LiteFold/DisProt huggingface dataset:
Protein: DP03628 (UniProt P52732)
Region: residues 1	to 14
Annotation: disorder (Structural state)
Evidence: X-ray crystallography-based structural model with missing residue coordinates used in manual assertion
Supporting statements:
The authors didn't specify the state of the first 14 residues, but were not observed in the PDB
Cross-references: PDB:3WPN
Protein: DP03629 (UniProt Q9QR99)
Region: residues 100	to 130
Annotation: disorder (Structural state)
Evidence: nuclear magnetic resonance spectroscopy evidence used in manual assertion
Supporting statements:
The MA structure consists of four a-helices and unstructured N- and C-termini.
2D 1H-15N HSQC data obtained for myr(–)MA and myr(–)MA99 confirmed that truncation of the C-terminal 31 residues did not adversely affect the structure and/or fold of the globular domain (Figures 1(A) and S2).
Protein: DP03629 (UniProt Q9QR99)
Region: residues 100	to 130
Annotation: disorder (Structural state)
Evidence: gel-filtration evidence used in manual assertion
Supporting statements:
The MA structure consists of four a-helices and unstructured N- and C-termini.
A gel filtration mobility assay with known protein standards revealed that the estimated molecular weight of myr(–)MA and myr(–) MA99 proteins are ~24 and 10 kDa, respectively (Figure S1). Whereas the estimated molecular weight of myr(–)MA appears to be higher than the calculated monomeric unit (~15 kDa), no evidence for protein self-association was observed at all tested protein concentrations. The migration behavior of myr(–)MA is likely attributed to its shape caused by the unstructured C-terminal 31 residues.
Protein: DP03630 (UniProt P07197)
Region: residues 790	to 916
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).
The Rh of wt NFM (3.31 ± 0.12) is determined here for the first time.
Experimentally determined Rh is even greater than the theoretical Rh for IDPs [Marsh & Forman-Kay, 2010].
Rt (nm) = 2.54
Protein: DP03630 (UniProt P07197)
Region: residues 790	to 916
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: DP03630 (UniProt P07197)
Region: residues 790	to 916
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 NFM.
Protein: DP03631 (UniProt P0A9J4)
Region: residues 294	to 303
Annotation: disorder (Structural state)
Evidence: X-ray crystallography-based structural model with missing residue coordinates used in manual assertion
Supporting statements:
The final structure includes residues 1-293 of KPR in complex with one molecule of bound NADP+.
The C-terminal 10 residues were disordered in the electron density and were not rebuilt. This reflects the situation in the apo crystal structure where the C-terminal 12 residues are disordered (14).
Cross-references: PDB:1YJQ
Protein: DP03632 (UniProt P49954)
Region: residues 132	to 141
Annotation: disorder (Structural state)
Evidence: X-ray crystallography-based structural model with missing residue coordinates used in manual assertion
Supporting statements:
The two α/β halves of the structure are connected at one end by 28 residues containing helix α4 and a disordered region between β5 and β6, and at the other by a six-residue loop between β11 and β12.
An internal loop region of 10 residues (132–141) and nine C-terminal residues are disordered and are not detected in the electron density of either monomer.
This cysteine is more accessible in P018 (16 Å2) than in DCases (8 Å2). However, this may be an artifact of missing residues 132–141 in P018.
Cross-references: PDB:1F89
Protein: DP03633 (UniProt P36421)
Region: residues 224	to 233
Annotation: disorder (Structural state)
Evidence: X-ray crystallography-based structural model with missing residue coordinates used in manual assertion
Supporting statements:
Residues 224–233 of SceTyrRS, the base moieties 16, 20, 31, 40, 41 and 46 of tRNATyr, and the whole nucleotides 17, 20a, 20b, 32 and 33 of tRNATyr, were disordered.
A loop region between the two domains (residues 224–233), including the KMSKS signature motif, which is one of the two consensus motifs conserved among the class I aaRSs, is disordered.
In the present structure of SceTyrRS, residues 224–233, including the KMSAS sequence (Figure 3), are disordered. This flexibility of the loop containing the KMSKS motif would allow the Tyr-AMP to be fully exposed and the 3′-CCA terminus of tRNA to access the aminoacyl transfer center.
Cross-references: PDB:2DLC
Protein: DP03633 (UniProt P36421)
Region: residues 224	to 233
Annotation: flexible linker (Disorder function)
Evidence: X-ray crystallography-based structural model with missing residue coordinates used in manual assertion
Supporting statements:
A loop region between the two domains (residues 224–233), including the KMSKS signature motif, which is one of the two consensus motifs conserved among the class I aaRSs, is disordered.
Cross-references: PDB:2DLC
Protein: DP03634 (UniProt Q92784-2)
Region: residues 60	to 200
Annotation: disorder (Structural state)
Evidence: combinatorial experimental and curator inference evidence used in manual assertion
Supporting statements:
Predictions, spectroscopy, and dynamic light scattering have revealed a high content in disorder: prevalence of random coil, aromatic residues partially to fully exposed to the solvent, and large hydrodynamic diameters.
From the N-terminus, the disorder profile includes the 2/3 domain (and beyond), which is considered mostly ordered (residues 1 to 90), although disorder scores varying between 0.2 and 0.5 indicate some chain flexibility, especially from residues 60 to 90. This is followed by a 110-residue-long IDR (IDR-1) up to the C2H2 zinc finger (ZnF), where the disorder score drops below the 0.5 threshold (residues 199 to 220), though retaining some flexibility.
Predictions and experimental evidence have been consistent with both isoforms being highly disordered proteins. CD spectroscopy has revealed similar footprints dominated by random coil, and measured hydrodynamic diameters by DLS indicate that they adopt expanded conformations. DPF3a has also exhibited more intrinsic disorder than DPF3b, as highlighted by structural predictors, UV–visible absorption spectroscopy, and the presence of additional IDR and MoRFs in its C-terminal domain.
The boundaries of this disordered region were determined by the combination of the structural predictors used in the publication (PONDR and IUPred), AlphaFold and Mobi DB.
Protein: DP03634 (UniProt Q92784-2)
Region: residues 222	to 259
Annotation: disorder (Structural state)
Evidence: combinatorial experimental and curator inference evidence used in manual assertion
Supporting statements:
Predictions, spectroscopy, and dynamic light scattering have revealed a high content in disorder: prevalence of random coil, aromatic residues partially to fully exposed to the solvent, and large hydrodynamic diameters.
A second shorter 40-residue-long IDR (IDR-2) is found between the C2H2 and PHD1 ZnFs (residues 221–260), followed by a gain in order at the level of the PHD1 finger (residues 261–292).
Predictions and experimental evidence have been consistent with both isoforms being highly disordered proteins. CD spectroscopy has revealed similar footprints dominated by random coil, and measured hydrodynamic diameters by DLS indicate that they adopt expanded conformations. DPF3a has also exhibited more intrinsic disorder than DPF3b, as highlighted by structural predictors, UV–visible absorption spectroscopy, and the presence of additional IDR and MoRFs in its C-terminal domain.
The boundaries of this disordered region were determined by the combination of the structural predictors used in the publication (PONDR and IUPred), AlphaFold and Mobi DB.
Protein: DP03634 (UniProt Q92784-2)
Region: residues 293	to 357
Annotation: disorder (Structural state)
Evidence: combinatorial experimental and curator inference evidence used in manual assertion
Supporting statements:
Predictions, spectroscopy, and dynamic light scattering have revealed a high content in disorder: prevalence of random coil, aromatic residues partially to fully exposed to the solvent, and large hydrodynamic diameters.
Towards the C-terminus, where isoforms sequence composition differs, DPF3b remains fully ordered due to the PHD2 ZnF (residues 293–378, Fig. 1B), whilst DPF3a shows a third 60-residue-long IDR (IDR-3) with high disorder scores (residues 293–357, Fig. 2).
Predictions and experimental evidence have been consistent with both isoforms being highly disordered proteins. CD spectroscopy has revealed similar footprints dominated by random coil, and measured hydrodynamic diameters by DLS indicate that they adopt expanded conformations. DPF3a has also exhibited more intrinsic disorder than DPF3b, as highlighted by structural predictors, UV–visible absorption spectroscopy, and the presence of additional IDR and MoRFs in its C-terminal domain.
The boundaries of this disordered region were determined by the combination of the structural predictors used in the publication (PONDR and IUPred), AlphaFold and Mobi DB.
Protein: DP03635 (UniProt P81605)
Region: residues 77	to 87
Annotation: disorder (Structural state)
Evidence: nuclear magnetic resonance spectroscopy evidence used in manual assertion
Supporting statements:
The α-helical structure of the N-terminal part of the peptide was preserved in membranes of different lipid compositions and at various peptide-to-lipid molar ratios, but the C-terminus was disordered and did not fold into a well-defined α-helical conformation.
Cross-references: PDB:2KSG
Protein: DP03635 (UniProt P81605)
Region: residues 63	to 87
Annotation: disorder (Structural state)
Evidence: far-UV circular dichroism evidence used in manual assertion
Supporting statements:
In 10 mM phosphate buffer (PB), a line shape typical of disordered peptides was found with negative ellipticities over the full spectral range from 185 to 260 nm and a pronounced negative CD band at approximately 198 nm.
Protein: DP03635 (UniProt P81605)
Region: residues 63	to 87
Annotation: lipid binding (Molecular function)
Evidence: nuclear magnetic resonance spectroscopy evidence used in manual assertion
Supporting statements:
Structure analysis of the membrane-bound dermcidin-derived peptide SSL-25 from human sweat.
Protein: DP03635 (UniProt P81605)
Region: residues 63	to 87
Annotation: disorder to order (Structural transition)
Evidence: far-UV circular dichroism evidence used in manual assertion
Supporting statements:
Like many AMPs, SSL-25 is unstructured in solution but folds into an amphipathic α-helix after binding to a membrane, as shown here by CD analysis (Fig. 2A).
Protein: DP03635 (UniProt P81605)
Region: residues 63	to 110
Annotation: disorder to order (Structural transition)
Evidence: circular dichroism evidence used in manual assertion
Supporting statements:
A, anionic DCD-1L is unstructured in aqueous solution according to CD and NMR. B, upon binding to a bacterial membrane the peptide folds into an amphiphilic α-helix, which is aligned parallel to the membrane surface according to OCD.
Protein: DP03635 (UniProt P81605)
Region: residues 63	to 110
Annotation: lipid binding (Molecular function)
Evidence: circular dichroism evidence used in manual assertion
Supporting statements:
A, anionic DCD-1L is unstructured in aqueous solution according to CD and NMR. B, upon binding to a bacterial membrane the peptide folds into an amphiphilic α-helix, which is aligned parallel to the membrane surface according to OCD.
and NMR. Upon binding to a bacterial membrane the peptide folds into an amphiphilic alpha-helix.
Protein: DP03635 (UniProt P81605)
Region: residues 63	to 110
Annotation: disorder (Structural state)
Evidence: circular dichroism evidence used in manual assertion
Supporting statements:
B, CD measurements of DCD-1L in water show an unstructured conformation, which changes into an α-helix in the detergents LDAO or DDM.
Protein: DP03635 (UniProt P81605)
Region: residues 63	to 110
Annotation: defense response to bacterium (Biological process)
Evidence: colony counting evidence used in manual assertion
Supporting statements:
We noticed that addition of divalent (Zn2+, Ca2+, Mg2+) and monovalent (Na+) ions enhances the antimicrobial activity of DCD-1L against S. aureus 113 significantly (Fig. 2C).
Protein: DP03635 (UniProt P81605)
Region: residues 63	to 110
Annotation: ion channel activity (Molecular function)
Evidence: reconstituted bilayer single-channel patch recording evidence used in manual assertion
Supporting statements:
The results clearly show that DCD-1L is very potent in ion channel formation after an initial reconstitution, which takes several minutes. An example for a recording at 50 mV is illustrated in Fig. 4A, showing the initial reconstitution of a peptide channel in the black lipid bilayer. Once inserted into the membrane, the current increases stepwise until the membrane finally breaks. The insertion of the first channel appears to trigger subsequent insertions and suggests a self-enhancing, cooperative mechanism of pore formation.
Due to the comparable conductance in either LiCl or potassium acetate, we conclude that the DCD-1L channel is neither anion- nor cation-selective.
Protein: DP03637 (UniProt Q8NC51)
Region: residues 149	to 288
Annotation: disorder (Structural state)
Evidence: nuclear magnetic resonance spectroscopy evidence used in manual assertion
Supporting statements:
Analysis of the Cα, Cβ, C’, HN, N, and Hα chemical shifts using the Secondary Structure Propensity (SSP) algorithm (Marsh et al., 2006) indicate that the majority of SERBP1 189–400 is disordered, except for residues 289–299, which have significant α-helical character (Figure 2A).
Protein: DP03637 (UniProt Q8NC51)
Region: residues 300	to 400
Annotation: disorder (Structural state)
Evidence: nuclear magnetic resonance spectroscopy evidence used in manual assertion
Supporting statements:
Analysis of the Cα, Cβ, C’, HN, N, and Hα chemical shifts using the Secondary Structure Propensity (SSP) algorithm (Marsh et al., 2006) indicate that the majority of SERBP1 189–400 is disordered, except for residues 289–299, which have significant α-helical character (Figure 2A).
Protein: DP03637 (UniProt Q8NC51)
Region: residues 387	to 400
Annotation: RNA binding (Molecular function)
Evidence: nuclear magnetic resonance evidence used in manual assertion
Supporting statements:
Plotting the maximal CSP (Δδmax) against the protein sequence reveals that the RNA interacts with residues spanning from the second RGG box to the C-terminus of SERBP1, with some Δδmax higher than 0.1 ppm (e.g., N383, T388, S394) (Figure 5B).
Protein: DP03637 (UniProt Q8NC51)
Region: residues 149	to 188
Annotation: non-membrane-bounded organelle (Cellular component)
Evidence: fluorescence recovery after photobleaching evidence used in manual assertion
Supporting statements:
At neutral pH, SERBP1 149–400 readily phase separates at a concentration of 10 µM in absence of NaCl.
Conversely, SERBP1 189–400 does not phase separate at all under the same physiochemical conditions (Supplementary Figure S8B).
Protein: DP03639 (UniProt P03101)
Region: residues 486	to 505
Annotation: disorder (Structural state)
Evidence: cryogenic electron microscopy evidence used in manual assertion
Supporting statements:
Flexibility analysis suggested that variation in capsid diameter is due to variable contraction or expansion of the flexible C-terminal arms linking the capsomers, which in turn move as rigid bodies.
Cross-references: PDB:7KZF
Protein: DP03639 (UniProt P03101)
Region: residues 486	to 505
Annotation: flexible C-terminal tail (Disorder function)
Evidence: cryogenic electron microscopy evidence used in manual assertion
Supporting statements:
Flexibility analysis suggested that variation in capsid diameter is due to variable contraction or expansion of the flexible C-terminal arms linking the capsomers, which in turn move as rigid bodies.
Cross-references: PDB:7KZF
Protein: DP03641 (UniProt Q9AXT8)
Region: residues 310	to 337
Annotation: disorder (Structural state)
Evidence: x-ray crystallography evidence used in manual assertion
Supporting statements:
Some disordered regions were not built in the final model and are shown as dashed lines.
Cross-references: PDB:4FT2
Protein: DP03641 (UniProt Q9AXT8)
Region: residues 417	to 441
Annotation: disorder (Structural state)
Evidence: x-ray crystallography evidence used in manual assertion
Supporting statements:
Some disordered regions were not built in the final model and are shown as dashed lines.
Cross-references: PDB:4FT2
Protein: DP03641 (UniProt Q9AXT8)
Region: residues 519	to 533
Annotation: disorder (Structural state)
Evidence: x-ray crystallography evidence used in manual assertion
Supporting statements:
Some disordered regions were not built in the final model and are shown as dashed lines.
Cross-references: PDB:4FT2
Protein: DP03641 (UniProt Q9AXT8)
Region: residues 887	to 912
Annotation: disorder (Structural state)
Evidence: x-ray crystallography evidence used in manual assertion
Supporting statements:
Some disordered regions were not built in the final model and are shown as dashed lines.
Cross-references: PDB:4FT2
Protein: DP03641 (UniProt Q9AXT8)
Region: residues 157	to 169
Annotation: disorder (Structural state)
Evidence: x-ray crystallography evidence used in manual assertion
Supporting statements:
Some disordered regions were not built in the final model and are shown as dashed lines.
Cross-references: PDB:4FT2
Protein: DP03642 (UniProt B4FUM2)
Region: residues 1	to 73
Annotation: disorder (Structural state)
Evidence: x-ray crystallography evidence used in manual assertion
Supporting statements:
In Zm-FNR2, the N-terminal was poorly resolved, presumably due to a high degree of flexibility.
Cross-references: PDB:3VO2
Protein: DP03643 (UniProt Q6L4L4)
Region: residues 87	to 105
Annotation: disorder (Structural state)
Evidence: nuclear magnetic resonance evidence used in manual assertion
Supporting statements:
The N-terminal 13 residues of ScSiz1 and the C-terminal 19 residues of OsSiz1 that are highly flexible are omitted to make the figures clear.
Cross-references: PDB:2RNO
BMRB:11030
Protein: DP03644 (UniProt D3TI84)
Region: residues 187	to 244
Annotation: disorder (Structural state)
Evidence: x-ray crystallography evidence used in manual assertion
Supporting statements:
Although the ~55 residue linker between CARD2 and Hel1 is invisible in the electron density due to disorder, the monomeric state of free RIG-I (Figure S3) indicates that the CARDs most likely bind to the Hel2i domain of the same molecule, rather than being swapped between monomers. 
Cross-references: PDB:4A2W
Protein: DP03644 (UniProt D3TI84)
Region: residues 492	to 503
Annotation: disorder (Structural state)
Evidence: x-ray crystallography evidence used in manual assertion
Supporting statements:
The PDB shows that this region lacks electron density, therefore indicating it is disordered.
Cross-references: PDB:4A2W
Protein: DP03644 (UniProt D3TI84)
Region: residues 663	to 690
Annotation: disorder (Structural state)
Evidence: x-ray crystallography evidence used in manual assertion
Supporting statements:
The PDB shows that this region lacks electron density, therefore indicating it is disordered.
Cross-references: PDB:4A2W
Protein: DP03644 (UniProt D3TI84)
Region: residues 795	to 933
Annotation: disorder (Structural state)
Evidence: x-ray crystallography evidence used in manual assertion
Supporting statements:
The PDB shows that this region lacks electron density, therefore indicating it is disordered.
Cross-references: PDB:4A2W
Protein: DP03644 (UniProt D3TI84)
Region: residues 806	to 899
Annotation: disorder to order (Structural transition)
Evidence: x-ray crystallography evidence used in manual assertion
Supporting statements:
 Conformational change of the dRIG-I helicase
domain upon ligand binding. The open state is
in orange (1–933, chain A), and the closed state
arising from simultaneous dsRNA (red and purple
strands) and ADP-AlF3-Mg++ (not shown) binding
is in black. 
Cross-references: PDB:4A2W
PDB:4A2X
Protein: DP03644 (UniProt D3TI84)
Region: residues 806	to 933
Annotation: RNA binding (Molecular function)
Evidence: x-ray crystallography evidence used in manual assertion
Supporting statements:
Despite the modest resolution, the structure is well defined, with clear electron density for the ADP-AlF3-Mg++ (Figure S2B) and the RNA (Figure S2C).
Cross-references: PDB:4A2X
Protein: DP03644 (UniProt D3TI84)
Region: residues 905	to 933
Annotation: disorder to order (Structural transition)
Evidence: x-ray crystallography evidence used in manual assertion
Supporting statements:
Conformational change of the dRIG-I helicase domain upon ligand binding. The open state is in orange (1–933, chain A), and the closed state arising from simultaneous dsRNA (red and purple strands) and ADP-AlF3-Mg++ (not shown) binding is in black. 
Cross-references: PDB:4A2W
PDB:4A2X
Protein: DP03645 (UniProt Q9Y4D1)
Region: residues 654	to 682
Annotation: disorder (Structural state)
Evidence: X-ray crystallography-based structural model with missing residue coordinates used in manual assertion
Supporting statements:
The Daam1 FH2 domain consists of an N-terminal “lasso” segment, a flexible linker that is largely disordered in the present structure, and a rod-shaped domain formed by three sub-domains termed the “knob”, “coiled-coil”, and “post”.
Although the linker is disordered, we can unambiguously assign the connectivity as that required to form the head-to-tail dimer shown in Figure 1(c) because the 30 residue linker is not long enough to allow intra-subunit interaction, nor is it long enough to connect the other pairs of subunits related by crystallographic symmetry in this space group (I222). 
The relative orientation of the two hemidimers in the present structure is quite different from that previously observed in Bni1, the divergent orientation is readily accommodated by rearrangement of the disordered linker segment.
The C-terminal tail region, including the DAD domain (residues 1025–1078), and the linker segment (residues 654–682) were not observed in the electron density map and are presumed to be disordered.
Cross-references: PDB:2J1D
Protein: DP03646 (UniProt Q76KU6)
Region: residues 567	to 586
Annotation: disorder (Structural state)
Evidence: x-ray crystallography evidence used in manual assertion
Supporting statements:
The disordered catalytic loop (CL) is shown by a dashed line.
Cross-references: PDB:4ONQ
Protein: DP03647 (UniProt Q9M2T2)
Region: residues 10	to 55
Annotation: disorder (Structural state)
Evidence: nuclear magnetic resonance evidence used in manual assertion
Supporting statements:
In the solution structure of the protein, secondary structural elements are formed by residues 3–9 (β1), 56–62 (β2), 133–135 (β3), and 96–110 (α-helix). Most of the rest of the chain segments are disordered.
Cross-references: PDB:5YQ3
Protein: DP03647 (UniProt Q9M2T2)
Region: residues 63	to 95
Annotation: disorder (Structural state)
Evidence: nuclear magnetic resonance evidence used in manual assertion
Supporting statements:
In the solution structure of the protein, secondary structural elements are formed by residues 3–9 (β1), 56–62 (β2), 133–135 (β3), and 96–110 (α-helix). Most of the rest of the chain segments are disordered.
Cross-references: PDB:5YQ3