LiteFold/DisProt huggingface dataset:
Protein: DP00136 (UniProt P15865)
Region: residues 1	to 219
Annotation: disorder to order (Structural transition)
Evidence: far-UV circular dichroism evidence used in manual assertion
Supporting statements:
The presence of 10 mM sodium phosphate (Pi) had a large effect on its CD spectrum (Fig. 1 A). The changes obtained in the presence of Pi are characteristic of a large increase in the α-helicity of H1.
As little as 100 μM ATP produced corresponding effects on the CD spectrum of H1 as 10 mM sodium phosphate (Pi) did (cf. Fig. 1A,C). An increase in the α-helicity of H1 to 10.4±0.5% was obtained at a concentration of 500 μM ATP (Fig. 1D).
Addition of double-stranded poly(dA-dT) or poly(dI-dC) DNA to H1 resulted in an increase in the α-helicity of H1 (Fig. 2B and 3A). It increased from 4.5% up to a maximum of 9.4±0.2% and 8.3±0.6% respectively. Increasing DNA concentrations increased linearly the α-helicity of H1 up to a concentration where the H1-binding sites on the DNA could be estimated to correspond to the amount of H1 (data not shown).
Protein: DP00136 (UniProt P15865)
Region: residues 1	to 219
Annotation: DNA binding (Molecular function)
Evidence: far-UV circular dichroism evidence used in manual assertion
Supporting statements:
Addition of double-stranded poly(dA-dT) or poly(dI-dC) DNA to H1 resulted in an increase in the α-helicity of H1 (Fig. 2B and 3A). It increased from 4.5% up to a maximum of 9.4±0.2% and 8.3±0.6% respectively. Increasing DNA concentrations increased linearly the α-helicity of H1 up to a concentration where the H1-binding sites on the DNA could be estimated to correspond to the amount of H1 (data not shown).
Protein: DP00137 (UniProt P01050)
Region: residues 50	to 65
Annotation: disorder (Structural state)
Evidence: nuclear magnetic resonance spectroscopy evidence used in manual assertion
Supporting statements:
Analysis of the NOE data indicates that hirudin consists of an N-terminal compact domain (residues 1-49) held together by three disulfide linkages and a disordered C-terminal tail (residues 50-65) which does not fold back on the rest of the protein.
This was important as residues 55, 56, 57, and 59 possess virtually degenerate NH chemical shifts under all conditions studied. 
We therefore conclude that there is no evidence that the C-terminus (residues 50-65) has an ordered structure or folds back onto the rest of the protein. The high degree of NH chemical shift degeneracy over a range of temperature and the absence of slowly exchanging amide protons are consistent with a “random-coil” structure for this portion of the molecule
Cross-references: PDB:6HIR
PDB:2HIR
PDB:5HIR
PDB:4HIR
Protein: DP00137 (UniProt P01050)
Region: residues 55	to 64
Annotation: protein binding (Molecular function)
Evidence: x-ray crystallography evidence used in manual assertion
Supporting statements:
Crystals of thrombin complexed with hirugen and APPA were obtained by soaking an α-thrombin-hirugen crystal in a solution of APPA.
The rest of the hirugen molecule from residue Asp55' to Gln64' is well defined.
Cross-references: PDB:1AHT
Protein: DP00137 (UniProt P01050)
Region: residues 55	to 64
Annotation: disorder to order (Structural transition)
Evidence: x-ray crystallography evidence used in manual assertion
Supporting statements:
Crystals of thrombin complexed with hirugen and APPA were obtained by soaking an α-thrombin-hirugen crystal in a solution of APPA.
The rest of the hirugen molecule from residue Asp55' to Gln64' is well defined.
Cross-references: PDB:1AHT
Protein: DP00137 (UniProt P01050)
Region: residues 50	to 65
Annotation: protein binding (Molecular function)
Evidence: x-ray crystallography evidence used in manual assertion
Supporting statements:
In the complex with bovine α-thrombin, hirudin variant 1, whose sequence is shown in Fig. 2, has a compact NH2-terminal domain, comprised of residues 1h through 48h, and an extended COOH-terminal polypeptide chain, comprised of residues 49h through 65h (Figs. 3 and 4).
Cross-references: PDB:1HRT
Protein: DP00137 (UniProt P01050)
Region: residues 50	to 65
Annotation: disorder to order (Structural transition)
Evidence: x-ray crystallography evidence used in manual assertion
Supporting statements:
In the complex with bovine α-thrombin, hirudin variant 1, whose sequence is shown in Fig. 2, has a compact NH2-terminal domain, comprised of residues 1h through 48h, and an extended COOH-terminal polypeptide chain, comprised of residues 49h through 65h (Figs. 3 and 4).
Cross-references: PDB:1HRT
Protein: DP00138 (UniProt P12272)
Region: residues 37	to 50
Annotation: disorder (Structural state)
Evidence: X-ray crystallography-based structural model with missing residue coordinates used in manual assertion
Supporting statements:
Of 108 residues, only residues 14–31 of PTHrP were visible in the final electron density map, with residues 14–29 adopting a helical conformation.
Cross-references: PDB:3FFD
Protein: DP00138 (UniProt P12272)
Region: residues 68	to 144
Annotation: disorder (Structural state)
Evidence: X-ray crystallography-based structural model with missing residue coordinates used in manual assertion
Supporting statements:
Of 108 residues, only residues 14–31 of PTHrP were visible in the final electron density map, with residues 14–29 adopting a helical conformation.
Cross-references: PDB:3FFD
Protein: DP00140 (UniProt P0A7L8)
Region: residues 1	to 85
Annotation: disorder (Structural state)
Evidence: far-UV circular dichroism evidence used in manual assertion
Supporting statements:
The CD spectrum of E. coli L27 (Fig. 3a) indicates that the protein is unstructured.
Protein: DP00140 (UniProt P0A7L8)
Region: residues 1	to 85
Annotation: disorder (Structural state)
Evidence: nuclear magnetic resonance spectroscopy evidence used in manual assertion
Supporting statements:
This inference was reinforced by 2D heteronuclear NMR analysis of a 15N-labeled sample of the E. coli protein, which demonstrated that there was no dispersion of the backbone amide or side-chain amine resonances (data not shown).
Protein: DP00141 (UniProt O95405)
Region: residues 766	to 823
Annotation: disorder (Structural state)
Evidence: nuclear magnetic resonance spectroscopy evidence used in manual assertion
Supporting statements:
The proton-nitrogen (1H,15N) HSQC spectrum of SARA SBD revealed a narrow range of amide proton chemical shifts characteristic of disordered proteins (Fig. 2).
These data provide strong evidence that the unbound SBD is disordered in solution.
Protein: DP00141 (UniProt O95405)
Region: residues 766	to 823
Annotation: protein binding (Molecular function)
Evidence: nuclear magnetic resonance spectroscopy evidence used in manual assertion
Supporting statements:
Although the full SBD bound with a dissociation constant of 240  30 nM, the affinities for any single element of the SBD were 2500 – 8500-fold lower.
Protein: DP00142 (UniProt P14602)
Region: residues 192	to 209
Annotation: disorder (Structural state)
Evidence: nuclear magnetic resonance spectroscopy evidence used in manual assertion
Supporting statements:
The C-terminal extension in Hsp25 (and those in c-crystallin) therefore have characteristics of many peptides in an aqueous environment, i.e. flexibility and no defined conformation [16].
Protein: DP00142 (UniProt P14602)
Region: residues 199	to 204
Annotation: protein stabilization (Biological process)
Evidence: loss-of-function mutant phenotype evidence used in manual assertion
Supporting statements:
Complete suppression [45] of yeast ADH precipitation was observed for wild-type Hsp25 at a molar ratio of 1.4 : 1.0 Hsp25 : ADH (Fig. 6). A decrease in suppression of ADH precipitation was observed at this ratio for all of the glutamic acid residue mutants. At all other ratios, the E199A mutant showed minor reductions in suppression of ADH precipitation compared with wild-type Hsp25, whereas the E190A and E204A mutants showed markedly reduced suppression. The Q194A mutant showed similar levels of suppression of aggregation to the wild-type protein at all ratios.
Protein: DP00142 (UniProt P14602)
Region: residues 199	to 204
Annotation: protein folding chaperone (Molecular function)
Evidence: loss-of-function mutant phenotype evidence used in manual assertion
Supporting statements:
 Taken together, the thermal and reduction stress assays demonstrate that each of the glutamic acid mutants, in particular E190A and E204A, are significantly less effective chaperones than is wild-type Hsp25 (Table 2).
Protein: DP00142 (UniProt P14602)
Region: residues 192	to 209
Annotation: protein folding chaperone (Molecular function)
Evidence: loss-of-function mutant phenotype evidence used in manual assertion
Supporting statements:
As is shown in Fig. 4B, however, Hsp25ΔC18 did not stabilize α-lactalbumin in such an assay. In fact, with increasing amounts of Hsp25ΔC18, a proportional increase in precipitation of protein was observed suggesting that in addition to the precipitation of α-lactalbumin, Hsp25ΔC18 also precipitated out of solution upon addition of dithiothreitol.
Protein: DP00144 (UniProt Q9VAN6)
Region: residues 258	to 276
Annotation: disorder (Structural state)
Evidence: X-ray crystallography-based structural model with missing residue coordinates used in manual assertion
Supporting statements:
Unexpectedly, the C-terminal region was disordered in structures of dSLBP with or without phosphorylation mimicry (dSLBP RPD-5E and dSLBP RPD-WT, respectively).
Cross-references: PDB:4TUX
Protein: DP00144 (UniProt Q9VAN6)
Region: residues 108	to 172
Annotation: disorder (Structural state)
Evidence: cleavage assay evidence used in manual assertion
Supporting statements:
Drosophila SLBP (dSLBP) gives two protease-resistant fragments when digested with a number of proteases ( 15). One fragment corresponds to the C-terminus of dSLBP, which contains the region necessary for histone pre-mRNA processing consisting of residues H172−D276, and the second fragment contains a portion of the amino terminus from residues G17−K108 (Figure 1). The remainder of the protein (amino acids 108−172) is very glycine- and serine-rich and likely unstructured.
Protein: DP00144 (UniProt Q9VAN6)
Region: residues 1	to 16
Annotation: disorder (Structural state)
Evidence: far-UV circular dichroism evidence used in manual assertion
Supporting statements:
The mean molar ellipticity at 222 nm is a rough measure of helical content in proteins, and this value is quite small for both N-terminal constructs (θ222 = −2110 and θ222 = −1842 for residues 1−175 and 17−108, respectively). Therefore, only a small percentage of the molecule exists in a helical conformation at neutral pH and 25 °C. Surprisingly, no appreciable increase in helical content (as interpreted from the ellipticity at 222 nm) is observed for the 175-residue construct compared to the 91 residue domain suggesting that residues that lie outside the 91-residue domain are mostly flexible and unstructured.
Protein: DP00144 (UniProt Q9VAN6)
Region: residues 109	to 175
Annotation: disorder (Structural state)
Evidence: far-UV circular dichroism evidence used in manual assertion
Supporting statements:
The mean molar ellipticity at 222 nm is a rough measure of helical content in proteins, and this value is quite small for both N-terminal constructs (θ222 = −2110 and θ222 = −1842 for residues 1−175 and 17−108, respectively). Therefore, only a small percentage of the molecule exists in a helical conformation at neutral pH and 25 °C. Surprisingly, no appreciable increase in helical content (as interpreted from the ellipticity at 222 nm) is observed for the 175-residue construct compared to the 91 residue domain suggesting that residues that lie outside the 91-residue domain are mostly flexible and unstructured.
Protein: DP00144 (UniProt Q9VAN6)
Region: residues 1	to 175
Annotation: disorder (Structural state)
Evidence: nuclear magnetic resonance spectroscopy evidence used in manual assertion
Supporting statements:
Remarkably, the chemical shifts of resonances in both the full-length protein and the 175-residue and 91-residue N-terminal domains have a very narrow dispersion in the amide proton region of 0.4 ppm that is centered around the random coil chemical shift (between 8.2 and 8.4 ppm) (Figure 3).
Protein: DP00144 (UniProt Q9VAN6)
Region: residues 17	to 108
Annotation: disorder (Structural state)
Evidence: nuclear magnetic resonance spectroscopy evidence used in manual assertion
Supporting statements:
Remarkably, the chemical shifts of resonances in both the full-length protein and the 175-residue and 91-residue N-terminal domains have a very narrow dispersion in the amide proton region of 0.4 ppm that is centered around the random coil chemical shift (between 8.2 and 8.4 ppm) (Figure 3).
Protein: DP00147 (UniProt P0A7U3)
Region: residues 82	to 92
Annotation: disorder (Structural state)
Evidence: X-ray crystallography-based structural model with missing residue coordinates used in manual assertion
Supporting statements:
The X-ray structure of the bacterial ribosome from Escherichia coli in complex with the antibiotic kasugamyin shows this region of the S19 protein lacks electron density, indicating it is disordered. 
Cross-references: PDB:4V4H
Protein: DP00148 (UniProt P03347)
Region: residues 378	to 389
Annotation: disorder (Structural state)
Evidence: nuclear magnetic resonance evidence used in manual assertion
Supporting statements:
An important observation was that no additional slowly exchanging protons arising from the (1-12) and (51-72) sequences surrounding the two fingers were observed in the spectrum of NCp7 (Figure 3c), suggesting that the N and C-terminal sequences were less structured than the central (13-51) domain of NCp7. 
The residues 1-12 of the Nucleocapsid protein p7 (NCp7) corresponds to the region  378-389 of the Gag polyprotein.
Protein: DP00148 (UniProt P03347)
Region: residues 428	to 449
Annotation: disorder (Structural state)
Evidence: nuclear magnetic resonance evidence used in manual assertion
Supporting statements:
An important observation was that no additional slowly exchanging protons arising from the (1-12) and (51-72) sequences surrounding the two fingers were observed in the spectrum of NCp7 (Figure 3c), suggesting that the N and C-terminal sequences were less structured than the central (13-51) domain of NCp7. 
The residues 51-72 of the Nucleocapsid protein p7 (NCp7) corresponds to the region 428-449 of the Gag polyprotein.
Protein: DP00151 (UniProt P02547)
Region: residues 444	to 549
Annotation: disorder (Structural state)
Evidence: Fourier-transform infrared spectroscopy evidence used in manual assertion
Supporting statements:
Band shape and maximum are very similar to those of polylysine at pH 7 (Kleinschmidt, 1993), myelin basic protein (Surewicz et al., 1987), and apocytochrome c (Muga et al., 1991a), all of which have predominantly random-coil structure.
Protein: DP00151 (UniProt P02547)
Region: residues 444	to 549
Annotation: flexible C-terminal tail (Disorder function)
Evidence: Fourier-transform infrared spectroscopy evidence used in manual assertion
Supporting statements:
Band shape and maximum are very similar to those of polylysine at pH 7 (Kleinschmidt, 1993), myelin basic protein (Surewicz et al., 1987), and apocytochrome c (Muga et al., 1991a), all of which have predominantly random-coil structure.
Protein: DP00152 (UniProt Q13426)
Region: residues 204	to 265
Annotation: disorder (Structural state)
Evidence: X-ray crystallography-based structural model with missing residue coordinates used in manual assertion
Supporting statements:
Even though residues 204–265 are present, they are disordered in the crystal structure.
Cross-references: PDB:1FU1
Protein: DP00152 (UniProt Q13426)
Region: residues 202	to 336
Annotation: disorder (Structural state)
Evidence: cryogenic electron microscopy-based structural model with missing residue coordinates used in manual assertion
Supporting statements:
The electron microscopy structures of the NHEJ super-complex, both in the monomer and dimer version, shows this region of the XRCC4 lacks electron density, indicating it is disordered. 
Cross-references: PDB:7NFC
PDB:7NFE
Protein: DP00152 (UniProt Q13426)
Region: residues 262	to 288
Annotation: DNA binding (Molecular function)
Evidence: heteronuclear single quantum coherence spectroscopy evidence used in manual assertion
Supporting statements:
When titrating the XRCC4CTR with 21mer double-stranded DNA, small changes in the chemical shift of residues within the DIM region were observed, suggesting that this region can bind transiently to DNA (Supplementary Fig. 8a,b).
Protein: DP00152 (UniProt Q13426)
Region: residues 202	to 336
Annotation: disorder (Structural state)
Evidence: heteronuclear single quantum coherence spectroscopy evidence used in manual assertion
Supporting statements:
The 1H–15N HSQC spectrum of XRCC4 and XRCC4CTR displayed low proton chemical shift dispersion, a signature of disordered protein regions (Fig. 3a and Supplementary Fig. 2e–g), with no detectable signal from the folded domain.
Cross-references: BMRB:52398
Protein: DP00153 (UniProt P01112)
Region: residues 170	to 189
Annotation: disorder (Structural state)
Evidence: X-ray crystallography-based structural model with missing residue coordinates used in manual assertion
Supporting statements:
The COOH-terminal 18 residues that are lacking or disordered in the crystal structures are represented as a shaded string.
Cross-references: PDB:4Q21
Protein: DP00155 (UniProt P32851)
Region: residues 10	to 26
Annotation: disorder (Structural state)
Evidence: x-ray crystallography evidence used in manual assertion
Supporting statements:
The dashed line represents residues 10–26 of syntaxin, which are not visible in the electron density maps.
Cross-references: PDB:3C98
Protein: DP00155 (UniProt P32851)
Region: residues 10	to 26
Annotation: disorder (Structural state)
Evidence: x-ray crystallography evidence used in manual assertion
Supporting statements:
Syx1a N-peptide residues 10–26 were disordered (dashed line).
Cross-references: PDB:4JEU
Protein: DP00156 (UniProt P54725)
Region: residues 79	to 160
Annotation: disorder (Structural state)
Evidence: nuclear magnetic resonance spectroscopy evidence used in manual assertion
Supporting statements:
The hHR23a protein has four structural domains (Fig. 1A), which are connected by unstructured linker regions.
The average backbone rms deviations to the mean structure for the UBL (3–78), UBA1 (161–200), XPC-binding (232–282), and UBA2 (317–359) domains are 0.410, 0.530, 0.461, and 0.402, respectively.
Cross-references: PDB:1OQY
PDB:1QZE
Protein: DP00156 (UniProt P54725)
Region: residues 79	to 160
Annotation: flexible linker (Disorder function)
Evidence: nuclear magnetic resonance spectroscopy evidence used in manual assertion
Supporting statements:
The hHR23a protein has four structural domains (Fig. 1A), which are connected by unstructured linker regions.
The average backbone rms deviations to the mean structure for the UBL (3–78), UBA1 (161–200), XPC-binding (232–282), and UBA2 (317–359) domains are 0.410, 0.530, 0.461, and 0.402, respectively.
Cross-references: PDB:1QZE
PDB:1OQY
Protein: DP00156 (UniProt P54725)
Region: residues 201	to 231
Annotation: disorder (Structural state)
Evidence: nuclear magnetic resonance spectroscopy evidence used in manual assertion
Supporting statements:
The hHR23a protein has four structural domains (Fig. 1A), which are connected by unstructured linker regions.
The average backbone rms deviations to the mean structure for the UBL (3–78), UBA1 (161–200), XPC-binding (232–282), and UBA2 (317–359) domains are 0.410, 0.530, 0.461, and 0.402, respectively.
Cross-references: PDB:1OQY
Protein: DP00156 (UniProt P54725)
Region: residues 201	to 231
Annotation: flexible linker (Disorder function)
Evidence: nuclear magnetic resonance spectroscopy evidence used in manual assertion
Supporting statements:
The hHR23a protein has four structural domains (Fig. 1A), which are connected by unstructured linker regions.
The average backbone rms deviations to the mean structure for the UBL (3–78), UBA1 (161–200), XPC-binding (232–282), and UBA2 (317–359) domains are 0.410, 0.530, 0.461, and 0.402, respectively.
Cross-references: PDB:1QZE
PDB:1OQY
Protein: DP00156 (UniProt P54725)
Region: residues 283	to 316
Annotation: disorder (Structural state)
Evidence: nuclear magnetic resonance spectroscopy evidence used in manual assertion
Supporting statements:
The hHR23a protein has four structural domains (Fig. 1A), which are connected by unstructured linker regions.
The average backbone rms deviations to the mean structure for the UBL (3–78), UBA1 (161–200), XPC-binding (232–282), and UBA2 (317–359) domains are 0.410, 0.530, 0.461, and 0.402, respectively.
Cross-references: PDB:1OQY
PDB:1QZE
Protein: DP00156 (UniProt P54725)
Region: residues 283	to 316
Annotation: flexible linker (Disorder function)
Evidence: nuclear magnetic resonance spectroscopy evidence used in manual assertion
Supporting statements:
The hHR23a protein has four structural domains (Fig. 1A), which are connected by unstructured linker regions.
The average backbone rms deviations to the mean structure for the UBL (3–78), UBA1 (161–200), XPC-binding (232–282), and UBA2 (317–359) domains are 0.410, 0.530, 0.461, and 0.402, respectively.
Cross-references: PDB:1QZE
PDB:1OQY
Protein: DP00157 (UniProt P0CL52)
Region: residues 497	to 513
Annotation: disorder (Structural state)
Evidence: X-ray crystallography-based structural model with missing residue coordinates used in manual assertion
Supporting statements:
In the crystal, the protein is ordered only between residues 513 and 657 (with 16 and 12 residues disordered at the N- and C-termini, respectively), and the termini are located at opposite sides of the molecule.
Cross-references: PDB:1Q5Z
Protein: DP00157 (UniProt P0CL52)
Region: residues 659	to 670
Annotation: disorder (Structural state)
Evidence: X-ray crystallography-based structural model with missing residue coordinates used in manual assertion
Supporting statements:
In the crystal, the protein is ordered only between residues 513 and 657 (with 16 and 12 residues disordered at the N- and C-termini, respectively), and the termini are located at opposite sides of the molecule.
Cross-references: PDB:1Q5Z
Protein: DP00157 (UniProt P0CL52)
Region: residues 446	to 513
Annotation: disorder (Structural state)
Evidence: electron microscopy evidence used in manual assertion
Supporting statements:
The density between the two SipA constructs differs most dramatically in the length of the elongated regions that extend from opposite ends of the globular core (Fig. 2, A and B). When the crystal structure is fit into the globular region of the EM density, the best positioning occurs with the N- and C-termini located proximal to each arm (Fig. 2, A and B). There is an ambiguity about the up-down orientation of the crystal structure within the reconstruction, but all reasonable fits place the disordered regions from the crystallized construct in a perfect position to contribute to the elongated density.
Protein: DP00157 (UniProt P0CL52)
Region: residues 659	to 685
Annotation: disorder (Structural state)
Evidence: electron microscopy evidence used in manual assertion
Supporting statements:
The density between the two SipA constructs differs most dramatically in the length of the elongated regions that extend from opposite ends of the globular core (Fig. 2, A and B). When the crystal structure is fit into the globular region of the EM density, the best positioning occurs with the N- and C-termini located proximal to each arm (Fig. 2, A and B). There is an ambiguity about the up-down orientation of the crystal structure within the reconstruction, but all reasonable fits place the disordered regions from the crystallized construct in a perfect position to contribute to the elongated density.