LiteFold/DisProt huggingface dataset:
Protein: DP00092 (UniProt Q08209)
Region: residues 388	to 466
Annotation: disorder to order (Structural transition)
Evidence: fluorescence resonance energy transfer evidence used in manual assertion
Supporting statements:
Ensemble average distances (rFRET) for this FRET pair in the RDc bound to CaM at 20 and 50 °C are shown in Figure 5a. At 20 °C, the average distance between the fluorophores is ∼10 Å, indicating that the two termini of RDc are relatively close to one another. 
This distance is ∼6 Å shorter than the ensemble average distance measured for the RDc alone and suggests that, in the complex, the N-terminus of the CaMBR is relatively close to the C-terminal end of the putative structured region. This supports the hypothesis that upon CaM binding the RD folds into a hairpinlike structure that provides sufficient free energy for the removal of the AID from the active site.
Protein: DP00092 (UniProt Q08209)
Region: residues 389	to 413
Annotation: calmodulin binding (Molecular function)
Evidence: native protein gel electrophoresis evidence used in manual assertion
Supporting statements:
In the absence of CaMBD and presence of either 2 mM or 10 mM Ca2+, only one CaM band was visible, which corresponds to CaM monomer. However, in the presence of CaMBD and presence of 2 mM or 10 mM Ca2+, two bands with molecular weight higher than CaM monomer, were clearly visible. The lower band corresponds to the monomer of the CaM/CaMBD complex, whilst the higher band matches CaM/CaMBD dimer (see Fig. 6). 
Native PAGE results verified that dimers of CaM/CaMBD do exist in solution and a CaM pull-down assay unambiguously revealed that CaM does adopt an elongated conformation to bind to CaMBD.
Protein: DP00092 (UniProt Q08209)
Region: residues 389	to 413
Annotation: calmodulin binding (Molecular function)
Evidence: bait-prey hybrid interaction evidence used in manual assertion
Supporting statements:
s shown in Figure 7(E), SDS-PAGE analysis revealed unbound, free CaM and CaMBD as well as unbound CaM/CaMBD in fractions containing the flow-through (Lane 3) and the washes (Lanes 4–5).
Native PAGE results verified that dimers of CaM/CaMBD do exist in solution and a CaM pull-down assay unambiguously revealed that CaM does adopt an elongated conformation to bind to CaMBD.
Protein: DP00092 (UniProt Q08209)
Region: residues 393	to 411
Annotation: calmodulin binding (Molecular function)
Evidence: x-ray crystallography evidence used in manual assertion
Supporting statements:
The refined final structure of the CaM/CaMBD complex is well-defined in the electron density map, with the following exceptions: Met-1, Ala-2, Asp-3, Gln-4, and Leu-5 in the first CaM molecule, and Met-1, Ala-2, Asp-3, and Gln-4 in the second CaM molecule. For the two peptides, out of 25 amino acids we were able to observe and model 15 residues (396–410 a.a.) in monomer A and 19 residues (393–411 a.a.) in monomer B, similar to those found in the fusion protein structure (15 and 21).24 These residues represent central core amino acids that make direct contact with CaM.
Cross-references: PDB:2R28
Protein: DP00092 (UniProt Q08209)
Region: residues 393	to 411
Annotation: order (Structural state)
Evidence: x-ray crystallography evidence used in manual assertion
Supporting statements:
The CaMBD peptides adopt α-helical conformation, as confirmed by the well-defined electron density (see Fig. 2).
Cross-references: PDB:2R28
Protein: DP00092 (UniProt Q08209)
Region: residues 393	to 411
Annotation: disorder to order (Structural transition)
Evidence: x-ray crystallography evidence used in manual assertion
Supporting statements:
The CaMBD peptides adopt α-helical conformation, as confirmed by the well-defined electron density (see Fig. 2).
Cross-references: PDB:2R28
Protein: DP00094 (UniProt P04177)
Region: residues 33	to 50
Annotation: disorder (Structural state)
Evidence: cleavage assay evidence used in manual assertion
Supporting statements:
From residue 33 to residue 50 of tyrosine hydroxylase, the sequence is RFIGRRQSLIEDARKERE. All of the observed cleavage sites are within this region, occurring after arginines 33, 37, 38, and 49.
When combined with the kinetics of digestion, the sequencing results establish that the conformation of the region from residue 33 to residue 50 in tyrosine hydroxylase is sensitive to the phosphorylation state and to dopamine binding. Phosphorylation of serine 40 by protein kinase A renders this region more susceptible to proteolysis, consistent with a more exposed conformation, whereas this region becomes less accessible when dopamine is bound.
Protein: DP00094 (UniProt P04177)
Region: residues 33	to 50
Annotation: phosphorylation display site (Disorder function)
Evidence: cleavage assay evidence used in manual assertion
Supporting statements:
When combined with the kinetics of digestion, the sequencing results establish that the conformation of the region from residue 33 to residue 50 in tyrosine hydroxylase is sensitive to the phosphorylation state and to dopamine binding. Phosphorylation of serine 40 by protein kinase A renders this region more susceptible to proteolysis, consistent with a more exposed conformation, whereas this region becomes less accessible when dopamine is bound.
Protein: DP00094 (UniProt P04177)
Region: residues 33	to 50
Annotation: small molecule binding (Molecular function)
Evidence: cleavage assay evidence used in manual assertion
Supporting statements:
When combined with the kinetics of digestion, the sequencing results establish that the conformation of the region from residue 33 to residue 50 in tyrosine hydroxylase is sensitive to the phosphorylation state and to dopamine binding. Phosphorylation of serine 40 by protein kinase A renders this region more susceptible to proteolysis, consistent with a more exposed conformation, whereas this region becomes less accessible when dopamine is bound.
Protein: DP00094 (UniProt P04177)
Region: residues 1	to 72
Annotation: disorder (Structural state)
Evidence: nuclear magnetic resonance spectroscopy evidence used in manual assertion
Supporting statements:
The backbone resonances of the N-terminal 70 residues of RDTyrH could be assigned using sensitivity-enhanced TROSY-based HNCACB, HN(CO)CACB, HNCA and HN(CO)CA triple-resonance experiments,22; 23 with the exception of the amide resonances of Met1, Pro11, Lys12, Gln39, Ser40, Leu41, and Pro68.
This indicated that RDTyrH is composed of a largely unstructured N-terminal region (residues 1-72) and a more ordered and well-folded C-terminal portion (residues 73-159).
Protein: DP00094 (UniProt P04177)
Region: residues 85	to 96
Annotation: disorder (Structural state)
Evidence: nuclear magnetic resonance spectroscopy evidence used in manual assertion
Supporting statements:
There are two highly flexible loop regions, L2 (residues 85-96) and L4 (residues 119-130).
Cross-references: PDB:2MDA
Protein: DP00094 (UniProt P04177)
Region: residues 119	to 130
Annotation: disorder (Structural state)
Evidence: nuclear magnetic resonance spectroscopy evidence used in manual assertion
Supporting statements:
There are two highly flexible loop regions, L2 (residues 85-96) and L4 (residues 119-130).
Cross-references: PDB:2MDA
Protein: DP00094 (UniProt P04177)
Region: residues 38	to 42
Annotation: phosphorylation display site (Disorder function)
Evidence: nuclear magnetic resonance spectroscopy evidence used in manual assertion
Supporting statements:
TyrH is phosphorylated at Ser40 by protein kinase A.
The backbone assignments of phosphorylated RDTyrH could be made using the same methods as for RDTyrH; these included Ser40 and the adjacent Gln39 and Leu41. All the assigned residues retain the same chemical shifts as in RDTyrH except for Gly36, Arg37, Gln39, Ser40, Leu41, Ile42, and Glu43. This suggests that after phosphorylation the core structure of RDTyrH remains the same as that in unphosphorylated RDTyrH, and a local structural change takes place around Ser40.
Protein: DP00094 (UniProt P04177)
Region: residues 28	to 71
Annotation: disorder (Structural state)
Evidence: protein hydrogen-deuterium exchange mass spectrometry evidence used in manual assertion
Supporting statements:
The most N-terminal peptides, illustrated in Figure 2A by residues 28-34, exhibit complete exchange after only 7 s, the earliest time point used here. This suggests that the very N-terminus of the protein is highly dynamic.
The three peptides covering residues 28-71 of the regulatory domain exhibit complete exchange in less than 7 s, illustrating that this portion of the protein is highly mobile.
Protein: DP00094 (UniProt P04177)
Region: residues 42	to 71
Annotation: small molecule binding (Molecular function)
Evidence: protein hydrogen-deuterium exchange mass spectrometry evidence used in manual assertion
Supporting statements:
Three peptides (35-41, 42-71, 295-299) show dramatic decreases in the rates of deuterium incorporation when dopamine is bound (Figure 4). The first two fragments are on the regulatory domain and show complete exchange within 7 s in the absence of dopamine.
Protein: DP00094 (UniProt P04177)
Region: residues 14	to 34
Annotation: disorder (Structural state)
Evidence: fluorescence anisotropy evidence used in manual assertion
Supporting statements:
This is consistent with increased flexibility at of the side chains at positions 14 and 34, with the largest effect on the residue closer to the phosphorylation site.
Protein: DP00096 (UniProt Q9HKT1)
Region: residues 179	to 193
Annotation: disorder (Structural state)
Evidence: cleavage assay evidence used in manual assertion
Supporting statements:
A second loop comprising residues 179-193 was disordered in the T.acidophilum structure; tryptic cleavage of the corresponding loop in the E.coli LplA under non-denaturing conditions rendered the enzyme catalytically inactive, emphasizing its importance.
Cross-references: PDB:2C8M
Protein: DP00096 (UniProt Q9HKT1)
Region: residues 179	to 193
Annotation: disorder (Structural state)
Evidence: X-ray crystallography-based structural model with missing residue coordinates used in manual assertion
Supporting statements:
A second loop comprising residues 179-193 was disordered in the T.acidophilum structure; tryptic cleavage of the corresponding loop in the E.coli LplA under non-denaturing conditions rendered the enzyme catalytically inactive, emphasizing its importance.
Cross-references: PDB:2C8M
Protein: DP00097 (UniProt P10922)
Region: residues 2	to 31
Annotation: disorder (Structural state)
Evidence: far-UV circular dichroism evidence used in manual assertion
Supporting statements:
The CD spectrum of both peptides in H2O was dominated by the contribution of the random coil. The mean residue molar ellipticity at 222 nm ([θ]222), taken as criterion of helix formation, was negligible in water. However, the small positive peak at 215 nm, characteristic of the random coil, was not observed, suggesting that a small amount of structure could be present in water (Fig.1).
Protein: DP00097 (UniProt P10922)
Region: residues 2	to 31
Annotation: disorder (Structural state)
Evidence: Fourier-transform infrared spectroscopy evidence used in manual assertion
Supporting statements:
In aqueous (D2O) solution, the amide I′ of both NH-1 and NH-2 was dominated by the random coil band at 1641 cm−1(representing 42% of the total amide I′ intensity in NH-1 and 44% in NH-2) (30).
Protein: DP00097 (UniProt P10922)
Region: residues 2	to 31
Annotation: DNA binding (Molecular function)
Evidence: Fourier-transform infrared spectroscopy evidence used in manual assertion
Supporting statements:
As the percentage of α-helix in aqueous solution was only 6–8%, these results indicate that interaction with the DNA stabilizes the helical structure of the peptides. The amounts of helical structure observed in the complexes with the DNA are similar to those observed in TFE solution, by both IR and CD.
Protein: DP00097 (UniProt P10922)
Region: residues 93	to 194
Annotation: disorder (Structural state)
Evidence: nuclear magnetic resonance spectroscopy evidence used in manual assertion
Supporting statements:
Furthermore, C-H1.0 is an intrinsically disorder protein, which shows very little dispersion in the 1HN nuclei; all amide protons appear in 0.51 ppm (Fig. 1c).
Cross-references: BMRB:27537
Protein: DP00097 (UniProt P10922)
Region: residues 93	to 194
Annotation: disorder (Structural state)
Evidence: far-UV circular dichroism evidence used in manual assertion
Supporting statements:
Circular dichroism (CD) data of C-H1.0 and pT-C-H1.0 also indicate that phosphorylation does not induce any conformational change (see Suppl. Fig. S2).
Fig. S2 shows this region is intrinsically unstructured by its large negative ellipticity at 200 nm and moderate ellipticity at 190 nm.
Protein: DP00097 (UniProt P10922)
Region: residues 21	to 25
Annotation: phosphorylation display site (Disorder function)
Evidence: mass spectrometry evidence used in manual assertion
Supporting statements:
The extent of phosphorylation was evaluated by MALDI-TOF mass spectrometry.
Therefore, we proceeded to acquire NMR spectra of pT-C-H1.0, in which the Thr residues of the three phosphorylation-motifs present in its sequence (22TPKK25, 44TPVK47, and 56TPKK59; Fig. 1a) are phosphorylated.
Protein: DP00098 (UniProt Q53654)
Region: residues 332	to 344
Annotation: disorder (Structural state)
Evidence: X-ray crystallography-based structural model with missing residue coordinates used in manual assertion
Supporting statements:
The N2 domain ends at residue 318 and the C-terminal extension of this domain (residues 319–329) stretches towards the N1 domain and forms a β strand (G′) that complements one of the β-sheets of the N1 domain (Figure 3A), while the following residues 332–344 are disordered and extend into the solvent region.
Cross-references: PDB:2F68
Protein: DP00098 (UniProt Q53654)
Region: residues 164	to 173
Annotation: disorder (Structural state)
Evidence: x-ray crystallography evidence used in manual assertion
Supporting statements:
The electron density for the main chain atoms of the 164–173 linker is poorly defined suggesting some flexibility in this linker segment.
Cross-references: PDB:2F68
Protein: DP00098 (UniProt Q53654)
Region: residues 164	to 173
Annotation: flexible linker (Disorder function)
Evidence: X-ray crystallography-based structural model with missing residue coordinates used in manual assertion
Supporting statements:
The electron density for the main chain atoms of the 164–173 linker is poorly defined suggesting some flexibility in this linker segment.
Cross-references: PDB:2F68
Protein: DP00099 (UniProt P50440)
Region: residues 38	to 63
Annotation: disorder (Structural state)
Evidence: X-ray crystallography-based structural model with missing residue coordinates used in manual assertion
Supporting statements:
Residues 38–63 as well as the 14 amino acid fusion peptide that had been cloned to the N-terminus of the protein for affinity purification are not visible in the electron density map and are mobile or disordered.
Cross-references: PDB:1JDW
PDB:4JDW
PDB:2JDW
PDB:3JDW
Protein: DP00100 (UniProt P0A6H5)
Region: residues 175	to 209
Annotation: disorder (Structural state)
Evidence: X-ray crystallography-based structural model with missing residue coordinates used in manual assertion
Supporting statements:
Their entirely disordered segment I175–Q209 may act as a bait and/or an adaptor to substrate molecules and promote binding.
Cross-references: PDB:1DO0
PDB:1DO2
Protein: DP00101 (UniProt P12493)
Region: residues 467	to 480
Annotation: disorder (Structural state)
Evidence: nuclear magnetic resonance spectroscopy evidence used in manual assertion
Supporting statements:
The quantitative NOE data for full-length sp6-(1–52) allow the definition of two α-helical structured regions extending from Ser-14 to Gly-18 and from Lys-33 to Ser-43 (Fig. 8, A and B, respectively), connected by a more flexible region that allows orientational freedom of the two helices.
The 19-32 region, described as disordered, corresponds to the 467-480 region of the Gag polyprotein.
Cross-references: PDB:2C55
Protein: DP00101 (UniProt P12493)
Region: residues 449	to 461
Annotation: disorder (Structural state)
Evidence: nuclear magnetic resonance spectroscopy evidence used in manual assertion
Supporting statements:
The quantitative NOE data for full-length sp6-(1–52) allow the definition of two α-helical structured regions extending from Ser-14 to Gly-18 and from Lys-33 to Ser-43 (Fig. 8, A and B, respectively), connected by a more flexible region that allows orientational freedom of the two helices.
The 1-13 region, described as disordered, corresponds to the 449-461 region of the Gag polyprotein.
Cross-references: PDB:2C55
Protein: DP00102 (UniProt P10587)
Region: residues 200	to 217
Annotation: disorder (Structural state)
Evidence: X-ray crystallography-based structural model with missing residue coordinates used in manual assertion
Supporting statements:
The PDB structure shows this region lacks electron density, indicating it is disordered.
Cross-references: PDB:1BR2
Protein: DP00102 (UniProt P10587)
Region: residues 406	to 415
Annotation: disorder (Structural state)
Evidence: X-ray crystallography-based structural model with missing residue coordinates used in manual assertion
Supporting statements:
The PDB structure shows this region lacks electron density, indicating it is disordered.
Cross-references: PDB:1BR2
Protein: DP00102 (UniProt P10587)
Region: residues 627	to 656
Annotation: disorder (Structural state)
Evidence: X-ray crystallography-based structural model with missing residue coordinates used in manual assertion
Supporting statements:
The PDB structure shows this region lacks electron density, indicating it is disordered.
Cross-references: PDB:1BR2
Protein: DP00103 (UniProt P09372)
Region: residues 1	to 32
Annotation: disorder (Structural state)
Evidence: X-ray crystallography-based structural model with missing residue coordinates used in manual assertion
Supporting statements:
The final model includes residues 3 to 383 of DnaK (except residues 184 and 210 to 213, which are disordered) and residues 34 to 197 (except residues 108 to 115) for the GrpE monomer that is proximal to DnaK in the complex, and residues 38 to 195 (except residues 108 to 115) for the GrpE monomer that is distal to DnaK, 28 water molecules, and 8 uranyl acetate ions, modeled as single sites. 
Cross-references: PDB:1DKG
Protein: DP00103 (UniProt P09372)
Region: residues 1	to 32
Annotation: flexible N-terminal tail (Disorder function)
Evidence: X-ray crystallography-based structural model with missing residue coordinates used in manual assertion
Supporting statements:
The final model includes residues 3 to 383 of DnaK (except residues 184 and 210 to 213, which are disordered) and residues 34 to 197 (except residues 108 to 115) for the GrpE monomer that is proximal to DnaK in the complex, and residues 38 to 195 (except residues 108 to 115) for the GrpE monomer that is distal to DnaK, 28 water molecules, and 8 uranyl acetate ions, modeled as single sites.
Protein: DP00104 (UniProt P32773)
Region: residues 210	to 240
Annotation: disorder (Structural state)
Evidence: X-ray crystallography-based structural model with missing residue coordinates used in manual assertion
Supporting statements:
The electron density for the N-terminal 31 amino acids of TOAlC (210-240) is not well defined, and indicates that this stretch of highly hydrophilic polypeptide is disordered (long shoelace).
Cross-references: PDB:1YTF
Protein: DP00107 (UniProt P69924)
Region: residues 342	to 376
Annotation: disorder (Structural state)
Evidence: X-ray crystallography-based structural model with missing residue coordinates used in manual assertion
Supporting statements:
The C-terminus is missing from the crystal structure but not mentioned in the article.
Cross-references: PDB:1XIK
Protein: DP00107 (UniProt P69924)
Region: residues 342	to 376
Annotation: flexible C-terminal tail (Disorder function)
Evidence: X-ray crystallography-based structural model with missing residue coordinates used in manual assertion
Supporting statements:
The C-terminus is missing from the crystal structure but not mentioned in the article.
Cross-references: PDB:1XIK
Protein: DP00108 (UniProt P07598)
Region: residues 399	to 421
Annotation: disorder (Structural state)
Evidence: X-ray crystallography-based structural model with missing residue coordinates used in manual assertion
Supporting statements:
The tracing of the large subunit of DdHase in the electron-density maps showed that the last 24 amino acid residues at the C terminus, as determined by DNA sequence analysis of the gene (Figure 1), were either missing or highly disordered.
Cross-references: PDB:1HFE
Protein: DP00108 (UniProt P07598)
Region: residues 399	to 421
Annotation: flexible C-terminal tail (Disorder function)
Evidence: X-ray crystallography-based structural model with missing residue coordinates used in manual assertion
Supporting statements:
The tracing of the large subunit of DdHase in the electron-density maps showed that the last 24 amino acid residues at the C terminus, as determined by DNA sequence analysis of the gene (Figure 1), were either missing or highly disordered.
Cross-references: PDB:1HFE
Protein: DP00110 (UniProt P40881)
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:
However, in the remainder of the models, the N-termini are disordered.
Cross-references: PDB:1QRE
PDB:1QQ0
Protein: DP00110 (UniProt P40881)
Region: residues 1	to 37
Annotation: flexible N-terminal tail (Disorder function)
Evidence: X-ray crystallography-based structural model with missing residue coordinates used in manual assertion
Supporting statements:
However, in the remainder of the models, the N-termini are disordered.
Cross-references: PDB:1QRE
PDB:1QQ0
Protein: DP00111 (UniProt P27577)
Region: residues 244	to 301
Annotation: disorder (Structural state)
Evidence: nuclear magnetic resonance spectroscopy evidence used in manual assertion
Supporting statements:
ΔN2445P, a form which is homogenously phosphorylated by CaMKII, contains five specific phosphoserines in the serine-rich region (SRR, residues 244 to 300) (Fig. 1C) and appears to undergo the same structural transition upon DNA binding as do unmodified ΔN244 (fig. S1E) and other Ets-1 species (3, 7, 11).
The phosphorylated SRR was found to be predominantly unstructured and highly flexible. Based on main-chain 1H and 13C chemical shifts, NMR spectra revealed no predominant secondary structure within this region (17) (Fig. 2A), and the amide hydrogen exchange (HX) rates were comparable to those of a random coil polypeptide (Fig. 2B).
Protein: DP00111 (UniProt P27577)
Region: residues 244	to 301
Annotation: flexible linker (Disorder function)
Evidence: nuclear magnetic resonance spectroscopy evidence used in manual assertion
Supporting statements:
ΔN2445P, a form which is homogenously phosphorylated by CaMKII, contains five specific phosphoserines in the serine-rich region (SRR, residues 244 to 300) (Fig. 1C) and appears to undergo the same structural transition upon DNA binding as do unmodified ΔN244 (fig. S1E) and other Ets-1 species (3, 7, 11).
Protein: DP00111 (UniProt P27577)
Region: residues 244	to 301
Annotation: disorder to order (Structural transition)
Evidence: nuclear magnetic resonance spectroscopy evidence used in manual assertion
Supporting statements:
ΔN2445P, a form which is homogenously phosphorylated by CaMKII, contains five specific phosphoserines in the serine-rich region (SRR, residues 244 to 300) (Fig. 1C) and appears to undergo the same structural transition upon DNA binding as do unmodified ΔN244 (fig. S1E) and other Ets-1 species (3, 7, 11).