LiteFold/DisProt huggingface dataset:
Protein: DP01092 (UniProt O66683)
Region: residues 1	to 17
Annotation: disorder to order (Structural transition)
Evidence: x-ray crystallography evidence used in manual assertion
Supporting statements:
In the A. aeolicus σ28/FlgM complex, most of the FlgM polypeptide is structured.
Cross-references: PDB:1SC5
PDB:1RP3
Protein: DP01092 (UniProt O66683)
Region: residues 1	to 88
Annotation: protein binding (Molecular function)
Evidence: x-ray crystallography evidence used in manual assertion
Supporting statements:
In the packed conformation of σ28, the β′ coiled-coil binding determinant in σ282 is facing outwards but is directly occluded by H1′-H2′ of FlgM (Figure 4A).
Cross-references: PDB:1SC5
PDB:1RP3
Protein: DP01092 (UniProt O66683)
Region: residues 1	to 88
Annotation: disorder to molten globule (Structural transition)
Evidence: far-UV circular dichroism evidence used in manual assertion
Supporting statements:
The results presented thus far demonstrate that the A. aeolicus FlgM protein forms a molten-globule like structure with significant α-helical character at room temperature. However, there is a 23% decrease in α-helical character upon heating the sample to physiological temperature for A. aeolicus (85 °C), suggesting that some regions of the protein become more disordered at higher temperature.
Taken together, our results demonstrate that the A. aeolicus FlgM exhibits a molten globular-like state at lower temperatures, in contrast to the extended-disordered nature observed for the S. typhimurium FlgM, consistent with disorder predictions. However, the A. aeolicus FlgM converts to an extended-disordered structure as the temperature approaches physiological temperature for A. aeolicus.
Protein: DP01092 (UniProt O66683)
Region: residues 1	to 88
Annotation: disorder (Structural state)
Evidence: far-UV circular dichroism evidence used in manual assertion
Supporting statements:
However, there is a 23% decrease in α-helical character upon heating the sample to physiological temperature for A. aeolicus (85 °C), suggesting that some regions of the protein become more disordered at higher temperature.
However, the A. aeolicus FlgM converts to an extended-disordered structure as the temperature approaches physiological temperature for A. aeolicus.
Protein: DP01092 (UniProt O66683)
Region: residues 30	to 88
Annotation: disorder to order (Structural transition)
Evidence: x-ray crystallography evidence used in manual assertion
Supporting statements:
In the A. aeolicus σ28/FlgM complex, most of the FlgM polypeptide is structured.
Cross-references: PDB:1SC5
PDB:1RP3
Protein: DP01094 (UniProt Q9BP37)
Region: residues 23	to 52
Annotation: disorder (Structural state)
Evidence: far-UV circular dichroism evidence used in manual assertion
Supporting statements:
These results indicate that both the AP7-1 and AP24-1 model polypeptides do not possess significant percentages of either α-helix or β-strand secondary structure, but adopt random coil or extended conformations in solution, consistent with the structural features observed for other calcium carbonate mineral binding sequences.
Protein: DP01094 (UniProt Q9BP37)
Region: residues 23	to 52
Annotation: disorder (Structural state)
Evidence: proton-based nuclear magnetic resonance evidence used in manual assertion
Supporting statements:
This suggests that AP7-1 adopts a open, unfolded conformation that features largely random coil-like and/or extended structure.
Protein: DP01094 (UniProt Q9BP37)
Region: residues 53	to 88
Annotation: disorder (Structural state)
Evidence: proton-based nuclear magnetic resonance evidence used in manual assertion
Supporting statements:
The 11H PFG-NOESY spectra of this region suggest its disordered nature. 1H chemical shifts are confined in the region 8.0 to 8.6 ppm while for globular proteins, 1H chemical shifts usually spread out in the region 9.5 to 6.0 ppm.
Cross-references: PDB:2JYP
Protein: DP01094 (UniProt Q9BP37)
Region: residues 53	to 88
Annotation: zinc ion binding (Molecular function)
Evidence: ion trap mass spectrometry evidence used in manual assertion
Supporting statements:
This C-terminal sequence can bind Zn (II), Co (II), and other multivalent metal ions (Figures 2 and3, and Table 1) in 1:1 and 2:1 metal ion:peptide stoichiometries, and the ligand coordination number for polypeptide:Zn (II) interaction is either mono, bi, or tridentate in nature.
Protein: DP01094 (UniProt Q9BP37)
Region: residues 53	to 88
Annotation: metal ion binding (Molecular function)
Evidence: ion trap mass spectrometry evidence used in manual assertion
Supporting statements:
This C-terminal sequence can bind Zn (II), Co (II), and other multivalent metal ions (Figures 2 and3, and Table 1) in 1:1 and 2:1 metal ion:peptide stoichiometries, and the ligand coordination number for polypeptide:Zn (II) interaction is either mono, bi, or tridentate in nature.
Protein: DP01094 (UniProt Q9BP37)
Region: residues 23	to 88
Annotation: protein homooligomerization (Biological process)
Evidence: dynamic light scattering assay evidence used in manual assertion
Supporting statements:
In summary, we find that under nonreducing conditions, AP7 is monomeric at pH 10 and exists as a high-molecular mass oligomer from pH 4 to 9 in solution.
Protein: DP01096 (UniProt Q25733)
Region: residues 605	to 618
Annotation: disorder (Structural state)
Evidence: X-ray crystallography-based structural model with missing residue coordinates used in manual assertion
Supporting statements:
The first helix (H1) of the bundle is joined to the second helix (H2) through a disordered fourteen-residue loop.
The function of the disordered loop cannot be inferred from the experiments; however, deleting the loop and at least one adjacent helix abolished binding to the human CD36 receptor. The length of the loop is variable between various homologoues.
Cross-references: PDB:3C64
Protein: DP01097 (UniProt P61244-2)
Region: residues 84	to 151
Annotation: disorder (Structural state)
Evidence: X-ray crystallography-based structural model with missing residue coordinates used in manual assertion
Supporting statements:
The X-ray crystal structure of the intact human Max protein homodimer in complex with a 13-mer DNA duplex was determined to 2.8 A resolution and refined to an R factor of 0.213. The C-terminal domains in both chains of the Max dimer are disordered.
The C-terminal domains in both chains of the Max dimer are disordered.
The disorder observed in the C-terminal domain suggests that contacts with additional protein components of the transcription machinery are necessary for ordering the secondary structure.
Although p21 Max is present in the crystals in its entirety, together with the 13 base pair duplex of DNA, in our crystals a large part of the C terminus is disordered. The present model includes residues 3–82 and 10–82 in monomers A and B, respectively.
Finally, regarding the C-terminal domain comprising residues 93–150, this entire region is disordered in the Max structure reported here.
The C-terminal domain following the leucine zipper is disordered in the crystal structure, suggesting that it is intrinsically flexible and that other components of the transcriptional machinery may be required for secondary structure formation.
Protein: DP01100 (UniProt P10636-8)
Region: residues 1	to 441
Annotation: disorder (Structural state)
Evidence: small-angle X-ray scattering evidence used in manual assertion
Supporting statements:
Again tau is clearly different from a globular protein (Fig. 3b, bottom), it has the characteristics of a denatured protein.
Protein: DP01100 (UniProt P10636-8)
Region: residues 1	to 441
Annotation: disorder (Structural state)
Evidence: Fourier-transform infrared spectroscopy evidence used in manual assertion
Supporting statements:
Soluble proteins K19, K18-ΔK280, and full-length htau40-ΔK280 exhibit FTIR maxima around 1645−1646 cm-1, consistent with the CD experiments and the dominance of the random coil conformation [Figure 6A−C (dashed lines)].
Protein: DP01100 (UniProt P10636-8)
Region: residues 1	to 441
Annotation: amyloid fibril formation (Biological process)
Evidence: far-UV circular dichroism evidence used in manual assertion
Supporting statements:
The CD spectra change when tau is induced to aggregate into PHFs. Figure 4A−C (solid lines) shows the PHF spectra after separation from soluble tau by a clearing spin. For three-repeat construct K19, the minimum shifts toward a higher wavelength, indicating a transition to a higher β-sheet content (Figure 4A). This change is even more pronounced for the FTDP-17 mutant of four-repeat construct K18 (K18-ΔK280, Figure 4B), consistent with the strong tendency of this mutant to form PHFs due to an increased propensity for β-sheet formation (20, 23).
Protein: DP01100 (UniProt P10636-8)
Region: residues 1	to 441
Annotation: amyloid fibril formation (Biological process)
Evidence: Fourier-transform infrared spectroscopy evidence used in manual assertion
Supporting statements:
Upon PHF polymerization, the spectra of the repeat constructs shift the maximum to ∼1629 and 1626 cm-1 [Figure 6A,B (solid lines)], indicating a shift toward a high β-structure content (55, 56).
Protein: DP01100 (UniProt P10636-8)
Region: residues 1	to 441
Annotation: amyloid fibril formation (Biological process)
Evidence: microscopy evidence used in manual assertion
Supporting statements:
In all cases, the filaments were mainly of the paired helical type, had a typical length of 100−500 nm, were 10−25 nm wide, and had a crossover repeat of ∼80 nm (Figure 2, top panel). Thus, they showed all characteristics of “Alzheimer PHFs” (39, 40).
Protein: DP01100 (UniProt P10636-8)
Region: residues 1	to 441
Annotation: amyloid fibril formation (Biological process)
Evidence: qualitative western immunoblotting evidence used in manual assertion
Supporting statements:
In a Western blot analysis, the samples were probed with the polyclonal antibody K9JA that recognizes the repeat region and the C-terminus of tau. The pattern was comparable to that of the Coomassie-stained gel with regard to the three- to four-band pattern and the high- and low-Mr smear, showing that most of the protein (∼75% as measured by densitometric methods) in the Alzheimer PHF preparations was indeed tau (Figure 3B).
Protein: DP01100 (UniProt P10636-8)
Region: residues 1	to 441
Annotation: amyloid fibril formation (Biological process)
Evidence: sodium dodecyl sulfate polyacrylamide gel electrophoresis evidence used in manual assertion
Supporting statements:
In the SDS gel, the three individual Alzheimer PHFs all exhibited the typical three- to four-band appearance [bands at 55, 64, and 69 kDa and a minor fourth band (72−74 kDa) which contain the six human tau isoforms in a highly phosphorylated form (43−45)] (Figure 3A).
Protein: DP01100 (UniProt P10636-8)
Region: residues 1	to 441
Annotation: disorder (Structural state)
Evidence: experimental evidence used in manual assertion
Supporting statements:
Tau can be boiled and dissolved in dilute acids, and yet it does not lose its microtubule-assembly promoting activity (Fellous et al., 1977); this argues that overall chain folding is not very important for the interaction of tau with microtubules (although other less obvious functions may be affected by this treatment).
Protein: DP01100 (UniProt P10636-8)
Region: residues 1	to 441
Annotation: disorder (Structural state)
Evidence: temperature-induced protein unfolding evidence used in manual assertion
Supporting statements:
Tau can be boiled and dissolved in dilute acids, and yet it does not lose its microtubule-assembly promoting activity (Fellous et al., 1977); this argues that overall chain folding is not very important for the interaction of tau with microtubules (although other less obvious functions may be affected by this treatment).
Protein: DP01100 (UniProt P10636-8)
Region: residues 1	to 441
Annotation: disorder (Structural state)
Evidence: spectrometry evidence used in manual assertion
Supporting statements:
Additional evidence for the apparent "denatured" state of tau comes from absorption spectroscopy (data not  shown).
Protein: DP01100 (UniProt P10636-8)
Region: residues 1	to 441
Annotation: amyloid fibril formation (Biological process)
Evidence: microscopy evidence used in manual assertion
Supporting statements:
Tau is difficult to visualize in the electron microscope because of its low contrast (Zingsheim et al., 1979), but the glycerol-spray technique reveals the structure of an elongated and flexible rod, about 35 nm in length (Fig. 2, Wille et al. (1992)).
Protein: DP01100 (UniProt P10636-8)
Region: residues 1	to 441
Annotation: amyloid fibril formation (Biological process)
Evidence: light scattering evidence used in manual assertion
Supporting statements:
Fig. 6, a and b, shows the wide and small angle pattern of pelleted microtubules. These structures can be oriented quite well by either of the above methods, but here we have chosen an example of rather poor orientation in order to facilitate the comparison with the PHF  pattern below (for an example of good orientation and its interpretation see Mandelkow et al. (1977) and Mandelkow (1986)).
Protein: DP01100 (UniProt P10636-8)
Region: residues 1	to 441
Annotation: amyloid fibril formation (Biological process)
Evidence: Fourier-transform infrared spectroscopy evidence used in manual assertion
Supporting statements:
The amide I maxima between 1600 and 1700 cm" arise from stretch vibrations of the amide carbonyl groups and vary depending on how the carbonyls are hydrogen bonded. Thus absorption maxima between 1617 and 1634 cm" are characteristic for β-sheets while α-helices, turns, or random coils have maxima between 1645 and 1663 cm" (Susi  and Byler,  1986).
Protein: DP01100 (UniProt P10636-8)
Region: residues 1	to 441
Annotation: disorder (Structural state)
Evidence: far-UV circular dichroism evidence used in manual assertion
Supporting statements:
All curves obtained for hτ23 show a minimum of around 200 nm, characteristic of largely random coil structures, which confirms our earlier observations (25).
Protein: DP01100 (UniProt P10636-8)
Region: residues 1	to 441
Annotation: disorder (Structural state)
Evidence: small-angle X-ray scattering evidence used in manual assertion
Supporting statements:
All the profiles are featureless, and the Kratky plots [s2I(s) vs s] are without apparent peaks (Supporting Information Figure 3), which is typical for unfolded proteins.
Table 1 indicates that the larger constructs (ht23 and ht40) have Rg values close to or smaller than the predicted random coil values, which are shown by ref 29 to agree well with the experimental data from chemically unfolded proteins (note that as tau constructs are not denatured using chemicals the random coil estimations cannot be considered ideal predictions, but they do provide a useful guidance).
For full length constructs (ht40 and ht23), little difference from the pool distribution was observed (typical models of ht40 selected from the random pools are displayed in Figure 4 to demonstrate that the protein is indeed rather unstructured).
Protein: DP01101 (UniProt P04370-5)
Region: residues 1	to 169
Annotation: disorder (Structural state)
Evidence: nuclear magnetic resonance spectroscopy evidence used in manual assertion
Supporting statements:
NMR assignment of an intrinsically disordered protein under physiological conditions: the 18.5 kDa isoform of murine myelin basic protein
The high degree of spin system overlap and chemical shift degeneracy inherent to intrinsically disordered proteins hinders resonance assignment. The 1H, 15N, and 13C backbone assignments were over 93% complete, excluding the carbonyl carbons, and residues Q3, L27, V91, and T92 for which no sequential crosspeaks were observed. Further, no resonances could be assigned for P96 and P97, which were part of a proline-rich domain.
Notably, an amphipathic α-helix (V83-T92) present in the protein under membrane-mimetic conditions appears disordered under these solution conditions.
Protein: DP01101 (UniProt P04370-5)
Region: residues 82	to 93
Annotation: order (Structural state)
Evidence: nuclear magnetic resonance spectroscopy evidence used in manual assertion
Supporting statements:
Here, we have extended these MD studies to determine experimentally the conformation of the considerably larger α2- peptide comprising residues S72−S107 of this region of the protein, in association with DPC micelles, using solution NMR spectroscopy.
Cross-references: PDB:2LUG
Protein: DP01101 (UniProt P04370-5)
Region: residues 82	to 93
Annotation: lipid binding (Molecular function)
Evidence: nuclear magnetic resonance spectroscopy evidence used in manual assertion
Supporting statements:
"The α2-peptide (S72−S107) from the 18.5 kDa murine MBP amino acid sequence was designed initially to include one region of three (specifically V83−T92) that are known to adopt a strongly amphipathic α-helical structure in association with detergent micelles and phospholipid
bilayers.
Cross-references: PDB:2LUG
Protein: DP01101 (UniProt P04370-5)
Region: residues 79	to 96
Annotation: disorder (Structural state)
Evidence: far-UV circular dichroism evidence used in manual assertion
Supporting statements:
In aqueous solution (pure water, and 100 mm KCl, pH 6.5), the spectra indicated that the polypeptide had little or no regular secondary structure. In organic and membrane-mimetic conditions (30% TFE and 20 mm DPC, respectively), the spectra clearly indicated an α-helical conformation.
Protein: DP01101 (UniProt P04370-5)
Region: residues 79	to 96
Annotation: order (Structural state)
Evidence: far-UV circular dichroism evidence used in manual assertion
Supporting statements:
In aqueous solution (pure water, and 100 mm KCl, pH 6.5), the spectra indicated that the polypeptide had little or no regular secondary structure. In organic and membrane-mimetic conditions (30% TFE and 20 mm DPC, respectively), the spectra clearly indicated an α-helical conformation.
Protein: DP01101 (UniProt P04370-5)
Region: residues 79	to 96
Annotation: disorder to order (Structural transition)
Evidence: far-UV circular dichroism evidence used in manual assertion
Supporting statements:
In aqueous solution (pure water, and 100 mm KCl, pH 6.5), the spectra indicated that the polypeptide had little or no regular secondary structure. In organic and membrane-mimetic conditions (30% TFE and 20 mm DPC, respectively), the spectra clearly indicated an α-helical conformation.
Protein: DP01101 (UniProt P04370-5)
Region: residues 79	to 96
Annotation: lipid binding (Molecular function)
Evidence: far-UV circular dichroism evidence used in manual assertion
Supporting statements:
In aqueous solution (pure water, and 100 mm KCl, pH 6.5), the spectra indicated that the polypeptide had little or no regular secondary structure. In organic and membrane-mimetic conditions (30% TFE and 20 mm DPC, respectively), the spectra clearly indicated an α-helical conformation.
Here, we focused on a conserved segment of MBP which is known to be a-helical when bound to a membrane, is a potential calmodulin-binding site, and also a primary immunodominant epitope in multiple sclerosis.
Protein: DP01101 (UniProt P04370-5)
Region: residues 83	to 93
Annotation: lipid binding (Molecular function)
Evidence: nuclear magnetic resonance spectroscopy evidence used in manual assertion
Supporting statements:
The CSI analyses of our assignments, shown in Fig. 3, indicate a noticeable tendency of a central 10-residue segment of the polypeptide to adopt a helical conformation from residues 5′ to 14′, for samples in TFE-d2 (Fig. 3B) and in DPC-d38 (Fig. 3C), but not in KCl (Fig. 3A).
Here, we focused on a conserved segment of MBP which is known to be a-helical when bound to a membrane, is a potential calmodulin-binding site, and also a primary immunodominant epitope in multiple sclerosis.
Protein: DP01101 (UniProt P04370-5)
Region: residues 79	to 96
Annotation: disorder (Structural state)
Evidence: nuclear magnetic resonance spectroscopy evidence used in manual assertion
Supporting statements:
The CSI analyses of our assignments, shown in Fig. 3, indicate a noticeable tendency of a central 10-residue segment of the polypeptide to adopt a helical conformation from residues 5′ to 14′, for samples in TFE-d2 (Fig. 3B) and in DPC-d38 (Fig. 3C), but not in KCl (Fig. 3A).
Cross-references: BMRB:6857
Protein: DP01101 (UniProt P04370-5)
Region: residues 83	to 93
Annotation: order (Structural state)
Evidence: nuclear magnetic resonance spectroscopy evidence used in manual assertion
Supporting statements:
The CSI analyses of our assignments, shown in Fig. 3, indicate a noticeable tendency of a central 10-residue segment of the polypeptide to adopt a helical conformation from residues 5′ to 14′, for samples in TFE-d2 (Fig. 3B) and in DPC-d38 (Fig. 3C), but not in KCl (Fig. 3A).
Cross-references: BMRB:6857
Protein: DP01101 (UniProt P04370-5)
Region: residues 83	to 93
Annotation: disorder to order (Structural transition)
Evidence: nuclear magnetic resonance spectroscopy evidence used in manual assertion
Supporting statements:
The CSI analyses of our assignments, shown in Fig. 3, indicate a noticeable tendency of a central 10-residue segment of the polypeptide to adopt a helical conformation from residues 5′ to 14′, for samples in TFE-d2 (Fig. 3B) and in DPC-d38 (Fig. 3C), but not in KCl (Fig. 3A).
Cross-references: BMRB:6857
Protein: DP01101 (UniProt P04370-5)
Region: residues 83	to 93
Annotation: lipid binding (Molecular function)
Evidence: electron paramagnetic resonance evidence used in manual assertion
Supporting statements:
These results demonstrate that the polypeptide α helix forms distinct hydrophobic and electrostatic contacts with the DPC micelles, and are in agreement with the SDSL/EPR mapping and positioning of the α-helical model of this epitope of MBP on the surface of a lipid bilayer [6,7].
Protein: DP01101 (UniProt P04370-5)
Region: residues 73	to 108
Annotation: disorder (Structural state)
Evidence: nuclear magnetic resonance spectroscopy evidence used in manual assertion
Supporting statements:
The central region of the α2-peptide (P82–V91) shows a strong tendency to form an α-helix, as fully expected, whereas the rest of the α2-peptide remains in a predominantly random coil conformation.
Protein: DP01101 (UniProt P04370-5)
Region: residues 92	to 101
Annotation: SH3 domain binding (Molecular function)
Evidence: nuclear magnetic resonance spectroscopy evidence used in manual assertion
Supporting statements:
The titration of Fyn-SH3 into a solution of fully 13C- and 15N-labeled α2-peptide showed chemical shift perturbations of several assigned regions (Figure 9).
Protein: DP01101 (UniProt P04370-5)
Region: residues 82	to 93
Annotation: disorder to order (Structural transition)
Evidence: nuclear magnetic resonance spectroscopy evidence used in manual assertion
Supporting statements:
The central region of the α2-peptide (P82–V91) shows a strong tendency to form an α-helix, as fully expected, whereas the rest of the α2-peptide remains in a predominantly random coil conformation
Here, we have extended these MD studies to determine experimentally the conformation of the considerably larger α2- peptide comprising residues S72−S107 of this region of the protein, in association with DPC micelles, using solution NMR spectroscopy.
Cross-references: PDB:2LUG
BMRB:18520
Protein: DP01102 (UniProt P35637)
Region: residues 1	to 507
Annotation: disorder (Structural state)
Evidence: X-ray crystallography-based structural model with missing residue coordinates used in manual assertion
Supporting statements:
The lack of stable Kapβ2•FUS contacts outside the PY-NLS is consistent with observations that only the PY-NLS is observed in crystal structures of Kapβ2 bound to FUS (full-length), FUS(371–526) and FUS(456–526)
Cross-references: PDB:5YVG
PDB:5YVH
PDB:5YVI