LiteFold/DisProt huggingface dataset:
Protein: DP00652 (UniProt P00441)
Region: residues 69	to 78
Annotation: disorder to order (Structural transition)
Evidence: x-ray crystallography evidence used in manual assertion
Supporting statements:
As expected, crystal structures of metal-bound forms of A4V SOD1 [30] and metal-bound and metal-reconstituted forms of G93A SOD1 (this study) are similar to that of the wild type enzyme in that they possess well-ordered zinc loop (loop IV, residues 50–83) and electrostatic loop (loop VII, residues 121–142) elements. The molecular basis for why the binding of metal ions (particularly zinc) exerts a stabilizing effect on the conformation of these loop elements is shown in Figure 1. First, in the Cu(II) form of the enzyme, H63 of the zinc loop bridges the copper and zinc ions. This “primary bridge”, also known as the “bridging imidazolate”, is a metal ion coordinating feature unique to SOD1 [51]. Second, the binding of zinc to the zinc-binding site by amino acid residues H63, H71, H80, and D83, induces the zinc loop to adopt a structure in which the proline residues at positions 62, 66, and 74 adopt the trans conformation [17, 52].
This region of the pathogenic variant (with the mutation Ala5Val, according to the UniProt sequence) is disordered in solution but when interacting with Cu+2 and Zn+2 ions gets structure, as shown in the cited publication (pmid:15056757, PDB 1UXM)
Cross-references: DisProt:DP00652r006
PDB:3GZQ
Protein: DP00652 (UniProt P00441)
Region: residues 127	to 142
Annotation: disorder to order (Structural transition)
Evidence: x-ray crystallography evidence used in manual assertion
Supporting statements:
As expected, crystal structures of metal-bound forms of A4V SOD1 [30] and metal-bound and metal-reconstituted forms of G93A SOD1 (this study) are similar to that of the wild type enzyme in that they possess well-ordered zinc loop (loop IV, residues 50–83) and electrostatic loop (loop VII, residues 121–142) elements. The molecular basis for why the binding of metal ions (particularly zinc) exerts a stabilizing effect on the conformation of these loop elements is shown in Figure 1. First, in the Cu(II) form of the enzyme, H63 of the zinc loop bridges the copper and zinc ions. This “primary bridge”, also known as the “bridging imidazolate”, is a metal ion coordinating feature unique to SOD1 [51]. Second, the binding of zinc to the zinc-binding site by amino acid residues H63, H71, H80, and D83, induces the zinc loop to adopt a structure in which the proline residues at positions 62, 66, and 74 adopt the trans conformation [17, 52].
This region of the pathogenic variant (with the mutation Ala5Val, according to the UniProt sequence) is disordered in solution but when interacting with Cu+2 and Zn+2 ions gets structure, as shown in the cited publication (pmid:15056757, PDB 1UXM)
Cross-references: PDB:3GZQ
DisProt:DP00652r005
Protein: DP00655 (UniProt P59113)
Region: residues 141	to 249
Annotation: disorder (Structural state)
Evidence: nuclear magnetic resonance spectroscopy evidence used in manual assertion
Supporting statements:
(b) 1-->H–15-->N HSQC spectrum of the F1 insert shows that it is predominantly unstructured as indicated by the poor signal dispersion, although some weaker signals may suggest some ordered elements.
Protein: DP00655 (UniProt P59113)
Region: residues 1	to 11
Annotation: disorder (Structural state)
Evidence: nuclear magnetic resonance spectroscopy evidence used in manual assertion
Supporting statements:
In the talin F0 structure, the secondary-structure elements begin at residue 3, but in kindlin-1, there are an additional 11 residues (MLSSGDLTSAS) at the N-terminus, which are unstructured (Fig. 2b), as indicated by the lack of long-range nuclear Overhauser enhancements (NOEs).
Cross-references: PDB:2KMC
Protein: DP00656 (UniProt P07674)
Region: residues 252	to 294
Annotation: disorder (Structural state)
Evidence: proton-based nuclear magnetic resonance evidence used in manual assertion
Supporting statements:
WT KorB, (N⌬150)KorB, (C⌬60)KorB, and (C⌬105)KorB all exhibited a definite peak in the Kratky plots, a signature of globular structure, although the
data did not go to zero at high Q value. This is indicative of some
degree of random coil component (40), again in line with the predictions of intrinsic disorder and the CD (Fig. 2B) and NMR (Fig. 3) measurements.
Protein: DP00656 (UniProt P07674)
Region: residues 252	to 294
Annotation: flexible linker (Disorder function)
Evidence: proton-based nuclear magnetic resonance evidence used in manual assertion
Supporting statements:
The disordered regions are also likely to be important for
DNA partitioning, as many of the partition proteins need to
span two DNA duplexes (or several proteins) to carry out their
function. Flexible interactions between the central and C-terminal domains of a ParB protein have been seen in the crystal
structures of central and C-terminal domains of ParB from P1
plasmid of Escherichia coli bound to different target sequences
Protein: DP00656 (UniProt P07674)
Region: residues 252	to 294
Annotation: disorder (Structural state)
Evidence: far-UV circular dichroism evidence used in manual assertion
Supporting statements:
The secondary structure content determined from the CD
analysis for (N⌬297)KorB agrees well with the crystal structure
of this domain, whereas that of (N⌬150)KorB agrees with that
predicted from the two known crystal structures of KorB with
random coil at residues 251–297
Protein: DP00656 (UniProt P07674)
Region: residues 252	to 294
Annotation: flexible linker (Disorder function)
Evidence: far-UV circular dichroism evidence used in manual assertion
Supporting statements:
The disordered regions are also likely to be important for
DNA partitioning, as many of the partition proteins need to
span two DNA duplexes (or several proteins) to carry out their
function. Flexible interactions between the central and C-ter-
minal domains of a ParB protein have been seen in the crystal
structures of central and C-terminal domains of ParB from P1
plasmid of Escherichia coli bound to different target sequences
Protein: DP00656 (UniProt P07674)
Region: residues 117	to 137
Annotation: disorder (Structural state)
Evidence: X-ray crystallography-based structural model with missing residue coordinates used in manual assertion
Supporting statements:
The KorB-N domain, for which no structural information is available, is probably connected to helix 1 of KorB-O via a flexible linker, as indicated by residues Arg117–Tyr137, which are disordered in the crystal structure of the KorB-O–DNA complex.
Cross-references: PDB:1R71
Protein: DP00656 (UniProt P07674)
Region: residues 117	to 137
Annotation: flexible linker (Disorder function)
Evidence: X-ray crystallography-based structural model with missing residue coordinates used in manual assertion
Supporting statements:
The KorB-N domain, for which no structural information is available, is probably connected to helix 1 of KorB-O via a flexible linker, as indicated by residues Arg117–Tyr137, which are disordered in the crystal structure of the KorB-O–DNA complex.
Protein: DP00656 (UniProt P07674)
Region: residues 1	to 50
Annotation: disorder (Structural state)
Evidence: far-UV circular dichroism evidence used in manual assertion
Supporting statements:
In all cases, the CD suggests that the N-terminal 50 amino acids of KorB and the linker between the central and DNA-binding domains are unstructured
Protein: DP00656 (UniProt P07674)
Region: residues 31	to 137
Annotation: order to disorder (Structural transition)
Evidence: nuclear magnetic resonance spectroscopy evidence used in manual assertion
Supporting statements:
The NMR data for the N-ter-
minal domain does show that there is some structure present
(Fig. 3), however, the peaks between 8.0 and 8.5 ppm could arise
from amide protons in either unstructured or alpha-helical regions.
This domain may exists in an equilibrium between a folded and
unfolded state, and the folded and unfolded conformations of
this domain we have generated represent limiting cases.
Protein: DP00656 (UniProt P07674)
Region: residues 253	to 294
Annotation: disorder (Structural state)
Evidence: X-ray crystallography-based structural model with missing residue coordinates used in manual assertion
Supporting statements:
KorB-O and KorB-C are connected by a linker that is probably flexible, as residue Lys253–Lys294 are disordered in the KorB-O–DNA crystal.
Cross-references: PDB:1R71
Protein: DP00656 (UniProt P07674)
Region: residues 253	to 294
Annotation: flexible linker (Disorder function)
Evidence: X-ray crystallography-based structural model with missing residue coordinates used in manual assertion
Supporting statements:
KorB-O and KorB-C are connected by a linker that is probably flexible, as residue Lys253–Lys294 are disordered in the KorB-O–DNA crystal.
Cross-references: PDB:1R71
Protein: DP00657 (UniProt P31168)
Region: residues 1	to 265
Annotation: disorder (Structural state)
Evidence: far-UV circular dichroism evidence used in manual assertion
Supporting statements:
In physiological buffer, the circular dichroism spectra of the full-length dehydrins reveal overall disordered structures with a variable content of poly-Pro helices, a type of elongated secondary structure relying on bridging water molecules.
Protein: DP00658 (UniProt P42758)
Region: residues 1	to 193
Annotation: disorder (Structural state)
Evidence: far-UV circular dichroism evidence used in manual assertion
Supporting statements:
In physiological buffer at 4°C, the circular dichroism (CD) spectra of all four full-length dehydrins display large minima around 200 nm and an ellipticity near zero around 220 nm, indicative of poorly structured conformations with low content of secondary structure (Fig. 2A
Protein: DP00658 (UniProt P42758)
Region: residues 1	to 193
Annotation: disorder (Structural state)
Evidence: Fourier-transform infrared spectroscopy evidence used in manual assertion
Supporting statements:
A strong band at 1,644 cm−1 and a weak band at 1,673 cm−1 at both pH 5 and 8.6 indicate random coil structure (Fig. 5A).
Protein: DP00658 (UniProt P42758)
Region: residues 1	to 193
Annotation: lipid binding (Molecular function)
Evidence: stopped-flow fluorescence spectroscopy evidence
Supporting statements:
As seen in Figure 2, 2% negatively charged lipids are adequate for Lti30 to bind and cluster the vesicles.
The conclusion is that Lti30 has a strong affinity for low concentrations of negative lipids and needs only a few negative lipids to bind and cluster vesicles. This indicates that Lti30 also can bind to different cellular membranes in vivo, since most of these contain higher concentrations of negatively charged phospholipids than tested here (Uemura et al., 1995).
Protein: DP00658 (UniProt P42758)
Region: residues 1	to 193
Annotation: lipid binding (Molecular function)
Evidence: microscopy evidence used in manual assertion
Supporting statements:
The large clusters formed due to Lti30 binding are detectable with a light microscope, and images of the clusters further support the stopped-flow data (Fig. 3).
The conclusion is that Lti30 has a strong affinity for low concentrations of negative lipids and needs only a few negative lipids to bind and cluster vesicles. This indicates that Lti30 also can bind to different cellular membranes in vivo, since most of these contain higher concentrations of negatively charged phospholipids than tested here (Uemura et al., 1995).
Protein: DP00658 (UniProt P42758)
Region: residues 1	to 193
Annotation: disorder to order (Structural transition)
Evidence: Fourier-transform infrared spectroscopy evidence used in manual assertion
Supporting statements:
Accordingly, in the absence of lipid vesicles, Lti30 displays the characteristic fingerprint of a fully disordered chain (Fig. 5A), consistent with previous reports (Mouillon et al., 2006, 2008). Then, upon interaction with DMPC:DMPG vesicles, Lti30 undergoes a conformational shift coupled to perturbation of the lipid bilayer (Fig. 5, B and C).
Protein: DP00658 (UniProt P42758)
Region: residues 62	to 82
Annotation: disorder (Structural state)
Evidence: proton-based nuclear magnetic resonance evidence used in manual assertion
Supporting statements:
The free KLti30 is soluble in buffer and gives a good one-dimensional 1H-NMR spectrum, typical for a fully disordered peptide (Fig. 6).
Protein: DP00658 (UniProt P42758)
Region: residues 35	to 55
Annotation: disorder (Structural state)
Evidence: proton-based nuclear magnetic resonance evidence used in manual assertion
Supporting statements:
The free KLti30 is soluble in buffer and gives a good one-dimensional 1H-NMR spectrum, typical for a fully disordered peptide (Fig. 6).
Protein: DP00658 (UniProt P42758)
Region: residues 35	to 55
Annotation: lipid binding (Molecular function)
Evidence: proton-based nuclear magnetic resonance evidence used in manual assertion
Supporting statements:
Upon the addition of bicelles, however, the chemical shift signatures of the KLti30 segment spectra undergo distinct alterations consistent with binding (Fig. 6).
Protein: DP00658 (UniProt P42758)
Region: residues 62	to 82
Annotation: lipid binding (Molecular function)
Evidence: proton-based nuclear magnetic resonance evidence used in manual assertion
Supporting statements:
Upon the addition of bicelles, however, the chemical shift signatures of the KLti30 segment spectra undergo distinct alterations consistent with binding (Fig. 6).
Protein: DP00658 (UniProt P42758)
Region: residues 40	to 49
Annotation: disorder to order (Structural transition)
Evidence: nuclear magnetic resonance spectroscopy evidence used in manual assertion
Supporting statements:
Although the chemical shifts induced upon bicelle binding are moderate at the level of population average (Fig. 6), we conclude from the diffusion data that the chemical shift perturbations of the bound population are twice the observed values and, consequently, in line with the folding of the KLti30 segment into an ordered structure. To determine at atomic resolution the structure of the membrane-bound KLti30, we used deuterated bicelles and two-dimensional NMR. The results reveal six αHi-NHi  +3 nuclear Overhauser effect (NOE) couplings in the central part of the KLti30 segment (Fig. 6C), constraining residues Gly-7 to Gln-15 into a well-ordered α-helix, when bound to bicelles (Figs. 6 and 7).
Structural analysis of membrane-bound KLti30 peptide by NMR. A, The five best structures of bicelle-bound KLti30 peptide from 1H-NMR constraints, where the central nine residues of the peptide adopt a fixed α-helix, whereas the N and C termini are more disordered.
Protein: DP00658 (UniProt P42758)
Region: residues 67	to 76
Annotation: disorder to order (Structural transition)
Evidence: nuclear magnetic resonance spectroscopy evidence used in manual assertion
Supporting statements:
Although the chemical shifts induced upon bicelle binding are moderate at the level of population average (Fig. 6), we conclude from the diffusion data that the chemical shift perturbations of the bound population are twice the observed values and, consequently, in line with the folding of the KLti30 segment into an ordered structure. To determine at atomic resolution the structure of the membrane-bound KLti30, we used deuterated bicelles and two-dimensional NMR. The results reveal six αHi-NHi  +3 nuclear Overhauser effect (NOE) couplings in the central part of the KLti30 segment (Fig. 6C), constraining residues Gly-7 to Gln-15 into a well-ordered α-helix, when bound to bicelles (Figs. 6 and 7).
Structural analysis of membrane-bound KLti30 peptide by NMR. A, The five best structures of bicelle-bound KLti30 peptide from 1H-NMR constraints, where the central nine residues of the peptide adopt a fixed α-helix, whereas the N and C termini are more disordered.
Protein: DP00661 (UniProt Q9CX60)
Region: residues 1	to 105
Annotation: disorder (Structural state)
Evidence: nuclear magnetic resonance spectroscopy evidence used in manual assertion
Supporting statements:
 As shown in Fig. 3C, the majority of backbone amide proton resonances exhibited poor chemical shift dispersion (~7.9–8.7 ppm), indicating substantial regions of structural disorder. In addition, many resonances were broadened, indicating interconversion between multiple conformations occurring within the "intermediate" NMR timescale.
Protein: DP00661 (UniProt Q9CX60)
Region: residues 1	to 105
Annotation: disorder (Structural state)
Evidence: chromatography evidence used in manual assertion
Supporting statements:
 This value is approximately three-fold greater than its theoretical molecular mass of 12.3 kD and could suggest that LBH exists as a higher-order oligomer in solution. However, since determination of molecular mass of proteins from such analysis is highly dependent upon their globular shape, an alternative scenario could be that LBH lacks an intrinsic globular fold allowing it to behave as a structurally disordered polymer.
Protein: DP00661 (UniProt Q9CX60)
Region: residues 1	to 105
Annotation: disorder (Structural state)
Evidence: far-UV circular dichroism evidence used in manual assertion
Supporting statements:
As shown in Fig. 3B, CD spectrum of LBH in the far-UV region (180–240 nm) is largely characterized by a negative band centered around 200 nm, which is reminiscent of a structurally disordered protein with little or no secondary structure.
Protein: DP00661 (UniProt Q9CX60)
Region: residues 1	to 105
Annotation: disorder (Structural state)
Evidence: near-UV circular dichroism evidence used in manual assertion
Supporting statements:
Additionally, the CD spectrum of LBH in the near-UV region (240–300 nm) is completely devoid of a band around 280 nm, which would be expected for a non-globular protein with one or more tryptophan residues.
Protein: DP00661 (UniProt Q9CX60)
Region: residues 1	to 105
Annotation: disorder (Structural state)
Evidence: static light scattering assay evidence used in manual assertion
Supporting statements:
Thus, the molecular mass determined for LBH from ALS analysis on the basis of first principles of hydrodynamics with no assumptions is in an excellent agreement with a theoretical value of 12.3 kD and suggests that LBH exists as a monomer in solution. Additionally, a value of 234 Å for the radius of gyration of LBH strongly suggests that LBH lacks a globular fold and most likely behaves as a rod-like macromolecule.
Protein: DP00661 (UniProt Q9CX60)
Region: residues 1	to 105
Annotation: disorder (Structural state)
Evidence: fluorescence evidence used in manual assertion
Supporting statements:
In Figure 3A, fluorescence spectrum of LBH shows that the single tryptophan residue (Trp-80) within the protein emits with λmax around 350 nm. Given that this is the λmax observed for free tryptophan residues in solution, it can be argued that the tryptophan residue within LBH is completely accessible to the aqueous solvent and that LBH is likely to contain a non-globular fold.
Protein: DP00666 (UniProt P32004)
Region: residues 1144	to 1257
Annotation: disorder (Structural state)
Evidence: nuclear magnetic resonance spectroscopy evidence used in manual assertion
Supporting statements:
On the basis of 13Cα and 13Cβ chemical shifts, which do not significantly deviate from the random coil values (Figure 1B), and the narrow distribution of the amide peaks in the 15N-HSQC spectrum (Figure 1C), we conclude that L1-CT is predominantly unstructured in aqueous solution.
Protein: DP00666 (UniProt P32004)
Region: residues 1144	to 1257
Annotation: protein binding (Molecular function)
Evidence: nuclear magnetic resonance spectroscopy evidence used in manual assertion
Supporting statements:
 Titrating the unlabeled proteins, the ezrin FERM domain and the AP2-μ2 chain, into the solution of isotopically labeled L1-CT and monitoring associated perturbations in the 15N-HSQC spectra allowed us to map the binding surface of L1-CT in both complexes.
Surprisingly, in addition to the two ERM binding sites identified in previous studies, the 1176YRSLE region and the juxtamembrane region, we identified a significant line broadening in a third one, composed of residues from 1213G to 1232K (Figure 3A,B). This site overlaps with the classical ankyrin binding motif, 1220NEDGS-FIGQY.
In the case of AP2-μ2, as expected, the1176YRSL motif of L1-CT is in the center of the cluster of resonances with reduced peak intensities (Figure 3E). Thus it is, indeed, the major binding determinant. The residue three amino acids upstream of 1176Y, 1173F, is also involved in the L1-AP2-μ2 complex. Contrary to the L1 interaction with ezrin, the C-terminus of L1-CT is not involved in the interaction with AP2-μ2. Surprisingly enough, we do see additional perturbations in the juxtamembrane region of L1-CT.
Protein: DP00666 (UniProt P32004)
Region: residues 1144	to 1257
Annotation: disorder (Structural state)
Evidence: dynamic light scattering assay evidence used in manual assertion
Supporting statements:
Dynamic light scattering experiments provided us with similar results. The normalized volume distribution for the L1-CT particles in aqueous solution (at 0.03 mM, pH 8.0, IS 300 mM) is presented in Figure 2B. The major peak is observed around a diameter of 5.93 nm with minor features near 15 nm for the higher order aggregates.
Protein: DP00666 (UniProt P32004)
Region: residues 1144	to 1257
Annotation: disorder (Structural state)
Evidence: chromatography evidence used in manual assertion
Supporting statements:
This elution position, however, does not correspond to a 14.4 kDa globular monomeric protein [Figure 2C (peak 5, myoglobin, 18 kDa; peak 6, cytochrome c, 13 kDa, shown for comparison)], which we believe is due to the disordered nature of the L1-CT monomer characterized by a significantly increased hydrodynamic radius.
Protein: DP00666 (UniProt P32004)
Region: residues 1144	to 1257
Annotation: disorder (Structural state)
Evidence: analytical ultracentrifugation evidence used in manual assertion
Supporting statements:
Global analysis of the two data sets using a hybrid continuous-discrete model yields a best fit molecular mass of 18.2 kDa for the major species, with a corrected sedimentation coefficient of s20,w = 1.63 S and a frictional ratio of f/f0 = 1.59. These data indicate that L1-CT exists as a monomer at this concentration range. However, the deduced molecular mass is somewhat higher than the monomer value of 14.4 kDa.
The frictional ratio is much higher than the value of 1.1–1.3 typically observed for globular proteins and is consistent with the NMR data indicating an unstructured extended conformation.
Protein: DP00667 (UniProt P42763)
Region: residues 1	to 185
Annotation: disorder (Structural state)
Evidence: nuclear magnetic resonance spectroscopy evidence used in manual assertion
Supporting statements:
The 1H-NMR spectra of ERD10 and ERD14 (Fig. 3A; only ERD10 is shown) also suggest their disordered nature, because the chemical shift dispersion is narrower than is typical for globular proteins. For globular proteins, 1H chemical shifts usually spread out in the region 9.5 to 6.0 ppm, whereas for IDPs, they are usually confined in the region 8.0 to 8.5 ppm (Dyson and Wright, 2004).
Protein: DP00667 (UniProt P42763)
Region: residues 1	to 185
Annotation: disorder (Structural state)
Evidence: sodium dodecyl sulfate polyacrylamide gel electrophoresis evidence used in manual assertion
Supporting statements:
In SDS-PAGE, they show a characteristic low mobility: the real molecular mass of ERD10 is 29 kD but it runs at 45 kD, whereas the real molecular mass of ERD14 is 20 kD but it runs at 37 kD (Fig. 2A). This high apparent molecular mass caused by a highly hydrophilic character is often diagnostic of IDPs (Tompa, 2002). In addition, both proteins are heat stable (Fig. 2B) and are very sensitive to proteases (Fig. 2A).