LiteFold/DisProt huggingface dataset:
Protein: DP03332 (UniProt P0A3B2)
Region: residues 32	to 47
Annotation: disorder (Structural state)
Evidence: X-ray crystallography-based structural model with missing residue coordinates used in manual assertion
Supporting statements:
The switch I region of BipA, which was disordered in all of the isolated structures as mentioned above, can be visualized in the presence of the ribosome (Fig. S3D), allowing us to explore the structural basis of GTPase activation by BipA.
Cross-references: PDB:5A9W
Protein: DP03332 (UniProt P0A3B2)
Region: residues 32	to 47
Annotation: disorder to order (Structural transition)
Evidence: cryogenic electron microscopy evidence used in manual assertion
Supporting statements:
The switch I region of BipA, which was disordered in all of the isolated structures as mentioned above, can be visualized in the presence of the ribosome (Fig. S3D), allowing us to explore the structural basis of GTPase activation by BipA.
The switch I region of BipA is ordered upon binding to ribosome. In addition to interacting with the GTP analog (GDPCP), the switch I region (Phe32 and Asp33) is stabilized by bilateral contacts with the SRL of the 50S subunit and h8 of the 30S subunit (Fig. 3B), resulting in an ordered structure.
Cross-references: PDB:5A9Z
Protein: DP03333 (UniProt P0AFF6)
Region: residues 201	to 495
Annotation: disorder (Structural state)
Evidence: cryogenic electron microscopy-based structural model with missing residue coordinates used in manual assertion
Supporting statements:
We observed clear density for the first 200 residues of NusA in the PTC60 map (Figures 2A and S4B); the more flexible NusA-CTD was not resolved.
Cross-references: PDB:6XAS
EMDB:EMD-22114
Protein: DP03333 (UniProt P0AFF6)
Region: residues 201	to 495
Annotation: disorder to order (Structural transition)
Evidence: cryogenic electron microscopy evidence used in manual assertion
Supporting statements:
The region characterized as unfolded was folded upon interaction.
Cross-references: PDB:6TQO
EMDB:EMD-10548
Protein: DP03333 (UniProt P0AFF6)
Region: residues 201	to 425
Annotation: disorder to order (Structural transition)
Evidence: cryogenic electron microscopy evidence used in manual assertion
Supporting statements:
The region characterized as unfolded was folded upon interaction.
Cross-references: PDB:5MS0
EMDB:EMD-3561
Protein: DP03334 (UniProt P90947)
Region: residues 527	to 537
Annotation: disorder (Structural state)
Evidence: X-ray crystallography-based structural model with missing residue coordinates used in manual assertion
Supporting statements:
The italicized residues are not visible in the structure
Several cycles of refinement with PHENIX (32) and manual rebuilding with COOT (33) were run to generate the final model, which consists of one copy with residues 270–352,356–526, and 538–641 and the other with residues 270–347,355–526, 540–606, and 609–640
Italicized residues on hrmp-1 sequence corresponds to residues 527-537 of Uniprot sequence
Cross-references: PDB:5H5M
Protein: DP03335 (UniProt P42573)
Region: residues 370	to 406
Annotation: disorder (Structural state)
Evidence: X-ray crystallography-based structural model with missing residue coordinates used in manual assertion
Supporting statements:
In contrast, the active site in the adjacent CED-3 molecule does not have a well-defined conformation, with the L2 loop largely disordered in the crystals'
L2 loop is located in 370-406 region
Cross-references: PDB:4M9R
Protein: DP03336 (UniProt P12996)
Region: residues 316	to 346
Annotation: disorder (Structural state)
Evidence: X-ray crystallography-based structural model with missing residue coordinates used in manual assertion
Supporting statements:
The structure of BioB has been determined to 3.4 Å resolution by iron multi-wavelength anomalous dispersion (MAD) techniques (21). The fold of each subunit of the BioB dimer is a triosephosphate isomerase (TIM) type (α/β)8 barrel, with two additional helices at the N terminus and a disordered region at the C terminus (Fig. 1).
Cross-references: PDB:1R30
Protein: DP03337 (UniProt P0A9H7)
Region: residues 2	to 13
Annotation: disorder (Structural state)
Evidence: X-ray crystallography-based structural model with missing residue coordinates used in manual assertion
Supporting statements:
The first 13 residues of the N-domain were disordered, as were residues from 100 to 120, which comprise a linker to the C-domain.
Cross-references: PDB:6BQC
Protein: DP03337 (UniProt P0A9H7)
Region: residues 100	to 120
Annotation: disorder (Structural state)
Evidence: X-ray crystallography-based structural model with missing residue coordinates used in manual assertion
Supporting statements:
The first 13 residues of the N-domain were disordered, as were residues from 100 to 120, which comprise a linker to the C-domain.
Cross-references: PDB:6BQC
Protein: DP03337 (UniProt P0A9H7)
Region: residues 100	to 120
Annotation: flexible linker (Disorder function)
Evidence: cleavage assay evidence used in manual assertion
Supporting statements:
The linker (100-120 aa) connects N- and C-domains.
Digestion of CFA synthase with a low concentration of trypsin
resulted in two major polypeptide fragments (Figure 3B, inset).
Analysis by sequential Edman degradation showed that cleavage
occurs between Arg111 and Ala112, in the linker between
the N- and C-domains. Following tryptic cleavage, the N- and
C-terminal fragments remained associated during gel-filtration
chromatography (Figure 3B).
Protein: DP03337 (UniProt P0A9H7)
Region: residues 100	to 120
Annotation: flexible linker (Disorder function)
Evidence: X-ray crystallography-based structural model with missing residue coordinates used in manual assertion
Supporting statements:
The first 13 residues of the N-domain were disordered, as were residues from 100 to 120, which comprise a linker to the C-domain.
The interface between the N- and C-domains is formed by an
extensive network of contacts between the a3 and a4 helices of
the N-domain and the a14 and a18 helices of the C-domain
(Figure 2C). The surface buried in this interface was calculated
to be 1,800 A°2 (Fraczkiewicz and Braun, 1998), representing
34% of the total surface area of the N-domain. A linker must
connect residue 99 in the N-domain with residue 121 in the
C-domain, a distance of 30 A°. However, electron density was
either poor or absent for these linker residues, suggesting that
they adopt multiple conformations.
Cross-references: PDB:6BQC
Protein: DP03338 (UniProt Q9A8N4)
Region: residues 1	to 133
Annotation: disorder (Structural state)
Evidence: nuclear magnetic resonance spectroscopy evidence used in manual assertion
Supporting statements:
The intrinsic disorder of PopZΔ134–177 is shown by the 2D 1H-15N HSQC spectrum with the characteristic narrow 1H chemical shift dispersion typically seen for IDPs (Figure S1), with the exception of sidechain amine and amide resonances from arginine and glutamine residues, respectively. Comparatively, ordered proteins tend to have a wider dispersion of 1H resonances than proteins without a well-defined fold.49 The disordered nature of PopZΔ134–177 is further supported by the distinct lack of abundance of long-range interactions in 1H-15N NOESY data. 
The 20 predicted structures show no other well folded secondary structure elements besides an N-terminal α-helix (M10-I17) (Figure 2).
PopZ (1-133) is globally unstructured but retains a short helical motif between residues (M10-I17) according to NMR data.
Cross-references: PDB:6XRY
Protein: DP03338 (UniProt Q9A8N4)
Region: residues 1	to 133
Annotation: disorder (Structural state)
Evidence: nuclear magnetic resonance spectroscopy evidence used in manual assertion
Supporting statements:
To determine the extent of structural disorder in this region of PopZ experimentally, we purified the PopZΔ134–177 fragment and analyzed it using solution NMR spectroscopy and circular dichroism. The 2D 1H-15N heteronuclear single quantum correlation (HSQC) spectrum (Fig. 5C, red signal, and SI Appendix, Fig. S7) shows well-defined peaks with roughly uniform intensities and line shapes for the majority of resonances. Notably, all the backbone proton peaks were clustered in the 7.80–8.85-ppm region. This narrow dispersion of proton chemical shifts is a strong indicator of an intrinsically disordered protein, compared with well-ordered proteins, which exhibit more broadly distributed peaks in the proton dimension (21).
Protein: DP03338 (UniProt Q9A8N4)
Region: residues 1	to 133
Annotation: disorder (Structural state)
Evidence: far-UV circular dichroism evidence used in manual assertion
Supporting statements:
Circular dichroism analysis suggests that PopZ∆134–177 is mostly composed of random coil (Fig. 5B), providing further evidence of structural disorder.
Protein: DP03338 (UniProt Q9A8N4)
Region: residues 9	to 23
Annotation: molecular function regulator (Molecular function)
Evidence: nuclear magnetic resonance spectroscopy evidence used in manual assertion
Supporting statements:
Binding residues were determined by comparing combined ΔHN chemical shifts for each
residue, where peaks undergoing a shift greater than the standard deviation were considered
binding [63]. Combined ΔHN chemical shift perturbations (Figure 3(C)) and peak intensity perturbations (Figure S7) of PopZΔ134-177 upon binding to RcdA reveals that the binding motif of PopZΔ134-177 is between T9-E23 (Figures 4 and S8), as peaks corresponding to these residues undergo both significant chemical shift perturbations and line broadening most likely due to direct interaction with RcdA, although potential secondary structure changes cannot be excluded.
We therefore conclude that residues T9-E23, which include an α-helix that spans M10-I17, act as a MoRF region that is directly responsible for interacting with at least two of its 15 binding partners.
Protein: DP03338 (UniProt Q9A8N4)
Region: residues 9	to 23
Annotation: protein binding (Molecular function)
Evidence: nuclear magnetic resonance spectroscopy evidence used in manual assertion
Supporting statements:
Combined ΔHN chemical shift perturbations (Figure 3(C)) and peak intensity perturbations (Figure S7) of PopZΔ134-177 upon binding to RcdA reveals that the binding motif of PopZΔ134-177 is between T9-E23 (Figures 4 and S8), as peaks corresponding to these residues undergo both significant chemical shift perturbations and line broadening most likely due to direct interaction with RcdA, although potential secondary structure changes cannot be excluded.
Protein: DP03338 (UniProt Q9A8N4)
Region: residues 1	to 133
Annotation: protein binding (Molecular function)
Evidence: nuclear magnetic resonance spectroscopy evidence used in manual assertion
Supporting statements:
To ask whether the structure of PopZ is affected by interaction with another protein, we repeated our NMR analysis on isotopically labeled PopZΔ134–177, after mixing with RcdA, ChpT, or a noninteracting control protein (Fig. 5C). Whereas the addition of the control protein had little effect on the spectra, the addition of RcdA or ChpT induced significant changes in some of the peaks. Notably, mixing with RcdA or ChpT affected the same set of resonances, suggesting these proteins interact with the same amino acids in PopZΔ134–177. Future analyses will determine whether the affected amino acids are in the N-terminal MoRF-like region, and whether this sequence adopts helical structure on binding
Protein: DP03338 (UniProt Q9A8N4)
Region: residues 1	to 133
Annotation: molecular function regulator (Molecular function)
Evidence: nuclear magnetic resonance spectroscopy evidence used in manual assertion
Supporting statements:
To ask whether the structure of PopZ is affected by interaction with another protein, we repeated our NMR analysis on isotopically labeled PopZΔ134–177, after mixing with RcdA, ChpT, or a noninteracting control protein (Fig. 5C). Whereas the addition of the control protein had little effect on the spectra, the addition of RcdA or ChpT induced significant changes in some of the peaks. Notably, mixing with RcdA or ChpT affected the same set of resonances, suggesting these proteins interact with the same amino acids in PopZΔ134–177. Future analyses will determine whether the affected amino acids are in the N-terminal MoRF-like region, and whether this sequence adopts helical structure on binding
Protein: DP03338 (UniProt Q9A8N4)
Region: residues 1	to 133
Annotation: self-assembly (Disorder function)
Evidence: microscopy evidence used in manual assertion
Supporting statements:
The polar organizing protein Z, PopZ, of Caulobacter functions as a hub protein.
The polar organizing protein Z (PopZ) is necessary for the formation of three-dimensional
microdomains at the cell poles in Caulobacter crescentus, where it functions as a hub protein
that recruits multiple regulatory proteins from the cytoplasm.
Here, RcdA was produced as a fusion protein with
green fluorescent protein (RcdA-GFP) and co-expressed with either full-length wildtype PopZ or
the full-length I17A mutant (each produced as fusions with mCherry for visualization by
fluorescence microscopy). Due to the presence of the C-terminal self-assembly domain in fulllength PopZ, both of the PopZ variants accumulated at the cell poles of the bacteria [39].. RcdAGFP exhibited strong co-localization with wildtype PopZ, but much weaker co-localization with
the I17A mutant, confirming the interaction defect
Protein: DP03338 (UniProt Q9A8N4)
Region: residues 1	to 133
Annotation: self-assembly (Disorder function)
Evidence: microscopy evidence used in manual assertion
Supporting statements:
Caulobacter PopZ forms an intrinsically disordered hub in organizing bacterial cell poles.
We used Escherichia coli cells to screen a pool of candidate proteins for the ability to interact with Caulobacter PopZ (Fig. 1 A–C). This was possible because PopZ self-assembles into macromolecular complexes that accumulate at E. coli cell poles (16), and these can be visualized as brightly fluorescent foci by expressing PopZ as a fusion with mCherry (mChy). When a PopZ binding protein such as ParA-GFP or GFP-ParB is coexpressed with mChy-PopZ, both proteins colocalize in polar foci (7, 16, 17).
Six other candidates exhibited the expected localization patterns for a PopZ binding protein: disperse when expressed without mChy-PopZ, and localized in polar foci with mChy-PopZ when the proteins were expressed simultaneously (Fig. 1C and SI Appendix, Figs. S1–S4).
Removing H3 and H4 (Δ134–177) from the DivIVA-mChy-PopZ fusion protein had no effect on the recruitment of binding partners (Fig. 4C), indicating that the homo-oligomerization and higher-order assembly determinants that enable polar localization of wild-type PopZ are not required for interactions with other proteins.
Protein: DP03339 (UniProt P07673)
Region: residues 1	to 105
Annotation: disorder (Structural state)
Evidence: nuclear magnetic resonance spectroscopy evidence used in manual assertion
Supporting statements:
In the 1
H–15N HSQC of IncC NTD, the peaks are
crowded in a narrow ~ 1 ppm (7.7–8.7 ppm) region of the
1
H dimension and many peaks overlap (Fig. 1a). This shows
that the protein is likely to be intrinsically disordered, as
expected from its sequence. 
The secondary chemical shifts of unmodifed IncC NTD
were examined using several programmes, namely CSI 3.0
(Hafsa et al. 2015), DANGLE (Cheung et al. 2010), TALOSN (Shen and Bax 2013), and SSP (Marsh et al. 2006). In
each case, the analysis suggests that the protein is nearly
entirely random coil.
Protein: DP03340 (UniProt O62479)
Region: residues 106	to 127
Annotation: disorder (Structural state)
Evidence: X-ray crystallography-based structural model with missing residue coordinates used in manual assertion
Supporting statements:
Loop α2-β5, which is unique to C. elegans, is not seen in the electron density presumably due to disorder and is indicated by a dashed line.
Cross-references: PDB:3PYI
Protein: DP03341 (UniProt P0A9D4)
Region: residues 263	to 273
Annotation: disorder (Structural state)
Evidence: X-ray crystallography-based structural model with missing residue coordinates used in manual assertion
Supporting statements:
Eleven residues from each of the 273-residue monomers are not visible at the carboxyl termini and the polyhistidine tag is not visible at the amino termini in the electron density maps (maps calculated with σA-weighted Fourier coefficients).
Cross-references: PDB:1T3D
Protein: DP03343 (UniProt Q9HCB6)
Region: residues 29	to 38
Annotation: disorder (Structural state)
Evidence: X-ray crystallography-based structural model with missing residue coordinates used in manual assertion
Supporting statements:
The construct actually begins at Phe29 after the signal peptide. The first 15 amino acid residues are mostly disordered in the crystal.
The first 14 N-termnal residues (FSDETLDKVPKSEG) and the last 10 C-terminal residues (DSTFDGVTDK) in the expression construct of the human F-spondin reelin-N domain in this study were not used for the alignment. Most of these residues are disordered in the structure.
The first 10 amino acid residues (29-38) are disordered in the crystal.
Cross-references: PDB:3COO
Protein: DP03343 (UniProt Q9HCB6)
Region: residues 185	to 198
Annotation: disorder (Structural state)
Evidence: X-ray crystallography-based structural model with missing residue coordinates used in manual assertion
Supporting statements:
As the quality of the electron-density map corresponding to the N-terminal nine residues (29–37, assuming that the mature protein starts with Phe29) and C-terminal 14 residues (185–198) of both molecules was poor, we omitted these segments from the final model.
Thus, the largely disordered N-terminal and C-terminal segments were removed, leaving the core 145-residue portion (Gly42–Ser186, referred to as FSP145).
Cross-references: PDB:2ZOT
Protein: DP03343 (UniProt Q9HCB6)
Region: residues 29	to 43
Annotation: disorder (Structural state)
Evidence: X-ray crystallography-based structural model with missing residue coordinates used in manual assertion
Supporting statements:
As the quality of the electron-density map corresponding to the N-terminal nine residues (29–37, assuming that the mature protein starts with Phe29) and C-terminal 14 residues (185–198) of both molecules was poor, we omitted these segments from the final model.
Thus, the largely disordered N-terminal and C-terminal segments were removed, leaving the core 145-residue portion (Gly42–Ser186, referred to as FSP145).
The N-terminal 15 residues (29-43) are completely missing in two chains and are presumably disordered. 
Cross-references: PDB:2ZOT
Protein: DP03344 (UniProt P36955)
Region: residues 21	to 35
Annotation: disorder (Structural state)
Evidence: X-ray crystallography-based structural model with missing residue coordinates used in manual assertion
Supporting statements:
However, 15 amino acids at the N terminus and 8 amino acids in the reactive center loop were not visible in the final electron density maps.
With the exception of the extreme 15 residues at the N terminus (residues 1–15) and 8 residues in the reactive center loop (residues 353–360), all of the molecule backbone is well ordered in the final crystal structure (Rcryst 18.8% and Rfree 22.7%; Table 1).
Region 1-15 corresponds to region 21-35 of the amino acid sequence.
Cross-references: PDB:1IMV
Protein: DP03344 (UniProt P36955)
Region: residues 22	to 26
Annotation: phosphorylation display site (Disorder function)
Evidence: mutant phenotype evidence used in manual assertion
Supporting statements:
CK2 phosphorylates PEDF on 2 main residues, Ser24 and Ser114, and PKA phosphorylates PEDF on one residue only, Ser227.
We report here that PEDF purified from human plasma is a phosphoprotein. It is phosphorylated in the serum mainly by CK2 on 2 main residues, Ser24 and Ser114, but also by PKA on Ser227.
Mutation of S24A significantly reduced CK2 phosphorylation (Figure 3), while the S24E mutation reduced phosphorylation only to a moderate extent. The S114A mutant significantly reduced CK2 phosphorylation, while the double mutant S24, 114A almost completely abolished this phosphorylation. We concluded that both Ser24 and Ser114 are the main sites for CK2 phosphorylation of PEDF.
Nonetheless, our results indicate that PEDF is phosphorylated by CK2 mainly on residues Ser24 and Ser114.
Protein: DP03345 (UniProt O00214)
Region: residues 154	to 175
Annotation: disorder (Structural state)
Evidence: X-ray crystallography-based structural model with missing residue coordinates used in manual assertion
Supporting statements:
In structures 4 and 5, the electron density of residues from Ser154 to the C-terminus was not visible, suggesting greater flexibility from this segment.
Cross-references: PDB:5GZF
PDB:5GZG
Protein: DP03345 (UniProt O00214)
Region: residues 154	to 175
Annotation: flexible linker (Disorder function)
Evidence: X-ray crystallography-based structural model with missing residue coordinates used in manual assertion
Supporting statements:
"In structures 4 and 5, the electron density of residues from Ser154 to the C-terminus was not visible, suggesting greater flexibility from this segment."
However, the conformation of these linkers remains unknown due likely to their high flexibility. 
Tandem-repeat-type galectins, like Gal-8, contain two distinct CRDs that are covalently connected via a peptide linker
Cross-references: PDB:5GZF
PDB:5GZG
Protein: DP03346 (UniProt P63090)
Region: residues 33	to 46
Annotation: disorder (Structural state)
Evidence: nuclear magnetic resonance spectroscopy evidence used in manual assertion
Supporting statements:
These studies show that HB-GAM contains two b-sheet domains connected by a flexible linker. Both of these domains contain three antiparallel b-strands. In addition to this domain structure, HB-GAM contains the N and C-terminal lysine-rich sequences that lack a detectable structure and appear to form random coils.
The N-terminal (amino acids 1–14) and C-terminal (amino acids 111–136) areas of HB-GAM are highly flexible, as indicated by the long T2 15N relaxation rates and by the heteronuclear NOE intensities presented in Fig. 4. For some parts of the flexible N and C termini it was not possible to obtain individual assignments because of strong overlap in 1H, 15N, and 13C frequencies (Fig. 1). Also, the linker (amino acids 59–66) shows some flexibility, as indicated by slightly longer 15N T2 and smaller NOE values.
The numbering is shifted since the authors don’t consider the residues in the signal peptide (res 1-32). Therefore, residue 1 corresponds to residue 33 and residue 136 corresponds to residue 168.
Protein: DP03346 (UniProt P63090)
Region: residues 133	to 168
Annotation: disorder (Structural state)
Evidence: nuclear magnetic resonance spectroscopy evidence used in manual assertion
Supporting statements:
These studies show that HB-GAM contains two b-sheet domains connected by a flexible linker. Both of these domains contain three antiparallel b-strands. In addition to this domain structure, HB-GAM contains the N and C-terminal lysine-rich sequences that lack a detectable structure and appear to form random coils.
The N-terminal (amino acids 1–14) and C-terminal (amino acids 111–136) areas of HB-GAM are highly flexible, as indicated by the long T2 15N relaxation rates and by the heteronuclear NOE intensities presented in Fig. 4. For some parts of the flexible N and C termini it was not possible to obtain individual assignments because of strong overlap in 1H, 15N, and 13C frequencies (Fig. 1). Also, the linker (amino acids 59–66) shows some flexibility, as indicated by slightly longer 15N T2 and smaller NOE values.
The numbering is shifted since the authors don’t consider the residues in the signal peptide (res 1-32). Therefore, residue 1 corresponds to residue 33 and residue 136 corresponds to residue 168.