LiteFold/DisProt huggingface dataset:
Protein: DP00697 (UniProt Q9IK92)
Region: residues 400	to 532
Annotation: disorder (Structural state)
Evidence: far-UV circular dichroism evidence used in manual assertion
Supporting statements:
The far-UV CD spectra of spin-labeled NTAIL proteins variants at neutral pH quite well superimpose onto that of parental NTAIL, andare all typical of unstructured proteins, as shown by their large negative ellipticity at 200 nm and moderate ellipticity at 190 nm (Figures 2(A), (B) and S2).
Protein: DP00697 (UniProt Q9IK92)
Region: residues 400	to 532
Annotation: protein binding (Molecular function)
Evidence: far-UV circular dichroism evidence used in manual assertion
Supporting statements:
Indeed, the observed CD spectra of the mixtures differed from the corresponding theoretical average curves calculated from the individual NTAIL and PXD spectra (Fig. 5).
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.
Protein: DP00697 (UniProt Q9IK92)
Region: residues 400	to 532
Annotation: molecular adaptor activity (Molecular function)
Evidence: far-UV circular dichroism evidence used in manual assertion
Supporting statements:
Indeed, the observed CD spectra of the mixtures differed from the corresponding theoretical average curves calculated from the individual NTAIL and PXD spectra (Fig. 5).
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.
Protein: DP00697 (UniProt Q9IK92)
Region: residues 400	to 532
Annotation: molecular adaptor activity (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: DP00698 (UniProt O89339)
Region: residues 400	to 532
Annotation: disorder (Structural state)
Evidence: cleavage assay evidence used in manual assertion
Supporting statements:
Henipavirus PNT and NTAIL were found to be highly sensitive to proteolysis, a property that constitutes a hallmark of structural disorder (see [47] and references therein cited).
Protein: DP00698 (UniProt O89339)
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: DP00698 (UniProt O89339)
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:
Taken together, the EPR analyses of the labeled variants within Box3 bring experimental support for the structural model of HeV NTAIL–PXD complex that we previously proposed (Habchi et al., 2011) (Figure 6(A)).
Protein: DP00698 (UniProt O89339)
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:
Taken together, the EPR analyses of the labeled variants
within Box3 bring experimental support for the
structural model of HeV NTAIL–PXD complex that we
previously proposed (Habchi et al., 2011) (Figure 6(A)).
Protein: DP00698 (UniProt O89339)
Region: residues 400	to 532
Annotation: disorder (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: DP00698 (UniProt O89339)
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: DP00698 (UniProt O89339)
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: DP00698 (UniProt O89339)
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: DP00698 (UniProt O89339)
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: DP00698 (UniProt O89339)
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: DP00698 (UniProt O89339)
Region: residues 400	to 532
Annotation: protein binding (Molecular function)
Evidence: proton-based nuclear magnetic resonance evidence used in manual assertion
Supporting statements:
The NMR titration experiments of Henipavirus NTAIL with increasing amounts of PXD confirmed that a complex is formed between the two partners. 
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.
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: DP00698 (UniProt O89339)
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: DP00698 (UniProt O89339)
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: DP00698 (UniProt O89339)
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: DP00698 (UniProt O89339)
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: DP00698 (UniProt O89339)
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).
Protein: DP00698 (UniProt O89339)
Region: residues 400	to 532
Annotation: disorder (Structural state)
Evidence: far-UV circular dichroism evidence used in manual assertion
Supporting statements:
The far-UV CD spectra of spin-labeled NTAIL proteins variants at neutral pH quite well superimpose onto that of parental NTAIL, and are all typical of unstructured proteins, as shown by their large negative ellipticity at 200 nm and moderate ellipticity at 190 nm (Figures 2(A), (B) and S2).
Protein: DP00698 (UniProt O89339)
Region: residues 400	to 532
Annotation: molecular adaptor activity (Molecular function)
Evidence: proton-based nuclear magnetic resonance evidence used in manual assertion
Supporting statements:
The NMR titration experiments of Henipavirus NTAIL with increasing amounts of PXD confirmed that a complex is formed between the two partners. 
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.
Protein: DP00698 (UniProt O89339)
Region: residues 400	to 532
Annotation: protein binding (Molecular function)
Evidence: far-UV circular dichroism evidence used in manual assertion
Supporting statements:
Indeed, the observed CD spectra of the mixtures differed from the corresponding theoretical average curves calculated from the individual NTAIL and PXD spectra (Fig. 5).
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.
Protein: DP00698 (UniProt O89339)
Region: residues 400	to 532
Annotation: molecular adaptor activity (Molecular function)
Evidence: far-UV circular dichroism evidence used in manual assertion
Supporting statements:
Indeed, the observed CD spectra of the mixtures differed from the corresponding theoretical average curves calculated from the individual NTAIL and PXD spectra (Fig. 5).
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.
Protein: DP00699 (UniProt Q9IK91)
Region: residues 1	to 406
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: DP00699 (UniProt Q9IK91)
Region: residues 1	to 406
Annotation: pre-molten globule (Structural state)
Evidence: cleavage assay evidence used in manual assertion
Supporting statements:
Henipavirus PNT and NTAIL were found to be highly sensitive to proteolysis, a property that constitutes a hallmark of structural disorder (see [47] and references therein cited).
Protein: DP00699 (UniProt Q9IK91)
Region: residues 1	to 406
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: DP00699 (UniProt Q9IK91)
Region: residues 1	to 406
Annotation: pre-molten globule (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: DP00699 (UniProt Q9IK91)
Region: residues 1	to 406
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: DP00699 (UniProt Q9IK91)
Region: residues 1	to 406
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: DP00699 (UniProt Q9IK91)
Region: residues 1	to 406
Annotation: disorder (Structural state)
Evidence: nuclear magnetic resonance spectroscopy evidence used in manual assertion
Supporting statements:
NiV PNT is a very large intrinsically disordered protein (412 residues including the C-terminal His tag and the initial methionine), as can be inferred by inspection of the two 2D spectra, the 1H–15N HSQC (Fig. 2A) and the 13C′–15N CON (Fig. 2B).
The relaxation rates show an overall trend consistent with the considerably disordered conformation of PNT.
The NMR data clearly suggest that NiV PNT is disordered and very flexible with few short and transient secondary structure elements.
Cross-references: BMRB:50370
Protein: DP00699 (UniProt Q9IK91)
Region: residues 1	to 406
Annotation: disorder (Structural state)
Evidence: small-angle X-ray scattering evidence used in manual assertion
Supporting statements:
The experimentally determined Rg is therefore very close to the value expected for an IDP (for comparison the Rg expected for a random coil conformation would be ~ 7253).
The flexible nature of NiV PNT was qualitatively assessed by using the normalized Kratky plot, where the absence of a well-defined bell shape indicates a protein with intrinsically disordered regions (Fig. 4C).
Cross-references: SASBDB:SASDJB5
Protein: DP00699 (UniProt Q9IK91)
Region: residues 1	to 100
Annotation: disorder (Structural state)
Evidence: nuclear magnetic resonance evidence used in manual assertion
Supporting statements:
In addition, the poor chemical-shift dispersion of amide resonances in the HSQC NMR spectrum was typical of disordered protein, but after assigning the NMR spectrum, the secondary-structure propensity (SSP) parameter calculated from Cα and Cβ secondary chemical shifts indicated the presence of five fluctuating α-helices (Supplementary Fig. 2c).
The poor chemical shift dispersion of amide 1H resonances in the heteronuclear single quantum coherence (HSQC) NMR spectrum (Supplementary Fig. 1d) is typical of disordered proteins.
Protein: DP00699 (UniProt Q9IK91)
Region: residues 1	to 100
Annotation: disorder (Structural state)
Evidence: chromatography evidence used in manual assertion
Supporting statements:
By SEC-MALLS, we showed that the peptide is monomeric in solution and that both its hydrodynamic radius measured by SEC and its radius of gyration measured by SAXS were larger than expected for a globular protein of this molecular mass (Supplementary Fig. 2a,b).
The hydrodynamic radius of 2.6 ± 0.5 nm measured by SEC (a) and the radius of gyration of 3.1 ± 0.5 nm measured by SAXS (b) are larger than expected for a compact domain of this size.
Protein: DP00699 (UniProt Q9IK91)
Region: residues 1	to 100
Annotation: disorder (Structural state)
Evidence: small-angle X-ray scattering evidence used in manual assertion
Supporting statements:
By SEC-MALLS, we showed that the peptide is monomeric in solution and that both its hydrodynamic radius measured by SEC and its radius of gyration measured by SAXS were larger than expected for a globular protein of this molecular mass (Supplementary Fig. 2a,b).
The hydrodynamic radius of 2.6 ± 0.5 nm measured by SEC (a) and the radius of gyration of 3.1 ± 0.5 nm measured by SAXS (b) are larger than expected for a compact domain of this size.
Protein: DP00699 (UniProt Q9IK91)
Region: residues 1	to 35
Annotation: protein binding (Molecular function)
Evidence: x-ray crystallography evidence used in manual assertion
Supporting statements:
The N-terminal chaperone region of P is stabilized upon binding to its N0 partner, but only the first 35 residues of P, corresponding to the first fluctuating helix observed in solution (helix αP1), were visible in the crystal structure of N32–3830–P50. 
Cross-references: PDB:4CO6
Protein: DP00699 (UniProt Q9IK91)
Region: residues 1	to 35
Annotation: disorder to order (Structural transition)
Evidence: x-ray crystallography evidence used in manual assertion
Supporting statements:
The N-terminal chaperone region of P is stabilized upon binding to its N0 partner, but only the first 35 residues of P, corresponding to the first fluctuating helix observed in solution (helix αP1), were visible in the crystal structure of N32–3830–P50. 
Cross-references: PDB:4CO6
Protein: DP00699 (UniProt Q9IK91)
Region: residues 1	to 50
Annotation: protein binding (Molecular function)
Evidence: small-angle X-ray scattering evidence used in manual assertion
Supporting statements:
By size-exclusion chromatography (SEC) combined with multiangle laser light scattering (MALLS) (Fig. 1b) and by small-angle X-ray scattering (SAXS), we found that these reconstituted N0–P core complexes are compact heterodimers with an overall bean-like shape typical of other NNV N proteins18.
(c) The heterodimeric N32-3830-P50 complex has a bean shape in solution. The ab initio bead model generated from SAXS data (in grey) accommodates a single N32-3830-P50 copy from the crystal.
Protein: DP00699 (UniProt Q9IK91)
Region: residues 1	to 50
Annotation: protein binding (Molecular function)
Evidence: heteronuclear single quantum coherence spectroscopy evidence used in manual assertion
Supporting statements:
We then analyzed the HSQC spectrum of P100 bound to N32–402. In a complex of this size (~50 kDa), NMR signals are strongly broadened in protonated samples, thus precluding their detection, but in the HSQC spectrum we observed resonances corresponding to residues 50 to 100, thus indicating that this region remains flexible in the complex and that the N0-binding region is comprised within the first 50 N-terminal amino acids of P (Fig. 1c and Supplementary Fig. 1d).
Protein: DP00699 (UniProt Q9IK91)
Region: residues 1	to 50
Annotation: molecular adaptor activity (Molecular function)
Evidence: heteronuclear single quantum coherence spectroscopy evidence used in manual assertion
Supporting statements:
We then analyzed the HSQC spectrum of P100 bound to N32–402. In a complex of this size (~50 kDa), NMR signals are strongly broadened in protonated samples, thus precluding their detection, but in the HSQC spectrum we observed resonances corresponding to residues 50 to 100, thus indicating that this region remains flexible in the complex and that the N0-binding region is comprised within the first 50 N-terminal amino acids of P (Fig. 1c and Supplementary Fig. 1d).
Protein: DP00699 (UniProt Q9IK91)
Region: residues 1	to 50
Annotation: molecular adaptor activity (Molecular function)
Evidence: small-angle X-ray scattering evidence used in manual assertion
Supporting statements:
By size-exclusion chromatography (SEC) combined with multiangle laser light scattering (MALLS) (Fig. 1b) and by small-angle X-ray scattering (SAXS), we found that these reconstituted N0–P core complexes are compact heterodimers with an overall bean-like shape typical of other NNV N proteins18.
(c) The heterodimeric N32-3830-P50 complex has a bean shape in solution. The ab initio bead model generated from SAXS data (in grey) accommodates a single N32-3830-P50 copy from the crystal.