LiteFold/DisProt huggingface dataset:
Protein: DP04423 (UniProt P0DXN6)
Region: residues 400	to 525
Annotation: pre-molten globule (Structural state)
Evidence: far-UV circular dichroism evidence used in manual assertion
Supporting statements:
The far-UV CD spectrum of NTAIL at neutral pH is typical of an unstructured protein, as seen from its large negative ellipticity at 198 nm and very low ellipticity at 185 nm (Fig. 2B). However, the observed ellipticity values at 200 and 222 nm (−9700 and −2400 degrees cm2 dmol−1, respectively) (Fig. 2B) are consistent with the existence of some residual secondary structure, typical of the premolten globule state (39).
Protein: DP04423 (UniProt P0DXN6)
Region: residues 400	to 525
Annotation: disorder (Structural state)
Evidence: cleavage assay evidence used in manual assertion
Supporting statements:
NCORE was obtained by limited proteolysis of purified N as described in Ref. 4, followed by gel filtration (data not shown).
Measles virus (MeV) nucleoprotein NCORE region is comprised within 1–399 residues. Its obtention trough this methodology  proves that 400-525 region is susceptible to proteolysis, hallmark of intrinsic disorder.
Protein: DP04423 (UniProt P0DXN6)
Region: residues 400	to 525
Annotation: protein binding (Molecular function)
Evidence: affinity chromatography evidence used in manual assertion
Supporting statements:
When both lysates were mixed, the IMAC resin selectively pulled down NTAIL together with an additional protein that has the same electrophoretic mobility of P (Fig. 5B,lane Nt + P). The identity of this protein band was confirmed by Western blotting using an anti-P mAb (data not shown), thus proving that the NTAIL domain on its own is able to bind its physiological partner in bacterial lysates.
Protein: DP04423 (UniProt P0DXN6)
Region: residues 400	to 525
Annotation: protein binding (Molecular function)
Evidence: far-UV circular dichroism evidence used in manual assertion
Supporting statements:
After mixing NTAIL with different molar excesses of PCT, the observed CD spectra of the mixtures differ from the corresponding theoretical average curves calculated from the individual spectra. Since the theoretical average curves correspond to the spectra that would be expected if no structural variations occur, deviations from these curves point out structural transitions.
Therefore, these results indicate that NTAIL undergoes an induced folding upon binding to PCT.
Protein: DP04423 (UniProt P0DXN6)
Region: residues 400	to 525
Annotation: disorder to order (Structural transition)
Evidence: far-UV circular dichroism evidence used in manual assertion
Supporting statements:
After mixing NTAIL with different molar excesses of PCT, the observed CD spectra of the mixtures differ from the corresponding theoretical average curves calculated from the individual spectra. Since the theoretical average curves correspond to the spectra that would be expected if no structural variations occur, deviations from these curves point out structural transitions.
In the presence of molar excesses of PCT, a random coil to α-helix transition can be observed, as indicated 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 (Fig. 6A).
Therefore, these results indicate that NTAIL undergoes an induced folding upon binding to PCT.
Protein: DP04423 (UniProt P0DXN6)
Region: residues 400	to 525
Annotation: pre-molten globule (Structural state)
Evidence: small-angle X-ray scattering evidence used in manual assertion
Supporting statements:
Therefore, the observedRg indicates that NTAIL is not globular. However, the protein is more compact than a random coil, suggesting that it possesses some residual structure.
The Kratky plot of NTAIL displays a bump atq ≈ 0.08 Å−1 followed by a plateau forq > 0.15 Å−1 (see Fig. 3B). The absence of a maximum clearly indicates that NTAIL is not globular and does not possess a tightly packed core. However, the observed bump may be indicative of some residual structure.
In the case of NTAIL, the RS andRg values obtained by DLS and SAXS, respectively, lead to a ratio of 1.1, which is consistent with a premolten globule.
Protein: DP04423 (UniProt P0DXN6)
Region: residues 400	to 525
Annotation: molecular adaptor activity (Molecular function)
Evidence: far-UV circular dichroism evidence used in manual assertion
Supporting statements:
After mixing NTAIL with different molar excesses of PCT, the observed CD spectra of the mixtures differ from the corresponding theoretical average curves calculated from the individual spectra. Since the theoretical average curves correspond to the spectra that would be expected if no structural variations occur, deviations from these curves point out structural transitions." Results "Therefore, these results indicate that NTAIL undergoes an induced folding upon binding to PCT
Protein: DP04423 (UniProt P0DXN6)
Region: residues 401	to 525
Annotation: molecular adaptor activity (Molecular function)
Evidence: far-UV circular dichroism evidence used in manual assertion
Supporting statements:
After mixing NTAILHNFC with different molar excesses of XD, the observed CD spectra differed from the corresponding theoretical average curves calculated from the individual spectra.
Protein: DP04423 (UniProt P0DXN6)
Region: residues 489	to 525
Annotation: molecular adaptor activity (Molecular function)
Evidence: surface plasmon resonance evidence used in manual assertion
Supporting statements:
In contrast, removal of either Box3 alone or Box2 plus Box3 results in a strong decrease (three orders of magnitude) in the equilibrium dissociation constant, where NTAILΔ3 and NTAILΔ2,3 display similar binding affinities (see Table 1).
Measles virus (MeV) nucleoprotein Box 2 and Box 3 region is comprised within the residues 488-525.
Protein: DP04423 (UniProt P0DXN6)
Region: residues 517	to 525
Annotation: molecular adaptor activity (Molecular function)
Evidence: surface plasmon resonance evidence used in manual assertion
Supporting statements:
In contrast, removal of either Box3 alone or Box2 plus Box3 results in a strong decrease (three orders of magnitude) in the equilibrium dissociation constant, where NTAILΔ3 and NTAILΔ2,3 display similar binding affinities (see Table 1). The strong decrease in the affinity resulting from removal of Box3 clearly indicates that Box2 is not the sole region involved in binding to XD, and attests that Box3 also plays a role in the interaction with XD, as already suggested by SAXS studies.
Measles virus (MeV) nucleoprotein Box 3 region is comprised within the residues 517-525.
Protein: DP04423 (UniProt P0DXN6)
Region: residues 401	to 525
Annotation: molecular adaptor activity (Molecular function)
Evidence: small-angle X-ray scattering evidence used in manual assertion
Supporting statements:
The molecular mass (MM) calculated from the forward scattering intensity I(0) is 23.5 ± 2 kDa, in agreement with the value expected for a 1:1 stoichiometric complex (21.3 kDa), thus suggesting that the complex did form in solution.
The high value of Rg indicated that the overall structure of the NTAILHN–XD complex is not compact.
Protein: DP04423 (UniProt P0DXN6)
Region: residues 401	to 525
Annotation: disorder (Structural state)
Evidence: mass spectrometry evidence used in manual assertion
Supporting statements:
The spectrum shows a very broad, bimodal charge-state distribution (CSD), indicating structural heterogeneity consistent with the intrinsically disordered nature of this protein.
The rest of the spectrum is characterized by a broad peak envelope that spans the region between the 10+ and the 24+ ions, with main charge state 16+. This component corresponds to disordered conformations, characterized by low compactness.
Protein: DP04423 (UniProt P0DXN6)
Region: residues 401	to 525
Annotation: disorder to order (Structural transition)
Evidence: mass spectrometry evidence used in manual assertion
Supporting statements:
 In this case, two slightly different conformations are found to populate the compact state of the NTAIL–PXD complex (charge states 8+ to 10+). Average CCS of 1326 and 1422 Å2 can be derived for the two main peaks detectable for the 8+ charge state. This result suggests that the compact state of the complex is characterized by further structural heterogeneity. Thus, although its overall ionization suggests a collapsed structure, its arrival-time distribution reveals distinct peaks rather than the single peak typically observed for normally folded proteins.
Protein: DP04423 (UniProt P0DXN6)
Region: residues 401	to 525
Annotation: protein binding (Molecular function)
Evidence: mass spectrometry evidence used in manual assertion
Supporting statements:
The spectra are dominated by the peaks of the free proteins, but signals specific to the NTAIL–PXD complex become evident at the higher protein concentration. The measured mass of the complex (21,187.4 ± 0.61 Da) corresponds closely to the sum of the theoretical values expected for NTAIL with the initial methionine and PXD without the initial methionine (21,187.46 Da), indicating a 1:1 stoichiometry.
Protein: DP04423 (UniProt P0DXN6)
Region: residues 401	to 525
Annotation: protein binding (Molecular function)
Evidence: nuclear magnetic resonance spectroscopy evidence used in manual assertion
Supporting statements:
Intermediate exchange between NTAIL and XD, especially at the binding interface, caused significant peak broadening thus reducing the number of resonance assignments possible for the NTAIL–XD complex.
Protein: DP04423 (UniProt P0DXN6)
Region: residues 475	to 525
Annotation: protein binding (Molecular function)
Evidence: heteronuclear single quantum coherence spectroscopy evidence used in manual assertion
Supporting statements:
At low XD concentrations (0.037, 0.075, and 0.150 mM), most resonances in the HSQC experience no chemical shift changes (residues 401–474), some resonances undergo fast exchange and experience chemical shift changes with minimal line broadening (residues 475–482 and residues 507–525), and some resonances undergo intermediate exchange and experience significant line broadening (residues 483–506). 
For all the affected resonances (residues 475–525), small chemical shift differences were observed when increasing the XD concentration from 0.3 to 0.6 mM, suggesting that binding is saturated.
Protein: DP04423 (UniProt P0DXN6)
Region: residues 485	to 505
Annotation: protein binding (Molecular function)
Evidence: heteronuclear single quantum coherence spectroscopy evidence used in manual assertion
Supporting statements:
The sole intermolecular hydrogen bonding interaction observed in a chimeric crystal structure of N486–505:PXD involves S491 of NTAIL interacting with K489 and D493 of PXD (7). Mutation of N (S491) has been shown to abrogate the NTAIL:PXD interaction—this is also the case under our experimental conditions (Fig. 3D)—and to significantly decrease viral transcription in vivo (11). The critical nature of this interaction for LLPS was demonstrated via the S491L mutation, which resulted in suppression of phase separation.
Protein: DP04423 (UniProt P0DXN6)
Region: residues 485	to 505
Annotation: molecular condensate scaffold activity (Molecular function)
Evidence: heteronuclear single quantum coherence spectroscopy evidence used in manual assertion
Supporting statements:
The sole intermolecular hydrogen bonding interaction observed in a chimeric crystal structure of N486–505:PXD involves S491 of NTAIL interacting with K489 and D493 of PXD (7). Mutation of N (S491) has been shown to abrogate the NTAIL:PXD interaction—this is also the case under our experimental conditions (Fig. 3D)—and to significantly decrease viral transcription in vivo (11). The critical nature of this interaction for LLPS was demonstrated via the S491L mutation, which resulted in suppression of phase separation.
Protein: DP04423 (UniProt P0DXN6)
Region: residues 400	to 525
Annotation: disorder (Structural state)
Evidence: gel-filtration evidence used in manual assertion
Supporting statements:
Size-exclusion chromatography was employed to estimate the Rh values of the three sets of model IDPs (Table 2). Experimental Rh values of wt NTAIL and wt PNT4 (2.71 ± 0.09 and 2.34 ± 0.11 nm, respectively) are close to the theoretical ones (Table 1) and similar to the previously determined ones [9].
Experimentally determined Rh matches the theoretical Rh for IDPs [Marsh & Forman-Kay, 2010].
Rt (nm) = 2.64
Protein: DP04423 (UniProt P0DXN6)
Region: residues 400	to 525
Annotation: disorder (Structural state)
Evidence: electrospray ionization fourier transform ion cyclotron resonance mass spectrometry evidence used in manual assertion
Supporting statements:
Native MS was employed to assess the conformational properties of the three sets of IDPs. In this approach, the CSDs resulting from the nanoESI process reflect the overall compactness and relative amounts of the main conformers in the original solution [17,18,22]. Native-MS spectra obtained under non-denaturing conditions for the three variants of NTAIL (Figure 4a), NFM, and PNT4 (Figure S3) display multimodal CSDs, highlighting the heterogeneous conformational ensemble typical of IDPs.
Protein: DP04423 (UniProt P0DXN6)
Region: residues 400	to 525
Annotation: disorder (Structural state)
Evidence: far-UV circular dichroism evidence used in manual assertion
Supporting statements:
Figure S2. Far-UV CD spectra of model IDPs. CD spectra of NTAIL (a), NFM (b), and PNT4 (c) variants.
Typical random coil-like far-UV CD spectrum is displayed for NTAIL.
Protein: DP04425 (UniProt A0A5P8YHT8)
Region: residues 21	to 112
Annotation: disorder (Structural state)
Evidence: far-UV circular dichroism evidence used in manual assertion
Supporting statements:
Far-UV CD of apoD1 showed a large negative ellipticity peak at 200 nm, suggesting that the protein is intrinsically unstructured (44), which disappeared on calcium addition and emerged as a positive peak (Fig. 7a).
Protein: DP04425 (UniProt A0A5P8YHT8)
Region: residues 21	to 112
Annotation: ion binding (Molecular function)
Evidence: far-UV circular dichroism evidence used in manual assertion
Supporting statements:
Calcium binding to D1 increased β-sheet content by 2-fold to 42.4%, largely at the expense of the unordered fraction, which reduced to 29.66%.
Protein: DP04425 (UniProt A0A5P8YHT8)
Region: residues 21	to 112
Annotation: disorder to order (Structural transition)
Evidence: far-UV circular dichroism evidence used in manual assertion
Supporting statements:
Calcium binding to D1 increased β-sheet content by 2-fold to 42.4%, largely at the expense of the unordered fraction, which reduced to 29.66%.
Protein: DP04425 (UniProt A0A5P8YHT8)
Region: residues 21	to 112
Annotation: disorder (Structural state)
Evidence: near-UV circular dichroism evidence used in manual assertion
Supporting statements:
Near-UV CD of apoD1 showed a very weak signal, confirming that the protein was in an unstructured state.
Protein: DP04425 (UniProt A0A5P8YHT8)
Region: residues 21	to 112
Annotation: ion binding (Molecular function)
Evidence: near-UV circular dichroism evidence used in manual assertion
Supporting statements:
Upon the addition of calcium, two strong bands emerged in the spectra of the holoprotein, one at ∼290 nm for the 1Lb band of Trp and a broad peak ∼255–270 nm, with peaks at 262 and 268 nm characteristic of Phe (Fig. 8).
Protein: DP04425 (UniProt A0A5P8YHT8)
Region: residues 21	to 112
Annotation: disorder to order (Structural transition)
Evidence: near-UV circular dichroism evidence used in manual assertion
Supporting statements:
Upon the addition of calcium, two strong bands emerged in the spectra of the holoprotein, one at ∼290 nm for the 1Lb band of Trp and a broad peak ∼255–270 nm, with peaks at 262 and 268 nm characteristic of Phe (Fig. 8).
Protein: DP04425 (UniProt A0A5P8YHT8)
Region: residues 110	to 215
Annotation: disorder (Structural state)
Evidence: far-UV circular dichroism evidence used in manual assertion
Supporting statements:
Far-UV CD spectra of domain D2 showed a negative trough at ∼200 nm with a negative peak at 220 nm (Fig. 7b). The secondary structure analysis of the spectra showed that the protein had 31.83% β-sheet, 35.2% unordered, and 23% turns, with 9.6% helix (Table II).
Protein: DP04425 (UniProt A0A5P8YHT8)
Region: residues 110	to 215
Annotation: disorder (Structural state)
Evidence: near-UV circular dichroism evidence used in manual assertion
Supporting statements:
Near-UV CD of the D2 domain showed a broad band between 280 and 290 nm for Trp and Tyr with weak ellipticity (data not shown).
Protein: DP04425 (UniProt A0A5P8YHT8)
Region: residues 110	to 215
Annotation: disorder (Structural state)
Evidence: far-UV circular dichroism evidence used in manual assertion
Supporting statements:
As shown in Fig. 6 (spectrum 1), the far-UV CD spectrum of D2 puriﬁed from inclusion bodies resembles that of a poorly folded protein with low regular secondary structure content.
Protein: DP04425 (UniProt A0A5P8YHT8)
Region: residues 110	to 215
Annotation: disorder (Structural state)
Evidence: fluorescence evidence used in manual assertion
Supporting statements:
When D2 puriﬁed from inclusion bodies is excited at 295 nm it shows ﬂuorescence emission maxima at 350 nm, indicating that the engineered Trp is solvent-exposed (Fig. 5, spectrum 1).
Protein: DP04425 (UniProt A0A5P8YHT8)
Region: residues 110	to 215
Annotation: ion binding (Molecular function)
Evidence: fluorescence evidence used in manual assertion
Supporting statements:
Calcium mimic dye Stains-all was used to probe calcium binding to D2 puriﬁed from insoluble fraction. As shown in Fig. 4, the dye–protein complex gives rise to a characteristic peak at 660 nm in the CD spectra. The intensity at 660 nm decreased upon calcium addition, indicating displacement of dye and calcium-binding to the protein. These results suggest that the refolded protein is able to bind calcium and is functionally active.
Protein: DP04425 (UniProt A0A5P8YHT8)
Region: residues 110	to 215
Annotation: ion binding (Molecular function)
Evidence: radioligand binding assay evidence used in manual assertion
Supporting statements:
Direct assay using radioactive 45Ca revealed that both domains, D1 and D2, bind calcium as shown in Fig. 5.
Protein: DP04425 (UniProt A0A5P8YHT8)
Region: residues 21	to 112
Annotation: ion binding (Molecular function)
Evidence: radioligand binding assay evidence used in manual assertion
Supporting statements:
Direct assay using radioactive 45Ca revealed that both domains, D1 and D2, bind calcium as shown in Fig. 5.
Protein: DP04425 (UniProt A0A5P8YHT8)
Region: residues 21	to 112
Annotation: calcium ion sequestering activity (Molecular function)
Evidence: chromatography evidence used in manual assertion
Supporting statements:
The presence of calcium drastically decreased the hydrodynamic volume, and the elution volume corresponds to a monomer (Fig. 10a). Thus, there is significant change in the Stokes radius of the D1 upon calcium binding, which could be attributed to the transition of the protein from an unstructured to a structured state and the resulting compaction (44, 46).
Protein: DP04425 (UniProt A0A5P8YHT8)
Region: residues 21	to 112
Annotation: disorder to order (Structural transition)
Evidence: chromatography evidence used in manual assertion
Supporting statements:
The presence of calcium drastically decreased the hydrodynamic volume, and the elution volume corresponds to a monomer (Fig. 10a). Thus, there is significant change in the Stokes radius of the D1 upon calcium binding, which could be attributed to the transition of the protein from an unstructured to a structured state and the resulting compaction (44, 46).
Protein: DP04425 (UniProt A0A5P8YHT8)
Region: residues 21	to 112
Annotation: ion binding (Molecular function)
Evidence: chromatography evidence used in manual assertion
Supporting statements:
The presence of calcium drastically decreased the hydrodynamic volume, and the elution volume corresponds to a monomer (Fig. 10a). Thus, there is significant change in the Stokes radius of the D1 upon calcium binding, which could be attributed to the transition of the protein from an unstructured to a structured state and the resulting compaction (44, 46).
Protein: DP04426 (UniProt A0A6L8PPD0)
Region: residues 326	to 344
Annotation: disorder (Structural state)
Evidence: X-ray crystallography-based structural model with missing residue coordinates used in manual assertion
Supporting statements:
Residues 326–344 could not be located because of weak electron density, and in the crystal cannot adopt the conformation of the corresponding region of apo ecMSA (residues 329–346) as they would clash with a symmetry mate.
Cross-references: PDB:3CUX
Protein: DP04427 (UniProt Q9EU62)
Region: residues 27	to 66
Annotation: disorder (Structural state)
Evidence: X-ray crystallography-based structural model with missing residue coordinates used in manual assertion
Supporting statements:
Electron density corresponding to the N-terminal domain was not visible suggesting that it is disordered.
The low complexity N-terminal regions (residues up to and including Asn41 of chain A, and Ala40 of chain B) were not visible in the electron density maps. These residues were assumed, therefore, to be disordered.
The Vap proteins of R. equi consist of β-barrel domains with disordered regions at their N-termini.
Cross-references: PDB:5AEO
Protein: DP04428 (UniProt A0A8I6XZQ2)
Region: residues 173	to 355
Annotation: disorder (Structural state)
Evidence: far-UV circular dichroism evidence used in manual assertion
Supporting statements:
The far-UV CD spectra showed a strong negative absorbance at 200 nm for His6-HvNAC005(173–355), His6-HvNAC013(177–346), and HvNAC013(177–346) with little ellipticity around 220 nm indicating lack of a significant amount of secondary structure and highly characteristic of unstructured proteins (Figs. 6, A and B, and ​77B).
HvNAC005 correspond to Hordeum vulgare NAC domain-containing protein.
Protein: DP04428 (UniProt A0A8I6XZQ2)
Region: residues 172	to 355
Annotation: molecular function regulator (Molecular function)
Evidence: loss-of-function mutant phenotype evidence used in manual assertion
Supporting statements:
When adenine was added to the plates, both full-length HvNAC005, HvNAC005(1–355), and the HvNAC005 C-terminus, HvNAC005(172–355), were able to activate transcription of the reporter gene HIS3, as measured by the ability of transformed yeast to grow in the absence of histidine (Fig. 3B). By contrast and, as expected, the NAC domain, HvNAC005(1–172) alone was unable to activate transcription.
HvNAC005 correspond to Hordeum vulgare NAC domain-containing protein.
Protein: DP04428 (UniProt A0A8I6XZQ2)
Region: residues 172	to 250
Annotation: molecular function regulator (Molecular function)
Evidence: loss-of-function mutant phenotype evidence used in manual assertion
Supporting statements:
Removal of the SC- and the KR-motifs from both full-length and C-terminal HvNAC005 did not affect the ability to activate transcription (Fig. 3B). By contrast, removal of the LL-motif abolished activity in both cases. 
The region 172-250 corresponds to the shorter construct retaining the activator function.
Protein: DP04429 (UniProt E6MVD9)
Region: residues 1021	to 1035
Annotation: disorder (Structural state)
Evidence: X-ray crystallography-based structural model with missing residue coordinates used in manual assertion
Supporting statements:
Amino acids not visible in the electron density of space group P6122 are indicated in blue.
In space group C2221, no interpretable electron density was observed for residues 816–817, 834–836, 915–917, 943–945, 972–973 and 1024–1036.
The missing regions corresponds to 1021-1035 in UniProt.
Cross-references: PDB:1UYO
PDB:1UYN
Protein: DP04430 (UniProt P38829)
Region: residues 1	to 102
Annotation: disorder (Structural state)
Evidence: circular dichroism evidence used in manual assertion
Supporting statements:
Herein, we determine that Cia2 contains five conserved motifs distributed between an intrinsically disordered N-terminal domain and a C-terminal domain of unknown function 59 (DUF59).