LiteFold/DisProt huggingface dataset:
Protein: DP00783 (UniProt P10279)
Region: residues 23	to 121
Annotation: disorder (Structural state)
Evidence: nuclear magnetic resonance spectroscopy evidence used in manual assertion
Supporting statements:
The NMR structures of the recombinant 217-residue polypeptide chain of the mature bovine prion protein, bPrP(23-230), and a C-terminal fragment, bPrP(121-230), include a globular domain extending from residue 125 to residue 227, a short flexible chain end of residues 228-230, and an N-terminal flexibly disordered "tail" comprising 108 residues for the intact protein and 4 residues for bPrP(121-230), respectively.
The NMR structure of the recombinant bPrP(23–230) (Fig. ​(Fig.11a) contains a globular domain that extends approximately from residue 122 to residue 227, where the residues 128–131 form the β-strand 1, 144–154 the α-helix 1 (which has 310-type structure from residue 153 onward), 161–164 the β-strand 2, 173–194 the α-helix 2, and 200–226 the α-helix 3. At both ends of the globular domain there are flexibly disordered polypeptide segments, as evidenced by near-random coil 1H chemical shifts (29) and negative values of the steady-state 15N{1H}-NOEs (Fig. ​2). The N-terminal tail comprising residues 23–121 (because of insertions relative to hPrP this segment includes 108 residues; see ref. 23 for the numeration used) shows exclusively negative NOEs, and because of signal overlap only one set of values was obtained for all six octapeptide segments (23), as indicated by the box in Fig. ​2. The positive NOEs for residues 122–227 are typical for a globular protein of this size (see also below), whereas increased flexibility is again indicated for the C-terminal tripeptide segment (Fig. 2).
Cross-references: PDB:1DX0
PDB:1DX1
Protein: DP00783 (UniProt P10279)
Region: residues 219	to 230
Annotation: disorder (Structural state)
Evidence: nuclear magnetic resonance spectroscopy evidence used in manual assertion
Supporting statements:
The NMR structure of the recombinant bPrP(23–230) ​(Fig.1) contains a globular domain that extends approximately from residue 122 to residue 227, where the residues 128–131 form the β-strand 1, 144–154 the α-helix 1 (which has 310-type structure from residue 153 onward), 161–164 the β-strand 2, 173–194 the α-helix 2, and 200–226 the α-helix 3. At both ends of the globular domain there are flexibly disordered polypeptide segments, as evidenced by near-random coil 1H chemical shifts (29) and negative values of the steady-state 15N{1H}-NOEs (Fig.2).
Cross-references: PDB:1DX0
PDB:1DX1
Protein: DP00783 (UniProt P10279)
Region: residues 108	to 119
Annotation: disorder to order (Structural transition)
Evidence: nuclear magnetic resonance spectroscopy evidence used in manual assertion
Supporting statements:
The structure of the aptamer remains unchanged in some cases, and disordered, flexible portions of its targets become structured upon binding.
Cross-references: PDB:2RU7
Protein: DP00783 (UniProt P10279)
Region: residues 108	to 119
Annotation: disorder (Structural state)
Evidence: nuclear magnetic resonance spectroscopy evidence used in manual assertion
Supporting statements:
The structure of the aptamer remains unchanged in some cases, and disordered, flexible portions of its targets become structured upon binding.
Protein: DP00783 (UniProt P10279)
Region: residues 108	to 119
Annotation: G-quadruplex RNA binding (Molecular function)
Evidence: nuclear magnetic resonance spectroscopy evidence used in manual assertion
Supporting statements:
The structure of the aptamer remains unchanged in some cases, and disordered, flexible portions of its targets become structured upon binding.
Cross-references: PDB:2RU7
Protein: DP00794 (UniProt P50616)
Region: residues 117	to 345
Annotation: disorder (Structural state)
Evidence: X-ray crystallography-based structural model with missing residue coordinates used in manual assertion
Supporting statements:
No density is visible for residues 117–345 of Vps36 crystals of Tob1
Cross-references: PDB:5CI9
PDB:5CI8
Protein: DP00797 (UniProt O15273)
Region: residues 91	to 167
Annotation: disorder (Structural state)
Evidence: X-ray crystallography-based structural model with missing residue coordinates used in manual assertion
Supporting statements:
While the N-terminal segment of telethonin in the current complex displays a virtually identical structure when being compared to the previously reported titin/telethonin (1–90) complex (RMSD, 0.826 Å), its C-terminus remained invisible, leading to the assumption that it is unstructured under the conditions used for crystallization.
Cross-references: PDB:2F8V
Protein: DP00797 (UniProt O15273)
Region: residues 91	to 167
Annotation: disorder (Structural state)
Evidence: far-UV circular dichroism evidence used in manual assertion
Supporting statements:
From this comparison, we conclude that the C-terminus of telethonin indeed is unstructured in solution, in agreement with the observations in the crystal structure.
Protein: DP00797 (UniProt O15273)
Region: residues 91	to 167
Annotation: molecular adaptor activity (Molecular function)
Evidence: small-angle X-ray scattering evidence used in manual assertion
Supporting statements:
Data derived from the crystal structure, the SAXS experiments as well as the in vivo experiments indicate that the presence of the telethonin C-terminus is required to trigger the formation of a dimeric assembly of titin/telethonin complexes.
Protein: DP00797 (UniProt O15273)
Region: residues 91	to 167
Annotation: molecular adaptor activity (Molecular function)
Evidence: x-ray crystallography evidence used in manual assertion
Supporting statements:
Data derived from the crystal structure, the SAXS experiments as well as the in vivo experiments indicate that the presence of the telethonin C-terminus is required to trigger the formation of a dimeric assembly of titin/telethonin complexes.
Protein: DP00799 (UniProt P9WNK3)
Region: residues 1	to 16
Annotation: disorder (Structural state)
Evidence: nuclear magnetic resonance spectroscopy evidence used in manual assertion
Supporting statements:
The core of the complex is well defined (residues 15–79 in EsxG and 17–75 in EsxH), although there appears to be significant flexibility in the hairpin loop of EsxG (residues 40–47) as well as the N and C termini of EsxG and EsxH, which form flexible arms at both ends of the complex (Fig. 1).
Cross-references: PDB:2KG7
Protein: DP00799 (UniProt P9WNK3)
Region: residues 76	to 96
Annotation: disorder (Structural state)
Evidence: nuclear magnetic resonance spectroscopy evidence used in manual assertion
Supporting statements:
The core of the complex is well defined (residues 15–79 in EsxG and 17–75 in EsxH), although there appears to be significant flexibility in the hairpin loop of EsxG (residues 40–47) as well as the N and C termini of EsxG and EsxH, which form flexible arms at both ends of the complex (Fig. 1).
Cross-references: PDB:2KG7
Protein: DP00799 (UniProt P9WNK3)
Region: residues 1	to 16
Annotation: flexible N-terminal tail (Disorder function)
Evidence: nuclear magnetic resonance spectroscopy evidence used in manual assertion
Supporting statements:
The core of the complex is well defined (residues 15–79 in EsxG and 17–75 in EsxH), although there appears to be significant flexibility in the hairpin loop of EsxG (residues 40–47) as well as the N and C termini of EsxG and EsxH, which form flexible arms at both ends of the complex (Fig. 1). 
Cross-references: PDB:2KG7
Protein: DP00799 (UniProt P9WNK3)
Region: residues 76	to 96
Annotation: flexible C-terminal tail (Disorder function)
Evidence: nuclear magnetic resonance spectroscopy evidence used in manual assertion
Supporting statements:
The core of the complex is well defined (residues 15–79 in EsxG and 17–75 in EsxH), although there appears to be significant flexibility in the hairpin loop of EsxG (residues 40–47) as well as the N and C termini of EsxG and EsxH, which form flexible arms at both ends of the complex (Fig. 1). 
Cross-references: PDB:2KG7
Protein: DP00808 (UniProt P24937)
Region: residues 158	to 239
Annotation: disorder (Structural state)
Evidence: x-ray crystallography evidence used in manual assertion
Supporting statements:
One copy of protein VI is found intimately associated with the base of each PPH on the capsid interior. We were able to resolve residues 6–31, 34–79, and 87–157 of protein VI, which interact primarily with the bases of PPHs; the remaining C-terminal residues (158–239) were disordered.
Protein: DP00808 (UniProt P24937)
Region: residues 25	to 250
Annotation: disorder (Structural state)
Evidence: x-ray crystallography evidence used in manual assertion
Supporting statements:
 A segment of N-terminal pro-peptide of VI is found in the interior cavities of peripentonal hexons, and the rest of VI is disordered.
From Table 2, 1–24 corresponds to the ordered region of VI and 25–250 corresponds to the disordered region of VI.
Cross-references: PDB:6CGV
Protein: DP00808 (UniProt P24937)
Region: residues 240	to 250
Annotation: disorder (Structural state)
Evidence: x-ray crystallography evidence used in manual assertion
Supporting statements:
The protein VI density we modeled is only a small fraction of the full-length mature protein VI (aa 109 to 143 versus aa 34 to 239 as numbered in pVI), suggesting that both its N- and C-terminal regions are flexible. 
The PDB show this bondaries disordered (240-250)
Cross-references: PDB:6B1T
EMDB:7034
Protein: DP00808 (UniProt P24937)
Region: residues 25	to 250
Annotation: viral life cycle (Biological process)
Evidence: plaque assay evidence used in manual assertion
Supporting statements:
We used the data from this experiment to calculate ID50 values for each virus and found that the G48C mutant required ∼3-fold higher p/c than wild type AdV to achieve the same level of infection. The decrease in infectivity for the G48C mutant was not as drastic as that of the AdV VI-L40Q virus, which was 12-fold reduced compared to wild type virus. Nonetheless, the phenotype of the G48C mutation is distinct from that of L40Q, as described below.
We further assayed infectivity of the G48C mutant in an AdV plaque assay that measures viral replication, and show that the mutant generated ∼3-fold less plaques than wild type AdV at 0.5 p/c (Fig. 2B), in good agreement with the data from the single-round infection (Fig. 2A). The L40Q virus was also reduced ∼13-fold in this assay. Taken together, the results of these assays clearly indicate that the AdV VI-G48C mutant impairs virus infectivity.
Protein: DP00808 (UniProt P24937)
Region: residues 25	to 250
Annotation: viral release from host cell (Biological process)
Evidence: fluorescence evidence used in manual assertion
Supporting statements:
Given the inherent decrease in membrane lytic activity of the disulfide bonded protein VI molecules, we next asked whether reduction of the disulfide bonds could restore membrane lytic activity to the G48C protein.
This small increase in membrane lytic activity was consistently observed in three independent experiments. Therefore, we conclude that disulfide bond formation not only restricts release of the membrane lytic protein from the viral capsid, but also impairs proper interaction with the host membrane that allows subsequent membrane lytic activity.
Protein: DP00808 (UniProt P24937)
Region: residues 147	to 151
Annotation: viral life cycle (Biological process)
Evidence: plaque assay evidence used in manual assertion
Supporting statements:
To identify possible trafficking determinants, we analyzed the sequences of protein VI from several Ad serotypes and identified a highly conserved ubiquitin-ligase interacting motif present in PPxY-type viral late domains (PPxY, Figure S2). To examine the role of this PPxY motif in Ad cell entry, we used an E1/E3-deleted Ad5 that had the protein VI PPSY motif mutated to PGAA (Ad5-VI-M1, detailed in Figure S3) [33],[34].
Plaques were significantly smaller for Ad5-VI-M1 versus Ad5-VI-wt (see below), suggesting that the altered PPxY domain affects some stages of virus propagation.
Protein: DP00808 (UniProt P24937)
Region: residues 147	to 151
Annotation: viral life cycle (Biological process)
Evidence: fluorescence microscopy evidence used in manual assertion
Supporting statements:
To identify possible trafficking determinants, we analyzed the sequences of protein VI from several Ad serotypes and identified a highly conserved ubiquitin-ligase interacting motif present in PPxY-type viral late domains (PPxY, Figure S2). To examine the role of this PPxY motif in Ad cell entry, we used an E1/E3-deleted Ad5 that had the protein VI PPSY motif mutated to PGAA (Ad5-VI-M1, detailed in Figure S3) [33],[34].
To determine whether the M1 mutation influences Ad cell entry, we performed a fluorescent focus forming assay and stained cells at 8, 12 and 24 h post-infection for expression of the E2A protein, which marks the appearance of viral replication centers (Figure 2D and data not shown). Compared to Ad5-VI-wt, the Ad5-VI-M1 virus produced approximately 20-fold fewer fluorescent foci when equivalent numbers of viral particles were used for infections. This suggested that steps prior to replication (i.e. internalization) require an intact PPxY motif in protein VI.
Protein: DP00808 (UniProt P24937)
Region: residues 147	to 151
Annotation: viral life cycle (Biological process)
Evidence: green fluorescent protein reporter gene assay evidence used in manual assertion
Supporting statements:
To identify possible trafficking determinants, we analyzed the sequences of protein VI from several Ad serotypes and identified a highly conserved ubiquitin-ligase interacting motif present in PPxY-type viral late domains (PPxY, Figure S2). To examine the role of this PPxY motif in Ad cell entry, we used an E1/E3-deleted Ad5 that had the protein VI PPSY motif mutated to PGAA (Ad5-VI-M1, detailed in Figure S3) [33],[34].
We repeated plaque forming assays (Figure 2E) and single round infection assays (Figure 2F), this time using GFP expression as the quantification method in non-complementing U2OS cells. We observed a reduction in infectivity in the same order of magnitude as previously (compare Figures 2C with 2E and 2D with 2F). In addition the GFP expression allowed us to follow the plaque formation over time. As shown in Figure S4 the spread of the M1 mutant virus was significantly slower and led to fewer and much smaller plaques (Figure 2E and Figure S4).
Protein: DP00808 (UniProt P24937)
Region: residues 147	to 151
Annotation: protein transport along microtubule (Biological process)
Evidence: fusion protein localization evidence used in manual assertion
Supporting statements:
To identify possible trafficking determinants, we analyzed the sequences of protein VI from several Ad serotypes and identified a highly conserved ubiquitin-ligase interacting motif present in PPxY-type viral late domains (PPxY, Figure S2). To examine the role of this PPxY motif in Ad cell entry, we used an E1/E3-deleted Ad5 that had the protein VI PPSY motif mutated to PGAA (Ad5-VI-M1, detailed in Figure S3) [33],[34].
Together these data suggested that protein VI is a highly mobile protein that moves along microtubules, presumably in association with vesicular structures whose motion depends on the PPxY motif.
Protein: DP00808 (UniProt P24937)
Region: residues 147	to 151
Annotation: ubiquitination display site (Disorder function)
Evidence: qualitative western immunoblotting evidence used in manual assertion
Supporting statements:
To address the role of the PPxY motif in protein VI ubiquitylation, we repeated the in vitro ubiquitylation assay using wt or M1 mutant protein VI purified from E. coli followed by western blot analysis. We detected protein VI-reactive bands, consistent with protein VI modified with two to three ubiquitin (Figure 6B, lane 2). In contrast, no modification was observed when the PPxY motif was mutated (Figure 6B, lane 1) or in the absence of ATP (Figure 6B, lane 3 and 4).
Protein: DP00808 (UniProt P24937)
Region: residues 147	to 151
Annotation: protein binding (Molecular function)
Evidence: green fluorescent protein fusion protein localization evidence used in manual assertion
Supporting statements:
Two ligases, Nedd4.1 and Nedd4.2, were highly enriched on VI-wt beads while none of the other ligases showed strong binding to VI-wt- or to VI-M1-beads (Figure 7B). Taken together, these data suggest a preferential interaction between Nedd4.1 and Nedd4.2 and the PPxY motif in protein VI, which leads to relocalization of the ligases from the cytoplasm to a membrane compartment.
Protein: DP00809 (UniProt P80870)
Region: residues 81	to 130
Annotation: disorder (Structural state)
Evidence: nuclear magnetic resonance spectroscopy evidence used in manual assertion
Supporting statements:
The structure of GSP13 mainly consists of a typical S1 domain along with a C-terminal 50-residue flexible tail, different from the other known S1 domain containing proteins.
Cross-references: PDB:2K4K
Protein: DP00814 (UniProt P01252)
Region: residues 1	to 110
Annotation: disorder (Structural state)
Evidence: dynamic light scattering assay evidence used in manual assertion
Supporting statements:
Measurements of the excess scattered intensity of protein solutions at finite concentrations yield apparent molar masses, Mapp. The molar mass can be estimated by a linear extrapolation to 0 protein concentration according to 1/Mapp=1/m + 2bC, where B is the second virial coefficient. The corresponding data for ProTα in PBS, pH 7.4, are shown in Figure 2. A linear least-squares fit yields M = (11700 ± 1200)g/mol and a second virial coefficient B=(2.84 ± 0.30)x10-3mol cm3/ g2.
Protein: DP00814 (UniProt P01252)
Region: residues 1	to 110
Annotation: disorder (Structural state)
Evidence: far-UV circular dichroism evidence used in manual assertion
Supporting statements:
Prothymosin alpha: a biologically active protein with random coil conformation
Our results unequivocally demonstrate that prothymosin is a monomer under physiological conditions. The protein adopts a random coillike conformation but exhibits persistence of direction and curvature. No regular secondary structure is detectable by CD.
The CD spectrum of ProTα in PBS, pH7.4, is shown in Figure 1. It has a pattern typical of a protein lacking regular secondary structure as it is observed usually in solutions containing high concentrations of guanidinium chloride or urea.
Protein: DP00814 (UniProt P01252)
Region: residues 1	to 110
Annotation: disorder (Structural state)
Evidence: small-angle X-ray scattering evidence used in manual assertion
Supporting statements:
Furthermore, the scattering curve is shown in the form of a Kratky plot (Figure 5). This scattering curve exhibits the characteristics typical of random coil molecules with persistence of direction and persistence of curvature (Kirste & Oberthiir,1982).
Protein: DP00814 (UniProt P01252)
Region: residues 1	to 110
Annotation: disorder (Structural state)
Evidence: spectrometry evidence used in manual assertion
Supporting statements:
Electrospray ionization mass spectrometry investigations yielded a single peak with an average molar mass of 11982.8 g/mol.
Protein: DP00814 (UniProt P01252)
Region: residues 1	to 110
Annotation: disorder (Structural state)
Evidence: static light scattering assay evidence used in manual assertion
Supporting statements:
Measurements of the excess scattered intensity of protein solutions at finite concentrations yield apparent molar masses, Mapp. The molar mass can be estimated by a linear extrapolation to 0 protein concentration according to 1/Mapp=1/m + 2bC, where B is the second virial coefficient. The corresponding data for ProTα in PBS, pH 7.4, are shown in Figure 2. A linear least-squares fit yields M = (11700 ± 1200)g/mol and a second virial coefficient B=(2.84 ± 0.30)x10-3mol cm3/ g2.
Protein: DP00818 (UniProt P40422)
Region: residues 1	to 25
Annotation: disorder (Structural state)
Evidence: cryogenic electron microscopy-based structural model with missing residue coordinates used in manual assertion
Supporting statements:
The Electron microscopy structure of the yeast RNA polymerase III elongation complex, shows this region of the subunit RPABC4 is disordered.
Cross-references: PDB:5FJ8
Protein: DP00820 (UniProt O73557)
Region: residues 1	to 29
Annotation: disorder (Structural state)
Evidence: nuclear magnetic resonance spectroscopy evidence used in manual assertion
Supporting statements:
In contrast, the N terminus (1–29) and C terminus (71–99) exhibit very low heteronuclear NOE values, consistent with these being disordered.
Cross-references: PDB:2M1S
Protein: DP00820 (UniProt O73557)
Region: residues 1	to 29
Annotation: flexible N-terminal tail (Disorder function)
Evidence: nuclear magnetic resonance spectroscopy evidence used in manual assertion
Supporting statements:
In contrast, the N terminus (1–29) and C terminus (71–99) exhibit very low heteronuclear NOE values, consistent with these being disordered.
Protein: DP00820 (UniProt O73557)
Region: residues 1	to 25
Annotation: disorder (Structural state)
Evidence: X-ray crystallography-based structural model with missing residue coordinates used in manual assertion
Supporting statements:
Although the construct used for crystallization encodes full-length Z, only residues 26 to 73 are ordered in monomer A and residues 26 to 75 are ordered in monomer B.
Indeed, residues 1 to 25 and 76 to 99 are disordered in the crystal structure and in solution studies by NMR.
Cross-references: PDB:5I72
Protein: DP00820 (UniProt O73557)
Region: residues 76	to 99
Annotation: disorder (Structural state)
Evidence: X-ray crystallography-based structural model with missing residue coordinates used in manual assertion
Supporting statements:
Although the construct used for crystallization encodes full-length Z, only residues 26 to 73 are ordered in monomer A and residues 26 to 75 are ordered in monomer B.
Indeed, residues 1 to 25 and 76 to 99 are disordered in the crystal structure and in solution studies by NMR.
Cross-references: PDB:5I72
Protein: DP00820 (UniProt O73557)
Region: residues 71	to 99
Annotation: disorder (Structural state)
Evidence: nuclear magnetic resonance spectroscopy evidence used in manual assertion
Supporting statements:
In contrast, the N terminus (1–29) and C terminus (71–99) exhibit very low heteronuclear NOE values, consistent with these being disordered.
Cross-references: PDB:2M1S
Protein: DP00820 (UniProt O73557)
Region: residues 71	to 99
Annotation: flexible C-terminal tail (Disorder function)
Evidence: nuclear magnetic resonance spectroscopy evidence used in manual assertion
Supporting statements:
In contrast, the N terminus (1–29) and C terminus (71–99) exhibit very low heteronuclear NOE values, consistent with these being disordered.
Protein: DP00820 (UniProt O73557)
Region: residues 1	to 25
Annotation: disorder (Structural state)
Evidence: nuclear magnetic resonance spectroscopy evidence used in manual assertion
Supporting statements:
The extreme N and C termini of Z (residues 1 to 25 and residues 76 to 99) showed very high H/D exchange rates, indicating that these regions are highly flexible. Indeed, residues 1 to 25 and 76 to 99 are disordered in the crystal structure and in solution studies by NMR.
Protein: DP00820 (UniProt O73557)
Region: residues 76	to 99
Annotation: disorder (Structural state)
Evidence: nuclear magnetic resonance spectroscopy evidence used in manual assertion
Supporting statements:
The extreme N and C termini of Z (residues 1 to 25 and residues 76 to 99) showed very high H/D exchange rates, indicating that these regions are highly flexible. Indeed, residues 1 to 25 and 76 to 99 are disordered in the crystal structure and in solution studies by NMR.
Protein: DP00824 (UniProt Q9NJS1)
Region: residues 54	to 83
Annotation: disorder (Structural state)
Evidence: X-ray crystallography-based structural model with missing residue coordinates used in manual assertion
Supporting statements:
Electron density maps were readily interpretable for mature anophelin residues AE32 to AP61 (Fig. 3A), but no significant
density was detectable for the remaining N-terminal residues AA1 to AD31.
Cross-references: PDB:4E05