LiteFold/DisProt huggingface dataset:
Protein: DP00675 (UniProt P19711)
Region: residues 170	to 260
Annotation: disorder (Structural state)
Evidence: far-UV circular dichroism evidence used in manual assertion
Supporting statements:
BVDV core protein, in agreement with the disorder prediction (Figure 1), was found to be completely unstructured at 20°C, as evidenced by the pronounced minimum in the CD spectrum observed at ∼200 nm (Figure 6D).
BVDV core protein was found to completely lack a well-defined structure, as evidenced by its CD spectrum at 20°C and 95°C (Figure 6D).
Protein: DP00675 (UniProt P19711)
Region: residues 170	to 260
Annotation: DNA binding (Molecular function)
Evidence: electrophoretic mobility shift assay evidence used in manual assertion
Supporting statements:
All four proteins bound both to RNA and DNA without a strict sequence specificity, and they caused complete retention of the nucleic acids at the top of the gel (indicative of the formation of large nucleoprotein complexes) at a protein-to-nucleotide molar ratio of ∼1:20 (data not shown).
Protein: DP00675 (UniProt P19711)
Region: residues 170	to 260
Annotation: RNA binding (Molecular function)
Evidence: electrophoretic mobility shift assay evidence used in manual assertion
Supporting statements:
All four proteins bound both to RNA and DNA without a strict sequence specificity, and they caused complete retention of the nucleic acids at the top of the gel (indicative of the formation of large nucleoprotein complexes) at a protein-to-nucleotide molar ratio of ∼1:20 (data not shown).
Protein: DP00675 (UniProt P19711)
Region: residues 170	to 260
Annotation: disorder (Structural state)
Evidence: temperature-induced protein unfolding evidence used in manual assertion
Supporting statements:
Surprisingly, both WNV core, a protein with a well-defined 3D structure (40), and BVDV core, which was predicted to be completely unstructured (Figure 1), retained their full activity upon boiling (compare lanes 36–38 and 39–41, and 43–45 and 46–48 in Figure 4B).
Protein: DP00675 (UniProt P19711)
Region: residues 170	to 260
Annotation: disorder (Structural state)
Evidence: enzymatic activity assay evidence used in manual assertion
Supporting statements:
As expected, all core proteins induced a considerable increase in the cleavage rates, with hepacivirus core proteins demonstrating a higher activity compared to WNV and BVDV cores (Figure 4C). 
Despite a lack of significant similarity with hepacivirus cores in amino acid sequence or domain organization (Figure 1), core proteins of the flavivirus WNV and the pestivirus BVDV both demonstrated potent RNA chaperone activities in vitro (Figures 2 and 3).
Protein: DP00675 (UniProt P19711)
Region: residues 169	to 270
Annotation: RNA binding (Molecular function)
Evidence: radioligand binding assay evidence used in manual assertion
Supporting statements:
After binding of protein and labeled RNA in solution, reaction mixtures were applied to nitrocellulose filters under vacuum and washed, and RNA retained on the filter was quantified. C87 and C90 were found to bind RNA equivalently and with approximately 1 μM affinity; a slight preference was seen for G and U homo-oligomers ​(Fig. 3 and Table 1).
Protein: DP00675 (UniProt P19711)
Region: residues 169	to 270
Annotation: RNA binding (Molecular function)
Evidence: luciferase reporter gene assay evidence used in manual assertion
Supporting statements:
At 24 h postelectroporation, cell culture supernatants were harvested, clarified by filtration, and used to infect naïve BHK 21 cells. The infected cells were incubated for 4 h before assay for luciferase activity. Sindbis/luc(CΔ2-96) was severely impaired in infectious virus production, while the less drastic deletions, Sindbis/luc(CΔ50-96) and Sindbis/luc(CΔ72-96), showed only moderate reductions (Fig. ​(Fig.8C).8C). In each case, the inclusion of BVDV sequences led to increased signal compared to the deletion mutants, suggesting that the BVDV residues positively influenced infectious virion production.
Taken together, these results suggest that the nonspecific RNA-binding properties of BVDV core observed in vitro are responsible for its ability to functionally replace a heterologous RNA condensation sequence in vivo, and they indicate that the BVDV core protein likely functions by a similar mechanism in packaging its own genomic RNA.
Protein: DP00675 (UniProt P19711)
Region: residues 169	to 270
Annotation: viral genome packaging (Biological process)
Evidence: luciferase reporter gene assay evidence used in manual assertion
Supporting statements:
At 24 h postelectroporation, cell culture supernatants were harvested, clarified by filtration, and used to infect naïve BHK 21 cells. The infected cells were incubated for 4 h before assay for luciferase activity. Sindbis/luc(CΔ2-96) was severely impaired in infectious virus production, while the less drastic deletions, Sindbis/luc(CΔ50-96) and Sindbis/luc(CΔ72-96), showed only moderate reductions (Fig. ​(Fig.8C).8C). In each case, the inclusion of BVDV sequences led to increased signal compared to the deletion mutants, suggesting that the BVDV residues positively influenced infectious virion production.
Taken together, these results suggest that the nonspecific RNA-binding properties of BVDV core observed in vitro are responsible for its ability to functionally replace a heterologous RNA condensation sequence in vivo, and they indicate that the BVDV core protein likely functions by a similar mechanism in packaging its own genomic RNA.
Protein: DP00683 (UniProt Q99801)
Region: residues 1	to 113
Annotation: disorder (Structural state)
Evidence: far-UV circular dichroism evidence used in manual assertion
Supporting statements:
The CD spectra of the NKX3.1 (1–184), (75–184), (97–184), and (114–184) constructs are consistent with the homeodomain containing significant α-helical content and the N-terminal region consisting of flexible, disordered structure (Figure 1D), as already shown in previous NMR studies (6, 7).
Protein: DP00685 (UniProt Q98157)
Region: residues 21	to 34
Annotation: disorder (Structural state)
Evidence: nuclear magnetic resonance spectroscopy evidence used in manual assertion
Supporting statements:
Residues 1−13 in the NMR structure are highly disordered; the subsequent residues (14−19) adopt a different conformation as compared to the crystal structure of vMIP-II.
Since the peptide used in this publication corresponds to residues 21−94 of vMIP-II,  the region the authors are describing is 21-34.
Cross-references: PDB:1CM9
Protein: DP00685 (UniProt Q98157)
Region: residues 21	to 32
Annotation: protein binding (Molecular function)
Evidence: competitive binding evidence used in manual assertion
Supporting statements:
However, the binding of vMIP-II(1–11)dimer is only 180-fold less than SDF-1 and is the most tightly binding small peptide that we have observed to date.
Two N-terminal peptides, vMIP-II(1–10) and vMIP-II(1–11)dimer (dimerised through Cys11) were synthesised. Both peptides are shown to bind the CXC chemokine receptor 4 (CXCR4). vMIP-II(1–10) was 1400-fold less potent than the native protein whilst the vMIP-II(1–11)dimer was only 180-fold less potent.
Since the peptide used in this publication corresponds to residues 21−94 of vMIP-II, the region the authors refered as 1-11 are the residues 21-32 of the Uniprot.
Protein: DP00685 (UniProt Q98157)
Region: residues 21	to 34
Annotation: disorder (Structural state)
Evidence: nuclear magnetic resonance spectroscopy evidence used in manual assertion
Supporting statements:
No long-range or medium-range NOEs were observed for the N-terminal residues 1–13 or the last two C-terminal residues.
The N-terminus (residues 1–13) is disordered up to the first cysteine (Cys14).
Since the peptide used in this publication corresponds to residues 21−94 of vMIP-II, the region the authors are describing as disordered is 21-34.
Cross-references: PDB:1HHV
Protein: DP00685 (UniProt Q98157)
Region: residues 21	to 34
Annotation: disorder (Structural state)
Evidence: nuclear magnetic resonance spectroscopy evidence used in manual assertion
Supporting statements:
The structure of vMIP-II, shown in Figures 2A and 2B, consists of a disordered N-terminal region having a substantial number of sequential NOE contacts beginning at residue Trp8, but having no long-range NOE contacts until Cys14, with these due largely to the participation of both Cys14 and Cys15 in disulfide bonds (to Cys38 and Cys54, respectively)
Since the peptide used in this publication corresponds to residues 21−94 of vMIP-II, the region the authors are describing as disordered is 21-34.
Cross-references: PDB:1VMP
Protein: DP00686 (UniProt Q9IH62)
Region: residues 579	to 590
Annotation: disorder (Structural state)
Evidence: X-ray crystallography-based structural model with high relative B-factor values used in manual assertion
Supporting statements:
In the unbound form of NiV-G, the 579-590 loop is relatively flexible in both molecules of the crystallographic asymmetric unit, and 2Fo-Fc electron density for the side chains is poor.
In addition, the 579-590 and 236-245 loops exhibit high B-factor values in the apo form (Fig. 1B and C).
Cross-references: PDB:2VWD
Protein: DP00686 (UniProt Q9IH62)
Region: residues 236	to 245
Annotation: disorder (Structural state)
Evidence: X-ray crystallography-based structural model with high relative B-factor values used in manual assertion
Supporting statements:
In addition, the 236-245 loop is rather disordered in the unbound structure." Results "In addition, the 579-590 and 236-245 loops exhibit high B-factor values in the apo form (Fig. 1B and C).
Cross-references: PDB:2VWD
Protein: DP00686 (UniProt Q9IH62)
Region: residues 579	to 590
Annotation: protein binding (Molecular function)
Evidence: x-ray crystallography evidence used in manual assertion
Supporting statements:
Structural differences are particularly pronounced in the 579-590 loop, a major component of the ephrin binding surface.
Both molecules in the crystallographic asymmetric unit of apo-NiV-G show structural differences from the EFNB2-bound form in the region of the 579-590 loop.
Protein: DP00689 (UniProt P30185)
Region: residues 1	to 186
Annotation: disorder (Structural state)
Evidence: far-UV circular dichroism evidence used in manual assertion
Supporting statements:
In physiological buffer at 4C, 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: DP00689 (UniProt P30185)
Region: residues 1	to 186
Annotation: disorder (Structural state)
Evidence: sodium dodecyl sulfate polyacrylamide gel electrophoresis evidence used in manual assertion
Supporting statements:
We conclude that the dehydrins analyzed in this study have an extended structure.
In Table 3 is possible to appreciate a difference between the calculated Molecular Weight (18,333 Da) and the one measured from the SDS-PAGE (25 KDa).
Protein: DP00689 (UniProt P30185)
Region: residues 1	to 186
Annotation: disorder (Structural state)
Evidence: chromatography evidence used in manual assertion
Supporting statements:
The elution volume (Ve) values under denaturing conditions were slightly lower as compared to the Ve values from native conditions (Table 3), indicating that dehydrins are not globular proteins and have an extended fibrous structure, which thereby gives rise to the anomalous elution behavior in gel filtration.
We conclude that the dehydrins analyzed in this study have an extended structure.
Protein: DP00689 (UniProt P30185)
Region: residues 1	to 186
Annotation: metal ion binding (Molecular function)
Evidence: affinity chromatography evidence used in manual assertion
Supporting statements:
We show that four A. thaliana dehydrins bind strongly to a Cu(II)- or Ni(II)-charged IDA–Sepharose column.
Protein: DP00696 (UniProt Q9Y258)
Region: residues 84	to 94
Annotation: disorder (Structural state)
Evidence: nuclear magnetic resonance spectroscopy evidence used in manual assertion
Supporting statements:
The N- and C-termini are highly flexible, as observed for all other chemokines and in line with the high rmsd values in this region of the structure.
Cross-references: PDB:1G2T
Protein: DP00697 (UniProt Q9IK92)
Region: residues 400	to 532
Annotation: disorder (Structural state)
Evidence: cleavage assay evidence used in manual assertion
Supporting statements:
In order to assess the extent of protease sensitivity, we submitted Henipavirus PNT and NTAIL to digestion by thermolysin. As shown in Fig. 4, all the proteins are readily degraded by thermolysin after one hour incubation, a behavior that is consistent with the lack of a packed core and with an overall solvent accessibility of Henipavirus PNT and NTAIL.
Protein: DP00697 (UniProt Q9IK92)
Region: residues 400	to 532
Annotation: disorder (Structural state)
Evidence: sodium dodecyl sulfate polyacrylamide gel electrophoresis evidence used in manual assertion
Supporting statements:
This abnormal behavior is therefore likely to be ascribed to a rather high content of acidic residues, as already been observed in the case of the intrinsically disordered MeV PNT [18] and NTAIL domains [6], [19], and, more generally, in other IDPs [46].
Protein: DP00697 (UniProt Q9IK92)
Region: residues 400	to 532
Annotation: disorder (Structural state)
Evidence: cleavage assay evidence used in manual assertion
Supporting statements:
On the other hand, no fragment corresponding to the remaining NTAIL domain was detected, indicating that it is hypersensitive to proteolysis and entirely degraded in the context of the entire N proteins either.
The results presented here show that both N proteins undergo proteolytic cleavage within their NTAIL domains, thus supporting the disordered nature of these domains not only in isolation but also in the context of the entire N proteins.
Protein: DP00697 (UniProt Q9IK92)
Region: residues 400	to 532
Annotation: molecular adaptor activity (Molecular function)
Evidence: nuclear magnetic resonance spectroscopy evidence used in manual assertion
Supporting statements:
In addition, both NMR and far-UV CD studies revealed a gain of α-helicity within NTAIL upon binding to PXD, and ITC studies showed that the interaction does not rely on electrostatic contacts, as the KD was not affected by NaCl concentrations as high as 1 m
The NMR titration experiments of Henipavirus NTAIL with increasing amounts of PXD confirmed that a complex is formed between the two partners.
Protein: DP00697 (UniProt Q9IK92)
Region: residues 400	to 532
Annotation: protein binding (Molecular function)
Evidence: nuclear magnetic resonance spectroscopy evidence used in manual assertion
Supporting statements:
In addition, both NMR and far-UV CD studies revealed a gain of α-helicity within NTAIL upon binding to PXD, and ITC studies showed that the interaction does not rely on electrostatic contacts, as the KD was not affected by NaCl concentrations as high as 1 m.
The NMR titration experiments of Henipavirus NTAIL with increasing amounts of PXD confirmed that a complex is formed between the two partners. 
These observations point toward the intermediate exchange regime often observed for IDPs undergoing folding-upon-binding events (for examples see Refs. 39, 54, 83, and 118).
Protein: DP00697 (UniProt Q9IK92)
Region: residues 400	to 532
Annotation: molecular adaptor activity (Molecular function)
Evidence: site-directed spin-labelling electron paramagnetic resonance evidence used in manual assertion
Supporting statements:
For all the spin labels grafted within
Box3, the number of possible rotamers built by MMM
on the structural model of the NiV NTAIL–PXD complex
(i.e. the number of possible rotamers that could be
accommodated in the available conformational space) is
comparable to that obtained with HeV (Figure 6(B)).
Protein: DP00697 (UniProt Q9IK92)
Region: residues 400	to 532
Annotation: protein binding (Molecular function)
Evidence: site-directed spin-labelling electron paramagnetic resonance evidence used in manual assertion
Supporting statements:
For all the spin labels grafted within
Box3, the number of possible rotamers built by MMM
on the structural model of the NiV NTAIL–PXD complex
(i.e. the number of possible rotamers that could be
accommodated in the available conformational space) is
comparable to that obtained with HeV (Figure 6(B)).
Protein: DP00697 (UniProt Q9IK92)
Region: residues 400	to 532
Annotation: disorder (Structural state)
Evidence: sodium dodecyl sulfate polyacrylamide gel electrophoresis evidence used in manual assertion
Supporting statements:
Hence, this anomalous electrophoretic mobility is rather due to a rather high content of acidic residues, as already observed for other intrinsically disordered domains (for examples see Ref. 6, 45, and 85) and, more generally, in other IDPs (86).
Protein: DP00697 (UniProt Q9IK92)
Region: residues 400	to 532
Annotation: pre-molten globule (Structural state)
Evidence: far-UV circular dichroism evidence used in manual assertion
Supporting statements:
Conversely, the CD spectra of both NTAIL proteins are typical of predominantly unfolded proteins, as seen by their large negative ellipticity at 198 nm and low ellipticity at 190 nm (Fig. 5, A and B, black lines). Nevertheless, and as already reported (14), the observed ellipticity values at 200 and 222 nm of both Henipavirus NTAIL proteins are consistent with the existence of some residual secondary structure typical of IDPs adopting a PMG conformation (21).
Protein: DP00697 (UniProt Q9IK92)
Region: residues 400	to 532
Annotation: pre-molten globule (Structural state)
Evidence: dynamic light scattering assay evidence used in manual assertion
Supporting statements:
The obtained RS values (37±2 Å for both NTAIL proteins, and either 55±2 Å or 57±2 Å for NiV and HeV PNT, respectively) highlight a significant increase in the hydrodynamic radius in the presence of urea (see Table 1). These results argue for the presence of residual intramolecular interactions within Henipavirus PNT and NTAIL proteins under native conditions, as expected for proteins adopting a PMG conformation.
Protein: DP00697 (UniProt Q9IK92)
Region: residues 400	to 532
Annotation: pre-molten globule to order (Structural transition)
Evidence: far-UV circular dichroism evidence used in manual assertion
Supporting statements:
The experimentally observed spectra of the mixtures support a random-coil to α-helix transition, as judged by the much more pronounced minima at 208 and 222 nm and by the higher ellipticity at 190 nm of the experimentally observed spectra compared with the corresponding theoretical average curves (see Fig. 5, A and B).
This analysis indicated a significant increase in the α-helical content of the mixtures as compared with average spectra, with this gain in α-helicity being paralleled by a decrease in the content of disordered structure (see Fig. 5, C and D).
Using the same approach, we showed that both NiV and HeV NTAIL undergo α-helical induced folding upon binding to the corresponding P X domain
Protein: DP00697 (UniProt Q9IK92)
Region: residues 400	to 532
Annotation: protein binding (Molecular function)
Evidence: isothermal titration calorimetry evidence used in manual assertion
Supporting statements:
The estimates for the model parameters (see Table 1) confirm a 1:1 stoichiometry and reveal that the binding reaction is both enthalpy- and entropy-driven, with the exception only of the NiV NTAIL-PXD couple for which a small unfavorable entropic contribution was found.
Similar experiments carried out in the presence of 1 m NaCl (data not shown) yielded similar results (see Table 1), suggesting that the NTAIL-PXD interaction relies mainly on hydrophobic interactions.
Protein: DP00697 (UniProt Q9IK92)
Region: residues 400	to 532
Annotation: protein binding (Molecular function)
Evidence: chromatography evidence used in manual assertion
Supporting statements:
In the case of the study of the NiV NTAIL-PXD complex, upon addition of stoichiometric amounts of PXD, the NTAIL peak shifted toward a lower elution volume (from 8.1 to 7.75 ml), indicating the formation of an NTAIL-PXD complex, as also judged from the estimated mass (25,610 ± 80 Da), a value consistent with the binding of one PXD molecule/NTAIL (expected mass ∼ 22 kDa) (data not shown).
Protein: DP00697 (UniProt Q9IK92)
Region: residues 400	to 532
Annotation: protein binding (Molecular function)
Evidence: surface plasmon resonance evidence used in manual assertion
Supporting statements:
The binding reaction conformed to a 1:1 ligand-substrate (Langmuir) binding model, exhibiting an excellent fit (i.e. χ2 < 1 and residuals within the range of ±2) following global kinetic analysis of sensorgrams as well as when plotting mean equilibrium responses of the data in the steady state analysis.
Protein: DP00697 (UniProt Q9IK92)
Region: residues 400	to 532
Annotation: disorder to pre-molten globule (Structural transition)
Evidence: heteronuclear single quantum coherence spectroscopy evidence used in manual assertion
Supporting statements:
Interestingly, in the case of the NiV NTAIL titration, but not of the HeV one, among the correlation peaks that were displaced by PXD, eight underwent an upfield shift (see Fig. 6A) consistent with a random coil to α-helix transition.
Protein: DP00697 (UniProt Q9IK92)
Region: residues 400	to 532
Annotation: pre-molten globule (Structural state)
Evidence: chromatography evidence used in manual assertion
Supporting statements:
These studies suggest that Henipavirus PNT and NTAIL proteins either adopt a PMG conformation or are folded trimers.
Protein: DP00697 (UniProt Q9IK92)
Region: residues 400	to 532
Annotation: pre-molten globule (Structural state)
Evidence: proton-based nuclear magnetic resonance evidence used in manual assertion
Supporting statements:
The very small spread of the resonance frequencies for amide protons (between 7.8 ppm and 8.7 ppm, see frames in Fig. 6) together with the scarcity of NOEs in the amide-amide region are typical of proteins without any stable secondary structure (for examples see [6], [18]), thereby supporting lack of a packed core within Henipavirus PNT and NTAIL domains.
Protein: DP00697 (UniProt Q9IK92)
Region: residues 400	to 532
Annotation: pre-molten globule (Structural state)
Evidence: far-UV circular dichroism evidence used in manual assertion
Supporting statements:
In further support of the absence of an ordered structure, the far-UV CD spectra of Henipavirus PNT and NTAIL at neutral pH are typical of unstructured proteins, as seen from their large negative ellipticity at 198 nm and low ellipticity at 190 nm (Fig. 7A). However, the observed ellipticity values at 200 and 222 nm of Henipavirus NTAIL and of NiV PNT are consistent with the existence of some residual secondary structure, as observed in IDPs adopting a PMG conformation (Fig. 7B).
Protein: DP00697 (UniProt Q9IK92)
Region: residues 400	to 532
Annotation: disorder (Structural state)
Evidence: sodium dodecyl sulfate polyacrylamide gel electrophoresis evidence used in manual assertion
Supporting statements:
This anomalous electrophoretic mobility is
frequently observed in IDPs and is to be ascribed to a
relatively high content in acidic residues (Tompa, 2002),
and/or to a high degree of protein extension in solution
(Blocquel et al., 2012).
Protein: DP00697 (UniProt Q9IK92)
Region: residues 400	to 532
Annotation: pre-molten globule (Structural state)
Evidence: chromatography evidence used in manual assertion
Supporting statements:
The Stokes radius value of the monomeric form of
all Henipavirus NTAIL variants (28 ± 2 Å), as inferred
from the apparent molecular mass observed in SEC, is
the same as that observed for both parental HeV and
NiV NTAIL proteins (data not shown). This value is consistent
with the value expected for IDPs adopting a premolten
globule state (Uversky, 2002b).