LiteFold/DisProt huggingface dataset:
Protein: DP00164 (UniProt P05318)
Region: residues 1	to 106
Annotation: disorder (Structural state)
Evidence: far-UV circular dichroism evidence used in manual assertion
Supporting statements:
The P1α CD spectra show features of a virtually unordered protein with some negative ellipticiy around 222 nm which disappears completely when high concentrations of urea are added to the protein (data not shown). This suggests a residual α-helical content even though the protein seems to be mainly random-coil.
Protein: DP00164 (UniProt P05318)
Region: residues 1	to 106
Annotation: disorder (Structural state)
Evidence: nuclear magnetic resonance spectroscopy evidence used in manual assertion
Supporting statements:
In agreement with the previous observations, NMR studies on the intact protein show very little signal dispersion (Figure 4) and very fast amide exchange when protein is incubated in the presence of deuterated water (data not shown).
Protein: DP00164 (UniProt P05318)
Region: residues 1	to 106
Annotation: protein binding (Molecular function)
Evidence: far-UV circular dichroism evidence used in manual assertion
Supporting statements:
Incubation of both proteins was followed by far-UV CD and 1D-NMR measurements, and spectra were compared with those of the isolated proteins under the same conditions. The CD spectra of the protein mixture, when compared to the arithmetical addition of spectra from the individual proteins indicate that some secondary structural changes take place upon incubation of both proteins together (Figure 9A).
Protein interactions seems to increase the secondary structure of one or both proteins.
Protein: DP00164 (UniProt P05318)
Region: residues 1	to 106
Annotation: protein binding (Molecular function)
Evidence: proton-based nuclear magnetic resonance evidence used in manual assertion
Supporting statements:
Incubation of both proteins was followed by far-UV CD and 1D-NMR measurements, and spectra were compared with those of the isolated proteins under the same conditions. The CD spectra of the protein mixture, when compared to the arithmetical addition of spectra from the individual proteins indicate that some secondary structural changes take place upon incubation of both proteins together (Figure 9A).
Protein: DP00166 (UniProt P19429)
Region: residues 192	to 210
Annotation: disorder (Structural state)
Evidence: X-ray crystallography-based structural model with missing residue coordinates used in manual assertion
Supporting statements:
As described above, most of the electron densities associated with the potential actin–tropomyosin interfaces are ambiguous. These include the inhibitory region (residues 137–148) and the C-terminus of TnI (residues 163–210 in Tn52KA and 192–210 in Tn52KB), and the C-TnT (residues 272–288).
Cross-references: PDB:1J1D
Protein: DP00166 (UniProt P19429)
Region: residues 137	to 148
Annotation: disorder (Structural state)
Evidence: X-ray crystallography-based structural model with missing residue coordinates used in manual assertion
Supporting statements:
As described above, most of the electron densities associated with the potential actin–tropomyosin interfaces are ambiguous. These include the inhibitory region (residues 137–148) and the C-terminus of TnI (residues 163–210 in Tn52KA and 192–210 in Tn52KB), and the C-TnT (residues 272–288).
Third, the link through TnI, the inhibitory region that connects H2(I) and H3(I), is not well defined in the present structures, indicating that this link is also flexible.
Cross-references: PDB:1J1E
PDB:1J1D
Protein: DP00166 (UniProt P19429)
Region: residues 137	to 148
Annotation: flexible linker (Disorder function)
Evidence: X-ray crystallography-based structural model with missing residue coordinates used in manual assertion
Supporting statements:
As described above, most of the electron densities associated with the potential actin–tropomyosin interfaces are ambiguous. These include the inhibitory region (residues 137–148) and the C-terminus of TnI (residues 163–210 in Tn52KA and 192–210 in Tn52KB), and the C-TnT (residues 272–288).
Third, the link through TnI, the inhibitory region that connects H2(I) and H3(I), is not well defined in the present structures, indicating that this link is also flexible.
Cross-references: PDB:1J1E
PDB:1J1D
Protein: DP00166 (UniProt P19429)
Region: residues 1	to 40
Annotation: disorder (Structural state)
Evidence: cryogenic electron microscopy-based structural model with missing residue coordinates used in manual assertion
Supporting statements:
The electron microscopy structure of the tropomyosin in human cardiac thin filament (both bounded and unbounded to calcium) show this region of the Troponin I protein lacks electron density, indicating it is disordered. 
Cross-references: PDB:7UTL
PDB:7UTI
Protein: DP00166 (UniProt P19429)
Region: residues 167	to 210
Annotation: disorder (Structural state)
Evidence: cryogenic electron microscopy-based structural model with missing residue coordinates used in manual assertion
Supporting statements:
The electron microscopy structure of the tropomyosin in human cardiac thin filament show this region of the Troponin I protein lacks electron density when bounded to calcium, indicating this region is disordered. 
Cross-references: PDB:7UTI
Protein: DP00166 (UniProt P19429)
Region: residues 167	to 210
Annotation: order to disorder (Structural transition)
Evidence: cryogenic electron microscopy-based structural model with missing residue coordinates used in manual assertion
Supporting statements:
The electron microscopy structure of the tropomyosin in human cardiac thin filament show this region of the Troponin I protein lacks electron density when bounded to calcium, indicating this region is disordered.
Cross-references: PDB:7UTI
PDB:7UTL
Protein: DP00168 (UniProt Q9NVS9)
Region: residues 1	to 48
Annotation: disorder (Structural state)
Evidence: X-ray crystallography-based structural model with missing residue coordinates used in manual assertion
Supporting statements:
 Like the E. coli (PDB code 1G79) and yeast PNPOx (PDB code IC10) structures, which are missing the first 19 and 23 N-terminal amino acid residues, the first 48 N-terminal amino acid residues of human PNPOx are also absent in the structure because of disorder.
Cross-references: PDB:1NRG
Protein: DP00169 (UniProt P32882)
Region: residues 432	to 445
Annotation: disorder (Structural state)
Evidence: nuclear magnetic resonance spectroscopy evidence used in manual assertion
Supporting statements:
Two-dimensional 1H-NMR parameters (nonsequential nuclear Overhauser effects (NOE) and conformational CaH shifts) in 30% TFE permitted to conclude that about 25% of a(404–451) and 40% of b(394–451) form well-defined helices encompassing residues 418–432 and 408–431, respectively, flanked by disordered N- and C-segments.
Protein: DP00171 (UniProt P04049)
Region: residues 236	to 255
Annotation: disorder (Structural state)
Evidence: X-ray crystallography-based structural model with missing residue coordinates used in manual assertion
Supporting statements:
The 20-amino‐acid stretch between pS233 and pS259 could not be traced, presumably due to its intrinsic disorder and lack of contacts to the 14-3-3ζ protein.
Cross-references: PDB:4FJ3
Protein: DP00171 (UniProt P04049)
Region: residues 238	to 254
Annotation: disorder (Structural state)
Evidence: X-ray crystallography-based structural model with missing residue coordinates used in manual assertion
Supporting statements:
The missing electron density region from PDB:4IHL corresponds to the disordered stretch between pS233 and pS259 described in PMID:22922483
Cross-references: PDB:4IHL
Protein: DP00173 (UniProt O00273)
Region: residues 1	to 100
Annotation: disorder (Structural state)
Evidence: far-UV circular dichroism evidence used in manual assertion
Supporting statements:
Because nonspecific aggregation can also lead to such an appearance of the HSQC spectra, we recorded a CD spectrum of DFF45 NTD (1), which showed a lack of secondary structure (Fig. ​2B) and confirmed that NTD of DFF45 is indeed disordered.
Protein: DP00173 (UniProt O00273)
Region: residues 1	to 100
Annotation: disorder (Structural state)
Evidence: nuclear magnetic resonance spectroscopy evidence used in manual assertion
Supporting statements:
In contrast, the NTD of DFF45 exhibits a spectrum typical for a disordered protein (Fig. ​2C).
Protein: DP00173 (UniProt O00273)
Region: residues 12	to 100
Annotation: disorder to order (Structural transition)
Evidence: nuclear magnetic resonance spectroscopy evidence used in manual assertion
Supporting statements:
To reconcile these conflicting observations, we performed NMR titration of 15N-labeled DFF45 NTD with unlabeled DFF40. The 1:1 complex displays well dispersed HSQC spectra (Fig. 2D), suggesting that folding of DFF45 NTD is induced upon binding to DFF40.
Cross-references: PDB:1IBX
Protein: DP00173 (UniProt O00273)
Region: residues 12	to 100
Annotation: protein binding (Molecular function)
Evidence: nuclear magnetic resonance spectroscopy evidence used in manual assertion
Supporting statements:
To reconcile these conflicting observations, we performed NMR titration of 15N-labeled DFF45 NTD with unlabeled DFF40. The 1:1 complex displays well dispersed HSQC spectra (Fig. ​2D), suggesting that folding of DFF45 NTD is induced upon binding to DFF40.
Cross-references: PDB:1IBX
Protein: DP00175 (UniProt Q9NQB0)
Region: residues 1	to 56
Annotation: disorder (Structural state)
Evidence: far-UV circular dichroism evidence used in manual assertion
Supporting statements:
TCF4 (1-53) as well as TCF4 (1-56; not shown) showed a strongly negative CD signal at 200 nM, indicative of random-coil structure.
Protein: DP00175 (UniProt Q9NQB0)
Region: residues 40	to 50
Annotation: disorder to order (Structural transition)
Evidence: X-ray crystallography-based structural model with missing residue coordinates used in manual assertion
Supporting statements:
The Tcf4 peptide (yellow) has two sites of interaction with the armadillo repeat region of β-catenin (blue): an 'extended region' composed of residues 13–25 (labeled N in yellow) and a more C-terminal helical region composed of residues 40–50 (labeled C in yellow). The intervening 14 residues are disordered, as are residues 8–12 at the N-terminus and 51–54 at the C-terminus.
Cross-references: PDB:1JPW
Protein: DP00175 (UniProt Q9NQB0)
Region: residues 40	to 50
Annotation: beta-catenin binding (Molecular function)
Evidence: X-ray crystallography-based structural model with missing residue coordinates used in manual assertion
Supporting statements:
The Tcf4 peptide (yellow) has two sites of interaction with the armadillo repeat region of β-catenin (blue): an 'extended region' composed of residues 13–25 (labeled N in yellow) and a more C-terminal helical region composed of residues 40–50 (labeled C in yellow). The intervening 14 residues are disordered, as are residues 8–12 at the N-terminus and 51–54 at the C-terminus.
Cross-references: PDB:1JPW
Protein: DP00175 (UniProt Q9NQB0)
Region: residues 13	to 25
Annotation: disorder to order (Structural transition)
Evidence: X-ray crystallography-based structural model with missing residue coordinates used in manual assertion
Supporting statements:
The Tcf4 peptide (yellow) has two sites of interaction with the armadillo repeat region of β-catenin (blue): an 'extended region' composed of residues 13–25 (labeled N in yellow) and a more C-terminal helical region composed of residues 40–50 (labeled C in yellow). The intervening 14 residues are disordered, as are residues 8–12 at the N-terminus and 51–54 at the C-terminus.
Cross-references: PDB:1JPW
Protein: DP00175 (UniProt Q9NQB0)
Region: residues 13	to 25
Annotation: beta-catenin binding (Molecular function)
Evidence: X-ray crystallography-based structural model with missing residue coordinates used in manual assertion
Supporting statements:
The Tcf4 peptide (yellow) has two sites of interaction with the armadillo repeat region of β-catenin (blue): an 'extended region' composed of residues 13–25 (labeled N in yellow) and a more C-terminal helical region composed of residues 40–50 (labeled C in yellow). The intervening 14 residues are disordered, as are residues 8–12 at the N-terminus and 51–54 at the C-terminus.
Cross-references: PDB:1JPW
Protein: DP00175 (UniProt Q9NQB0)
Region: residues 1	to 53
Annotation: disorder (Structural state)
Evidence: far-UV circular dichroism evidence used in manual assertion
Supporting statements:
TCF4 (1-53) as well as TCF4 (1-56; not shown) showed a strongly negative CD signal at 200 nM, indicative of random-coil structure.
Protein: DP00175 (UniProt Q9NQB0)
Region: residues 1	to 130
Annotation: disorder (Structural state)
Evidence: far-UV circular dichroism evidence used in manual assertion
Supporting statements:
A similar spectrum was observed for the elongated construct (TCF4 1-130; Figure 2). Therefore, the lack of defined secondary-structure formation is not a result of the short construct length.
Protein: DP00175 (UniProt Q9NQB0)
Region: residues 1	to 53
Annotation: beta-catenin binding (Molecular function)
Evidence: surface plasmon resonance evidence used in manual assertion
Supporting statements:
The observed binding curves revealed a tight and reversible binding of β-catenin to immobilized TCF4 with a dissociation constant (KD) of 8.4(±0.3) nM (KB=1.2×108 M−1; Figure 3).
Protein: DP00175 (UniProt Q9NQB0)
Region: residues 1	to 53
Annotation: beta-catenin binding (Molecular function)
Evidence: static fluorescence quenching evidence used in manual assertion
Supporting statements:
Titration of TCF4 (1-53) into a solution of β-catenin resulted in the determination of a dissociation constant (KD) of 11.7(±0.3)nM at 25 °C (Table 1) which corresponds to a change in free energy of −10.8 kcal/mol.
The comparison of this dissociation constant with the one measured using full-length β-catenin indicates that the armadillo region is sufficient for the high-affinity interaction with TCF4 in solution.
Protein: DP00175 (UniProt Q9NQB0)
Region: residues 1	to 53
Annotation: beta-catenin binding (Molecular function)
Evidence: isothermal titration calorimetry evidence used in manual assertion
Supporting statements:
The analysis revealed that the binding thermodynamics of TCF4 (1-53) and TCF4 (1-56) were indistinguishable within the error of the measurements. Furthermore, elongation of the construct length to 130 residues altered neither the binding constants nor the thermodynamic parameters.
Since comparable binding constants and thermodynamic parameters were obtained for the three constructs, it can be concluded that the first 53 amino acid residues of TCF4 are sufficient for high-affinity binding to β-catenin/armadillo.
Protein: DP00175 (UniProt Q9NQB0)
Region: residues 26	to 39
Annotation: disorder (Structural state)
Evidence: isothermal titration calorimetry evidence used in manual assertion
Supporting statements:
The Tcf4 peptide (yellow) has two sites of interaction with the armadillo repeat region of β-catenin (blue): an 'extended region' composed of residues 13–25 (labeled N in yellow) and a more C-terminal helical region composed of residues 40–50 (labeled C in yellow). The intervening 14 residues are disordered, as are residues 8–12 at the N-terminus and 51–54 at the C-terminus.
Cross-references: PDB:1JPW
Protein: DP00176 (UniProt P42512)
Region: residues 38	to 55
Annotation: disorder (Structural state)
Evidence: x-ray crystallography evidence used in manual assertion
Supporting statements:
 No electron density is observed for the N-terminal part of the receptor (residues Asp38 to Gly55) and the first residues observed in the electron density have high B-factors (B-factor average from Glu56 to Ser59: 47.14 Å2).
Cross-references: PDB:1XKW
Protein: DP00176 (UniProt P42512)
Region: residues 504	to 513
Annotation: disorder (Structural state)
Evidence: X-ray crystallography-based structural model with missing residue coordinates used in manual assertion
Supporting statements:
The poor quality of the electron density from Gln504 to Glu513 prevented the rebuilding of loop L7. The analysis of electron density maps calculated in space group P1 before and after the density modification by solvent flattening and density averaging did not provide details for the disordered parts of the model observed at 2.0 Å resolution.
Cross-references: PDB:1XKW
Protein: DP00177 (UniProt Q9Y5B0)
Region: residues 879	to 944
Annotation: disorder (Structural state)
Evidence: nuclear magnetic resonance spectroscopy evidence used in manual assertion
Supporting statements:
Interestingly, the cterFCP protein is completely disordered in the unbound state, but forms an α-helix (H1'; E945–M961) in the complex.
The free cterFCP protein is devoid of any stable structural element but adopts a 17-residue α-helix (H1') at its carboxyl terminus (E945-M961) on inter- action with cterRAP74 (Fig. 1A).
Cross-references: PDB:1ONV
BMRB:5685
Protein: DP00177 (UniProt Q9Y5B0)
Region: residues 879	to 961
Annotation: disorder (Structural state)
Evidence: nuclear magnetic resonance spectroscopy evidence used in manual assertion
Supporting statements:
NMR assignment of the intrinsically disordered C-terminal region of Homo sapiens FCP1 in the unbound state
The acidic C-terminal region of FCP1 is disordered in the free state, but adopts an alpha-helical conformation upon binding to the heavy chain of TFIIF. Here we report (1)H, (13)C, and (15)N resonance assignments for the intrinsically disordered unbound form of human C-terminal FCP1 (residues 879-961).
Cross-references: BMRB:16296
Protein: DP00177 (UniProt Q9Y5B0)
Region: residues 945	to 961
Annotation: disorder to order (Structural transition)
Evidence: nuclear magnetic resonance spectroscopy evidence used in manual assertion
Supporting statements:
Interestingly, the cterFCP protein is completely disordered in the unbound state, but forms an α-helix (H1'; E945–M961) in the complex.
The free cterFCP protein is devoid of any stable structural element but adopts a 17-residue α-helix (H1') at its carboxyl terminus (E945-M961) on interaction with cterRAP74 (Fig. 1A). These residues of cterFCP
that are involved in formation of the alpha-helix display significant
changes in amide 1 H and 15 N chemical shifts between the free
state and the complex. Chemical shift index (CSI) analysis of
the H-alpha , C-alpha , C-beta, and C' chemical shifts of cterFCP also supports
the presence of the H1' helix for residues E945–M961 in the
complex, but not in the free form.
Cross-references: PDB:1ONV
Protein: DP00177 (UniProt Q9Y5B0)
Region: residues 945	to 961
Annotation: protein binding (Molecular function)
Evidence: nuclear magnetic resonance spectroscopy evidence used in manual assertion
Supporting statements:
The importance of the H1' helix for interaction with cterRAP74 is supported by numerous intermolecular NOEs between the H1' alpha-helix of
cterFCP and cterRAP74
Those amino acids that show intermolecular NOEs are indicated by an asterisk below the residue.
Cross-references: BMRB:5685
PDB:1ONV
Protein: DP00177 (UniProt Q9Y5B0)
Region: residues 944	to 961
Annotation: disorder (Structural state)
Evidence: far-UV circular dichroism evidence used in manual assertion
Supporting statements:
We therefore chose to measure circular dichroism
using both the ctFCP1 construct from the NMR samples and a
shorter synthetic peptide (comprising residues 944–961) in which
the fraction of helical residues should be enriched. The spectra for
the peptide and for ctFCP1 are shown black in Fig. 3A and B, respec-
tively. While both are characteristic of CD spectra for IDPs, they
also feature a subtle minimum near 222 nm – the hallmark of an
alpha-helix.
Protein: DP00177 (UniProt Q9Y5B0)
Region: residues 950	to 961
Annotation: disorder (Structural state)
Evidence: nuclear magnetic resonance spectroscopy evidence used in manual assertion
Supporting statements:
Consensus analysis of chemical shifts indicates strong enough secondary shifting to assign a helical conformation to residues 945–949, which are found in the
N-terminal portion of the RAP74 binding helix. The analysis indicates that the remainder of ctFCP1 is in a disordered state, although there is signiﬁcant tendency towards helical chemical shifts in many other residues composing the RAP74 binding interface as well.
Protein: DP00179 (UniProt P01094)
Region: residues 1	to 68
Annotation: disorder (Structural state)
Evidence: far-UV circular dichroism evidence used in manual assertion
Supporting statements:
Circular dichroism (CD) measurements were also performed on the peptide (residues 2–34) and protein forms of the free inhibitor in solution. Inspection of both spectra (data not shown) gave no indication of the presence of any ordered structure, be it helical or extended. Instead, the spectra were compatible with random coil.
Protein: DP00179 (UniProt P01094)
Region: residues 2	to 34
Annotation: disorder (Structural state)
Evidence: far-UV circular dichroism evidence used in manual assertion
Supporting statements:
Circular dichroism (CD) measurements were also performed on the peptide (residues 2–34) and protein forms of the free inhibitor in solution. Inspection of both spectra (data not shown) gave no indication of the presence of any ordered structure, be it helical or extended. Instead, the spectra were compatible with random coil.
Protein: DP00179 (UniProt P01094)
Region: residues 33	to 68
Annotation: disorder (Structural state)
Evidence: X-ray crystallography-based structural model with missing residue coordinates used in manual assertion
Supporting statements:
In the resulting structures (Fig. 1 ), residues 2–32 of IA3 become ordered and form a near-perfect amphipathic α-helix (Fig. 2). In contrast, the remaining 36 residues from the C-terminus of the inhibitor are unstructured.
Cross-references: PDB:1DP5
Protein: DP00179 (UniProt P01094)
Region: residues 2	to 32
Annotation: disorder to order (Structural transition)
Evidence: x-ray crystallography evidence used in manual assertion
Supporting statements:
In the resulting structures (Fig. 1 ), residues 2–32 of IA3 become ordered and form a near-perfect amphipathic α-helix (Fig. 2). In contrast, the remaining 36 residues from the C-terminus of the inhibitor are unstructured.
Cross-references: PDB:1DPJ
PDB:1DP5
Protein: DP00179 (UniProt P01094)
Region: residues 2	to 32
Annotation: protein binding (Molecular function)
Evidence: X-ray crystallography-based structural model with missing residue coordinates used in manual assertion
Supporting statements:
In the resulting structures (Fig. 1 ), residues 2–32 of IA3 become ordered and form a near-perfect amphipathic α-helix (Fig. 2). In contrast, the remaining 36 residues from the C-terminus of the inhibitor are unstructured.
Cross-references: PDB:1DPJ
PDB:1DP5
Protein: DP00179 (UniProt P01094)
Region: residues 1	to 68
Annotation: disorder (Structural state)
Evidence: far-UV circular dichroism evidence used in manual assertion
Supporting statements:
Although Figure 2B shows a slight inflection around 222 nm that may represent a very small amount of α-helix, the CD spectrum of IA3 is characteristic of an unfolded protein with a strong minimum peak at ∼200 nm for all of the above temperatures.
Protein: DP00179 (UniProt P01094)
Region: residues 1	to 68
Annotation: disorder (Structural state)
Evidence: nuclear magnetic resonance spectroscopy evidence used in manual assertion
Supporting statements:
The 15N HSQC NMR spectrum of free IA3 in solution is characteristic of an unfolded protein (Figure 4A).
Therefore, we measured heteronuclear 1H−15N NOEs ( 18) on [15N]IA3 (Figure 5). As expected for an unfolded protein, all of the NOEs in IA3 are very small (<0.3) or negative, clearly indicating that the protein is disordered in solution.
Cross-references: BMRB:6078
Protein: DP00179 (UniProt P01094)
Region: residues 1	to 68
Annotation: protein binding (Molecular function)
Evidence: nuclear magnetic resonance spectroscopy evidence used in manual assertion
Supporting statements:
The 15N−1H HSQC spectrum of the IA3−YprA complex (Figure 4B) is largely different from the spectrum of free IA3 (Figure 4A).
YprA corresponds to the yeast aspartic protease A (yscA, NC_001148.4), absent in UniProt resource.