
T
Y
G
L
G
D
R
K
D
25
26
Q
G
G
Y
T
M
H
Q
D
Q
E
G
D
T
D
A
G
L
K
E
S
P
L
Q
T
50
51
P
T
E
D
G
S
E
E
P
G
S
E
T
S
D
A
K
S
T
P
T
A
E
D
V
75
76
T
A
P
L
V
D
E
G
A
P
G
K
Q
A
A
A
Q
P
H
T
E
I
P
E
G
100
101
T
T
A
E
E
A
G
I
G
D
T
P
S
L
E
D
E
A
A
G
H
V
T
Q
A
125
126
R
M
V
S
K
S
K
D
G
T
G
S
D
D
K
K
A
K
G
A
D
G
K
T
K
150
151
I
A
T
P
R
G
A
A
P
P
G
Q
K
G
Q
A
N
A
T
R
I
P
A
K
T
175
176
P
P
A
P
K
T
P
P
S
S
G
E
P
P
K
S
G
D
R
S
G
Y
S
S
P
200
201
G
S
P
G
T
P
G
S
R
S
R
T
P
S
L
P
T
P
P
T
R
E
P
K
K
225
226
V
A
V
V
R
T
P
P
K
S
P
S
S
A
K
S
R
L
Q
T
A
P
V
P
M
250
251
P
D
L
K
N
V
K
S
K
I
G
S
T
E
N
L
K
H
Q
P
G
G
G
K
V
275
276
Q
I
I
N
K
K
L
D
L
S
N
V
Q
S
K
C
G
S
K
D
N
I
K
H
V
300
301
P
G
G
G
S
V
Q
I
V
Y
K
P
V
D
L
S
K
V
T
S
K
C
G
S
L
325
326
G
N
I
H
H
K
P
G
G
G
Q
V
E
V
K
S
E
K
L
D
F
K
D
R
V
350
351
Q
S
K
I
G
S
L
D
N
I
T
H
V
P
G
G
G
N
K
K
I
E
T
H
K
375
376
L
T
F
R
E
N
A
K
A
K
T
D
H
G
A
E
I
V
Y
K
S
P
V
V
S
400
401
G
D
T
S
P
R
H
L
S
N
V
S
S
T
G
S
I
D
M
V
D
S
P
Q
L
425
426
A
T
L
A
D
E
V
S
A
S
L
A
K
Q
G
L
441
Chain 4
1
M
A
E
P
R
Q
E
F
E
V
M
E
D
H
A
G
T
Y
G
L
G
D
R
K
D
25
26
Q
G
G
Y
T
M
H
Q
D
Q
E
G
D
T
D
A
G
L
K
E
S
P
L
Q
T
50
51
P
T
E
D
G
S
E
E
P
G
S
E
T
S
D
A
K
S
T
P
T
A
E
D
V
75
76
T
A
P
L
V
D
E
G
A
P
G
K
Q
A
A
A
Q
P
H
T
E
I
P
E
G
100
101
T
T
A
E
E
A
G
I
G
D
T
P
S
L
E
D
E
A
A
G
H
V
T
Q
A
125
126
R
M
V
S
K
S
K
D
G
T
G
S
D
D
K
K
A
K
G
A
D
G
K
T
K
150
151
I
A
T
P
R
G
A
A
P
P
G
Q
K
G
Q
A
N
A
T
R
I
P
A
K
T
175
176
P
P
A
P
K
T
P
P
S
S
G
E
P
P
K
S
G
D
R
S
G
Y
S
S
P
200
201
G
S
P
G
T
P
G
S
R
S
R
T
P
S
L
P
T
P
P
T
R
E
P
K
K
225
226
V
A
V
V
R
T
P
P
K
S
P
S
S
A
K
S
R
L
Q
T
A
P
V
P
M
250
251
P
D
L
K
N
V
K
S
K
I
G
S
T
E
N
L
K
H
Q
P
G
G
G
K
V
275
276
Q
I
I
N
K
K
L
D
L
S
N
V
Q
S
K
C
G
S
K
D
N
I
K
H
V
300
301
P
G
G
G
S
V
Q
I
V
Y
K
P
V
D
L
S
K
V
T
S
K
C
G
S
L
325
326
G
N
I
H
H
K
P
G
G
G
Q
V
E
V
K
S
E
K
L
D
F
K
D
R
V
350
351
Q
S
K
I
G
S
L
D
N
I
T
H
V
P
G
G
G
N
K
K
I
E
T
H
K
375
376
L
T
F
R
E
N
A
K
A
K
T
D
H
G
A
E
I
V
Y
K
S
P
V
V
S
400
401
G
D
T
S
P
R
H
L
S
N
V
S
S
T
G
S
I
D
M
V
D
S
P
Q
L
425
426
A
T
L
A
D
E
V
S
A
S
L
A
K
Q
G
L
441
Chain 5
1
M
A
E
P
R
Q
E
F
E
V
M
E
D
H
A
G
T
Y
G
L
G
D
R
K
D
25
26
Q
G
G
Y
T
M
H
Q
D
Q
E
G
D
T
D
A
G
L
K
E
S
P
L
Q
T
50
51
P
T
E
D
G
S
E
E
P
G
S
E
T
S
D
A
K
S
T
P
T
A
E
D
V
75
76
T
A
P
L
V
D
E
G
A
P
G
K
Q
A
A
A
Q
P
H
T
E
I
P
E
G
100
101
T
T
A
E
E
A
G
I
G
D
T
P
S
L
E
D
E
A
A
G
H
V
T
Q
A
125
126
R
M
V
S
K
S
K
D
G
T
G
S
D
D
K
K
A
K
G
A
D
G
K
T
K
150
151
I
A
T
P
R
G
A
A
P
P
G
Q
K
G
Q
A
N
A
T
R
I
P
A
K
T
175
176
P
P
A
P
K
T
P
P
S
S
G
E
P
P
K
S
G
D
R
S
G
Y
S
S
P
200
201
G
S
P
G
T
P
G
S
R
S
R
T
P
S
L
P
T
P
P
T
R
E
P
K
K
225
226
V
A
V
V
R
T
P
P
K
S
P
S
S
A
K
S
R
L
Q
T
A
P
V
P
M
250
251
P
D
L
K
N
V
K
S
K
I
G
S
T
E
N
L
K
H
Q
P
G
G
G
K
V
275
276
Q
I
I
N
K
K
L
D
L
S
N
V
Q
S
K
C
G
S
K
D
N
I
K
H
V
300
301
P
G
G
G
S
V
Q
I
V
Y
K
P
V
D
L
S
K
V
T
S
K
C
G
S
L
325
326
G
N
I
H
H
K
P
G
G
G
Q
V
E
V
K
S
E
K
L
D
F
K
D
R
V
350
351
Q
S
K
I
G
S
L
D
N
I
T
H
V
P
G
G
G
N
K
K
I
E
T
H
K
375
376
L
T
F
R
E
N
A
K
A
K
T
D
H
G
A
E
I
V
Y
K
S
P
V
V
S
400
401
G
D
T
S
P
R
H
L
S
N
V
S
S
T
G
S
I
D
M
V
D
S
P
Q
L
425
426
A
T
L
A
D
E
V
S
A
S
L
A
K
Q
G
L
441
Chain 6
1
M
A
E
P
R
Q
E
F
E
V
M
E
D
H
A
G
T
Y
G
L
G
D
R
K
D
25
26
Q
G
G
Y
T
M
H
Q
D
Q
E
G
D
T
D
A
G
L
K
E
S
P
L
Q
T
50
51
P
T
E
D
G
S
E
E
P
G
S
E
T
S
D
A
K
S
T
P
T
A
E
D
V
75
76
T
A
P
L
V
D
E
G
A
P
G
K
Q
A
A
A
Q
P
H
T
E
I
P
E
G
100
101
T
T
A
E
E
A
G
I
G
D
T
P
S
L
E
D
E
A
A
G
H
V
T
Q
A
125
126
R
M
V
S
K
S
K
D
G
T
G
S
D
D
K
K
A
K
G
A
D
G
K
T
K
150
151
I
A
T
P
R
G
A
A
P
P
G
Q
K
G
Q
A
N
A
T
R
I
P
A
K
T
175
176
P
P
A
P
K
T
P
P
S
S
G
E
P
P
K
S
G
D
R
S
G
Y
S
S
P
200
201
G
S
P
G
T
P
G
S
R
S
R
T
P
S
L
P
T
P
P
T
R
E
P
K
K
225
226
V
A
V
V
R
T
P
P
K
S
P
S
S
A
K
S
R
L
Q
T
A
P
V
P
M
250
251
P
D
L
K
N
V
K
S
K
I
G
S
T
E
N
L
K
H
Q
P
G
G
G
K
V
275
276
Q
I
I
N
K
K
L
D
L
S
N
V
Q
S
K
C
G
S
K
D
N
I
K
H
V
300
301
P
G
G
G
S
V
Q
I
V
Y
K
P
V
D
L
S
K
V
T
S
K
C
G
S
L
325
326
G
N
I
H
H
K
P
G
G
G
Q
V
E
V
K
S
E
K
L
D
F
K
D
R
V
350
351
Q
S
K
I
G
S
L
D
N
I
T
H
V
P
G
G
G
N
K
K
I
E
T
H
K
375
376
L
T
F
R
E
N
A
K
A
K
T
D
H
G
A
E
I
V
Y
K
S
P
V
V
S
400
401
G
D
T
S
P
R
H
L
S
N
V
S
S
T
G
S
I
D
M
V
D
S
P
Q
L
425
426
A
T
L
A
D
E
V
S
A
S
L
A
K
Q
G
L
441
Helix: Magenta; Strand: Yellow; Coil & Turn: White.
Charged residues and Proline are highlighed in blue.
Description
Straight filament from sporadic Alzheimer's disease brain
The high-resolution structures of PHFs and SFs from the frontal cortex of 3 cases of AD, 2 sporadic and 1 inherited, were determined by cryo-EM. PHFs and SFs were made of two C-shaped protofilaments with a combined cross-Beta/Beta-helix structure. The higher resolution structures obtained here showed two additional amino acids at each end of the protofilament. The immuno-EM findings, which indicated the presence of repeats 3 and 4, but not of the N-terminal regions of repeats 1 and 2, of tau in the filament cores of all AD cases, were consistent with the cryo-EM results.
Literature
PMID:
30276465
Author(s):
Falcon, B., Zhang, W., Schweighauser, M., Murzin, A.G., Vidal, R., Garringer, H.J., Ghetti, B., Scheres, S.H.W., Goedert, M.
Reference:
Acta Neuropathol. 2018 Nov;136(5):699-708.
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Entry:
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Structure:
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FASTA
Contact Network:
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JSON
Protein Information
Protein Name:
Microtubule-associated protein tau
Alternative Name:
Neurofibrillary tangle protein, Paired helical filament-tau
Gene Name:
MAPT, MAPTL, MTBT1, TAU
Sequence Length:
441
Species:
Homo sapiens
Mutation(s):
No
E.C. Number:
UniProt ID:
P10636
Keyword(s):
Microtubule-associated protein tau
Structure Information
PDB ID:
6HRF
Amyloid Category:
Amyloid
Type:
Fibril
Global Stoichiometry:
Homo 6-mer - A6
PDB Classification:
PROTEIN FIBRIL
Method:
ELECTRON MICROSCOPY
Resolution (
Å
):
3.3
R free:
Entry:S-0554
PDB ID: 6HUD
CSV
JSON
Close ×
Structure
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Sequence & Sec. Str.
Chain 1
1
N
F
M
L
T
Q
P
H
S
V
S
E
S
P
G
K
T
L
T
I
S
C
T
G
S
25
26
S
A
S
I
A
S
H
Y
V
Q
W
Y
Q
Q
R
P
G
G
A
P
T
T
L
I
Y
50
51
E
N
D
Q
R
P
S
E
V
P
D
R
F
S
G
S
I
D
S
S
S
N
S
A
S
75
76
L
T
I
S
G
L
K
T
E
D
E
A
D
Y
Y
C
Q
S
Y
D
G
N
N
H
W
100
101
V
F
G
G
G
T
K
L
T
V
L
S
Q
P
K
A
A
P
S
V
T
L
F
P
P
125
126
S
S
E
E
L
Q
A
N
K
A
T
136
Chain 2
1
N
F
M
L
T
Q
P
H
S
V
S
E
S
P
G
K
T
L
T
I
S
C
T
G
S
25
26
S
A
S
I
A
S
H
Y
V
Q
W
Y
Q
Q
R
P
G
G
A
P
T
T
L
I
Y
50
51
E
N
D
Q
R
P
S
E
V
P
D
R
F
S
G
S
I
D
S
S
S
N
S
A
S
75
76
L
T
I
S
G
L
K
T
E
D
E
A
D
Y
Y
C
Q
S
Y
D
G
N
N
H
W
100
101
V
F
G
G
G
T
K
L
T
V
L
S
Q
P
K
A
A
P
S
V
T
L
F
P
P
125
126
S
S
E
E
L
Q
A
N
K
A
T
136
Chain 3
1
N
F
M
L
T
Q
P
H
S
V
S
E
S
P
G
K
T
L
T
I
S
C
T
G
S
25
26
S
A
S
I
A
S
H
Y
V
Q
W
Y
Q
Q
R
P
G
G
A
P
T
T
L
I
Y
50
51
E
N
D
Q
R
P
S
E
V
P
D
R
F
S
G
S
I
D
S
S
S
N
S
A
S
75
76
L
T
I
S
G
L
K
T
E
D
E
A
D
Y
Y
C
Q
S
Y
D
G
N
N
H
W
100
101
V
F
G
G
G
T
K
L
T
V
L
S
Q
P
K
A
A
P
S
V
T
L
F
P
P
125
126
S
S
E
E
L
Q
A
N
K
A
T
136
Chain 4
1
N
F
M
L
T
Q
P
H
S
V
S
E
S
P
G
K
T
L
T
I
S
C
T
G
S
25
26
S
A
S
I
A
S
H
Y
V
Q
W
Y
Q
Q
R
P
G
G
A
P
T
T
L
I
Y
50
51
E
N
D
Q
R
P
S
E
V
P
D
R
F
S
G
S
I
D
S
S
S
N
S
A
S
75
76
L
T
I
S
G
L
K
T
E
D
E
A
D
Y
Y
C
Q
S
Y
D
G
N
N
H
W
100
101
V
F
G
G
G
T
K
L
T
V
L
S
Q
P
K
A
A
P
S
V
T
L
F
P
P
125
126
S
S
E
E
L
Q
A
N
K
A
T
136
Chain 5
1
N
F
M
L
T
Q
P
H
S
V
S
E
S
P
G
K
T
L
T
I
S
C
T
G
S
25
26
S
A
S
I
A
S
H
Y
V
Q
W
Y
Q
Q
R
P
G
G
A
P
T
T
L
I
Y
50
51
E
N
D
Q
R
P
S
E
V
P
D
R
F
S
G
S
I
D
S
S
S
N
S
A
S
75
76
L
T
I
S
G
L
K
T
E
D
E
A
D
Y
Y
C
Q
S
Y
D
G
N
N
H
W
100
101
V
F
G
G
G
T
K
L
T
V
L
S
Q
P
K
A
A
P
S
V
T
L
F
P
P
125
126
S
S
E
E
L
Q
A
N
K
A
T
136
Helix: Magenta; Strand: Yellow; Coil & Turn: White.
Charged residues and Proline are highlighed in blue.
Description
Cryo-EM structure of cardiac amyloid fibrils from an immunoglobulin light chain (AL) amyloidosis patient.
The cryo-electron microscopy map and molecular model of amyloid fibrils extracted from the heart of an AL amyloidosis patient with severe amyloid cardiomyopathy. The helical fibrils are composed of a single protofilament, showing typical stacking and cross-Beta architecture.
Literature
PMID:
30894521
Author(s):
Swuec, P., Lavatelli, F., Tasaki, M., Paissoni, C., Rognoni, P., Maritan, M., Brambilla, F., Milani, P., Mauri, P., Camilloni, C., Palladini, G., Merlini, G., Ricagno, S., Bolognesi, M.
Reference:
Nat Commun. 2019 Mar 20;10(1):1269.
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Entry:
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Structure:
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Contact Network:
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Protein Information
Protein Name:
Immunoglobulin Light-Chain
Alternative Name:
Gene Name:
Sequence Length:
136
Species:
Homo sapiens
Mutation(s):
No
E.C. Number:
UniProt ID:
Keyword(s):
Monoclonal immunoglobulin light chains (LC)
Structure Information
PDB ID:
6HUD
Amyloid Category:
Amyloid
Type:
Fibril
Global Stoichiometry:
Homo 5-mer - A5
PDB Classification:
PROTEIN FIBRIL
Method:
ELECTRON MICROSCOPY
Resolution (
Å
):
4.0
R free:
Entry:S-0555
PDB ID: 6IC3
CSV
JSON
Close ×
Structure
Press 'p' to pause
View interactive contact network
Sequence & Sec. Str.
Chain 1
1
V
L
T
Q
P
P
S
A
S
G
T
P
G
Q
R
V
T
I
S
C
S
G
R
S
S
25
26
N
I
G
R
N
L
V
K
W
Y
Q
Q
F
P
G
T
A
P
K
L
L
I
Y
S
N
50
51
D
Q
R
P
S
G
V
P
D
R
F
S
G
S
K
S
G
T
S
A
S
L
A
V
S
75
76
G
L
Q
S
E
D
E
A
D
Y
Y
C
A
A
W
D
A
T
L
N
A
W
V
F
G
100
101
G
G
T
K
L
T
V
L
S
Q
P
K
A
A
P
S
116
Chain 2
1
V
L
T
Q
P
P
S
A
S
G
T
P
G
Q
R
V
T
I
S
C
S
G
R
S
S
25
26
N
I
G
R
N
L
V
K
W
Y
Q
Q
F
P
G
T
A
P
K
L
L
I
Y
S
N
50
51
D
Q
R
P
S
G
V
P
D
R
F
S
G
S
K
S
G
T
S
A
S
L
A
V
S
75
76
G
L
Q
S
E
D
E
A
D
Y
Y
C
A
A
W
D
A
T
L
N
A
W
V
F
G
100
101
G
G
T
K
L
T
V
L
S
Q
P
K
A
A
P
S
116
Chain 3
1
V
L
T
Q
P
P
S
A
S
G
T
P
G
Q
R
V
T
I
S
C
S
G
R
S
S
25
26
N
I
G
R
N
L
V
K
W
Y
Q
Q
F
P
G
T
A
P
K
L
L
I
Y
S
N
50
51
D
Q
R
P
S
G
V
P
D
R
F
S
G
S
K
S
G
T
S
A
S
L
A
V
S
75
76
G
L
Q
S
E
D
E
A
D
Y
Y
C
A
A
W
D
A
T
L
N
A
W
V
F
G
100
101
G
G
T
K
L
T
V
L
S
Q
P
K
A
A
P
S
116
Chain 4
1
V
L
T
Q
P
P
S
A
S
G
T
P
G
Q
R
V
T
I
S
C
S
G
R
S
S
25
26
N
I
G
R
N
L
V
K
W
Y
Q
Q
F
P
G
T
A
P
K
L
L
I
Y
S
N
50
51
D
Q
R
P
S
G
V
P
D
R
F
S
G
S
K
S
G
T
S
A
S
L
A
V
S
75
76
G
L
Q
S
E
D
E
A
D
Y
Y
C
A
A
W
D
A
T
L
N
A
W
V
F
G
100
101
G
G
T
K
L
T
V
L
S
Q
P
K
A
A
P
S
116
Chain 5
1
V
L
T
Q
P
P
S
A
S
G
T
P
G
Q
R
V
T
I
S
C
S
G
R
S
S
25
26
N
I
G
R
N
L
V
K
W
Y
Q
Q
F
P
G
T
A
P
K
L
L
I
Y
S
N
50
51
D
Q
R
P
S
G
V
P
D
R
F
S
G
S
K
S
G
T
S
A
S
L
A
V
S
75
76
G
L
Q
S
E
D
E
A
D
Y
Y
C
A
A
W
D
A
T
L
N
A
W
V
F
G
100
101
G
G
T
K
L
T
V
L
S
Q
P
K
A
A
P
S
116
Chain 6
1
V
L
T
Q
P
P
S
A
S
G
T
P
G
Q
R
V
T
I
S
C
S
G
R
S
S
25
26
N
I
G
R
N
L
V
K
W
Y
Q
Q
F
P
G
T
A
P
K
L
L
I
Y
S
N
50
51
D
Q
R
P
S
G
V
P
D
R
F
S
G
S
K
S
G
T
S
A
S
L
A
V
S
75
76
G
L
Q
S
E
D
E
A
D
Y
Y
C
A
A
W
D
A
T
L
N
A
W
V
F
G
100
101
G
G
T
K
L
T
V
L
S
Q
P
K
A
A
P
S
116
Chain 7
1
V
L
T
Q
P
P
S
A
S
G
T
P
G
Q
R
V
T
I
S
C
S
G
R
S
S
25
26
N
I
G
R
N
L
V
K
W
Y
Q
Q
F
P
G
T
A
P
K
L
L
I
Y
S
N
50
51
D
Q
R
P
S
G
V
P
D
R
F
S
G
S
K
S
G
T
S
A
S
L
A
V
S
75
76
G
L
Q
S
E
D
E
A
D
Y
Y
C
A
A
W
D
A
T
L
N
A
W
V
F
G
100
101
G
G
T
K
L
T
V
L
S
Q
P
K
A
A
P
S
116
Chain 8
1
V
L
T
Q
P
P
S
A
S
G
T
P
G
Q
R
V
T
I
S
C
S
G
R
S
S
25
26
N
I
G
R
N
L
V
K
W
Y
Q
Q
F
P
G
T
A
P
K
L
L
I
Y
S
N
50
51
D
Q
R
P
S
G
V
P
D
R
F
S
G
S
K
S
G
T
S
A
S
L
A
V
S
75
76
G
L
Q
S
E
D
E
A
D
Y
Y
C
A
A
W
D
A
T
L
N
A
W
V
F
G
100
101
G
G
T
K
L
T
V
L
S
Q
P
K
A
A
P
S
116
Helix: Magenta; Strand: Yellow; Coil & Turn: White.
Charged residues and Proline are highlighed in blue.
Description
AL amyloid fibril from a lambda 1 light chain
The structure of a Lambda1 AL amyloid fibril from an explanted human heart. The fibril core consists of a 91-residue segment presenting an all-beta fold with ten mutagenic changes compared to the germ line. The conformation differs substantially from natively folded light chains: a rotational switch around the intramolecular disulphide bond being the crucial structural rearrangement underlying fibril formation.
Literature
PMID:
30894526
Author(s):
Radamaker, L., Lin, Y.H., Annamalai, K., Huhn, S., Hegenbart, U., Schonland, S.O., Fritz, G., Schmidt, M., Fandrich, M.
Reference:
Nat Commun. 2019 Mar 20;10(1):1103.
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Structure:
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FASTA
Contact Network:
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Protein Information
Protein Name:
Immunoglobulin lambda 1 light chain
Alternative Name:
Gene Name:
Sequence Length:
116
Species:
Homo sapiens
Mutation(s):
No
E.C. Number:
UniProt ID:
Keyword(s):
lambda 1 light chain fragment, residues 3-118
Structure Information
PDB ID:
6IC3
Amyloid Category:
Amyloid
Type:
Fibril
Global Stoichiometry:
Homo 8-mer - A8
PDB Classification:
PROTEIN FIBRIL
Method:
ELECTRON MICROSCOPY
Resolution (
Å
):
3.3
R free:
Entry:S-0556
PDB ID: 6IMX
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Protein Contacts Atlas
Sequence & Sec. Str.
Chain 1
1
M
R
G
S
H
H
H
H
H
H
G
S
M
A
S
H
R
L
L
L
L
C
L
A
G
25
26
L
V
F
V
S
E
A
G
P
T
G
T
G
E
S
K
C
P
L
M
V
K
V
L
D
50
51
A
V
R
G
S
P
A
I
N
V
A
M
H
V
F
R
K
A
A
D
D
T
W
E
P
75
76
F
A
S
G
K
T
S
E
S
G
E
L
H
G
L
T
T
E
E
E
F
V
E
G
I
100
101
Y
K
V
E
I
D
T
K
S
Y
W
K
A
L
G
I
S
P
F
H
E
H
A
E
V
125
126
V
F
T
A
N
D
S
G
P
R
R
Y
T
I
A
A
L
L
S
P
Y
S
Y
S
T
150
151
T
A
V
V
T
N
P
K
E
159
Chain 2
1
M
R
G
S
H
H
H
H
H
H
G
S
M
A
S
H
R
L
L
L
L
C
L
A
G
25
26
L
V
F
V
S
E
A
G
P
T
G
T
G
E
S
K
C
P
L
M
V
K
V
L
D
50
51
A
V
R
G
S
P
A
I
N
V
A
M
H
V
F
R
K
A
A
D
D
T
W
E
P
75
76
F
A
S
G
K
T
S
E
S
G
E
L
H
G
L
T
T
E
E
E
F
V
E
G
I
100
101
Y
K
V
E
I
D
T
K
S
Y
W
K
A
L
G
I
S
P
F
H
E
H
A
E
V
125
126
V
F
T
A
N
D
S
G
P
R
R
Y
T
I
A
A
L
L
S
P
Y
S
Y
S
T
150
151
T
A
V
V
T
N
P
K
E
159
Helix: Magenta; Strand: Yellow; Coil & Turn: White.
Charged residues and Proline are highlighed in blue.
Description
Crystal structure of V30M mutated transthyretin in complex with 18-Crown-6; Crown Ethers as Transthyretin Amyloidogenesis Inhibitors.
Development of a small molecule that binds to TTR and stabilizes the TTR tetramer is an efficient strategy for the treatment of amyloidosis. They report the discovery of anti-TTR amyloidogenesis activities of crown ethers. The 4'-carboxybenzo-18C6 (4) stabilized the TTR tetramer by binding to the allosteric sites on the molecular surface of the TTR tetramer.
Literature
PMID:
30688456
Author(s):
Yokoyama, T., Mizuguchi, M.
Reference:
J Med Chem. 2019 Feb 28;62(4):2076-2082.
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Entry:
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Structure:
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FASTA
Contact Network:
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Protein Information
Protein Name:
Transthyretin
Alternative Name:
ATTR, Prealbumin, TBPA
Gene Name:
TTR, PALB
Sequence Length:
159
Species:
Homo sapiens
Mutation(s):
V30M
E.C. Number:
UniProt ID:
P02766
Keyword(s):
Transthyretin
Structure Information
PDB ID:
6IMX
Amyloid Category:
Non-amyloid
Type:
Inhibitor complex
Global Stoichiometry:
Homo 4-mer - A4
PDB Classification:
TRANSPORT PROTEIN
Method:
X-RAY DIFFRACTION
Resolution (
Å
):
1.6
R free:
0.22399999
Ligand Information
Ligand ID
Chain ID
Ligand Formula
Ligand MW
Ligand Name
Ligand SMILES
InChI Key
O4B
A
C12 H24 O6
264.32
1,4,7,10,13,16-HEXAOXACYCLOOCTADECANE
C1COCCOCCOCCOCCOCCO1
XEZNGIUYQVAUSS-UHFFFAOYSA-N
O4B
B
C12 H24 O6
264.32
1,4,7,10,13,16-HEXAOXACYCLOOCTADECANE
C1COCCOCCOCCOCCOCCO1
XEZNGIUYQVAUSS-UHFFFAOYSA-N
Entry:S-0557
PDB ID: 6IMY
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Protein Contacts Atlas
Sequence & Sec. Str.
Chain 1
1
M
R
G
S
H
H
H
H
H
H
G
S
M
A
S
H
R
L
L
L
L
C
L
A
G
25
26
L
V
F
V
S
E
A
G
P
T
G
T
G
E
S
K
C
P
L
M
V
K
V
L
D
50
51
A
V
R
G
S
P
A
I
N
V
A
M
H
V
F
R
K
A
A
D
D
T
W
E
P
75
76
F
A
S
G
K
T
S
E
S
G
E
L
H
G
L
T
T
E
E
E
F
V
E
G
I
100
101
Y
K
V
E
I
D
T
K
S
Y
W
K
A
L
G
I
S
P
F
H
E
H
A
E
V
125
126
V
F
T
A
N
D
S
G
P
R
R
Y
T
I
A
A
L
L
S
P
Y
S
Y
S
T
150
151
T
A
V
V
T
N
P
K
E
159
Chain 2
1
M
R
G
S
H
H
H
H
H
H
G
S
M
A
S
H
R
L
L
L
L
C
L
A
G
25
26
L
V
F
V
S
E
A
G
P
T
G
T
G
E
S
K
C
P
L
M
V
K
V
L
D
50
51
A
V
R
G
S
P
A
I
N
V
A
M
H
V
F
R
K
A
A
D
D
T
W
E
P
75
76
F
A
S
G
K
T
S
E
S
G
E
L
H
G
L
T
T
E
E
E
F
V
E
G
I
100
101
Y
K
V
E
I
D
T
K
S
Y
W
K
A
L
G
I
S
P
F
H
E
H
A
E
V
125
126
V
F
T
A
N
D
S
G
P
R
R
Y
T
I
A
A
L
L
S
P
Y
S
Y
S
T
150
151
T
A
V
V
T
N
P
K
E
159
Helix: Magenta; Strand: Yellow; Coil & Turn: White.
Charged residues and Proline are highlighed in blue.
Description
Crystal structure of V30M mutated transthyretin in complex with 4'-caroboxybenzo-18-Crown-6
Development of a small molecule that binds to TTR and stabilizes the TTR tetramer is an efficient strategy for the treatment of amyloidosis. They report the discovery of anti-TTR amyloidogenesis activities of crown ethers. The 4'-carboxybenzo-18C6 (4) stabilized the TTR tetramer by binding to the allosteric sites on the molecular surface of the TTR tetramer.
Literature
PMID:
30688456
Author(s):
Yokoyama, T., Mizuguchi, M.
Reference:
J Med Chem. 2019 Feb 28;62(4):2076-2082.
Download
Entry:
CSV
JSON
Structure:
PDB
CIF
FASTA
Contact Network:
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JSON
Protein Information
Protein Name:
Transthyretin
Alternative Name:
ATTR, Prealbumin, TBPA
Gene Name:
TTR, PALB
Sequence Length:
159
Species:
Homo sapiens
Mutation(s):
V30M
E.C. Number:
UniProt ID:
P02766
Keyword(s):
Transthyretin
Structure Information
PDB ID:
6IMY
Amyloid Category:
Non-amyloid
Type:
Inhibitor complex
Global Stoichiometry:
Homo 4-mer - A4
PDB Classification:
TRANSPORT PROTEIN
Method:
X-RAY DIFFRACTION
Resolution (
Å
):
1.5
R free:
0.209
Ligand Information
Ligand ID
Chain ID
Ligand Formula
Ligand MW
Ligand Name
Ligand SMILES
InChI Key
AJU
A
C17 H24 O8
356.37
2,3,5,6,8,9,11,12,14,15-decahydro-1,4,7,10,13,16-benzohexaoxacyclooctadecine-18-carboxylic acid
c1cc2c(cc1C(=O)O)OCCOCCOCCOCCOCCO2
GFQYJVLOPVAPGJ-UHFFFAOYSA-N
AJU
B
C17 H24 O8
356.37
2,3,5,6,8,9,11,12,14,15-decahydro-1,4,7,10,13,16-benzohexaoxacyclooctadecine-18-carboxylic acid
c1cc2c(cc1C(=O)O)OCCOCCOCCOCCOCCO2
GFQYJVLOPVAPGJ-UHFFFAOYSA-N
Entry:S-0558
PDB ID: 6J60
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Sequence & Sec. Str.
Chain 1
1
G
F
G
G
N
D
N
F
G
9
Helix: Magenta; Strand: Yellow; Coil & Turn: White.
Charged residues and Proline are highlighed in blue.
Description
hnRNP A1 reversible amyloid core GFGGNDNFG (residues 209-217)
They synthesized the two segments and observed that both of them formed reversible fibrils and hydrogels, similar to the behavior of hnRAC1. The reversible fibrils formed by hnRAC2 and hnRAC3 exhibited typical cross-? architectures by X-ray fibril diffraction.
Literature
PMID:
Author(s):
Luo, F., Zhou, H., Gui, X., Li, D., Li, X., Liu, C.
Reference:
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Protein Information
Protein Name:
hnRNP A1
Alternative Name:
Gene Name:
Sequence Length:
9
Species:
Homo sapiens
Mutation(s):
No
E.C. Number:
UniProt ID:
Keyword(s):
9-mer peptide (GFGGNDNFG) from Heterogeneous nuclear ribonucleoprotein A1
Structure Information
PDB ID:
6J60
Amyloid Category:
Amyloid
Type:
Peptide
Global Stoichiometry:
PDB Classification:
RNA BINDING PROTEIN
Method:
ELECTRON CRYSTALLOGRAPHY
Resolution (
Å
):
0.96
R free:
0.248
Entry:S-0559
PDB ID: 6M7M
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Sequence & Sec. Str.
Chain 1
1
G
S
T
S
T
A
6
Helix: Magenta; Strand: Yellow; Coil & Turn: White.
Charged residues and Proline are highlighed in blue.
Description
rac-GSTSTA from degenerate octameric repeats in InaZ, residues 707-712
Homochiral and racemic GSTSTA form amyloid-like protofibrils with labile, corrugated antiparallel Beta-sheets that mate face to back. The racemic GSTSTA protofibril represents a new class of amyloid assembly in which all-left-handed sheets mate with their all-right-handed counterparts. This determination of racemic amyloid assemblies by MicroED reveals complex amyloid architectures and illustrates the racemic advantage in macromolecular crystallography
Literature
PMID:
30867917
Author(s):
Zee, C.T., Glynn, C., Gallagher-Jones, M., Miao, J., Santiago, C.G., Cascio, D., Gonen, T., Sawaya, M.R., Rodriguez, J.A.
Reference:
IUCrJ. 2019 Jan 24;6(Pt 2):197-205.
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Protein Information
Protein Name:
InaZ protein
Alternative Name:
Gene Name:
Sequence Length:
6
Species:
Pseudomonas syringae
Mutation(s):
No
E.C. Number:
UniProt ID:
Keyword(s):
L-GSTSTA from ice nucleation protein, inaZ, and its enantiomer, D-GSTSTA
Structure Information
PDB ID:
6M7M
Amyloid Category:
Amyloid
Type:
Fibril
Global Stoichiometry:
PDB Classification:
PROTEIN FIBRIL
Method:
X-RAY DIFFRACTION
Resolution (
Å
):
1.1
R free:
0.23600000
Entry:S-0560
PDB ID: 6M9I
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Sequence & Sec. Str.
Chain 1
1
G
S
T
S
T
A
6
Helix: Magenta; Strand: Yellow; Coil & Turn: White.
Charged residues and Proline are highlighed in blue.
Description
L-GSTSTA from degenerate octameric repeats in InaZ, residues 707-712
Homochiral and racemic GSTSTA form amyloid-like protofibrils with labile, corrugated antiparallel Beta-sheets that mate face to back. The racemic GSTSTA protofibril represents a new class of amyloid assembly in which all-left-handed sheets mate with their all-right-handed counterparts. This determination of racemic amyloid assemblies by MicroED reveals complex amyloid architectures and illustrates the racemic advantage in macromolecular crystallography
Literature
PMID:
30867917
Author(s):
Zee, C.T., Glynn, C., Gallagher-Jones, M., Miao, J., Santiago, C.G., Cascio, D., Gonen, T., Sawaya, M.R., Rodriguez, J.A.
Reference:
IUCrJ. 2019 Jan 24;6(Pt 2):197-205.
Download
Entry:
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Structure:
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FASTA
Contact Network:
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Protein Information
Protein Name:
Ice nucleation protein
Alternative Name:
Gene Name:
Sequence Length:
6
Species:
Pseudomonas syringae
Mutation(s):
No
E.C. Number:
UniProt ID:
P06620
Keyword(s):
Ice nucleation protein
Structure Information
PDB ID:
6M9I
Amyloid Category:
Amyloid
Type:
Fibril
Global Stoichiometry:
PDB Classification:
PROTEIN FIBRIL
Method:
ELECTRON CRYSTALLOGRAPHY
Resolution (
Å
):
0.9
R free:
0.23199999
Entry:S-0561
PDB ID: 6M9J
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Sequence & Sec. Str.
Chain 1
1
G
S
T
S
T
A
6
Helix: Magenta; Strand: Yellow; Coil & Turn: White.
Charged residues and Proline are highlighed in blue.
Description
Racemic-GSTSTA from degenerate octameric repeats in InaZ, residues 707-712
Homochiral and racemic GSTSTA form amyloid-like protofibrils with labile, corrugated antiparallel Beta-sheets that mate face to back. The racemic GSTSTA protofibril represents a new class of amyloid assembly in which all-left-handed sheets mate with their all-right-handed counterparts. This determination of racemic amyloid assemblies by MicroED reveals complex amyloid architectures and illustrates the racemic advantage in macromolecular crystallography
Literature
PMID:
30867917
Author(s):
Zee, C.T., Glynn, C., Gallagher-Jones, M., Miao, J., Santiago, C.G., Cascio, D., Gonen, T., Sawaya, M.R., Rodriguez, J.A.
Reference:
IUCrJ. 2019 Jan 24;6(Pt 2):197-205.
Download
Entry:
CSV
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Structure:
PDB
CIF
FASTA
Contact Network:
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Protein Information
Protein Name:
Ice nucleation protein
Alternative Name:
Gene Name:
Sequence Length:
6
Species:
Pseudomonas syringae
Mutation(s):
No
E.C. Number:
UniProt ID:
P06620
Keyword(s):
Ice nucleation protein
Structure Information
PDB ID:
6M9J
Amyloid Category:
Amyloid
Type:
Fibril
Global Stoichiometry:
PDB Classification:
PROTEIN FIBRIL
Method:
ELECTRON CRYSTALLOGRAPHY
Resolution (
Å
):
0.9
R free:
0.252
Entry:S-0562
PDB ID: 6MST
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Sequence & Sec. Str.
Chain 1
1
S
F
F
S
F
L
G
E
A
F
D
G
A
R
D
M
W
R
A
Y
S
D
M
R
E
25
26
A
N
Y
I
G
S
D
K
Y
F
H
A
R
G
N
Y
D
A
A
K
R
G
P
G
G
50
51
V
W
A
A
E
A
I
S
D
A
R
E
N
I
Q
R
66
Chain 2
1
S
F
F
S
F
L
G
E
A
F
D
G
A
R
D
M
W
R
A
Y
S
D
M
R
E
25
26
A
N
Y
I
G
S
D
K
Y
F
H
A
R
G
N
Y
D
A
A
K
R
G
P
G
G
50
51
V
W
A
A
E
A
I
S
D
A
R
E
N
I
Q
R
66
Chain 3
1
S
F
F
S
F
L
G
E
A
F
D
G
A
R
D
M
W
R
A
Y
S
D
M
R
E
25
26
A
N
Y
I
G
S
D
K
Y
F
H
A
R
G
N
Y
D
A
A
K
R
G
P
G
G
50
51
V
W
A
A
E
A
I
S
D
A
R
E
N
I
Q
R
66
Chain 4
1
S
F
F
S
F
L
G
E
A
F
D
G
A
R
D
M
W
R
A
Y
S
D
M
R
E
25
26
A
N
Y
I
G
S
D
K
Y
F
H
A
R
G
N
Y
D
A
A
K
R
G
P
G
G
50
51
V
W
A
A
E
A
I
S
D
A
R
E
N
I
Q
R
66
Chain 5
1
S
F
F
S
F
L
G
E
A
F
D
G
A
R
D
M
W
R
A
Y
S
D
M
R
E
25
26
A
N
Y
I
G
S
D
K
Y
F
H
A
R
G
N
Y
D
A
A
K
R
G
P
G
G
50
51
V
W
A
A
E
A
I
S
D
A
R
E
N
I
Q
R
66
Chain 6
1
S
F
F
S
F
L
G
E
A
F
D
G
A
R
D
M
W
R
A
Y
S
D
M
R
E
25
26
A
N
Y
I
G
S
D
K
Y
F
H
A
R
G
N
Y
D
A
A
K
R
G
P
G
G
50
51
V
W
A
A
E
A
I
S
D
A
R
E
N
I
Q
R
66
Chain 7
1
S
F
F
S
F
L
G
E
A
F
D
G
A
R
D
M
W
R
A
Y
S
D
M
R
E
25
26
A
N
Y
I
G
S
D
K
Y
F
H
A
R
G
N
Y
D
A
A
K
R
G
P
G
G
50
51
V
W
A
A
E
A
I
S
D
A
R
E
N
I
Q
R
66
Chain 8
1
S
F
F
S
F
L
G
E
A
F
D
G
A
R
D
M
W
R
A
Y
S
D
M
R
E
25
26
A
N
Y
I
G
S
D
K
Y
F
H
A
R
G
N
Y
D
A
A
K
R
G
P
G
G
50
51
V
W
A
A
E
A
I
S
D
A
R
E
N
I
Q
R
66
Chain 9
1
S
F
F
S
F
L
G
E
A
F
D
G
A
R
D
M
W
R
A
Y
S
D
M
R
E
25
26
A
N
Y
I
G
S
D
K
Y
F
H
A
R
G
N
Y
D
A
A
K
R
G
P
G
G
50
51
V
W
A
A
E
A
I
S
D
A
R
E
N
I
Q
R
66
Chain 10
1
S
F
F
S
F
L
G
E
A
F
D
G
A
R
D
M
W
R
A
Y
S
D
M
R
E
25
26
A
N
Y
I
G
S
D
K
Y
F
H
A
R
G
N
Y
D
A
A
K
R
G
P
G
G
50
51
V
W
A
A
E
A
I
S
D
A
R
E
N
I
Q
R
66
Chain 11
1
S
F
F
S
F
L
G
E
A
F
D
G
A
R
D
M
W
R
A
Y
S
D
M
R
E
25
26
A
N
Y
I
G
S
D
K
Y
F
H
A
R
G
N
Y
D
A
A
K
R
G
P
G
G
50
51
V
W
A
A
E
A
I
S
D
A
R
E
N
I
Q
R
66
Chain 12
1
S
F
F
S
F
L
G
E
A
F
D
G
A
R
D
M
W
R
A
Y
S
D
M
R
E
25
26
A
N
Y
I
G
S
D
K
Y
F
H
A
R
G
N
Y
D
A
A
K
R
G
P
G
G
50
51
V
W
A
A
E
A
I
S
D
A
R
E
N
I
Q
R
66
Helix: Magenta; Strand: Yellow; Coil & Turn: White.
Charged residues and Proline are highlighed in blue.
Description
Cryo-EM structure of human AA amyloid fibril
They analyse amyloid fibrils from a mouse and a human patient with systemic AA amyloidosis. The two fibrils differ in fundamental properties, such as presence of right-hand or left-hand twisted cross-Beta sheets and overall fold of the fibril proteins. Yet, both proteins adopt highly similar Beta-arch conformations within the N-terminal 21 residues.
Literature
PMID:
Author(s):
Liberta, F., Loerch, S., Rennegarbe, M., Schierhorn, A., Westermark, P., Westermark, G.T., Hazenberg, B.P.C., Grigorieff, N., Fandrich, M., Schmidt, M.
Reference:
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Entry:
CSV
JSON
Structure:
PDB
CIF
FASTA
Contact Network:
CSV
JSON
Protein Information
Protein Name:
Serum amyloid A-1 protein
Alternative Name:
Gene Name:
SAA1
Sequence Length:
66
Species:
Homo sapiens
Mutation(s):
No
E.C. Number:
UniProt ID:
P0DJI8
Keyword(s):
Serum amyloid A-1 protein
Structure Information
PDB ID:
6MST
Amyloid Category:
Amyloid
Type:
Fibril
Global Stoichiometry:
Homo 12-mer - A12
PDB Classification:
PROTEIN FIBRIL
Method:
ELECTRON MICROSCOPY
Resolution (
Å
):
2.7
R free:
Entry:S-0563
PDB ID: 6NWP
CSV
JSON
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Structure
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Sequence & Sec. Str.
Chain 1
1
M
A
E
P
R
Q
E
F
E
V
M
E
D
H
A
G
T
Y
G
L
G
D
R
K
D
25
26
Q
G
G
Y
T
M
H
Q
D
Q
E
G
D
T
D
A
G
L
K
E
S
P
L
Q
T
50
51
P
T
E
D
G
S
E
E
P
G
S
E
T
S
D
A
K
S
T
P
T
A
E
D
V
75
76
T
A
P
L
V
D
E
G
A
P
G
K
Q
A
A
A
Q
P
H
T
E
I
P
E
G
100
101
T
T
A
E
E
A
G
I
G
D
T
P
S
L
E
D
E
A
A
G
H
V
T
Q
A
125
126
R
M
V
S
K
S
K
D
G
T
G
S
D
D
K
K
A
K
G
A
D
G
K
T
K
150
151
I
A
T
P
R
G
A
A
P
P
G
Q
K
G
Q
A
N
A
T
R
I
P
A
K
T
175
176
P
P
A
P
K
T
P
P
S
S
G
E
P
P
K
S
G
D
R
S
G
Y
S
S
P
200
201
G
S
P
G
T
P
G
S
R
S
R
T
P
S
L
P
T
P
P
T
R
E
P
K
K
225
226
V
A
V
V
R
T
P
P
K
S
P
S
S
A
K
S
R
L
Q
T
A
P
V
P
M
250
251
P
D
L
K
N
V
K
S
K
I
G
S
T
E
N
L
K
H
Q
P
G
G
G
K
V
275
276
Q
I
I
N
K
K
L
D
L
S
N
V
Q
S
K
C
G
S
K
D
N
I
K
H
V
300
301
P
G
G
G
S
V
Q
I
V
Y
K
P
V
D
L
S
K
V
T
S
K
C
G
S
L
325
326
G
N
I
H
H
K
P
G
G
G
Q
V
E
V
K
S
E
K
L
D
F
K
D
R
V
350
351
Q
S
K
I
G
S
L
D
N
I
T
H
V
P
G
G
G
N
K
K
I
E
T
H
K
375
376
L
T
F
R
E
N
A
K
A
K
T
D
H
G
A
E
I
V
Y
K
S
P
V
V
S
400
401
G
D
T
S
P
R
H
L
S
N
V
S
S
T
G
S
I
D
M
V
D
S
P
Q
L
425
426
A
T
L
A
D
E
V
S
A
S
L
A
K
Q
G
L
441
Chain 2
1
M
A
E
P
R
Q
E
F
E
V
M
E
D
H
A
G
T
Y
G
L
G
D
R
K
D
25
26
Q
G
G
Y
T
M
H
Q
D
Q
E
G
D
T
D
A
G
L
K
E
S
P
L
Q
T
50
51
P
T
E
D
G
S
E
E
P
G
S
E
T
S
D
A
K
S
T
P
T
A
E
D
V
75
76
T
A
P
L
V
D
E
G
A
P
G
K
Q
A
A
A
Q
P
H
T
E
I
P
E
G
100
101
T
T
A
E
E
A
G
I
G
D
T
P
S
L
E
D
E
A
A
G
H
V
T
Q
A
125
126
R
M
V
S
K
S
K
D
G
T
G
S
D
D
K
K
A
K
G
A
D
G
K
T
K
150
151
I
A
T
P
R
G
A
A
P
P
G
Q
K
G
Q
A
N
A
T
R
I
P
A
K
T
175
176
P
P
A
P
K
T
P
P
S
S
G
E
P
P
K
S
G
D
R
S
G
Y
S
S
P
200
201
G
S
P
G
T
P
G
S
R
S
R
T
P
S
L
P
T
P
P
T
R
E
P
K
K
225
226
V
A
V
V
R
T
P
P
K
S
P
S
S
A
K
S
R
L
Q
T
A
P
V
P
M
250
251
P
D
L
K
N
V
K
S
K
I
G
S
T
E
N
L
K
H
Q
P
G
G
G
K
V
275
276
Q
I
I
N
K
K
L
D
L
S
N
V
Q
S
K
C
G
S
K
D
N
I
K
H
V
300
301
P
G
G
G
S
V
Q
I
V
Y
K
P
V
D
L
S
K
V
T
S
K
C
G
S
L
325
326
G
N
I
H
H
K
P
G
G
G
Q
V
E
V
K
S
E
K
L
D
F
K
D
R
V
350
351
Q
S
K
I
G
S
L
D
N
I
T
H
V
P
G
G
G
N
K
K
I
E
T
H
K
375
376
L
T
F
R
E
N
A
K
A
K
T
D
H
G
A
E
I
V
Y
K
S
P
V
V
S
400
401
G
D
T
S
P
R
H
L
S
N
V
S
S
T
G
S
I
D
M
V
D
S
P
Q
L
425
426
A
T
L
A
D
E
V
S
A
S
L
A
K
Q
G
L
441
Chain 3
1
M
A
E
P
R
Q
E
F
E
V
M
E
D
H
A
G
T
Y
G
L
G
D
R
K
D
25
26
Q
G
G
Y
T
M
H
Q
D
Q
E
G
D
T
D
A
G
L
K
E
S
P
L
Q
T
50
51
P
T
E
D
G
S
E
E
P
G
S
E
T
S
D
A
K
S
T
P
T
A
E
D
V
75
76
T
A
P
L
V
D
E
G
A
P
G
K
Q
A
A
A
Q
P
H
T
E
I
P
E
G
100
101
T
T
A
E
E
A
G
I
G
D
T
P
S
L
E
D
E
A
A
G
H
V
T
Q
A
125
126
R
M
V
S
K
S
K
D
G
T
G
S
D
D
K
K
A
K
G
A
D
G
K
T
K
150
151
I
A
T
P
R
G
A
A
P
P
G
Q
K
G
Q
A
N
A
T
R
I
P
A
K
T
175
176
P
P
A
P
K
T
P
P
S
S
G
E
P
P
K
S
G
D
R
S
G
Y
S
S
P
200
201
G
S
P
G
T
P
G
S
R
S
R
T
P
S
L
P
T
P
P
T
R
E
P
K
K
225
226
V
A
V
V
R
T
P
P
K
S
P
S
S
A
K
S
R
L
Q
T
A
P
V
P
M
250
251
P
D
L
K
N
V
K
S
K
I
G
S
T
E
N
L
K
H
Q
P
G
G
G
K
V
275
276
Q
I
I
N
K
K
L
D
L
S
N
V
Q
S
K
C
G
S
K
D
N
I
K
H
V
300
301
P
G
G
G
S
V
Q
I
V
Y
K
P
V
D
L
S
K
V
T
S
K
C
G
S
L
325
326
G
N
I
H
H
K
P
G
G
G
Q
V
E
V
K
S
E
K
L
D
F
K
D
R
V
350
351
Q
S
K
I
G
S
L
D
N
I
T
H
V
P
G
G
G
N
K
K
I
E
T
H
K
375
376
L
T
F
R
E
N
A
K
A
K
T
D
H
G
A
E
I
V
Y
K
S
P
V
V
S
400
401
G
D
T
S
P
R
H
L
S
N
V
S
S
T
G
S
I
D
M
V
D
S
P
Q
L
425
426
A
T
L
A
D
E
V
S
A
S
L
A
K
Q
G
L
441
Chain 4
1
M
A
E
P
R
Q
E
F
E
V
M
E
D
H
A
G
T
Y
G
L
G
D
R
K
D
25
26
Q
G
G
Y
T
M
H
Q
D
Q
E
G
D
T
D
A
G
L
K
E
S
P
L
Q
T
50
51
P
T
E
D
G
S
E
E
P
G
S
E
T
S
D
A
K
S
T
P
T
A
E
D
V
75
76
T
A
P
L
V
D
E
G
A
P
G
K
Q
A
A
A
Q
P
H
T
E
I
P
E
G
100
101
T
T
A
E
E
A
G
I
G
D
T
P
S
L
E
D
E
A
A
G
H
V
T
Q
A
125
126
R
M
V
S
K
S
K
D
G
T
G
S
D
D
K
K
A
K
G
A
D
G
K
T
K
150
151
I
A
T
P
R
G
A
A
P
P
G
Q
K
G
Q
A
N
A
T
R
I
P
A
K
T
175
176
P
P
A
P
K
T
P
P
S
S
G
E
P
P
K
S
G
D
R
S
G
Y
S
S
P
200
201
G
S
P
G
T
P
G
S
R
S
R
T
P
S
L
P
T
P
P
T
R
E
P
K
K
225
226
V
A
V
V
R
T
P
P
K
S
P
S
S
A
K
S
R
L
Q
T
A
P
V
P
M
250
251
P
D
L
K
N
V
K
S
K
I
G
S
T
E
N
L
K
H
Q
P
G
G
G
K
V
275
276
Q
I
I
N
K
K
L
D
L
S
N
V
Q
S
K
C
G
S
K
D
N
I
K
H
V
300
301
P
G
G
G
S
V
Q
I
V
Y
K
P
V
D
L
S
K
V
T
S
K
C
G
S
L
325
326
G
N
I
H
H
K
P
G
G
G
Q
V
E
V
K
S
E
K
L
D
F
K
D
R
V
350
351
Q
S
K
I
G
S
L
D
N
I
T
H
V
P
G
G
G
N
K
K
I
E
T
H
K
375
376
L
T
F
R
E
N
A
K
A
K
T
D
H
G
A
E
I
V
Y
K
S
P
V
V
S
400
401
G
D
T
S
P
R
H
L
S
N
V
S
S
T
G
S
I
D
M
V
D
S
P
Q
L
425
426
A
T
L
A
D
E
V
S
A
S
L
A
K
Q
G
L
441
Chain 5
1
M
A
E
P
R
Q
E
F
E
V
M
E
D
H
A
G
T
Y
G
L
G
D
R
K
D
25
26
Q
G
G
Y
T
M
H
Q
D
Q
E
G
D
T
D
A
G
L
K
E
S
P
L
Q
T
50
51
P
T
E
D
G
S
E
E
P
G
S
E
T
S
D
A
K
S
T
P
T
A
E
D
V
75
76
T
A
P
L
V
D
E
G
A
P
G
K
Q
A
A
A
Q
P
H
T
E
I
P
E
G
100
101
T
T
A
E
E
A
G
I
G
D
T
P
S
L
E
D
E
A
A
G
H
V
T
Q
A
125
126
R
M
V
S
K
S
K
D
G
T
G
S
D
D
K
K
A
K
G
A
D
G
K
T
K
150
151
I
A
T
P
R
G
A
A
P
P
G
Q
K
G
Q
A
N
A
T
R
I
P
A
K
T
175
176
P
P
A
P
K
T
P
P
S
S
G
E
P
P
K
S
G
D
R
S
G
Y
S
S
P
200
201
G
S
P
G
T
P
G
S
R
S
R
T
P
S
L
P
T
P
P
T
R
E
P
K
K
225
226
V
A
V
V
R
T
P
P
K
S
P
S
S
A
K
S
R
L
Q
T
A
P
V
P
M
250
251
P
D
L
K
N
V
K
S
K
I
G
S
T
E
N
L
K
H
Q
P
G
G
G
K
V
275
276
Q
I
I
N
K
K
L
D
L
S
N
V
Q
S
K
C
G
S
K
D
N
I
K
H
V
300
301
P
G
G
G
S
V
Q
I
V
Y
K
P
V
D
L
S
K
V
T
S
K
C
G
S
L
325
326
G
N
I
H
H
K
P
G
G
G
Q
V
E
V
K
S
E
K
L
D
F
K
D
R
V
350
351
Q
S
K
I
G
S
L
D
N
I
T
H
V
P
G
G
G
N
K
K
I
E
T
H
K
375
376
L
T
F
R
E
N
A
K
A
K
T
D
H
G
A
E
I
V
Y
K
S
P
V
V
S
400
401
G
D
T
S
P
R
H
L
S
N
V
S
S
T
G
S
I
D
M
V
D
S
P
Q
L
425
426
A
T
L
A
D
E
V
S
A
S
L
A
K
Q
G
L
441
Chain 6
1
M
A
E
P
R
Q
E
F
E
V
M
E
D
H
A
G
T
Y
G
L
G
D
R
K
D
25
26
Q
G
G
Y
T
M
H
Q
D
Q
E
G
D
T
D
A
G
L
K
E
S
P
L
Q
T
50
51
P
T
E
D
G
S
E
E
P
G
S
E
T
S
D
A
K
S
T
P
T
A
E
D
V
75
76
T
A
P
L
V
D
E
G
A
P
G
K
Q
A
A
A
Q
P
H
T
E
I
P
E
G
100
101
T
T
A
E
E
A
G
I
G
D
T
P
S
L
E
D
E
A
A
G
H
V
T
Q
A
125
126
R
M
V
S
K
S
K
D
G
T
G
S
D
D
K
K
A
K
G
A
D
G
K
T
K
150
151
I
A
T
P
R
G
A
A
P
P
G
Q
K
G
Q
A
N
A
T
R
I
P
A
K
T
175
176
P
P
A
P
K
T
P
P
S
S
G
E
P
P
K
S
G
D
R
S
G
Y
S
S
P
200
201
G
S
P
G
T
P
G
S
R
S
R
T
P
S
L
P
T
P
P
T
R
E
P
K
K
225
226
V
A
V
V
R
T
P
P
K
S
P
S
S
A
K
S
R
L
Q
T
A
P
V
P
M
250
251
P
D
L
K
N
V
K
S
K
I
G
S
T
E
N
L
K
H
Q
P
G
G
G
K
V
275
276
Q
I
I
N
K
K
L
D
L
S
N
V
Q
S
K
C
G
S
K
D
N
I
K
H
V
300
301
P
G
G
G
S
V
Q
I
V
Y
K
P
V
D
L
S
K
V
T
S
K
C
G
S
L
325
326
G
N
I
H
H
K
P
G
G
G
Q
V
E
V
K
S
E
K
L
D
F
K
D
R
V
350
351
Q
S
K
I
G
S
L
D
N
I
T
H
V
P
G
G
G
N
K
K
I
E
T
H
K
375
376
L
T
F
R
E
N
A
K
A
K
T
D
H
G
A
E
I
V
Y
K
S
P
V
V
S
400
401
G
D
T
S
P
R
H
L
S
N
V
S
S
T
G
S
I
D
M
V
D
S
P
Q
L
425
426
A
T
L
A
D
E
V
S
A
S
L
A
K
Q
G
L
441
Helix: Magenta; Strand: Yellow; Coil & Turn: White.
Charged residues and Proline are highlighed in blue.
Description
Chronic traumatic encephalopathy Type I Tau filament
The structures of tau filaments from the brains of three individuals. Filament structures are identical in the three cases but are distinct from those of Alzheimer's and Pick's diseases, and from those formed in vitro. Chronic traumatic encephalopathy Type I Tau filament.
Literature
PMID:
30894745
Author(s):
Falcon, B., Zivanov, J., Zhang, W., Murzin, A.G., Garringer, H.J., Vidal, R., Crowther, R.A., Newell, K.L., Ghetti, B., Goedert, M., Scheres, S.H.W.
Reference:
Nature. 2019 Apr;568(7752):420-423.
Download
Entry:
CSV
JSON
Structure:
PDB
CIF
FASTA
Contact Network:
CSV
JSON
Protein Information
Protein Name:
Microtubule-associated protein tau
Alternative Name:
Neurofibrillary tangle protein, Paired helical filament-tau
Gene Name:
MAPT, MAPTL, MTBT1, TAU
Sequence Length:
441
Species:
Homo sapiens
Mutation(s):
No
E.C. Number:
UniProt ID:
P10636
Keyword(s):
Microtubule-associated protein tau
Structure Information
PDB ID:
6NWP
Amyloid Category:
Amyloid
Type:
Fibril
Global Stoichiometry:
Homo 6-mer - A6
PDB Classification:
PROTEIN FIBRIL
Method:
ELECTRON MICROSCOPY
Resolution (
Å
):
2.3
R free:
Entry:S-0564
PDB ID: 6NWQ
CSV
JSON
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Structure
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Sequence & Sec. Str.
Chain 1
1
M
A
E
P
R
Q
E
F
E
V
M
E
D
H
A
G
T
Y
G
L
G
D
R
K
D
25
26
Q
G
G
Y
T
M
H
Q
D
Q
E
G
D
T
D
A
G
L
K
E
S
P
L
Q
T
50
51
P
T
E
D
G
S
E
E
P
G
S
E
T
S
D
A
K
S
T
P
T
A
E
D
V
75
76
T
A
P
L
V
D
E
G
A
P
G
K
Q
A
A
A
Q
P
H
T
E
I
P
E
G
100
101
T
T
A
E
E
A
G
I
G
D
T
P
S
L
E
D
E
A
A
G
H
V
T
Q
A
125
126
R
M
V
S
K
S
K
D
G
T
G
S
D
D
K
K
A
K
G
A
D
G
K
T
K
150
151
I
A
T
P
R
G
A
A
P
P
G
Q
K
G
Q
A
N
A
T
R
I
P
A
K
T
175
176
P
P
A
P
K
T
P
P
S
S
G
E
P
P
K
S
G
D
R
S
G
Y
S
S
P
200
201
G
S
P
G
T
P
G
S
R
S
R
T
P
S
L
P
T
P
P
T
R
E
P
K
K
225
226
V
A
V
V
R
T
P
P
K
S
P
S
S
A
K
S
R
L
Q
T
A
P
V
P
M
250
251
P
D
L
K
N
V
K
S
K
I
G
S
T
E
N
L
K
H
Q
P
G
G
G
K
V
275
276
Q
I
I
N
K
K
L
D
L
S
N
V
Q
S
K
C
G
S
K
D
N
I
K
H
V
300
301
P
G
G
G
S
V
Q
I
V
Y
K
P
V
D
L
S
K
V
T
S
K
C
G
S
L
325
326
G
N
I
H
H
K
P
G
G
G
Q
V
E
V
K
S
E
K
L
D
F
K
D
R
V
350
351
Q
S
K
I
G
S
L
D
N
I
T
H
V
P
G
G
G
N
K
K
I
E
T
H
K
375
376
L
T
F
R
E
N
A
K
A
K
T
D
H
G
A
E
I
V
Y
K
S
P
V
V
S
400
401
G
D
T
S
P
R
H
L
S
N
V
S
S
T
G
S
I
D
M
V
D
S
P
Q
L
425
426
A
T
L
A
D
E
V
S
A
S
L
A
K
Q
G
L
441
Chain 2
1
M
A
E
P
R
Q
E
F
E
V
M
E
D
H
A
G
T
Y
G
L
G
D
R
K
D
25
26
Q
G
G
Y
T
M
H
Q
D
Q
E
G
D
T
D
A
G
L
K
E
S
P
L
Q
T
50
51
P
T
E
D
G
S
E
E
P
G
S
E
T
S
D
A
K
S
T
P
T
A
E
D
V
75
76
T
A
P
L
V
D
E
G
A
P
G
K
Q
A
A
A
Q
P
H
T
E
I
P
E
G
100
101
T
T
A
E
E
A
G
I
G
D
T
P
S
L
E
D
E
A
A
G
H
V
T
Q
A
125
126
R
M
V
S
K
S
K
D
G
T
G
S
D
D
K
K
A
K
G
A
D
G
K
T
K
150
151
I
A
T
P
R
G
A
A
P
P
G
Q
K
G
Q
A
N
A
T
R
I
P
A
K
T
175
176
P
P
A
P
K
T
P
P
S
S
G
E
P
P
K
S
G
D
R
S
G
Y
S
S
P
200
201
G
S
P
G
T
P
G
S
R
S
R
T
P
S
L
P
T
P
P
T
R
E
P
K
K
225
226
V
A
V
V
R
T
P
P
K
S
P
S
S
A
K
S
R
L
Q
T
A
P
V
P
M
250
251
P
D
L
K
N
V
K
S
K
I
G
S
T
E
N
L
K
H
Q
P
G
G
G
K
V
275
276
Q
I
I
N
K
K
L
D
L
S
N
V
Q
S
K
C
G
S
K
D
N
I
K
H
V
300
301
P
G
G
G
S
V
Q
I
V
Y
K
P
V
D
L
S
K
V
T
S
K
C
G
S
L
325
326
G
N
I
H
H
K
P
G
G
G
Q
V
E
V
K
S
E
K
L
D
F
K
D
R
V
350
351
Q
S
K
I
G
S
L
D
N
I
T
H
V
P
G
G
G
N
K
K
I
E
T
H
K
375
376
L
T
F
R
E
N
A
K
A
K
T
D
H
G
A
E
I
V
Y
K
S
P
V
V
S
400
401
G
D
T
S
P
R
H
L
S
N
V
S
S
T
G
S
I
D
M
V
D
S
P
Q
L
425
426
A
T
L
A
D
E
V
S
A
S
L
A
K
Q
G
L
441
Chain 3
1
M
A
E
P
R
Q
E
F
E
V
M
E
D
H
A
G
T
Y
G
L
G
D
R
K
D
25
26
Q
G
G
Y
T
M
H
Q
D
Q
E
G
D
T
D
A
G
L
K
E
S
P
L
Q
T
50
51
P
T
E
D
G
S
E
E
P
G
S
E
T
S
D
A
K
S
T
P
T
A
E
D
V
75
76
T
A
P
L
V
D
E
G
A
P
G
K
Q
A
A
A
Q
P
H
T
E
I
P
E
G
100
101
T
T
A
E
E
A
G
I
G
D
T
P
S
L
E
D
E
A
A
G
H
V
T
Q
A
125
126
R
M
V
S
K
S
K
D
G
T
G
S
D
D
K
K
A
K
G
A
D
G
K
T
K
150
151
I
A
T
P
R
G
A
A
P
P
G
Q
K
G
Q
A
N
A
T
R
I
P
A
K
T
175
176
P
P
A
P
K
T
P
P
S
S
G
E
P
P
K
S
G
D
R
S
G
Y
S
S
P
200
201
G
S
P
G
T
P
G
S
R
S
R
T
P
S
L
P
T
P
P
T
R
E
P
K
K
225
226
V
A
V
V
R
T
P
P
K
S
P
S
S
A
K
S
R
L
Q
T
A
P
V
P
M
250
251
P
D
L
K
N
V
K
S
K
I
G
S
T
E
N
L
K
H
Q
P
G
G
G
K
V
275
276
Q
I
I
N
K
K
L
D
L
S
N
V
Q
S
K
C
G
S
K
D
N
I
K
H
V
300
301
P
G
G
G
S
V
Q
I
V
Y
K
P
V
D
L
S
K
V
T
S
K
C
G
S
L
325
326
G
N
I
H
H
K
P
G
G
G
Q
V
E
V
K
S
E
K
L
D
F
K
D
R
V
350
351
Q
S
K
I
G
S
L
D
N
I
T
H
V
P
G
G
G
N
K
K
I
E
T
H
K
375
376
L
T
F
R
E
N
A
K
A
K
T
D
H
G
A
E
I
V
Y
K
S
P
V
V
S
400
401
G
D
T
S
P
R
H
L
S
N
V
S
S
T
G
S
I
D
M
V
D
S
P
Q
L
425
426
A
T
L
A
D
E
V
S
A
S
L
A
K
Q
G
L
441
Chain 4
1
M
A
E
P
R
Q
E
F
E
V
M
E
D
H
A
G
T
Y
G
L
G
D
R
K
D
25
26
Q
G
G
Y
T
M
H
Q
D
Q
E
G
D
T
D
A
G
L
K
E
S
P
L
Q
T
50
51
P
T
E
D
G
S
E
E
P
G
S
E
T
S
D
A
K
S
T
P
T
A
E
D
V
75
76
T
A
P
L
V
D
E
G
A
P
G
K
Q
A
A
A
Q
P
H
T
E
I
P
E
G
100
101
T
T
A
E
E
A
G
I
G
D
T
P
S
L
E
D
E
A
A
G
H
V
T
Q
A
125
126
R
M
V
S
K
S
K
D
G
T
G
S
D
D
K
K
A
K
G
A
D
G
K
T
K
150
151
I
A
T
P
R
G
A
A
P
P
G
Q
K
G
Q
A
N
A
T
R
I
P
A
K
T
175
176
P
P
A
P
K
T
P
P
S
S
G
E
P
P
K
S
G
D
R
S
G
Y
S
S
P
200
201
G
S
P
G
T
P
G
S
R
S
R
T
P
S
L
P
T
P
P
T
R
E
P
K
K
225
226
V
A
V
V
R
T
P
P
K
S
P
S
S
A
K
S
R
L
Q
T
A
P
V
P
M
250
251
P
D
L
K
N
V
K
S
K
I
G
S
T
E
N
L
K
H
Q
P
G
G
G
K
V
275
276
Q
I
I
N
K
K
L
D
L
S
N
V
Q
S
K
C
G
S
K
D
N
I
K
H
V
300
301
P
G
G
G
S
V
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I
V
Y
K
P
V
D
L
S
K
V
T
S
K
C
G
S
L
325
326
G
N
I
H
H
K
P
G
G
G
Q
V
E
V
K
S
E
K
L
D
F
K
D
R
V
350
351
Q
S
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I
G
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D
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I
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H
V
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G
G
G
N
K
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E
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H
K
375
376
L
T
F
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E
N
A
K
A
K
T
D
H
G
A
E
I
V
Y
K
S
P
V
V
S
400
401
G
D
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P
R
H
L
S
N
V
S
S
T
G
S
I
D
M
V
D
S
P
Q
L
425
426
A
T
L
A
D
E
V
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A
S
L
A
K
Q
G
L
441
Chain 5
1
M
A
E
P
R
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E
F
E
V
M
E
D
H
A
G
T
Y
G
L
G
D
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D
25
26
Q
G
G
Y
T
M
H
Q
D
Q
E
G
D
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D
A
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E
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T
50
51
P
T
E
D
G
S
E
E
P
G
S
E
T
S
D
A
K
S
T
P
T
A
E
D
V
75
76
T
A
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L
V
D
E
G
A
P
G
K
Q
A
A
A
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P
H
T
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I
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E
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100
101
T
T
A
E
E
A
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I
G
D
T
P
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L
E
D
E
A
A
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A
125
126
R
M
V
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D
G
T
G
S
D
D
K
K
A
K
G
A
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G
K
T
K
150
151
I
A
T
P
R
G
A
A
P
P
G
Q
K
G
Q
A
N
A
T
R
I
P
A
K
T
175
176
P
P
A
P
K
T
P
P
S
S
G
E
P
P
K
S
G
D
R
S
G
Y
S
S
P
200
201
G
S
P
G
T
P
G
S
R
S
R
T
P
S
L
P
T
P
P
T
R
E
P
K
K
225
226
V
A
V
V
R
T
P
P
K
S
P
S
S
A
K
S
R
L
Q
T
A
P
V
P
M
250
251
P
D
L
K
N
V
K
S
K
I
G
S
T
E
N
L
K
H
Q
P
G
G
G
K
V
275
276
Q
I
I
N
K
K
L
D
L
S
N
V
Q
S
K
C
G
S
K
D
N
I
K
H
V
300
301
P
G
G
G
S
V
Q
I
V
Y
K
P
V
D
L
S
K
V
T
S
K
C
G
S
L
325
326
G
N
I
H
H
K
P
G
G
G
Q
V
E
V
K
S
E
K
L
D
F
K
D
R
V
350
351
Q
S
K
I
G
S
L
D
N
I
T
H
V
P
G
G
G
N
K
K
I
E
T
H
K
375
376
L
T
F
R
E
N
A
K
A
K
T
D
H
G
A
E
I
V
Y
K
S
P
V
V
S
400
401
G
D
T
S
P
R
H
L
S
N
V
S
S
T
G
S
I
D
M
V
D
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P
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L
425
426
A
T
L
A
D
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V
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A
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L
A
K
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G
L
441
Chain 6
1
M
A
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P
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E
F
E
V
M
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A
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G
L
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25
26
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50
51
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75
76
T
A
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A
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100
101
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T
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E
A
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125
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150
151
I
A
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A
A
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G
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A
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T
175
176
P
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R
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225
226
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250
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V
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I
G
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N
L
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G
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275
276
Q
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I
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L
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N
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K
C
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K
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N
I
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H
V
300
301
P
G
G
G
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V
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K
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L
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T
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K
C
G
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L
325
326
G
N
I
H
H
K
P
G
G
G
Q
V
E
V
K
S
E
K
L
D
F
K
D
R
V
350
351
Q
S
K
I
G
S
L
D
N
I
T
H
V
P
G
G
G
N
K
K
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E
T
H
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375
376
L
T
F
R
E
N
A
K
A
K
T
D
H
G
A
E
I
V
Y
K
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P
V
V
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400
401
G
D
T
S
P
R
H
L
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N
V
S
S
T
G
S
I
D
M
V
D
S
P
Q
L
425
426
A
T
L
A
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A
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A
K
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G
L
441
Helix: Magenta; Strand: Yellow; Coil & Turn: White.
Charged residues and Proline are highlighed in blue.
Description
Chronic traumatic encephalopathy Type II Tau filament
The structures of tau filaments from the brains of three individuals. Filament structures are identical in the three cases but are distinct from those of Alzheimer's and Pick's diseases, and from those formed in vitro. Chronic traumatic encephalopathy Type II Tau filament.
Literature
PMID:
30894745
Author(s):
Falcon, B., Zivanov, J., Zhang, W., Murzin, A.G., Garringer, H.J., Vidal, R., Crowther, R.A., Newell, K.L., Ghetti, B., Goedert, M., Scheres, S.H.W.
Reference:
Nature. 2019 Apr;568(7752):420-423.
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Entry:
CSV
JSON
Structure:
PDB
CIF
FASTA
Contact Network:
CSV
JSON
Protein Information
Protein Name:
Microtubule-associated protein tau
Alternative Name:
Neurofibrillary tangle protein, Paired helical filament-tau
Gene Name:
MAPT, MAPTL, MTBT1, TAU
Sequence Length:
441
Species:
Homo sapiens
Mutation(s):
No
E.C. Number:
UniProt ID:
P10636
Keyword(s):
Microtubule-associated protein tau
Structure Information
PDB ID:
6NWQ
Amyloid Category:
Amyloid
Type:
Fibril
Global Stoichiometry:
Homo 6-mer - A6
PDB Classification:
PROTEIN FIBRIL
Method:
ELECTRON MICROSCOPY
Resolution (
Å
):
3.4
R free:
Entry:S-0565
PDB ID: 6O3N
CSV
JSON
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Structure
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Protein Contacts Atlas
Sequence & Sec. Str.
Chain 1
1
X
S
K
L
L
E
L
L
R
K
L
A
E
A
L
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I
E
L
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26
G
X
27
Chain 2
1
X
S
K
L
L
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L
L
R
K
L
A
E
A
L
H
K
A
I
E
L
L
E
K
W
25
26
G
X
27
Chain 3
1
X
S
K
L
L
E
L
L
R
K
L
A
E
A
L
H
K
A
I
E
L
L
E
K
W
25
26
G
X
27
Chain 4
1
X
S
K
L
L
E
L
L
R
K
L
A
E
A
L
H
K
A
I
E
L
L
E
K
W
25
26
G
X
27
Chain 5
1
X
S
K
L
L
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L
L
R
K
L
A
E
A
L
H
K
A
I
E
L
L
E
K
W
25
26
G
X
27
Chain 6
1
X
S
K
L
L
E
L
L
R
K
L
A
E
A
L
H
K
A
I
E
L
L
E
K
W
25
26
G
X
27
Chain 7
1
X
S
K
L
L
E
L
L
R
K
L
A
E
A
L
H
K
A
I
E
L
L
E
K
W
25
26
G
X
27
Chain 8
1
X
S
K
L
L
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L
L
R
K
L
A
E
A
L
H
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A
I
E
L
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W
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26
G
X
27
Chain 9
1
X
S
K
L
L
E
L
L
R
K
L
A
E
A
L
H
K
A
I
E
L
L
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K
W
25
26
G
X
27
Chain 10
1
X
S
K
L
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E
L
L
R
K
L
A
E
A
L
H
K
A
I
E
L
L
E
K
W
25
26
G
X
27
Chain 11
1
X
S
K
L
L
E
L
L
R
K
L
A
E
A
L
H
K
A
I
E
L
L
E
K
W
25
26
G
X
27
Chain 12
1
X
S
K
L
L
E
L
L
R
K
L
A
E
A
L
H
K
A
I
E
L
L
E
K
W
25
26
G
X
27
Chain 13
1
X
S
K
L
L
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L
L
R
K
L
A
E
A
L
H
K
A
I
E
L
L
E
K
W
25
26
G
X
27
Chain 14
1
X
S
K
L
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E
L
L
R
K
L
A
E
A
L
H
K
A
I
E
L
L
E
K
W
25
26
G
X
27
Chain 15
1
X
S
K
L
L
E
L
L
R
K
L
A
E
A
L
H
K
A
I
E
L
L
E
K
W
25
26
G
X
27
Chain 16
1
X
S
K
L
L
E
L
L
R
K
L
A
E
A
L
H
K
A
I
E
L
L
E
K
W
25
26
G
X
27
Helix: Magenta; Strand: Yellow; Coil & Turn: White.
Charged residues and Proline are highlighed in blue.
