CPAD 2.0

Entry	PDB ID	Protein Name	Species	Length	Mutation(s)	Class	Type	Method	PMID
S-0121	2LFN	Hydrophobin	Neurospora crassa	68	[del]25-39	Amyloid	Protein	SOLUTION NMR	22308366
S-0122	2LI9	Amyloid-beta A4 protein	Rattus norvegicus	18	No	Non-amyloid	Inhibitor complex	SOLUTION NMR	22225807
S-0123	2LMN	Amyloid-beta A4 protein	Homo sapiens	40	No	Amyloid	Fibril	SOLID-STATE NMR	19015532
S-0124	2LMO	Amyloid-beta A4 protein	Homo sapiens	40	No	Amyloid	Fibril	SOLID-STATE NMR	19015532
S-0125	2LMP	Amyloid-beta A4 protein	Homo sapiens	40	No	Amyloid	Fibril	SOLID-STATE NMR	19015532
S-0126	2LMQ	Amyloid-beta A4 protein	Homo sapiens	40	No	Amyloid	Fibril	SOLID-STATE NMR	19015532
S-0127	2LNQ	Amyloid-beta A4 protein	Homo sapiens	40	D23N	Amyloid	Fibril	SOLID-STATE NMR	22403062
S-0128	2LP5	Tyrosine-protein kinase Fyn	Gallus gallus	66	A39V/N53P/V55L	Amyloid	Protein	SOLUTION NMR	22517863
S-0129	2LSH	Spore-wall fungal hydrophobin dewA	Aspergillus nidulans	118	No	Amyloid	Protein	SOLUTION NMR	23137797
S-0130	2M4J	Amyloid-beta A4 protein	Homo sapiens	40	No	Amyloid	Fibril	SOLID-STATE NMR	24034249
S-0131	2M5K	Transthyretin	Rattus norvegicus	11	No	Amyloid	Fibril	ELECTRON MICROSCOPY, SOLID-STATE NMR	23513222
S-0132	2M5M	Transthyretin	Rattus norvegicus	11	No	Amyloid	Fibril	ELECTRON MICROSCOPY, SOLID-STATE NMR	23513222
S-0133	2M5N	Transthyretin	Homo sapiens	11	No	Amyloid	Fibril	SOLID-STATE NMR	23513222
S-0134	2M9R	Amyloid-beta A4 protein	Homo sapiens	40	No	Non-amyloid	Inhibitor complex	SOLUTION NMR	23830862
S-0135	2M9S	Amyloid-beta A4 protein	Homo sapiens	40	No	Non-amyloid	Inhibitor complex	SOLUTION NMR	23830862
S-0136	2MGT	Amyloid-beta A4 protein	Homo sapiens	18	H6R	Amyloid	Aggregating complex	SOLUTION NMR
S-0137	2MI1	Somatostatin	Homo sapiens	14	No	Amyloid	Peptide	SOLUTION NMR
S-0138	2MJ1	Amyloid-beta A4 protein	Homo sapiens	18	Yes	Amyloid	Peptide	SOLUTION NMR	25284368
S-0139	2MKW	V1-22 protein	Homo sapiens	111	R24G	Amyloid	Protein	SOLUTION NMR	25522882
S-0140	2MMX	V1-22 protein	Homo sapiens	111	No	Amyloid	Protein	SOLUTION NMR	25522882
S-0141	2MPZ	Amyloid-beta A4 protein	Homo sapiens	26	D23N	Amyloid	Fibril	SOLID-STATE NMR	25543257
S-0142	2MUS	Heterokaryon incompatibility protein s	Podospora anserina	79	No	Amyloid	Fibril	SOLUTION NMR	26246168
S-0143	2MVX	Amyloid-beta A4 protein	Homo sapiens	39	E22[del]	Amyloid	Fibril	SOLID-STATE NMR	25395337
S-0144	2MXU	Amyloid-beta A4 protein	Homo sapiens	42	No	Amyloid	Fibril	SOLID-STATE NMR	25938662
S-0145	2N0A	Alpha-synuclein	Homo sapiens	140	No	Amyloid	Fibril	SOLID-STATE NMR	27018801
S-0146	2N1E	MAX1 peptide fibril		21	No	Amyloid	Fibril	SOLID-STATE NMR	26216960
S-0147	2N4O	Hydrophobin-like protein MPG1	Pyricularia oryzae	95	No	Amyloid	Protein	SOLUTION NMR	27142249
S-0148	2N59	Uncharacterized protein	Rhodopseudomonas palustris	106	No	Non-amyloid	Protein	SOLUTION NMR	27098162
S-0149	2NA4	Curli production assembly/transport component CsgE	Escherichia coli	114	W48A/F79A	Non-amyloid	Protein	SOLUTION NMR	27298344
S-0150	2NAO	Amyloid-beta A4 protein	Homo sapiens	42	No	Amyloid	Fibril	SOLUTION NMR	27469165

Structure

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Sequence & Sec. Str.

Chain 1

1

S

A

T

I

G

P

N

T

C

S

I

D

Y

K

P

Y

C

Q

S

M

S

G

25

26

S

A

S

L

G

C

V

G

V

I

G

S

Q

C

G

A

S

V

K

C

K

D

50

51

V

T

N

T

G

N

S

G

L

I

N

A

N

C

V

A

68

Helix: Magenta; Strand: Yellow; Coil & Turn: White.

Charged residues and Proline are highlighed in blue.

Description

Identification of the key regions that drive functional amyloid formation by the fungal hydrophobin EAS

The hydrophobin EAS from the fungus Neurospora crassa forms functional amyloid fibrils called rodlets that facilitate spore formation and dispersal. Self-assembly of EAS into fibrillar rodlets occurs spontaneously at hydrophobic:hydrophilic interfaces and the rodlets further associate laterally to form amphipathic monolayers.

Literature

PMID:	22308366
Author(s):	Macindoe, I., Kwan, A.H., Ren, Q., Morris, V.K., Yang, W., Mackay, J.P., Sunde, M.
Reference:	Proc Natl Acad Sci U S A. 2012 Apr 3;109(14):E804-11.

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Entry:	CSV JSON
Structure:	PDB CIF FASTA
Contact Network:	CSV JSON

Protein Information

Protein Name:	Hydrophobin
Alternative Name:	Blue light-induced protein 7, Clock-controlled gene protein 2, Rodlet protein
Gene Name:	eas, bli-7, ccg-2, NCU08457
Sequence Length:	68
Species:	Neurospora crassa
Mutation(s):	[del]25-39
E.C. Number:
UniProt ID:	Q04571
Keyword(s):	Hydrophobin

Structure Information

PDB ID:	2LFN
Amyloid Category:	Amyloid
Type:	Protein
Global Stoichiometry:	Monomer - A
PDB Classification:	STRUCTURAL PROTEIN
Method:	SOLUTION NMR
Resolution (Å):
R free:

Structure

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Sequence & Sec. Str.

Chain 1

1

X

D

A

E

F

G

H

D

S

G

F

E

V

R

H

Q

K

X

18

Chain 2

1

X

D

A

E

F

G

H

D

S

G

F

E

V

R

H

Q

K

X

18

Helix: Magenta; Strand: Yellow; Coil & Turn: White.

Charged residues and Proline are highlighed in blue.

Description

Metal binding domain of rat beta-amyloid

the structure of the metal-binding domain 1-16 of rat Beta-amyloid (rat ABeta(1-16)) in solution in the absence and presence of zinc ions was determined to reveal the mechanism of rats' resistance to Alzheimer's disease. A zinc-induced dimerization of the domain was detected. The zinc coordination site was found to involve residues His-6 and His-14 of both peptide chains. the C-tails of the two polypeptide chains of the rat ABeta(1-16) dimer are oriented in opposite directions to each other, which hinders the assembly of rat ABeta dimers into oligomeric aggregates. Thus, the differences in the structure of zinc-binding sites of human and rat ABeta(1-16), their ability to form regular cross-monomer bonds, and the orientation of their hydrophobic C-tails could be responsible for the resistance of rats to Alzheimer's disease.

Literature

PMID:	22225807
Author(s):	Istrate, A.N., Tsvetkov, P.O., Mantsyzov, A.B., Kulikova, A.A., Kozin, S.A., Makarov, A.A., Polshakov, V.I.
Reference:	Biophys J. 2012 Jan 4;102(1):136-43.

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Entry:	CSV JSON
Structure:	PDB CIF FASTA
Contact Network:	CSV JSON

Protein Information

Protein Name:	Amyloid-beta A4 protein
Alternative Name:
Gene Name:
Sequence Length:	18
Species:	Rattus norvegicus
Mutation(s):	No
E.C. Number:
UniProt ID:	P08592
Keyword(s):	Amyloid beta A4 protein

Structure Information

PDB ID:	2LI9
Amyloid Category:	Non-amyloid
Type:	Inhibitor complex
Global Stoichiometry:	Homo 2-mer - A2
PDB Classification:	CELL ADHESION
Method:	SOLUTION NMR
Resolution (Å):
R free:

Ligand Information

Ligand ID	Chain ID	Ligand Formula	Ligand MW	Ligand Name	Ligand SMILES	InChI Key
ACE	A	C2 H4 O	44.05	ACETYL GROUP	CC=O	IKHGUXGNUITLKF-UHFFFAOYSA-N
NH2	A	H2 N	16.02	AMINO GROUP	[NH2]	QGZKDVFQNNGYKY-UHFFFAOYAF
ZN	A	Zn 2	65.41	ZINC ION	[Zn+2]	PTFCDOFLOPIGGS-UHFFFAOYSA-N
ACE	B	C2 H4 O	44.05	ACETYL GROUP	CC=O	IKHGUXGNUITLKF-UHFFFAOYSA-N
NH2	B	H2 N	16.02	AMINO GROUP	[NH2]	QGZKDVFQNNGYKY-UHFFFAOYAF

Structure

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Sequence & Sec. Str.

Chain 1

1

D

A

E

F

R

H

D

S

G

Y

E

V

H

Q

K

L

V

F

A

E

D

V

G

25

26

S

N

K

G

A

I

G

L

M

V

G

V

40

Helix: Magenta; Strand: Yellow; Coil & Turn: White.

Charged residues and Proline are highlighed in blue.

Description

3D NMR structure of a complex between the amyloid beta peptide (1-40) and the polyphenol epsilon-viniferin glucoside

Polyphenols are known to have wide-ranging properties with regard to health and for helping to prevent various diseases like neurodegenerative disorders. Thus inhibiting the formation of toxic ABeta assemblies is a reasonable hypothesis to prevent and perhaps treat AD METHODS: Solution NMR and molecular modeling were used to obtain more information about the interaction between the ABeta1-40 and the polyphenol ?-viniferin glucoside (EVG) and particularly the ABeta residues involved in the complex.

Literature

PMID:	23830862
Author(s):	Richard, T., Papastamoulis, Y., Pierre, W.T., Monti, J.P.
Reference:	Biochim Biophys Acta. 2013 Nov;1830(11):5068-74.

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Entry:	CSV JSON
Structure:	PDB CIF FASTA
Contact Network:	CSV JSON

Protein Information

Protein Name:	Amyloid-beta A4 protein
Alternative Name:	ABPP, APPI, Alzheimer disease amyloid protein, Amyloid precursor protein, Amyloid-beta precursor protein, Cerebral vascular amyloid peptide, PreA4, Protease nexin-II
Gene Name:	APP, A4, AD1
Sequence Length:	40
Species:	Homo sapiens
Mutation(s):	No
E.C. Number:
UniProt ID:	P05067
Keyword(s):	Amyloid beta A4 protein

Structure Information

PDB ID:	2M9R
Amyloid Category:	Non-amyloid
Type:	Inhibitor complex
Global Stoichiometry:	Monomer - A
PDB Classification:	PROTEIN FIBRIL
Method:	SOLUTION NMR
Resolution (Å):
R free:

Ligand Information

Ligand ID	Chain ID	Ligand Formula	Ligand MW	Ligand Name	Ligand SMILES	InChI Key
23Y	A	C34 H32 O11	616.61	(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	c1cc(ccc1/C=C/c2cc(cc3c2[C@@H]([C@H](O3)c4ccc(cc4)O)c5cc(cc(c5)O)O)O[C@H]6[C@@H]([C@H]([C@@H]([C@H](O6)CO)O)O)O)O	NHYFNLFVNSLRES-YNVKLIFMSA-N

Structure

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View interactive contact network

Sequence & Sec. Str.

Chain 1

1

D

A

E

F

R

H

D

S

G

Y

E

V

H

Q

K

L

V

F

A

E

D

V

G

25

26

S

N

K

G

A

I

G

L

M

V

G

V

40

Helix: Magenta; Strand: Yellow; Coil & Turn: White.

Charged residues and Proline are highlighed in blue.

Description

3D NMR structure of a complex between the amyloid beta peptide (1-40) and the polyphenol epsilon-viniferin glucoside

Polyphenols are known to have wide-ranging properties with regard to health and for helping to prevent various diseases like neurodegenerative disorders. Thus inhibiting the formation of toxic ABeta assemblies is a reasonable hypothesis to prevent and perhaps treat AD METHODS: Solution NMR and molecular modeling were used to obtain more information about the interaction between the ABeta1-40 and the polyphenol ?-viniferin glucoside (EVG) and particularly the ABeta residues involved in the complex.

Literature

PMID:	23830862
Author(s):	Richard, T., Papastamoulis, Y., Pierre, W.T., Monti, J.P.
Reference:	Biochim Biophys Acta. 2013 Nov;1830(11):5068-74.

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Entry:	CSV JSON
Structure:	PDB CIF FASTA
Contact Network:	CSV JSON

Protein Information

Protein Name:	Amyloid-beta A4 protein
Alternative Name:	ABPP, APPI, Alzheimer disease amyloid protein, Amyloid precursor protein, Amyloid-beta precursor protein, Cerebral vascular amyloid peptide, PreA4, Protease nexin-II
Gene Name:	APP, A4, AD1
Sequence Length:	40
Species:	Homo sapiens
Mutation(s):	No
E.C. Number:
UniProt ID:	P05067
Keyword(s):	Amyloid beta A4 protein

Structure Information

PDB ID:	2M9S
Amyloid Category:	Non-amyloid
Type:	Inhibitor complex
Global Stoichiometry:	Monomer - A
PDB Classification:	PROTEIN FIBRIL
Method:	SOLUTION NMR
Resolution (Å):
R free:

Ligand Information

Ligand ID	Chain ID	Ligand Formula	Ligand MW	Ligand Name	Ligand SMILES	InChI Key
23Y	A	C34 H32 O11	616.61	(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	c1cc(ccc1/C=C/c2cc(cc3c2[C@@H]([C@H](O3)c4ccc(cc4)O)c5cc(cc(c5)O)O)O[C@H]6[C@@H]([C@H]([C@@H]([C@H](O6)CO)O)O)O)O	NHYFNLFVNSLRES-YNVKLIFMSA-N

Structure

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Sequence & Sec. Str.

Chain 1

1

X

D

A

E

F

R

D

S

G

Y

E

V

H

Q

K

X

18

Chain 2

1

X

D

A

E

F

R

D

S

G

Y

E

V

H

Q

K

X

18

Helix: Magenta; Strand: Yellow; Coil & Turn: White.

Charged residues and Proline are highlighed in blue.

Description

Zinc induced dimer of the metal binding domain 1-16 of human amyloid beta-peptide

Interplay of histidine residues of the Alzheimer s disease ABeta peptide governs its Zn-induced oligomerization

Literature

PMID:
Author(s):	Istrate, A.N., Kozin, S.A., Zhokhov, S.S., Mantsyzov, A.B., Kechko, O.I., Pastore, A., Makarov, A.A., Polshakov, V.I.
Reference:

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Entry:	CSV JSON
Structure:	PDB CIF FASTA
Contact Network:	CSV JSON

Protein Information

Protein Name:	Amyloid-beta A4 protein
Alternative Name:
Gene Name:
Sequence Length:	18
Species:	Homo sapiens
Mutation(s):	H6R
E.C. Number:
UniProt ID:	P05067
Keyword(s):	Amyloid beta A4 protein

Structure Information

PDB ID:	2MGT
Amyloid Category:	Amyloid
Type:	Aggregating complex
Global Stoichiometry:	Homo 2-mer - A2
PDB Classification:	PROTEIN FIBRIL
Method:	SOLUTION NMR
Resolution (Å):
R free:

Ligand Information

Ligand ID	Chain ID	Ligand Formula	Ligand MW	Ligand Name	Ligand SMILES	InChI Key
ACE	A	C2 H4 O	44.05	ACETYL GROUP	CC=O	IKHGUXGNUITLKF-UHFFFAOYSA-N
NH2	A	H2 N	16.02	AMINO GROUP	[NH2]	QGZKDVFQNNGYKY-UHFFFAOYAF
ZN	A	Zn 2	65.41	ZINC ION	[Zn+2]	PTFCDOFLOPIGGS-UHFFFAOYSA-N
ACE	B	C2 H4 O	44.05	ACETYL GROUP	CC=O	IKHGUXGNUITLKF-UHFFFAOYSA-N
NH2	B	H2 N	16.02	AMINO GROUP	[NH2]	QGZKDVFQNNGYKY-UHFFFAOYAF

Structure

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View interactive contact network

Sequence & Sec. Str.

Chain 1

1

M

K

I

D

A

I

V

G

R

N

S

A

K

D

I

R

T

E

R

A

R

V

Q

L

25

26

G

N

V

T

A

L

H

G

I

R

I

S

D

Q

T

N

S

V

K

T

50

51

V

G

K

G

E

S

R

V

L

I

G

N

E

Y

G

K

G

F

W

D

N

H

75

76

H

79

Chain 2

1

M

K

I

D

A

I

V

G

R

N

S

A

K

D

I

R

T

E

R

A

R

V

Q

L

25

26

G

N

V

T

A

L

H

G

I

R

I

S

D

Q

T

N

S

V

K

T

50

51

V

G

K

G

E

S

R

V

L

I

G

N

E

Y

G

K

G

F

W

D

N

H

75

76

H

79

Chain 3

1

M

K

I

D

A

I

V

G

R

N

S

A

K

D

I

R

T

E

R

A

R

V

Q

L

25

26

G

N

V

T

A

L

H

G

I

R

I

S

D

Q

T

N

S

V

K

T

50

51

V

G

K

G

E

S

R

V

L

I

G

N

E

Y

G

K

G

F

W

D

N

H

75

76

H

79

Chain 4

1

M

K

I

D

A

I

V

G

R

N

S

A

K

D

I

R

T

E

R

A

R

V

Q

L

25

26

G

N

V

T

A

L

H

G

I

R

I

S

D

Q

T

N

S

V

K

T

50

51

V

G

K

G

E

S

R

V

L

I

G

N

E

Y

G

K

G

F

W

D

N

H

75

76

H

79

Chain 5

1

M

K

I

D

A

I

V

G

R

N

S

A

K

D

I

R

T

E

R

A

R

V

Q

L

25

26

G

N

V

T

A

L

H

G

I

R

I

S

D

Q

T

N

S

V

K

T

50

51

V

G

K

G

E

S

R

V

L

I

G

N

E

Y

G

K

G

F

W

D

N

H

75

76

H

79

Helix: Magenta; Strand: Yellow; Coil & Turn: White.

Charged residues and Proline are highlighed in blue.

Description

HADDOCK calculated model of LIN5001 bound to the HET-s amyloid

They explored antiprion properties of luminescent conjugated polythiophenes (LCPs) that bind and stabilize ordered protein aggregates. That antiprion activity required a minimum of five thiophene rings bearing regularly spaced carboxyl side groups. Solid-state nuclear magnetic resonance analyses and molecular dynamics simulations revealed that anionic side chains interacted with complementary, regularly spaced cationic amyloid residues of model prions. The new set of LCPs showed robust prophylactic and therapeutic potency in prion-infected mice, with the lead compound extending survival by >80% and showing activity against both mouse and hamster prions as well as efficacy upon intraperitoneal administration into mice.

Literature

PMID:	26246168
Author(s):	Herrmann, U.S., Schutz, A.K., Shirani, H., Huang, D., Saban, D., Nuvolone, M., Li, B., Ballmer, B., Aslund, A.K., Mason, J.J., Rushing, E., Budka, H., Nystrom, S., Hammarstrom, P., Bockmann, A., Caflisch, A., Meier, B.H., Nilsson, K.P., Hornemann, S., Agu
Reference:	Sci Transl Med. 2015 Aug 5;7(299):299ra123.

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Entry:	CSV JSON
Structure:	PDB CIF FASTA
Contact Network:	CSV JSON

Protein Information

Protein Name:	Heterokaryon incompatibility protein s
Alternative Name:	Small s protein, Vegetative incompatibility protein s
Gene Name:	het-s, small s
Sequence Length:	79
Species:	Podospora anserina
Mutation(s):	No
E.C. Number:
UniProt ID:	Q03689
Keyword(s):	Heterokaryon incompatibility protein s

Structure Information

PDB ID:	2MUS
Amyloid Category:	Amyloid
Type:	Fibril
Global Stoichiometry:	Homo 5-mer - A5
PDB Classification:	PROTEIN FIBRIL
Method:	SOLUTION NMR
Resolution (Å):
R free:

Ligand Information

Ligand ID	Chain ID	Ligand Formula	Ligand MW	Ligand Name	Ligand SMILES	InChI Key
3LS	B	C26 H16 O8 S5	616.72	3''',4'-bis(carboxymethyl)-2,2'	5',2''	5''',2''''-quinquethiophene-5,5''''-dicarboxylic acid	c1cc(sc1c2c(cc(s2)c3ccc(s3)C(=O)O)CC(=O)O)c4c(cc(s4)c5ccc(s5)C(=O)O)CC(=O)O	InChI=1S/C26H16O8S5/c27-21(28)9-11-7-19(13-1-5-17(35-13)25(31)32)38-23(11)15-3-4-16(37-15)24-12(10-22(29)30)8-20(39-24)14-2-6-18(36-14)26(33)34/h1-8H,9-10H2,(H,27,28)(H,29,30)(H,31,32)(H,33,34)	SZFMXSCJFCPHEZ-UHFFFAOYSA-N

Structure

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Sequence & Sec. Str.

Chain 1

1

V

K

V

K

V

K

V

K

V

P

T

K

V

K

V

K

V

K

V

X

21

Chain 2

1

V

K

V

K

V

K

V

K

V

P

T

K

V

K

V

K

V

K

V

X

21

Chain 3

1

V

K

V

K

V

K

V

K

V

P

T

K

V

K

V

K

V

K

V

X

21

Chain 4

1

V

K

V

K

V

K

V

K

V

P

T

K

V

K

V

K

V

K

V

X

21

Chain 5

1

V

K

V

K

V

K

V

K

V

P

T

K

V

K

V

K

V

K

V

X

21

Chain 6

1

V

K

V

K

V

K

V

K

V

P

T

K

V

K

V

K

V

K

V

X

21

Chain 7

1

V

K

V

K

V

K

V

K

V

P

T

K

V

K

V

K

V

K

V

X

21

Chain 8

1

V

K

V

K

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21

Helix: Magenta; Strand: Yellow; Coil & Turn: White.

Charged residues and Proline are highlighed in blue.

Description

MAX1 peptide fibril

They have used solid-state NMR to determine the molecular and supramolecular structure of MAX1, a de novo designed gel-forming peptide, in its fibrillar state. MAX1 adopts a Beta-hairpin conformation and self-assembles with high fidelity into a double-layered cross-Beta structure. Hairpins assemble with an in-register Syn orientation within each Beta-sheet layer and with an Anti orientation between layers.

Literature

PMID:	26216960
Author(s):	Nagy-Smith, K., Moore, E., Schneider, J., Tycko, R.
Reference:	Proc Natl Acad Sci U S A. 2015 Aug 11;112(32):9816-21.

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Entry:	CSV JSON
Structure:	PDB CIF FASTA
Contact Network:	CSV JSON

Protein Information

Protein Name:	MAX1 peptide fibril
Alternative Name:
Gene Name:
Sequence Length:	21
Species:
Mutation(s):	No
E.C. Number:
UniProt ID:
Keyword(s):	MAX1 peptide

Structure Information

PDB ID:	2N1E
Amyloid Category:	Amyloid
Type:	Fibril
Global Stoichiometry:	Homo 8-mer - A8
PDB Classification:	PROTEIN FIBRIL
Method:	SOLID-STATE NMR
Resolution (Å):
R free:

Ligand Information

Ligand ID	Chain ID	Ligand Formula	Ligand MW	Ligand Name	Ligand SMILES	InChI Key
DPR	A	C5 H9 N O2	115.13	D-PROLINE	C1C[C@@H](NC1)C(=O)O	ONIBWKKTOPOVIA-SCSAIBSYSA-N
NH2	A	H2 N	16.02	AMINO GROUP	[NH2]	QGZKDVFQNNGYKY-UHFFFAOYAF
DPR	B	C5 H9 N O2	115.13	D-PROLINE	C1C[C@@H](NC1)C(=O)O	ONIBWKKTOPOVIA-SCSAIBSYSA-N
NH2	B	H2 N	16.02	AMINO GROUP	[NH2]	QGZKDVFQNNGYKY-UHFFFAOYAF
DPR	C	C5 H9 N O2	115.13	D-PROLINE	C1C[C@@H](NC1)C(=O)O	ONIBWKKTOPOVIA-SCSAIBSYSA-N
NH2	C	H2 N	16.02	AMINO GROUP	[NH2]	QGZKDVFQNNGYKY-UHFFFAOYAF
DPR	D	C5 H9 N O2	115.13	D-PROLINE	C1C[C@@H](NC1)C(=O)O	ONIBWKKTOPOVIA-SCSAIBSYSA-N
NH2	D	H2 N	16.02	AMINO GROUP	[NH2]	QGZKDVFQNNGYKY-UHFFFAOYAF
DPR	E	C5 H9 N O2	115.13	D-PROLINE	C1C[C@@H](NC1)C(=O)O	ONIBWKKTOPOVIA-SCSAIBSYSA-N
NH2	E	H2 N	16.02	AMINO GROUP	[NH2]	QGZKDVFQNNGYKY-UHFFFAOYAF
DPR	F	C5 H9 N O2	115.13	D-PROLINE	C1C[C@@H](NC1)C(=O)O	ONIBWKKTOPOVIA-SCSAIBSYSA-N
NH2	F	H2 N	16.02	AMINO GROUP	[NH2]	QGZKDVFQNNGYKY-UHFFFAOYAF
DPR	G	C5 H9 N O2	115.13	D-PROLINE	C1C[C@@H](NC1)C(=O)O	ONIBWKKTOPOVIA-SCSAIBSYSA-N
NH2	G	H2 N	16.02	AMINO GROUP	[NH2]	QGZKDVFQNNGYKY-UHFFFAOYAF
DPR	H	C5 H9 N O2	115.13	D-PROLINE	C1C[C@@H](NC1)C(=O)O	ONIBWKKTOPOVIA-SCSAIBSYSA-N
NH2	H	H2 N	16.02	AMINO GROUP	[NH2]	QGZKDVFQNNGYKY-UHFFFAOYAF

Structure database of aggregation related proteins and peptides

Displaying 121 to 150 records out of 565 records fetched.

PMID:
Author(s):	Anoop, A., Ranganathan, S., Dhaked, B., Jha, N., Pratihar, S., Ghosh, S., Sahay, S., Kumar, S., Das, S., Kombrabail, M., Agarwal, K., Jacob, R.S., Singru, P., Bhaumik, P., Padinhateeri, R., Kumar, A., Maji, S.K.
Reference: