LiteFold/DisProt huggingface dataset:
Protein: DP01925 (UniProt Q02078)
Region: residues 75	to 86
Annotation: disorder (Structural state)
Evidence: nuclear magnetic resonance spectroscopy evidence used in manual assertion
Supporting statements:
Note that the protein sequence starts at Gly1, and the N-terminal methionine is completely excised.
"Residues 74–85 of the protein are disordered in solution."
Protein: DP01926 (UniProt C4M7X2)
Region: residues 583	to 769
Annotation: disorder (Structural state)
Evidence: X-ray crystallography-based structural model with missing residue coordinates used in manual assertion
Supporting statements:
In all structures, residues 304–368 between strands β13 and β14, residues 507–513 between helices α15 and α16, and residues after position 583 are disordered.
Cross-references: PDB:4UP7
PDB:4UP8
PDB:4UPA
PDB:4UP9
Protein: DP01928 (UniProt P03254)
Region: residues 1	to 137
Annotation: disorder (Structural state)
Evidence: nuclear magnetic resonance spectroscopy evidence used in manual assertion
Supporting statements:
The 2D 1H–15N correlation NMR experiments acquired on E1A289 and E1A243 (Figure 2 A,B) confirm that both isoforms of E1A are highly disordered and flexible, as inferred from the small chemical shift dispersion of the NMR signals.[27] (Figure 2)
Protein: DP01928 (UniProt P03254)
Region: residues 191	to 289
Annotation: disorder (Structural state)
Evidence: nuclear magnetic resonance spectroscopy evidence used in manual assertion
Supporting statements:
The 2D 1H–15N correlation NMR experiments acquired on E1A289 and E1A243 (Figure 2 A,B) confirm that both isoforms of E1A are highly disordered and flexible, as inferred from the small chemical shift dispersion of the NMR signals.[27] (figure 2)
Protein: DP01928 (UniProt P03254)
Region: residues 1	to 289
Annotation: disorder (Structural state)
Evidence: nuclear magnetic resonance spectroscopy evidence used in manual assertion
Supporting statements:
The 2D 1H–15N correlation NMR experiments acquired on E1A289 and E1A243 (Figure 2 A,B) confirm that both isoforms of E1A are highly disordered and flexible, as inferred from the small chemical shift dispersion of the NMR signals.
Protein: DP01928 (UniProt P03254)
Region: residues 154	to 174
Annotation: metal ion binding (Molecular function)
Evidence: nuclear magnetic resonance spectroscopy evidence used in manual assertion
Supporting statements:
The five cysteine residues were assigned and the chemical shifts values for the Cα and Cβ of Cys 154, 157, 171, and 174 are consistent with their involvement in ZnII-binding.
On the other hand, the results on the E1ACR3 clearly indicate the presence of a minimal fold composed by just two helices of less than 10 amino acids embedded in a relatively flexible polypeptide. The binding of ZnII restricts the conformational space for the two helices, which should face each other to properly locate the ligand cysteines.
Protein: DP01928 (UniProt P03254)
Region: residues 153	to 180
Annotation: disorder to order (Structural transition)
Evidence: nuclear magnetic resonance spectroscopy evidence used in manual assertion
Supporting statements:
A similar analysis was accomplished for E1ACR3. The SSP plot derived for the amino acids of this construct indicates the presence of two α-helices beginning with the CXXC motifs and including residues 153–165 and 170–180 (Figure 3).
On the other hand, the results on the E1ACR3 clearly indicate the presence of a minimal fold composed by just two helices of less than 10 amino acids embedded in a relatively flexible polypeptide. The binding of ZnII restricts the conformational space for the two helices, which should face each other to properly locate the ligand cysteines.
Protein: DP01929 (UniProt P17763)
Region: residues 1649	to 1661
Annotation: disorder (Structural state)
Evidence: X-ray crystallography-based structural model with missing residue coordinates used in manual assertion
Supporting statements:
While residues C terminal to Glu173 are disordered in the DEN1proΔ11-20 structure, they are visible and stabilized through crystal contacts in the S135A structure.
The PDB 3L6P shows the structure without the mutation S135A (S1610A in the Uniprot) and has the C-terminal disordered. 
Cross-references: PDB:3L6P
PDB:3LKW
Protein: DP01930 (UniProt P29990)
Region: residues 883	to 903
Annotation: disorder (Structural state)
Evidence: x-ray crystallography evidence used in manual assertion
Supporting statements:
The second domain (amino acids 30-180) of each monomer protrudes from the central β-domain like a wing (Fig. 1A, yellow). Each “wing” domain contains two glycosylation sites (Asn130, Asn175), an internal disulfide (Cys55-Cys143), and two discreet subdomains. An α/β subdomain (amino acids 38 – 151) comprises a four-stranded β-sheet, two α-helices and a disordered distal tip (amino acids 108 – 128; Fig. 1A, dotted line).
Region 108-128 of NS1 protein corresponds to the region 884-904 of the polyprotein of Dengue virus type 2 (strain Thailand/16681/1984).
Cross-references: PDB:4O6B
Protein: DP01931 (UniProt Q2YHF0)
Region: residues 1644	to 1654
Annotation: disorder (Structural state)
Evidence: X-ray crystallography-based structural model with missing residue coordinates used in manual assertion
Supporting statements:
A flexible linker region is identified which joins the NS3 protease and helicase domains allowing alternative conformations. The flexibility in this region is important for protease and helicase activity: "Our results indicate that the linker region has evolved to an optimum length to confer flexibility to the NS3 protein that is required both for polyprotein processing and RNA replication.
Thus, in both crystal forms, the protease domain appears significantly more mobile, which is consistent with proteolysis data showing that the protease domain is more labile. In the second conformation, only a few interactions are observed between the linker and either of the two domains: Glu169, Gly172, and Glu173 from the linker interact with Lys88 and Tyr83 from the protease and Arg202 and Ala197 from the P-loop (Fig. 2A). However, as a caveat, the electron density map for the linker region is less well defined for side chains of residues 169–176 (Fig. 2A). The overall B factor for the linker is 73.2 Å2, a value significantly higher than the average value for the other domains of NS3. This suggests some intrinsic degree of freedom conferred to the protein by the linker in solution.
Cross-references: PDB:2WZQ
PDB:2WHX
Protein: DP01931 (UniProt Q2YHF0)
Region: residues 1644	to 1654
Annotation: flexible linker (Disorder function)
Evidence: X-ray crystallography-based structural model with missing residue coordinates used in manual assertion
Supporting statements:
The two domains of NS3 are linked by a polypeptide segment spanning residues 169–179. This interdomain (“linker”) acid-rich segment displays some sequence variation, yet its overall length appears to be restricted to 11 or 12 amino acids across flaviviruses. In both conformation I and II, the linker region was partially disordered with only clear electron density for the backbone (Fig. 2) (10).
Cross-references: PDB:2WHX
PDB:2WZQ
Protein: DP01931 (UniProt Q2YHF0)
Region: residues 1475	to 1494
Annotation: disorder (Structural state)
Evidence: X-ray crystallography-based structural model with missing residue coordinates used in manual assertion
Supporting statements:
The PDB shows a disordered region that corresponds to the N-terminal region of the NS3 protein.
Cross-references: PDB:2WHX
Protein: DP01933 (UniProt P07986)
Region: residues 357	to 376
Annotation: disorder (Structural state)
Evidence: nuclear magnetic resonance spectroscopy evidence used in manual assertion
Supporting statements:
Nevertheless, it is readily apparent that all of the linker threonines have poorly dispersed amide 1HN chemical shifts within the range expected for a random coil polypeptide
Protein: DP01933 (UniProt P07986)
Region: residues 357	to 376
Annotation: flexible linker (Disorder function)
Evidence: nuclear magnetic resonance spectroscopy evidence used in manual assertion
Supporting statements:
Cex Is Composed of Independent Catalytic and Cellulosebinding Domains Tethered by a Flexible PT Linker
Protein: DP01934 (UniProt Q9RJY2)
Region: residues 235	to 264
Annotation: disorder (Structural state)
Evidence: nuclear magnetic resonance spectroscopy evidence used in manual assertion
Supporting statements:
The result was an ensemble showing large  conformational variation as a result of the low structural restriction in the linker region
Protein: DP01934 (UniProt Q9RJY2)
Region: residues 235	to 264
Annotation: flexible linker (Disorder function)
Evidence: nuclear magnetic resonance spectroscopy evidence used in manual assertion
Supporting statements:
The  linker  in ScLPMO10C serves  as  a flexible spacer, maintaining a distance between the carbohydrate-binding and catalytic domains, while simultaneously  enabling  these domains to  move independently of each other
Protein: DP01935 (UniProt P83731)
Region: residues 123	to 157
Annotation: disorder (Structural state)
Evidence: cryogenic electron microscopy-based structural model with missing residue coordinates used in manual assertion
Supporting statements:
Chain: AW; Unified name: eL24; Human name: L24; Template: 3U5E chain W; Swiss-Prot: P83731; Seq. length: 157; Residues modelled: 2-122
Cross-references: PDB:5AJ0
Protein: DP01937 (UniProt Q9EPH0)
Region: residues 564	to 636
Annotation: disorder (Structural state)
Evidence: far-UV circular dichroism evidence used in manual assertion
Supporting statements:
Prestin STAS constructs without the variable loop, which is predicted to be mostly disordered, showed a better behavior in solution, with circular dichroism (CD)
Cross-references: PDB:3LLO
Protein: DP01938 (UniProt P11021)
Region: residues 1	to 24
Annotation: disorder (Structural state)
Evidence: X-ray crystallography-based structural model with missing residue coordinates used in manual assertion
Supporting statements:
Schematic of human BiP domain structure. The positions for key elements are indicated. The first 24 residues (signal sequence) and the last 20 residues (largely disordered) are not colored
Cross-references: PDB:6ASY
Protein: DP01938 (UniProt P11021)
Region: residues 634	to 654
Annotation: disorder (Structural state)
Evidence: X-ray crystallography-based structural model with missing residue coordinates used in manual assertion
Supporting statements:
Schematic of human BiP domain structure. The positions for key elements are indicated. The first 24 residues (signal sequence) and the last 20 residues (largely disordered) are not colored
Cross-references: PDB:6ASY
Protein: DP01939 (UniProt Q5JJ98)
Region: residues 493	to 588
Annotation: disorder (Structural state)
Evidence: nuclear magnetic resonance spectroscopy evidence used in manual assertion
Supporting statements:
We analyzed the interdomain region of Thermococcus kodakarensis Hef and demonstrated its disordered structure by CD, NMR, and high speed atomic force microscopy (AFM).
Protein: DP01939 (UniProt Q5JJ98)
Region: residues 493	to 588
Annotation: protein binding (Molecular function)
Evidence: nuclear magnetic resonance spectroscopy evidence used in manual assertion
Supporting statements:
two-hybrid screen
Cross-references: uniprot:Q5JFJ4
Protein: DP01939 (UniProt Q5JJ98)
Region: residues 493	to 588
Annotation: protein binding (Molecular function)
Evidence: nuclear magnetic resonance spectroscopy evidence used in manual assertion
Supporting statements:
two-hybrid screen
Cross-references: uniprot:Q5JCW9
Protein: DP01939 (UniProt Q5JJ98)
Region: residues 493	to 588
Annotation: protein binding (Molecular function)
Evidence: nuclear magnetic resonance spectroscopy evidence used in manual assertion
Supporting statements:
two-hybrid screen
Cross-references: uniprot:Q5JG97
Protein: DP01939 (UniProt Q5JJ98)
Region: residues 493	to 588
Annotation: protein binding (Molecular function)
Evidence: nuclear magnetic resonance spectroscopy evidence used in manual assertion
Supporting statements:
two-hybrid screen
Cross-references: uniprot:Q5JF12
Protein: DP01939 (UniProt Q5JJ98)
Region: residues 493	to 588
Annotation: protein binding (Molecular function)
Evidence: nuclear magnetic resonance spectroscopy evidence used in manual assertion
Supporting statements:
two-hybrid screen
Cross-references: uniprot:Q5JJ48
Protein: DP01939 (UniProt Q5JJ98)
Region: residues 493	to 588
Annotation: protein binding (Molecular function)
Evidence: nuclear magnetic resonance spectroscopy evidence used in manual assertion
Supporting statements:
two-hybrid screen
Cross-references: uniprot:Q5JII4
Protein: DP01939 (UniProt Q5JJ98)
Region: residues 493	to 588
Annotation: protein binding (Molecular function)
Evidence: nuclear magnetic resonance spectroscopy evidence used in manual assertion
Supporting statements:
two-hybrid screen
Cross-references: uniprot:Q5JDD8
Protein: DP01939 (UniProt Q5JJ98)
Region: residues 493	to 588
Annotation: protein binding (Molecular function)
Evidence: nuclear magnetic resonance spectroscopy evidence used in manual assertion
Supporting statements:
two-hybrid screen
Cross-references: uniprot:Q52500
Protein: DP01939 (UniProt Q5JJ98)
Region: residues 493	to 593
Annotation: disorder (Structural state)
Evidence: protein thermal shift assay evidence used in manual assertion
Supporting statements:
Although the detailed temperature dependence of Rg was unclear only from the SANS results owing to large error bars, at least a tendency for a reduction in Rg was observed with increasing temperature (Figs. S2 and S3). In the case of unfolding of
FGPs by an increment of temperature, the collapse of secondary structures such as the a helix and b sheet occurs, leading to an increment of Rg with increasing temperature (27). This process is normally irreversible in FGPs, whereas heat-induced structural changes are reversible in IDPs (3).
Protein: DP01939 (UniProt Q5JJ98)
Region: residues 493	to 593
Annotation: disorder (Structural state)
Evidence: circular dichroism evidence used in manual assertion
Supporting statements:
As shown in Fig. 2 a, only a broad band at 222 nm was observed in the
CD spectra. Therefore, we focused on the temperature dependence of ellipticity at 222 nm (q222nm). The variation of the q222nm value against temperature was almost flat up to 313 K, whereas a reduction of the q222nm value was
observed in the temperature range above 313 K. (Fig. 2 b). The transition temperature (Ttra), which ranged from 313 to 323 K, was observed in the SAXS and CD measurements. Structural changes in other IDPs have been observed in similar temperature ranges (2).
Protein: DP01939 (UniProt Q5JJ98)
Region: residues 493	to 593
Annotation: disorder (Structural state)
Evidence: nuclear magnetic resonance spectroscopy evidence used in manual assertion
Supporting statements:
Although the 13C chemical shifts have been corrected by the sodium trimethylsilylpropanesulfonate (DSS) peak, the chemical shifts of both 13C0 and 13Ca shifted upfield with increasing temperature. It was reported that these chemical shifts in IDPs exhibited temperature dependency (31,32); hence, we focused on the largest differences in the 13Ca and 13C0 chemical shifts between 298 and 349 K. Fig. 3, c and d, shows a histogram of the difference in the 13Ca chemical shifts between 298 and 349 K (D13Ca 349–298K) and the 13C0 chemical shifts between 298 and 349 K (D13C0 349–298K), respectively.
Protein: DP01939 (UniProt Q5JJ98)
Region: residues 493	to 593
Annotation: disorder (Structural state)
Evidence: small-angle neutron scattering evidence used in manual assertion
Supporting statements:
As the scattering cross section of a hydrogen (H) atom is significantly larger than those of other constituent atoms in Hef-IDR, the observed QENS profile is mainly dominated by incoherent dynamic scattering laws.
Protein: DP01940 (UniProt Q8BH64)
Region: residues 1	to 18
Annotation: disorder (Structural state)
Evidence: X-ray crystallography-based structural model with missing residue coordinates used in manual assertion
Supporting statements:
The helical domain is composed of helix a1 and a2 from the N-terminal region (residues 18–55, which follow disordered residues 1–18)
Cross-references: PDB:2QPT
Protein: DP01940 (UniProt Q8BH64)
Region: residues 110	to 130
Annotation: disorder (Structural state)
Evidence: X-ray crystallography-based structural model with missing residue coordinates used in manual assertion
Supporting statements:
Residues 110–130, which are distal to switch I, are disordered and contain predicted EH-domain binding motifs, KPFxxxNPF
Cross-references: PDB:2QPT
Protein: DP01940 (UniProt Q8BH64)
Region: residues 110	to 130
Annotation: disorder (Structural state)
Evidence: X-ray crystallography-based structural model with missing residue coordinates used in manual assertion
Supporting statements:
Superposition showing the KPFxxxNPF loop from EHD2 Q410A (blue, pdb 2QPT) and EHD2 L5M Q410A (lightblue)
Cross-references: PDB:4CID
Protein: DP01941 (UniProt Q4JC68)
Region: residues 99	to 143
Annotation: disorder (Structural state)
Evidence: X-ray crystallography-based structural model with missing residue coordinates used in manual assertion
Supporting statements:
Disordered regions (1-9, 72-76, 89-96, 98-144) show the 4Fe-4S cluster acts in ordering the 4FeS domain, the Arch interface, and parts of HD1.
Cross-references: PDB:3CRW
Protein: DP01942 (UniProt P50553)
Region: residues 1	to 236
Annotation: disorder (Structural state)
Evidence: nuclear magnetic resonance spectroscopy evidence used in manual assertion
Supporting statements:
Ascl1 forms an extended polypeptide chain lacking persistent tertiary interactions, similar to a string of several loosely coupled peptide segments with a high propensity to adopt α-helical conformation
Protein: DP01942 (UniProt P50553)
Region: residues 1	to 236
Annotation: nucleic acid binding (Molecular function)
Evidence: nuclear magnetic resonance spectroscopy evidence used in manual assertion
Supporting statements:
a central bHLH domain (residues 122–179) that is responsible for homo- and heterodimerization of the protein, as well as for DNA binding through interaction of positively charged residues (basic region) with the negatively charged DNA backbone
Protein: DP01942 (UniProt P50553)
Region: residues 1	to 236
Annotation: protein binding (Molecular function)
Evidence: nuclear magnetic resonance spectroscopy evidence used in manual assertion
Supporting statements:
Phosphorylation through proline-directed kinases of these serine residues contributes to the regulation of Ascl1 activity
Protein: DP01943 (UniProt Q9NRY2)
Region: residues 1	to 62
Annotation: disorder (Structural state)
Evidence: X-ray crystallography-based structural model with missing residue coordinates used in manual assertion
Supporting statements:
Several regions of the polypeptide chains are disordered, namely, residues 1–32 and 499–500 in SOSSAN, residues 1–4, 11–18, 28–37, 71–81, 87–90, and 110–211 in SOSSB1, and residues 1–62 and 102–104 in SOSSC.
Cross-references: PDB:4OWT
Protein: DP01944 (UniProt P31324)
Region: residues 1	to 103
Annotation: disorder (Structural state)
Evidence: X-ray crystallography-based structural model with missing residue coordinates used in manual assertion
Supporting statements:
Although residues 1 to 103, 122 to 129, and 394 to 416 of RIIβ and residues 1 to 13 of C are missing in the electron density, we validated by using gel electrophoresis that the full-length RIIβ2:C2 complex is in the protein crystal. The absence of density for the N-terminal D/D domain and the following linker is likely related to the flexible nature of this region.
Cross-references: PDB:3TNP
Protein: DP01944 (UniProt P31324)
Region: residues 394	to 416
Annotation: disorder (Structural state)
Evidence: X-ray crystallography-based structural model with missing residue coordinates used in manual assertion
Supporting statements:
Although residues 1 to 103, 122 to 129, and 394 to 416 of RIIβ and residues 1 to 13 of C are missing in the electron density, we validated by using gel electrophoresis that the full-length RIIβ2:C2 complex is in the protein crystal. The absence of density for the N-terminal D/D domain and the following linker is likely related to the flexible nature of this region.
Cross-references: PDB:3TNP
Protein: DP01945 (UniProt A0A2K8FR49)
Region: residues 1	to 172
Annotation: disorder (Structural state)
Evidence: proton-based nuclear magnetic resonance evidence used in manual assertion
Supporting statements:
Narrow signal distribution in amide region, between 6.5 and 8.5 ppm, strongly suggest the lack of a well-defined tridimentional structure distintive of intrinsically disordered proteins.
Protein: DP01945 (UniProt A0A2K8FR49)
Region: residues 1	to 172
Annotation: disorder (Structural state)
Evidence: far-UV circular dichroism evidence used in manual assertion
Supporting statements:
The lack of a temperature-induced transition strongly suggests that if secondary structure segments are formed, those segments are fluctuating and do not participate in the compact core structure.
Protein: DP01946 (UniProt S6AWC2)
Region: residues 1	to 158
Annotation: disorder (Structural state)
Evidence: nuclear magnetic resonance spectroscopy evidence used in manual assertion
Supporting statements:
No significant secondary shifts were observed in the high-field-shifted methyl region (0–1.0 p.p.m.), suggesting that hydrophobic side chains including aromatic rings do not form any clustered regions in WCI16. [...] WCI16 does not form definitive secondary structure, such as an α-helix or β-strand. [...] there is no significant specific three-dimensional structure in WCI16.
Protein: DP01947 (UniProt O65934)
Region: residues 104	to 230
Annotation: disorder (Structural state)
Evidence: nuclear magnetic resonance spectroscopy evidence used in manual assertion
Supporting statements:
In addition to lacking any predominant secondary structure, the linker residues exhibited MICS-calculated random coil index squared order parameters (RCI-S2) indicative of conformational disorder
Protein: DP01947 (UniProt O65934)
Region: residues 104	to 230
Annotation: protein binding (Molecular function)
Evidence: nuclear magnetic resonance spectroscopy evidence used in manual assertion
Supporting statements:
FHA-1 and FHA-2 Bind the Phosphorylated Linker to Form Inter- and Intramolecular Complexes
FHA-2 Exhibits Larger NMR Spectral Perturbations than FHA-1 upon Phosphopeptide Binding

The NMR-monitored titration experiments also provide insights into the mechanism of phosphopeptide binding. When mapped onto the structures of FHA-1 and FHA-2, residues showing pronounced amide chemical shift perturbations upon addition of either the pT152 or pT210 peptides cluster near the canonical FHA domain binding interface (Figures 4B–4D). However, a visual comparison of the 15 N-HSQC titration spectra presented in Figures 4A, S4, and S5 shows clear differences in the effects of the peptides on the two FHA domains. In the case of FHA-1, only a relatively small number of amides had perturbed NMR signals and, of those, most exhibited progressive chemical shift changes upon titration with either phosphopeptide
Overall, our NMR titrations reveal that pT152 and pT210 phosphopeptide binding leads to significantly more amides showing larger chemical shift perturbations and exchange broadening in FHA-2 compared with FHA-1. 
FHA-1 and FHA-2 Bind the Phosphorylated Linker to Form Inter- and Intramolecular Complexes
Protein: DP01947 (UniProt O65934)
Region: residues 104	to 230
Annotation: flexible linker (Disorder function)
Evidence: nuclear magnetic resonance spectroscopy evidence used in manual assertion
Supporting statements:
Rv1747 has a cytoplasmic regulatory module consisting of two pThr-interacting Forkhead-associated (FHA) domains connected by a conformationally disordered linker with two phospho-acceptor threonines (pThr).
Rv1747 Regulatory Module Is Composed of Independent FHA-1 and FHA-2 Domains Joined by a Disordered Linker
Collectively, these data demonstrate that the Rv1747 regulatory module has a beads-on-a-string organization with two structurally independent FHA domains joined by an ID linker.