LiteFold/DisProt huggingface dataset:
Protein: DP02069 (UniProt P38919)
Region: residues 1	to 20
Annotation: disorder (Structural state)
Evidence: X-ray crystallography-based structural model with missing residue coordinates used in manual assertion
Supporting statements:
No ordered electron density was present for the N-terminal region of eIF4AIII (residues 1–20) and for the N-terminal residues and a disordered loop of CWC22 (residues 116–122 and 142–148).
Cross-references: PDB:4C9B
Protein: DP02071 (UniProt P04383)
Region: residues 1	to 81
Annotation: disorder (Structural state)
Evidence: X-ray crystallography-based structural model with missing residue coordinates used in manual assertion
Supporting statements:
The  electron  density  maps  did  not  show  any  ordered  density  for  the  N-terminal  arm  of  any  of  three protein  subunits.
Cross-references: PDB:1OPO
Protein: DP02072 (UniProt Q13415)
Region: residues 662	to 673
Annotation: disorder (Structural state)
Evidence: cryogenic electron microscopy-based structural model with missing residue coordinates used in manual assertion
Supporting statements:
The helix of ORC1 that includes residues 661–674 is disordered in our structure, but by homology to ORC4, they would contain the R-finger as R666 and the tether as R670 in the proper position.
Cross-references: PDB:5UJ7
PDB:5UJM
Protein: DP02072 (UniProt Q13415)
Region: residues 471	to 489
Annotation: disorder (Structural state)
Evidence: cryogenic electron microscopy-based structural model with missing residue coordinates used in manual assertion
Supporting statements:
The PDB structures show this region lacks electron density, indicating it is disordered. 
Cross-references: PDB:5UJM
PDB:5UJ7
Protein: DP02073 (UniProt P33411)
Region: residues 198	to 217
Annotation: disorder (Structural state)
Evidence: X-ray crystallography-based structural model with missing residue coordinates used in manual assertion
Supporting statements:
The main chain electron density is continuous except for a 20-aa segment (Thr-198–Ala-217), which was disordered in both of the molecules in the asymmetric unit and could not be modeled reliably. 
Part of loop-5, residues 198–217, is disordered and appears to be entirely exposed to the solvent.
Cross-references: PDB:1DVK
Protein: DP02075 (UniProt P28300)
Region: residues 22	to 168
Annotation: disorder (Structural state)
Evidence: far-UV circular dichroism evidence used in manual assertion
Supporting statements:
Circular dichroism spectra of LOX-PP showed a single minimum near 200 nm, which is characteristic of an intrinsically disordered protein (IDP) (Fig. 2a). 
The presence of intrinsic disorder has been confirmed experimentally by CD and SAXS experiments. However, LOX-PP is partially structured as shown by deconvolution of CD spectra, which demonstrated the presence of a low amount of α-helix and β-strands.
Protein: DP02075 (UniProt P28300)
Region: residues 22	to 168
Annotation: disorder (Structural state)
Evidence: small-angle X-ray scattering evidence used in manual assertion
Supporting statements:
The experimental Rg/Rh ratio (1.2) was higher than 0.7, which indicates that LOX-PP behaves as a non-globular protein, and is likely to be extended, which is consistent with the presence of intrinsic disorder in LOX-PP. Furthermore, the Kratky plot was indicative of a non-globular natively unfolded molecule (Fig. 4c), and the normalized Kratky plot confirmed that LOX-PP is indeed flexible (Fig. 4d).
The presence of intrinsic disorder has been confirmed experimentally by CD and SAXS experiments. However, LOX-PP is partially structured as shown by deconvolution of CD spectra, which demonstrated the presence of a low amount of α-helix and β-strands.
Protein: DP02075 (UniProt P28300)
Region: residues 22	to 168
Annotation: protein binding (Molecular function)
Evidence: surface plasmon resonance evidence used in manual assertion
Supporting statements:
Potential partners of LOX-PP were screened by Surface Plasmon Resonance imaging (SPRi), SPR, and Bio-Layer Interferometry (BLI) (Supplementary Tables 6 and 7). We have identified 17 new partners of LOX-PP including four GAGs (chondroitin sulfate, dermatan sulfate, heparan sulfate, hyaluronan), collagen I, cross-linking and proteolytic enzymes (lysyl oxidase-like 2, transglutaminase-2, and MMP-2), one proteoglycan (fibromodulin), one matricryptin (anastellin), and the ectodomain of one membrane protein (Tumor Endothelial Marker-8 also known as anthrax receptor-137).
Protein: DP02075 (UniProt P28300)
Region: residues 22	to 168
Annotation: small molecule binding (Molecular function)
Evidence: surface plasmon resonance evidence used in manual assertion
Supporting statements:
Potential partners of LOX-PP were screened by Surface Plasmon Resonance imaging (SPRi), SPR, and Bio-Layer Interferometry (BLI) (Supplementary Tables 6 and 7). We have identified 17 new partners of LOX-PP including four GAGs (chondroitin sulfate, dermatan sulfate, heparan sulfate, hyaluronan), collagen I, cross-linking and proteolytic enzymes (lysyl oxidase-like 2, transglutaminase-2, and MMP-2), one proteoglycan (fibromodulin), one matricryptin (anastellin), and the ectodomain of one membrane protein (Tumor Endothelial Marker-8 also known as anthrax receptor-137).
Protein: DP02075 (UniProt P28300)
Region: residues 22	to 168
Annotation: protein binding (Molecular function)
Evidence: interferometric reflectance imaging sensor evidence used in manual assertion
Supporting statements:
Moreover, LOX-PP bound with very high affinity to tropoelastin and to plasminogen, and with high affinity to anastellin, a fragment of fibronectin (Table 3, Supplementary Fig. 8b).
Protein: DP02075 (UniProt P28300)
Region: residues 22	to 168
Annotation: molecular adaptor activity (Molecular function)
Evidence: surface plasmon resonance evidence used in manual assertion
Supporting statements:
 LOX-PP likely participates in collagen fibrillogenesis in association with fibromodulin, in fibronectin supramolecular assembly and in elastic fiber formation. Several LOX-PP partners such as fibrillar collagen I45, elastin10, fibronectin23, dermatopontin46,47, and fibromodulin48 bind to mature LOX, suggesting that both mature LOX and the propeptide are involved in ECM assembly and organization.
This suggests new roles for the propeptide in ECM assembly and cross-linking, cell-matrix adhesion, and in the regulation of EGF signaling pathways.
Protein: DP02076 (UniProt O69245)
Region: residues 1	to 37
Annotation: disorder (Structural state)
Evidence: X-ray crystallography-based structural model with missing residue coordinates used in manual assertion
Supporting statements:
Due to the lack of electron density at the N terminus, the first 37 amino acids of FixK2(C183S)-His6 could not be modeled.
Cross-references: PDB:4I2O
Protein: DP02077 (UniProt C6ECL5)
Region: residues 144	to 161
Annotation: disorder (Structural state)
Evidence: X-ray crystallography-based structural model with missing residue coordinates used in manual assertion
Supporting statements:
Residues that were not observed in the electron density map due to disorder include N-terminal residues 24–52 and C-terminal residues 144–161 ​[Fig. 3(C)].
Cross-references: PDB:3OEO
Protein: DP02077 (UniProt C6ECL5)
Region: residues 24	to 52
Annotation: disorder (Structural state)
Evidence: X-ray crystallography-based structural model with missing residue coordinates used in manual assertion
Supporting statements:
Residues that were not observed in the electron density map due to disorder include N-terminal residues 24–52 and C-terminal residues 144–161 ​[Fig. 3(C)].
Cross-references: PDB:3OEO
Protein: DP02078 (UniProt P02686-5)
Region: residues 1	to 171
Annotation: disorder (Structural state)
Evidence: nuclear magnetic resonance spectroscopy evidence used in manual assertion
Supporting statements:
In aqueous solution, the classic 18.5 kDa isoform of MBP is primarily disordered, but has transient α-helices that are stabilized by membrane-mimetic conditions
Protein: DP02078 (UniProt P02686-5)
Region: residues 1	to 171
Annotation: protein binding (Molecular function)
Evidence: nuclear magnetic resonance spectroscopy evidence used in manual assertion
Supporting statements:
, although the amphipathic α-helix represents the well-studied, canonical CaM-target, it has become recognized that CaM-binding sites and modes of interaction are quite diverse
Protein: DP02078 (UniProt P02686-5)
Region: residues 1	to 171
Annotation: lipid binding (Molecular function)
Evidence: nuclear magnetic resonance spectroscopy evidence used in manual assertion
Supporting statements:
These conditions were chosen to mimic the membrane environment of the myelin sheath, while keeping the system experimentally tractable to solution NMR methodology (7). We argue that 30% TFE stabilizes transient α-helices within the protein (83–85) on the basis of multiple, complementary studies on the immunodominant epitope of MBP
Protein: DP02078 (UniProt P02686-5)
Region: residues 1	to 171
Annotation: disorder (Structural state)
Evidence: cleavage assay evidence used in manual assertion
Supporting statements:
An activity check of the thrombin showed that HMBP-I, the nonphosphorylated 18.5 kDa protein, was completely digested by 2 hr (data not shown; described for bovine MBP-1 by Deibler et al., 1990).
Protein: DP02078 (UniProt P02686-5)
Region: residues 82	to 99
Annotation: disorder (Structural state)
Evidence: nuclear magnetic resonance spectroscopy evidence used in manual assertion
Supporting statements:
The CSI analyses of our assignments, shown in Fig. 3, indicate a noticeable tendency of a central 10-residue segment of the polypeptide to adopt a helical conformation from residues 5′ to 14′, for samples in TFE-d2 (Fig. 3B) and in DPC-d38 (Fig. 3C), but not in KCl (Fig. 3A).
Cross-references: BMRB:6857
Protein: DP02078 (UniProt P02686-5)
Region: residues 86	to 96
Annotation: disorder to order (Structural transition)
Evidence: nuclear magnetic resonance spectroscopy evidence used in manual assertion
Supporting statements:
The CSI analyses of our assignments, shown in Fig. 3, indicate a noticeable tendency of a central 10-residue segment of the polypeptide to adopt a helical conformation from residues 5′ to 14′, for samples in TFE-d2 (Fig. 3B) and in DPC-d38 (Fig. 3C), but not in KCl (Fig. 3A).
Cross-references: BMRB:6857
Protein: DP02078 (UniProt P02686-5)
Region: residues 86	to 96
Annotation: order (Structural state)
Evidence: nuclear magnetic resonance spectroscopy evidence used in manual assertion
Supporting statements:
The CSI analyses of our assignments, shown in Fig. 3, indicate a noticeable tendency of a central 10-residue segment of the polypeptide to adopt a helical conformation from residues 5′ to 14′, for samples in TFE-d2 (Fig. 3B) and in DPC-d38 (Fig. 3C), but not in KCl (Fig. 3A).
Cross-references: BMRB:6857
Protein: DP02078 (UniProt P02686-5)
Region: residues 82	to 99
Annotation: order (Structural state)
Evidence: far-UV circular dichroism evidence used in manual assertion
Supporting statements:
In aqueous solution (pure water, and 100 mm KCl, pH 6.5), the spectra indicated that the polypeptide had little or no regular secondary structure. In organic and membrane-mimetic conditions (30% TFE and 20 mm DPC, respectively), the spectra clearly indicated an α-helical conformation.
Protein: DP02078 (UniProt P02686-5)
Region: residues 82	to 99
Annotation: disorder to order (Structural transition)
Evidence: far-UV circular dichroism evidence used in manual assertion
Supporting statements:
In aqueous solution (pure water, and 100 mm KCl, pH 6.5), the spectra indicated that the polypeptide had little or no regular secondary structure. In organic and membrane-mimetic conditions (30% TFE and 20 mm DPC, respectively), the spectra clearly indicated an α-helical conformation.
Protein: DP02078 (UniProt P02686-5)
Region: residues 82	to 99
Annotation: disorder (Structural state)
Evidence: far-UV circular dichroism evidence used in manual assertion
Supporting statements:
In aqueous solution (pure water, and 100 mm KCl, pH 6.5), the spectra indicated that the polypeptide had little or no regular secondary structure. In organic and membrane-mimetic conditions (30% TFE and 20 mm DPC, respectively), the spectra clearly indicated an α-helical conformation.
Protein: DP02078 (UniProt P02686-5)
Region: residues 86	to 96
Annotation: lipid binding (Molecular function)
Evidence: electron paramagnetic resonance evidence used in manual assertion
Supporting statements:
These results demonstrate that the polypeptide α helix forms distinct hydrophobic and electrostatic contacts with the DPC micelles, and are in agreement with the SDSL/EPR mapping and positioning of the α-helical model of this epitope of MBP on the surface of a lipid bilayer [6,7].
Protein: DP02078 (UniProt P02686-5)
Region: residues 82	to 99
Annotation: lipid binding (Molecular function)
Evidence: far-UV circular dichroism evidence used in manual assertion
Supporting statements:
In aqueous solution (pure water, and 100 mm KCl, pH 6.5), the spectra indicated that the polypeptide had little or no regular secondary structure. In organic and membrane-mimetic conditions (30% TFE and 20 mm DPC, respectively), the spectra clearly indicated an α-helical conformation.
Here, we focused on a conserved segment of MBP which is known to be a-helical when bound to a membrane, is a potential calmodulin-binding site, and also a primary immunodominant epitope in multiple sclerosis.
Protein: DP02078 (UniProt P02686-5)
Region: residues 86	to 96
Annotation: lipid binding (Molecular function)
Evidence: nuclear magnetic resonance spectroscopy evidence used in manual assertion
Supporting statements:
The CSI analyses of our assignments, shown in Fig. 3, indicate a noticeable tendency of a central 10-residue segment of the polypeptide to adopt a helical conformation from residues 5′ to 14′, for samples in TFE-d2 (Fig. 3B) and in DPC-d38 (Fig. 3C), but not in KCl (Fig. 3A).
Here, we focused on a conserved segment of MBP which is known to be a-helical when bound to a membrane, is a potential calmodulin-binding site, and also a primary immunodominant epitope in multiple sclerosis.
Protein: DP02079 (UniProt E1BSW7)
Region: residues 107	to 139
Annotation: disorder (Structural state)
Evidence: X-ray crystallography-based structural model with missing residue coordinates used in manual assertion
Supporting statements:
. Boxes (a1 - a4), solid lines, and dashed
lines indicate a helices, random coil regions, and disordered residues, respectively
Protein: DP02086 (UniProt Q9JPP1)
Region: residues 133	to 274
Annotation: disorder (Structural state)
Evidence: X-ray crystallography-based structural model with missing residue coordinates used in manual assertion
Supporting statements:
The crystal structure of NHBA133-427 was solved by molecular replacement (MR) at 1.8 Å resolution (Table 1), revealing a β-hairpin and a β-barrel encompassing residues 275–427
 In agreement with the fact that the N-terminal region of NHBA is predicted to lack secondary structures, and is thus annotated as an intrinsically disordered protein (IDP), we were unable to solve the structures of this region.
Cross-references: PDB:6CUJ
Protein: DP02086 (UniProt Q9JPP1)
Region: residues 245	to 275
Annotation: disorder (Structural state)
Evidence: nuclear magnetic resonance spectroscopy evidence used in manual assertion
Supporting statements:
The protein is connected to the membrane by a flexible linker, which leaves it mostly solvent exposed (10, 11).
We show that although the N terminus of NHBA is annotated as an intrinsically unfolded region by the most common prediction methods, the C terminus has all the features of an independently folded globular domain.
However, we realized very early on that the number of resonances present in the 15N-HSQC spectrum, which represents the protein fingerprint, contained at least 10–20% resonances more than expected, suggesting the presence in solution of different forms. Particularly diagnostic was, for instance, the resonance that resulted that corresponds to residue 287 (12.1 and 128.5 ppm), which was clearly doubled.
Cross-references: PDB:2LFU
Protein: DP02094 (UniProt P49427)
Region: residues 183	to 236
Annotation: disorder (Structural state)
Evidence: nuclear magnetic resonance spectroscopy evidence used in manual assertion
Supporting statements:
The  (HSQC) spectrum of CDC34C (Fig. 1a) shows a collapsed amide peak profile in the 1 H dimension, denoting that the protein assumes a disordered conformation with little regular secondary structure.
We also confirmed the disordered state of CDC34C using the chemical shift index for Cα , Cβ, CO, and Hα resonances.
To further support the disordered state for the C-terminus of CDC34, we utilized  (NOE) experiments.
Protein: DP02094 (UniProt P49427)
Region: residues 101	to 115
Annotation: disorder (Structural state)
Evidence: nuclear magnetic resonance spectroscopy evidence used in manual assertion
Supporting statements:
Reduced 15N{1 H} NOEs were observed for residues
V101–N115 corresponding to the acidic loop in
CDC34. Several of these residues are not visible in
the crystal structure of CDC34.
Protein: DP02096 (UniProt P28698)
Region: residues 1	to 13
Annotation: disorder (Structural state)
Evidence: nuclear magnetic resonance spectroscopy evidence used in manual assertion
Supporting statements:
MZF1 includes a novel N-terminal region that is 13 residues in length and shares no homology to any established protein interaction modules
Further inspection of the MZF1(1-128) spectrum identified ∼30 additional sharp
resonances clustered around the random coil chemical shift value of ∼8.2 ppm. The presence of these resonances only in the longer construct suggests that the novel N-terminal region is unstructured
Protein: DP02097 (UniProt P27472)
Region: residues 640	to 705
Annotation: disorder (Structural state)
Evidence: X-ray crystallography-based structural model with missing residue coordinates used in manual assertion
Supporting statements:
As previously described, residues C-terminal from position 639 are disordered and were not included in the models.
Cross-references: PDB:4KQ2
Protein: DP02097 (UniProt P27472)
Region: residues 640	to 705
Annotation: disorder (Structural state)
Evidence: X-ray crystallography-based structural model with missing residue coordinates used in manual assertion
Supporting statements:
The structure exhibited defined electron density for residues 2–277; 283–401and 415–639 in one monomer of the dimer and for residues 2–277; 283–401 and 415–626 in the other monomer. Both the monomers lacked interpretable electron density for the C-terminal 60–70 residues.
The X-ray structure of the mutated inhibited state structure of yGsy2p, shows the disordered region boundaries are 640-705.
Cross-references: PDB:5SUL
Protein: DP02097 (UniProt P27472)
Region: residues 640	to 705
Annotation: disorder (Structural state)
Evidence: X-ray crystallography-based structural model with missing residue coordinates used in manual assertion
Supporting statements:
In all cases, the subunits lack interpretable electron density C-terminal to residue 646, and both activity states of yeast glycogen synthase are tetramers (Fig. 1).
The X-ray structure of the basal state of Gsy2p, shows the disordered region boundaries are 640-705.
Cross-references: PDB:3NCH
Protein: DP02097 (UniProt P27472)
Region: residues 402	to 413
Annotation: disorder (Structural state)
Evidence: X-ray crystallography-based structural model with missing residue coordinates used in manual assertion
Supporting statements:
A 12-residue loop between these two helices (residues 401–412) is disordered in the basal state but becomes ordered as the interface changes in response to glucose-6-phosphate binding.
Cross-references: PDB:3NCH
Protein: DP02097 (UniProt P27472)
Region: residues 402	to 413
Annotation: disorder to order (Structural transition)
Evidence: X-ray crystallography-based structural model with missing residue coordinates used in manual assertion
Supporting statements:
A 12-residue loop between these two helices (residues 401–412) is disordered in the basal state but becomes ordered as the interface changes in response to glucose-6-phosphate binding.
As might be expected for an allosteric ligand that induces such large conformational changes, the interactions between the enzyme and glucose-6-phosphate are extensive and involve residues from more than one subunit.
Cross-references: PDB:3NCH
PDB:3NB0
Protein: DP02097 (UniProt P27472)
Region: residues 648	to 705
Annotation: disorder (Structural state)
Evidence: X-ray crystallography-based structural model with missing residue coordinates used in manual assertion
Supporting statements:
In all cases, the subunits lack interpretable electron density C-terminal to residue 646, and both activity states of yeast glycogen synthase are tetramers (Fig. 1).
The X-ray structure of the glucose-6-phosphate activated state of Gsy2p, shows the disordered region boundaries are 648-705
Cross-references: PDB:3NB0
Protein: DP02100 (UniProt P60604)
Region: residues 95	to 109
Annotation: disorder (Structural state)
Evidence: nuclear magnetic resonance spectroscopy evidence used in manual assertion
Supporting statements:
the 13-residue insertion (residues 95–107) and the loop spanning residues 130–135. These loops are in fact very poorly defined in the NMR structural ensemble, with an average backbone RMSD (from the closest to mean NMR model) of 1.8 A˚ for residues 96–109 and 1.07 A˚ for residues 130–135. The poor definition
of the insert loop and the 130s loop  clearly arises from the near absence of long range NOE.
Cross-references: PDB:2KLY
Protein: DP02105 (UniProt P74518)
Region: residues 100	to 191
Annotation: disorder (Structural state)
Evidence: combinatorial experimental and author inference evidence used in manual assertion
Supporting statements:
Our modelling and molecular dynamics (MD) simulations indicate that the protein adopted the same fold observed in other members of the HPF family (β-α-β-β-β-α) at its N-terminal region (residues 1–100), whereas the C terminus (residues 100–197) appeared disordered and collapsed, supporting the overall percentage of overall secondary structure obtained by CD deconvolution.
The first-half of LrtA sequence (residues 1–100) more distinctly belonged to the region occupied by ordered polypeptides. In contrast, the second-half (residues 100–191) fell in the region of the diagram that is populated by IDPs, although also accessible to some well-folded proteins.
Protein: DP02105 (UniProt P74518)
Region: residues 102	to 191
Annotation: disorder (Structural state)
Evidence: nuclear magnetic resonance spectroscopy-based hydrogen-deuterium exchange evidence used in manual assertion
Supporting statements:
The NMR spectrum showed significant broadening in all the signals. On the basis of the results of the other techniques (see below in this section, and later in Section 2.2), this could be due to the presence of conformational exchange (equilibria) among protein species with different self-associated order. However, given the mobility of the protein (see MD simulations results, below in this section), we cannot exclude that the broadening observed could be due to conformational exchange in a single protein species. Therefore, we can conclude from the NMR spectrum that C-LrtA was disordered.
The intrinsically disordered nature of C-LrtA was suggested by several pieces of evidence: (i) the lack of dispersion in NMR spectra (Figure 1); (ii) the shape (Figure 2A) and the deconvolution of far-UV CD spectrum; (iii) the absence of all-or-none co-operative transitions in the thermal and chemical denaturations (Figure 2B,C); and (iv) a model of the structure without the His-tag obtained with MD simulation (Figure 3).