LiteFold/DisProt huggingface dataset:
Protein: DP03853 (UniProt P28307)
Region: residues 1	to 151
Annotation: amyloid fibril formation (Biological process)
Evidence: electron microscopy evidence used in manual assertion
Supporting statements:
However, after prolonged incubation (4°C for 4 to 12 hours), the CsgA-his solutions became opaque and noticeably viscous. EM analysis revealed that fibers had formed that were similar to those produced by wild-type bacteria (Fig. 4D).
Cross-references: AmyPro:AP00036
Protein: DP03853 (UniProt P28307)
Region: residues 1	to 151
Annotation: disorder (Structural state)
Evidence: far-UV circular dichroism evidence used in manual assertion
Supporting statements:
Circular dichroism spectrum indicated that immediately after purification, CsgA was largely unstructured (Fig. 1B).
Protein: DP03853 (UniProt P28307)
Region: residues 1	to 151
Annotation: disorder to order (Structural transition)
Evidence: far-UV circular dichroism evidence used in manual assertion
Supporting statements:
Circular dichroism spectrum indicated that immediately after purification, CsgA was largely unstructured (Fig. 1B). However, CsgA adopted a β-sheet-rich structure after 2 days of incubation at room temperature (Fig. 1B).
Protein: DP03853 (UniProt P28307)
Region: residues 1	to 151
Annotation: disorder (Structural state)
Evidence: nuclear magnetic resonance evidence used in manual assertion
Supporting statements:
Use of higher strength magnetic fields (950 MHz) improved resolution for regions with the limited dispersion that is typical of IDPs.
Backbone assignment of the disordered, pre-fibril CsgA.
Protein: DP03853 (UniProt P28307)
Region: residues 1	to 22
Annotation: protein binding (Molecular function)
Evidence: surface plasmon resonance evidence used in manual assertion
Supporting statements:
Our N22 peptide data showed a specific interaction with a dissociation constant in the micromolar range (0.53 μM; Fig. 3).
Protein: DP03853 (UniProt P28307)
Region: residues 1	to 151
Annotation: amyloid fibril formation (Biological process)
Evidence: transmission electron microscopy evidence used in manual assertion
Supporting statements:
Immediately after purification, there was no apparent fiber formation or aggregation by TEM (Fig. 1C). Two hours after purification, regular, unbranched fibers were readily observed (Fig. 1D). Dense fiber aggregates were also observed 7 days after purification (Fig. 1E).
Cross-references: AmyPro:AP00036
Protein: DP03853 (UniProt P28307)
Region: residues 43	to 65
Annotation: amyloid fibril formation (Biological process)
Evidence: transmission electron microscopy evidence used in manual assertion
Supporting statements:
Peptides corresponding to repeating unit 1, 3 or 5 (R1, R3, or R5) produced a ThT-positive signal and self-assembled into fibers as evidenced by TEM when incubated at 0.2 mg/ml (Fig. 4, B–E).
Protein: DP03853 (UniProt P28307)
Region: residues 43	to 65
Annotation: amyloid fibril formation (Biological process)
Evidence: fluorescence evidence used in manual assertion
Supporting statements:
Peptides corresponding to repeating unit 1, 3 or 5 (R1, R3, or R5) produced a ThT-positive signal and self-assembled into fibers as evidenced by TEM when incubated at 0.2 mg/ml (Fig. 4, B–E).
Protein: DP03853 (UniProt P28307)
Region: residues 88	to 110
Annotation: amyloid fibril formation (Biological process)
Evidence: fluorescence evidence used in manual assertion
Supporting statements:
Peptides corresponding to repeating unit 1, 3 or 5 (R1, R3, or R5) produced a ThT-positive signal and self-assembled into fibers as evidenced by TEM when incubated at 0.2 mg/ml (Fig. 4, B–E).
Protein: DP03853 (UniProt P28307)
Region: residues 88	to 110
Annotation: amyloid fibril formation (Biological process)
Evidence: transmission electron microscopy evidence used in manual assertion
Supporting statements:
Peptides corresponding to repeating unit 1, 3 or 5 (R1, R3, or R5) produced a ThT-positive signal and self-assembled into fibers as evidenced by TEM when incubated at 0.2 mg/ml (Fig. 4, B–E).
Protein: DP03853 (UniProt P28307)
Region: residues 133	to 151
Annotation: amyloid fibril formation (Biological process)
Evidence: transmission electron microscopy evidence used in manual assertion
Supporting statements:
Peptides corresponding to repeating unit 1, 3 or 5 (R1, R3, or R5) produced a ThT-positive signal and self-assembled into fibers as evidenced by TEM when incubated at 0.2 mg/ml (Fig. 4, B–E).
Protein: DP03853 (UniProt P28307)
Region: residues 133	to 151
Annotation: amyloid fibril formation (Biological process)
Evidence: fluorescence evidence used in manual assertion
Supporting statements:
Peptides corresponding to repeating unit 1, 3 or 5 (R1, R3, or R5) produced a ThT-positive signal and self-assembled into fibers as evidenced by TEM when incubated at 0.2 mg/ml (Fig. 4, B–E).
Protein: DP03853 (UniProt P28307)
Region: residues 66	to 87
Annotation: amyloid fibril formation (Biological process)
Evidence: transmission electron microscopy evidence used in manual assertion
Supporting statements:
Neither R2 nor R4 showed evidence of amyloidogenesis when resuspended at a concentration of 0.2 mg/ml, although fibers were observed by TEM when R2 or R4 was incubated at 2 mg/ml (Fig. 4B and data not shown)
Protein: DP03853 (UniProt P28307)
Region: residues 111	to 132
Annotation: amyloid fibril formation (Biological process)
Evidence: transmission electron microscopy evidence used in manual assertion
Supporting statements:
Neither R2 nor R4 showed evidence of amyloidogenesis when resuspended at a concentration of 0.2 mg/ml, although fibers were observed by TEM when R2 or R4 was incubated at 2 mg/ml (Fig. 4B and data not shown)
Protein: DP03853 (UniProt P28307)
Region: residues 1	to 151
Annotation: regulation of amyloid fibril formation (Biological process)
Evidence: fluorescence evidence used in manual assertion
Supporting statements:
We tested the hypothesis that preformed CsgA fibers could catalyze CsgA polymerization. The addition of 2.5% (w/w) sonicated CsgA fibers to freshly purified, soluble CsgA resulted in a significant reduction of the lag phase (Fig. 3A).
Protein: DP03854 (UniProt Q99714)
Region: residues 95	to 113
Annotation: disorder (Structural state)
Evidence: X-ray crystallography-based structural model with missing residue coordinates used in manual assertion
Supporting statements:
However, no electron density is observed for Aβ, suggesting that Aβ itself and the region of ABAD that binds to Aβ must be disordered in the crystal.
Cross-references: PDB:1SO8
Protein: DP03854 (UniProt Q99714)
Region: residues 208	to 228
Annotation: disorder (Structural state)
Evidence: X-ray crystallography-based structural model with missing residue coordinates used in manual assertion
Supporting statements:
The majority of the LD loop, the beginning of the following αD helix, and the latter part of the LF loop of human ABAD are disordered.
Cross-references: PDB:1SO8
Protein: DP03854 (UniProt Q99714)
Region: residues 97	to 102
Annotation: protein binding (Molecular function)
Evidence: loss-of-function mutant phenotype evidence used in manual assertion
Supporting statements:
Site-directed mutagenesis within and beyond the disordered LD loop region (residues 95 to 113) specifically located two stretches of ABAD residues important for Aβ binding: residues S98 to Y101 (10) and residues T108 to T110. An ABAD mutant bearing Ser98->Ala98 (S98A), K99A, and Y101A mutations exhibited no specific interaction to Aβ in a surface plasmon resonance experiment, although wild-type ABAD displayed dosedependent interaction with Aβ (Fig. 3A)
Protein: DP03856 (UniProt P35475)
Region: residues 643	to 653
Annotation: disorder (Structural state)
Evidence: X-ray crystallography-based structural model with missing residue coordinates used in manual assertion
Supporting statements:
The last residue that is visible in our electron density maps is Pro642. The remaining 11 residues are disordered in the present structures (from Val643 to Pro653).
Cross-references: PDB:4MJ2
PDB:4MJ4
PDB:4KGL
PDB:4KGJ
PDB:4KH2
Protein: DP03857 (UniProt P05019)
Region: residues 70	to 90
Annotation: disorder (Structural state)
Evidence: X-ray crystallography-based structural model with missing residue coordinates used in manual assertion
Supporting statements:
The PDB shows the protein lacks electron density in this region, indicating it is disordered.
Cross-references: PDB:6FF3
Protein: DP03859 (UniProt Q2M1P5)
Region: residues 349	to 543
Annotation: disorder (Structural state)
Evidence: cryogenic electron microscopy-based structural model with missing residue coordinates used in manual assertion
Supporting statements:
The PDB shows the protein lacks electron density in this region, indicating it is disordered.
Cross-references: PDB:7RX0
Protein: DP03859 (UniProt Q2M1P5)
Region: residues 349	to 398
Annotation: disorder (Structural state)
Evidence: cryogenic electron microscopy-based structural model with missing residue coordinates used in manual assertion
Supporting statements:
The PDB shows the protein lacks electron density in this region, indicating it is disordered.
Cross-references: PDB:6MLR
PDB:6MLQ
Protein: DP03859 (UniProt Q2M1P5)
Region: residues 261	to 273
Annotation: disorder (Structural state)
Evidence: X-ray crystallography-based structural model with missing residue coordinates used in manual assertion
Supporting statements:
The final structure included residues 12–347 (missing regions: 107–114, 207–211, 230–241, 260–273) with bound Mg2+ADP (octahedrally co­ordinated) in the catalytic site and 328 water molecules.
Cross-references: PDB:2XT3
PDB:4A14
Protein: DP03859 (UniProt Q2M1P5)
Region: residues 230	to 241
Annotation: disorder (Structural state)
Evidence: X-ray crystallography-based structural model with missing residue coordinates used in manual assertion
Supporting statements:
The final structure included residues 12–347 (missing regions: 107–114, 207–211, 230–241, 260–273) with bound Mg2+ADP (octahedrally co­ordinated) in the catalytic site and 328 water molecules.
Cross-references: PDB:4A14
Protein: DP03860 (UniProt P01116)
Region: residues 174	to 189
Annotation: disorder (Structural state)
Evidence: X-ray crystallography-based structural model with missing residue coordinates used in manual assertion
Supporting statements:
The PDB shows the protein lacks electron density in this region, indicating it is disordered.
Cross-references: PDB:5OCG
Protein: DP03860 (UniProt P01116)
Region: residues 167	to 189
Annotation: disorder (Structural state)
Evidence: X-ray crystallography-based structural model with missing residue coordinates used in manual assertion
Supporting statements:
The PDB shows the protein lacks electron density in this region, indicating it is disordered.
Cross-references: PDB:7VVB
Protein: DP03860 (UniProt P01116)
Region: residues 60	to 70
Annotation: disorder (Structural state)
Evidence: X-ray crystallography-based structural model with missing residue coordinates used in manual assertion
Supporting statements:
The structure of Q61L mutant form of KRAS showed good density for all regions of the protein except for residues 60 to 70 (including L61) on switch 2 that were disordered and the density was insufficient to build this region into our model.
Cross-references: PDB:4WA7
Protein: DP03860 (UniProt P01116)
Region: residues 60	to 64
Annotation: GTPase activity (Molecular function)
Evidence: loss-of-function mutant phenotype evidence used in manual assertion
Supporting statements:
The G12C mutation had minimal impact on the intrinsic hydrolysis rate while mutation of G12 to A or R and mutation of Q61 to H or L lead to an approximately 40- to 80-fold decrease in GTP hydrolysis rate.
Protein: DP03861 (UniProt P36776)
Region: residues 1	to 122
Annotation: disorder (Structural state)
Evidence: X-ray crystallography-based structural model with missing residue coordinates used in manual assertion
Supporting statements:
All three models indicated residues 355-407 to form a long α-helix extending away from the globular domain and residues 1-123 and 221-272 to form unstructured loops.
Cross-references: PDB:7OXO
Protein: DP03861 (UniProt P36776)
Region: residues 222	to 271
Annotation: disorder (Structural state)
Evidence: X-ray crystallography-based structural model with missing residue coordinates used in manual assertion
Supporting statements:
All three models indicated residues 355-407 to form a long α-helix extending away from the globular domain and residues 1-123 and 221-272 to form unstructured loops.
Cross-references: PDB:7OXO
PDB:7NG4
PDB:7NGP
PDB:7NGQ
PDB:7NG5
PDB:7NFY
Protein: DP03862 (UniProt P21397)
Region: residues 465	to 527
Annotation: disorder (Structural state)
Evidence: X-ray crystallography-based structural model with missing residue coordinates used in manual assertion
Supporting statements:
 In crystal form X1, the C-terminal residues are disordered after residue 464 (hMAO A contains 527 residues) most likely because of crystal-packing interactions.
Cross-references: PDB:2BXR
Protein: DP03862 (UniProt P21397)
Region: residues 1	to 11
Annotation: disorder (Structural state)
Evidence: X-ray crystallography-based structural model with missing residue coordinates used in manual assertion
Supporting statements:
Residues 1–12, 111–115, and 507–527 are not visible in the electron density map.
Cross-references: PDB:2BXR
PDB:2BXS
Protein: DP03862 (UniProt P21397)
Region: residues 507	to 527
Annotation: disorder (Structural state)
Evidence: X-ray crystallography-based structural model with missing residue coordinates used in manual assertion
Supporting statements:
Residues 1–12, 111–115, and 507–527 are not visible in the electron density map.
Cross-references: PDB:2BXS
Protein: DP03863 (UniProt O43318)
Region: residues 66	to 80
Annotation: disorder (Structural state)
Evidence: X-ray crystallography-based structural model with missing residue coordinates used in manual assertion
Supporting statements:
The PDB shows the protein lacks electron density in this region, indicating it is disordered.
Cross-references: PDB:5E7R
Protein: DP03863 (UniProt O43318)
Region: residues 178	to 190
Annotation: disorder (Structural state)
Evidence: X-ray crystallography-based structural model with missing residue coordinates used in manual assertion
Supporting statements:
The PDB shows the protein lacks electron density in this region, indicating it is disordered.
Cross-references: PDB:5E7R
PDB:5JH6
PDB:5J8I
PDB:5J7S
PDB:5J9I
PDB:5JK3
Protein: DP03864 (UniProt P28482)
Region: residues 1	to 15
Annotation: disorder (Structural state)
Evidence: X-ray crystallography-based structural model with missing residue coordinates used in manual assertion
Supporting statements:
The PDB shows the protein lacks electron density in residues 1-15, indicating this region is disordered.
No electron density was observed for ERK2(5X) amino acids 1-13, 31-33, and 328-335, so these residues were not included in the  model.
Cross-references: PDB:1PME
Protein: DP03864 (UniProt P28482)
Region: residues 175	to 189
Annotation: disorder (Structural state)
Evidence: X-ray crystallography-based structural model with missing residue coordinates used in manual assertion
Supporting statements:
The PDB shows the protein lacks electron density in this region, indicating it is disordered.
Cross-references: PDB:5BUE
PDB:5BUJ
Protein: DP03865 (UniProt O95822)
Region: residues 344	to 371
Annotation: disorder (Structural state)
Evidence: X-ray crystallography-based structural model with missing residue coordinates used in manual assertion
Supporting statements:
Residues 60–65, 115 and 116, 276–281, and 344–371, which represent surface-exposed regions in the structure, are disordered and not modeled.
Cross-references: PDB:2YGW
Protein: DP03866 (UniProt Q8IVH4)
Region: residues 182	to 197
Annotation: disorder (Structural state)
Evidence: X-ray crystallography-based structural model with missing residue coordinates used in manual assertion
Supporting statements:
Several loops connecting the G-domain β-strands are disordered, suggesting their intrinsic flexibility. These include aa 182–197 (L1, Switch I motif), aa 212–220 (L2), aa 246–248 (L3, part of Switch II motif), and aa 268–279 (L4).
Cross-references: PDB:2WWW
Protein: DP03866 (UniProt Q8IVH4)
Region: residues 268	to 279
Annotation: disorder (Structural state)
Evidence: X-ray crystallography-based structural model with missing residue coordinates used in manual assertion
Supporting statements:
Several loops connecting the G-domain β-strands are disordered, suggesting their intrinsic flexibility. These include aa 182–197 (L1, Switch I motif), aa 212–220 (L2), aa 246–248 (L3, part of Switch II motif), and aa 268–279 (L4).
Cross-references: PDB:2WWW
Protein: DP03866 (UniProt Q8IVH4)
Region: residues 182	to 197
Annotation: flexible linker (Disorder function)
Evidence: X-ray crystallography-based structural model with missing residue coordinates used in manual assertion
Supporting statements:
Several loops connecting the G-domain β-strands are disordered, suggesting their intrinsic flexibility. These include aa 182–197 (L1, Switch I motif), aa 212–220 (L2), aa 246–248 (L3, part of Switch II motif), and aa 268–279 (L4).
Cross-references: PDB:2WWW
Protein: DP03866 (UniProt Q8IVH4)
Region: residues 268	to 279
Annotation: flexible linker (Disorder function)
Evidence: X-ray crystallography-based structural model with missing residue coordinates used in manual assertion
Supporting statements:
Several loops connecting the G-domain β-strands are disordered, suggesting their intrinsic flexibility. These include aa 182–197 (L1, Switch I motif), aa 212–220 (L2), aa 246–248 (L3, part of Switch II motif), and aa 268–279 (L4).
Cross-references: PDB:2WWW
Protein: DP03867 (UniProt Q9Y4U1)
Region: residues 231	to 282
Annotation: disorder (Structural state)
Evidence: X-ray crystallography-based structural model with missing residue coordinates used in manual assertion
Supporting statements:
The refined monomeric model comprises aa 5–230 (Figure 1a), while the C-terminal 52 residues (aa 231–282), encompassing a Pro-rich region absent in many MMACHC orthologues (Figure S1 of the Supporting Information), are disordered.
Cross-references: PDB:3SOM
Protein: DP03868 (UniProt Q9H3L0)
Region: residues 108	to 133
Annotation: disorder (Structural state)
Evidence: X-ray crystallography-based structural model with missing residue coordinates used in manual assertion
Supporting statements:
The N-terminal region (residues 108–131), with the exception of a very short polypeptide (118–122) in one of the molecules in the asymmetric unit, was not modeled because no visible electron density corresponding to this region could be discerned. Therefore, the N-terminal region even in the truncated CblDΔN108 variant is unstructured and disordered.

Even though the authors made an exception for 188-122 region, it is still disordered in the PDB structure and the 118-122 region is too short to be ordered so the IDR is considered to be 108-133.
Cross-references: PDB:5CUZ
PDB:5CV0
Protein: DP03868 (UniProt Q9H3L0)
Region: residues 108	to 132
Annotation: disorder (Structural state)
Evidence: X-ray crystallography-based structural model with missing residue coordinates used in manual assertion
Supporting statements:
The PDB shows the protein lacks electron density in this region, indicating it is disordered.
Cross-references: PDB:6X8Z
Protein: DP03869 (UniProt P22033)
Region: residues 12	to 35
Annotation: disorder (Structural state)
Evidence: X-ray crystallography-based structural model with missing residue coordinates used in manual assertion
Supporting statements:
The PDB shows that when bounded to adenosylcobalamin the protein lacks electron density in this region, indicating it is disordered.
Cross-references: PDB:2XIJ
PDB:2XIQ
Protein: DP03869 (UniProt P22033)
Region: residues 12	to 26
Annotation: disorder (Structural state)
Evidence: X-ray crystallography-based structural model with missing residue coordinates used in manual assertion
Supporting statements:
The PDB shows the protein lacks electron density in this region, indicating it is disordered.
Cross-references: PDB:3BIC
Protein: DP03870 (UniProt A0A6L0XH39)
Region: residues 304	to 323
Annotation: disorder (Structural state)
Evidence: X-ray crystallography-based structural model with missing residue coordinates used in manual assertion
Supporting statements:
Moreover, additionally to region P253-E303 removed from the recombinant protein, electron density was missing for residues A304 to P323 in both monomers, suggesting potential flexibility of this region.
Cross-references: PDB:5OL0
Protein: DP03870 (UniProt A0A6L0XH39)
Region: residues 268	to 284
Annotation: disorder (Structural state)
Evidence: cleavage assay evidence used in manual assertion
Supporting statements:
These results suggest LiSir2rp1 is composed of two tightly associated proteolytically stable polypeptides (nominally 29 kDa N-terminal and 9 kDa C-terminal) linked minimally by a 17 residue surface-exposed, serine-rich peptide region 268–284, EGRSSSSQSRSPSASPR.
Protein: DP03870 (UniProt A0A6L0XH39)
Region: residues 268	to 284
Annotation: flexible linker (Disorder function)
Evidence: cleavage assay evidence used in manual assertion
Supporting statements:
These results suggest LiSir2rp1 is composed of two tightly associated proteolytically stable polypeptides (nominally 29 kDa N-terminal and 9 kDa C-terminal) linked minimally by a 17 residue surface-exposed, serine-rich peptide region 268–284, EGRSSSSQSRSPSASPR.
Protein: DP03870 (UniProt A0A6L0XH39)
Region: residues 361	to 373
Annotation: disorder (Structural state)
Evidence: X-ray crystallography-based structural model with missing residue coordinates used in manual assertion
Supporting statements:
In addition to a small number of residues missing at both N- and C- terminal ends of the protein (N-ter M1-R6 and C-ter A371-T373 are missing in both monomers), region R52-P70 could not be modeled in monomer B.
Authors are referring to the 361-373 region, that lacks electron density in the PDB: 5OL0.
Cross-references: PDB:5OL0
Protein: DP03871 (UniProt O77299)
Region: residues 1	to 80
Annotation: disorder (Structural state)
Evidence: far-UV circular dichroism evidence used in manual assertion
Supporting statements:
The average CD spectrum obtained for r-LdHASPA showed a major negative band with maximum dip at around 200 nm, which indicated that secondary structure of r-LdHASPA consists of random coils or unstructured regions.
Protein: DP03872 (UniProt O75970)
Region: residues 1171	to 1183
Annotation: disorder (Structural state)
Evidence: X-ray crystallography-based structural model with missing residue coordinates used in manual assertion
Supporting statements:
In each of the four protein chains the position 0 residue is slightly disordered, in particular with significantly weaker electron density around the C-terminal carboxylate (Fig. 5A).
Cross-references: PDB:2FCF
Protein: DP03873 (UniProt P42898)
Region: residues 161	to 171
Annotation: disorder (Structural state)
Evidence: X-ray crystallography-based structural model with missing residue coordinates used in manual assertion
Supporting statements:
 In fact, this is reflected in our structure whereby the catalytic domain of one dimer subunit (chain A) is ordered, while that of the other dimer subunit (chain B) is highly disordered, to the extent that only main chain atoms of the amino acid 40–58, 129–134 and 155–342 in chain B could be modelled.
The 129-134 region the authors mention corresponds to the residues 161-171 of the Uniprot sequence that lacks electron density in the PDB.
Cross-references: PDB:6FCX
Protein: DP03874 (UniProt P42345)
Region: residues 290	to 355
Annotation: disorder (Structural state)
Evidence: cryogenic electron microscopy-based structural model with missing residue coordinates used in manual assertion
Supporting statements:
The PDB shows the protein lacks electron density in this region, indicating it is disordered.
Cross-references: PDB:6ZWM