LiteFold/DisProt huggingface dataset:
Protein: DP03313 (UniProt P00488)
Region: residues 2	to 38
Annotation: order to disorder (Structural transition)
Evidence: nuclear magnetic resonance spectroscopy evidence used in manual assertion
Supporting statements:
Recombinant AP-FXIII was largely flexible both in plasma and water, differing significantly from the rigid structure in the bound state. 
Finally, NMR analysis of 15N-labeled recombinant AP-FXIII in water and in plasma proved the peptide to be largely unstructured. 
The [15N,1H]-HSQC spectra of the AP-FXIII in water revealed the presence of too many peaks, and the extra peaks were attributed to the presence of cis conformers about the Pro-peptide bonds. The presence of these additional peaks already indicated that AP-FXIII in water was mainly unstructured.
To assess whether segments of the polypeptide chain are folded, a 15N{1H}-NOE experiment was recorded. Typically, amide nitrogen atoms of well-structured regions adopt values larger than 0.5, whereas for fully flexible regions the values are negative. In our experience secondary structure can only be reliably determined by NMR if the H-NOE in the corresponding segment is larger than 0.4. Values of the 15N{1H}-NOE of AP-FXIII are depicted in Figure 5 for both environments. Clearly, no values larger than 0.4 are encountered, and for many residues the heteronuclear NOE is close to 0.2, indicating that they are not fully flexible but that structure determination using NMR is not possible.
Coagulation factor XIII A chain activation peptide suffers a order to disorder transition upon cleavage. In the bound state, this activation peptide is structured as can be observed in PDB:1EVU
Cross-references: PDB:1EVU
Protein: DP03313 (UniProt P00488)
Region: residues 2	to 38
Annotation: disorder (Structural state)
Evidence: far-UV circular dichroism evidence used in manual assertion
Supporting statements:
In addition circular dichroism spectra were recorded at physiologic pH 7.0 and the lower pH 5.5. The data indicate that neither α-helical nor β-strand type secondary structural elements become populated at the greater pH value, although slightly more polyproline-type absorption at 208 nm occurs at the greater pH value (data not shown).
Protein: DP03314 (UniProt Q06141)
Region: residues 27	to 36
Annotation: disorder (Structural state)
Evidence: X-ray crystallography-based structural model with missing residue coordinates used in manual assertion
Supporting statements:
The reference is to the structure obtained by X-ray crystallography. In the paper there is no mention to missing electron density but It can be found in the structure
Cross-references: PDB:1UV0
Protein: DP03314 (UniProt Q06141)
Region: residues 27	to 36
Annotation: disorder (Structural state)
Evidence: X-ray crystallography-based structural model with missing residue coordinates used in manual assertion
Supporting statements:
The disordered N-terminal 10 amino acids are indicated by a dotted line , and the locations of the N-terminal disulfide bond( red )and the trypsin cleavage site are indicated.
The position number 10 from the structure (cited in the paper 1UV0) corresponds to position number 36 from UniProt sequence. The statement from the paper claims that the first 10 residues are disordered and actually are 9 residues. 
In particular, N-terminal residues 27–35 are disordered and thus absent from the structure (Fig. 5 A ) and residues 36–41 appear to be involved in crystal packing interactions, raising questions about the observed structure of this essential region of the protein.
Protein: DP03314 (UniProt Q06141)
Region: residues 27	to 37
Annotation: self-inhibition (Disorder function)
Evidence: cleavage assay evidence used in manual assertion
Supporting statements:
These data demonstrate that removal of the N-terminal prosegment by trypsin enhances RegIIIand HIP/PAP antibacterial activity. 
Collectively, these data establish that the RegIII lectin N-terminal prosegment inhibits antibacterial activity in cis, but does not affect peptidoglycan binding.
Overall, these results suggested a model in which the prosegment maintains HIP/PAP in an inactive state through transient interactions between acidic N-terminal residues and basic residues positioned C-terminal to the trypsin site. 
 The inhibitory activity of the N-terminal segment depends on charge-charge interactions with the main body of the protein. Derepression of antibacterial activity occurs when these interactions are perturbed, either through proteolytic removal of the prosegment or by mutation of the charged residues
Protein: DP03314 (UniProt Q06141)
Region: residues 27	to 37
Annotation: disorder (Structural state)
Evidence: nuclear magnetic resonance spectroscopy evidence used in manual assertion
Supporting statements:
This indicates a high degree of backbone conformational mobility at the N terminus. Furthermore, TALOS analyses of backbone chemical shifts (17) and 1H-1H NOEs indicated that the prosegment adopts an extended structure.
The results corresponds to the prosegment specifically for the region comprising residue 27 to residue 37
Protein: DP03314 (UniProt Q06141)
Region: residues 27	to 37
Annotation: self-inhibition (Disorder function)
Evidence: nuclear magnetic resonance spectroscopy evidence used in manual assertion
Supporting statements:
Together, these data suggest that the prosegment is flexible and transiently interacts with the rest of the protein.
The results corresponds to the prosegment specifically for the region comprising residue 27 to residue 37.
Protein: DP03315 (UniProt P0ADC1)
Region: residues 20	to 32
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 first 15 N-terminal residues and the final 18 C-terminal residues of mature LptE are missing. It is possible that the N terminus of LptE is flexible to allow it to be connected to its membrane anchor at the N terminus, while forming a plug within the lumen of the β-barrel of LptD (11, 15).
The IDR characterized in the publication and spanning residues the N-terminal corresponds to region 20-32 of the amino acid sequence, since the natural precursor form of the protein contains a signal peptide (1-18) that is cleaved in the mature secreted protein. 
Cross-references: PDB:4NHR
Protein: DP03315 (UniProt P0ADC1)
Region: residues 170	to 182
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 first 15 N-terminal residues and the final 18 C-terminal residues of mature LptE are missing. It is possible that the N terminus of LptE is flexible to allow it to be connected to its membrane anchor at the N terminus, while forming a plug within the lumen of the β-barrel of LptD (11, 15). The disordered C-terminal portion of LptE is consistent with the observation that it is readily cleaved by limited proteolysis of the LptDE complex (11). In any event, genetic studies have established
that this construct is functional (20).
The IDR characterized in the publication and spanning residues the C-terminal corresponds to region 170-182 of the amino acid sequence, since the natural precursor form of the protein contains a signal peptide (1-18) that is cleaved in the mature secreted protein. 
Cross-references: PDB:4NHR
Protein: DP03317 (UniProt O16299)
Region: residues 261	to 285
Annotation: disorder (Structural state)
Evidence: X-ray crystallography-based structural model with missing residue coordinates used in manual assertion
Supporting statements:
Residues that are not visible in the crystal structure are indicated with dashed lines
Dashed line corresponds to the region comprised from residue 261 to residue 285
Cross-references: PDB:4L16
PDB:4L15
Protein: DP03318 (UniProt Q95ZK7)
Region: residues 260	to 269
Annotation: disorder (Structural state)
Evidence: X-ray crystallography-based structural model with missing residue coordinates used in manual assertion
Supporting statements:
The linkers connecting the head-to-toe dimers consist of a single amino-acid residue (Cys 188 for KH2–KH3 and Leu 343 for KH4–KH5, while the side-by-side positioning of the consecutive KH3–KH4 domains is mediated by a 10-residue-long linker (residues 260–269) that is disordered in the structure.
Cross-references: PDB:3N89
Protein: DP03318 (UniProt Q95ZK7)
Region: residues 260	to 269
Annotation: flexible linker (Disorder function)
Evidence: x-ray crystallography evidence used in manual assertion
Supporting statements:
Results: The linkers connecting the head-to-toe dimers consist of a single amino-acid residue (Cys 188 for KH2–KH3 and Leu 343 for KH4–KH5, while the side-by-side positioning of the consecutive KH3–KH4 domains is mediated by a 10-residue-long linker (residues 260–269) that is disordered in the structure.
Cross-references: PDB:3N89
Protein: DP03319 (UniProt O17087)
Region: residues 815	to 860
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 544–922 of GLD-2 (with the exception of missing or disordered residues between 815–860 and 879–882) and residues 177–222 of RNP-8.
Cross-references: PDB:5JNB
Protein: DP03319 (UniProt O17087)
Region: residues 813	to 846
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 546–923 of GLD-2ΔI (with the exception of disordered loops between residues 766 and 773, 804 and 812, 847 and 854, and 876 and 881), residues 25–88 of GLD-3NT, and a chloride ion
Disordered regions are shown with dotted lines. The region deleted for crystallization (residues 813–846) resides in the disordered loop region between α-helices 7 and 8. 
Cross-references: PDB:4ZRL
Protein: DP03320 (UniProt P46580)
Region: residues 359	to 380
Annotation: disorder to order (Structural transition)
Evidence: x-ray crystallography evidence used in manual assertion
Supporting statements:
In particular, a segment including a N-terminal loop (L0) and a following helix (αA) (a.a. 359–380) became ordered upon SAH binding. Helix αA is positioned similar to that found in type-I enzymes, sheltering SAH from exposing to the solvent and creating a secluded catalytic active site. However, key residues responsible for the disordered-to-ordered conformational transition upon SAH/SAM binding are separately conserved among PRMT5 family members (Fig. 1B).
Cross-references: PDB:3UA4
PDB:3UA3
Protein: DP03322 (UniProt Q94218-2)
Region: residues 222	to 243
Annotation: disorder (Structural state)
Evidence: X-ray crystallography-based structural model with missing residue coordinates used in manual assertion
Supporting statements:
In cUfSP, the ten residues at the N-terminus of all chains, the loops between the a1 helix and b2 strand (residues 34–41) of four chains (chains C, D, E, F), and the regions between b10 and b11 (residues 222–243) of all chains are disordered.
Protein: DP03322 (UniProt Q94218-2)
Region: residues 1	to 10
Annotation: disorder (Structural state)
Evidence: X-ray crystallography-based structural model with missing residue coordinates used in manual assertion
Supporting statements:
In cUfSP, the ten residues at the N-terminus of all chains, the loops between the a1 helix and b2 strand (residues 34–41) of four chains (chains C, D, E, F), and the regions between b10 and b11 (residues 222–243) of all chains are disordered.
Protein: DP03323 (UniProt Q13316)
Region: residues 17	to 217
Annotation: disorder (Structural state)
Evidence: chromatography evidence used in manual assertion
Supporting statements:
The elution volumes (Ve) of standard proteins obtained by the gel filtration were used to calculate the partition coefficients  (Kav) and Stokes radii (RS).65 About 44K was eluted from the Superdex 75 10/300 GL column with a Ve corresponding to 41.4 Å for the 0.5 mg/mL and 40.9 Å for the 2.5 mg/ mL sample. 
 RS values were significantly higher than the theoretical values calculated  under the assumption that the proteins are globular (20.4  Å  for 44K).
Protein: DP03323 (UniProt Q13316)
Region: residues 218	to 513
Annotation: disorder (Structural state)
Evidence: chromatography evidence used in manual assertion
Supporting statements:
The elution volumes (Ve) of standard proteins obtained by the gel filtration were used to calculate the partition coefficients  (Kav) and Stokes radii (RS). The calculated RS value for 56K was 47.8 Å for the 0.1 mg/mL and 48.1 Å for both (0.5 mg/mL and 2.5 mg/ mL) sample concentrations. RS values were significantly higher than the theoretical values calculated under the assumption that the proteins are globular (25.1  Å for 56K).
Protein: DP03323 (UniProt Q13316)
Region: residues 17	to 217
Annotation: disorder (Structural state)
Evidence: analytical ultracentrifugation evidence used in manual assertion
Supporting statements:
The disordered nature of 44K and 56K fragments was confirmed by AUC. For globular compact proteins most common f/f0 values are within the range of 1.2-1.3, depending on the molecular weight. For IDPs, the f/f0 is higher due to the asymmetry and conformational flexibility that results in  higher friction and slows down sedimentation.80 The average f/f0 values calculated for 44K (2.26) and 56K (2.33) are high. These results indicate that both proteins have an elongated  shape and a high degree of conformational freedom.
Protein: DP03323 (UniProt Q13316)
Region: residues 218	to 513
Annotation: disorder (Structural state)
Evidence: analytical ultracentrifugation evidence used in manual assertion
Supporting statements:
The disordered nature of 44K and 56K fragments was confirmed by AUC. For globular compact proteins most common f/f0 values are within the range of 1.2-1.3, depending on the molecular weight. For IDPs, the f/f0 is higher due to the asymmetry and conformational flexibility that results in  higher friction and slows down sedimentation.80 The average f/f0 values calculated for 44K (2.26) and 56K (2.33) are high. These results indicate that both proteins have an elongated  shape and a high degree of conformational freedom.
Protein: DP03323 (UniProt Q13316)
Region: residues 17	to 217
Annotation: disorder (Structural state)
Evidence: far-UV circular dichroism evidence used in manual assertion
Supporting statements:
The CD spectra of 44K (Figure 6A) and 56K (Figure 6B) exhibit such properties.  The analysis conducted using CDPro revealed that 44K is mostly disordered (70.7%±6.3%). The dominant type of ordered structures are β-strands (15.1%±5.9%) and turns  (9.7%±3.8%). Only 2.9%±2.5% are predicted to be α-helices (Table 3).
Protein: DP03323 (UniProt Q13316)
Region: residues 218	to 513
Annotation: disorder (Structural state)
Evidence: far-UV circular dichroism evidence used in manual assertion
Supporting statements:
The same calculations were conducted for the 56K protein. The results suggest that 56K may be more disordered than 44K, but the differences do not seem to be significant (Table 3).
Protein: DP03323 (UniProt Q13316)
Region: residues 17	to 217
Annotation: disorder to molten globule (Structural transition)
Evidence: far-UV circular dichroism evidence used in manual assertion
Supporting statements:
For 44K and 56K we observed an increase in the ellipticity minimum at 200 nm and the simultaneous appearance of two minima at 208 nm and 222 nm with increasing concentrations of TFE (Supporting Figure S1). We conclude  that fragments of both 44K and 56K may become ordered  in a hydrophobic and/or crowded environment,87,88 for example, in contact with interaction partners or in the biomineralizing extracellular matrix
Protein: DP03323 (UniProt Q13316)
Region: residues 218	to 513
Annotation: disorder to molten globule (Structural transition)
Evidence: far-UV circular dichroism evidence used in manual assertion
Supporting statements:
For 44K and 56K we observed an increase in the ellipticity minimum at 200 nm and the simultaneous appearance of two minima at 208 nm and 222 nm with increasing concentrations of TFE (Supporting Figure S1). We conclude  that fragments of both 44K and 56K may become ordered  in a hydrophobic and/or crowded environment,87,88 for example, in contact with interaction partners or in the biomineralizing extracellular matrix
Protein: DP03323 (UniProt Q13316)
Region: residues 17	to 217
Annotation: disorder (Structural state)
Evidence: sodium dodecyl sulfate polyacrylamide gel electrophoresis evidence used in manual assertion
Supporting statements:
For 44K, the experiment has revealed two values (22 788 ± 6 Da and 22 773 ± 6 Da) which were in agreement with theoretical value calculated by the ProtParam tool50 (22 774.7 Da)
The observed discrepancy between the theoretical and SDS-PAGE-based molecular mass values is typical for members of the family of IDPs,  which fail to form the rigid 3D structures under physiological  conditions.
Protein: DP03323 (UniProt Q13316)
Region: residues 218	to 513
Annotation: disorder (Structural state)
Evidence: sodium dodecyl sulfate polyacrylamide gel electrophoresis evidence used in manual assertion
Supporting statements:
The experimental MW for 56K (34 025 ± 6 Da) was higher by 10.7 Da than the theoretical value (34 014.3 Da). The small mass differences observed may come from the methylation of the amino groups, probably from the N-terminal methionine. 
The observed discrepancy between the theoretical and SDS-PAGE-based molecular mass values is typical for members of the family of IDPs,  which fail to form the rigid 3D structures under physiological  conditions.
Protein: DP03323 (UniProt Q13316)
Region: residues 17	to 217
Annotation: disorder to molten globule (Structural transition)
Evidence: chromatography evidence used in manual assertion
Supporting statements:
In contrast, a series of SEC experiments  revealed that calcium ions influenced the conformations of  both fragments. Concomitantly to the increase of concentration of calcium ions, the RS of 44K and 56K fragments decreased from 47.8 to 39.6 Å and from 62.0 to 53.3 Å, respectively (Figure 7D)
Protein: DP03323 (UniProt Q13316)
Region: residues 218	to 513
Annotation: disorder to molten globule (Structural transition)
Evidence: chromatography evidence used in manual assertion
Supporting statements:
In contrast, a series of SEC experiments  revealed that calcium ions influenced the conformations of  both fragments. Concomitantly to the increase of concentration of calcium ions, the RS of 44K and 56K fragments decreased from 47.8 to 39.6 Å and from 62.0 to 53.3 Å, respectively (Figure 7D)
Protein: DP03323 (UniProt Q13316)
Region: residues 17	to 217
Annotation: disorder to molten globule (Structural transition)
Evidence: analytical ultracentrifugation evidence used in manual assertion
Supporting statements:
 The RS values calculated for 44K (42.3-41.6  Å) (Table  4) are in good  agreement with the values derived from SEC (47.7-39.6 Å).  10 mM of calcium ions was enough to decrease the RS of 44K from 46.7 to 42.3 Å. The frictional coefficient f/f0 decreased from 2.331 to 2.192, while the sedimentation coefficient  s20,w increased from 1.686 to 1.794 S. There was no signif-icant change in the MW. These results clearly indicate that  44K becomes more compact in the presence of calcium ions.  Increasing the concentration of calcium ions above 10  mM  did not result in significant changes.
Protein: DP03323 (UniProt Q13316)
Region: residues 218	to 513
Annotation: disorder to molten globule (Structural transition)
Evidence: analytical ultracentrifugation evidence used in manual assertion
Supporting statements:
In the case of 56K, adding 10 mM of calcium ions induced a decrease in the RS from 49.3 to 44.3  Å. The f/f0 decreased from 2.336 to 2.135, the s20,w increased from 2.008 to 2.125, and the apparent MW decreased slightly from 34.9 to 33.2 kDa. At higher concentrations of calcium ions, small amounts of heavier species were detected.
Protein: DP03323 (UniProt Q13316)
Region: residues 17	to 217
Annotation: calcium ion binding (Molecular function)
Evidence: analytical ultracentrifugation evidence used in manual assertion
Supporting statements:
The RS values calculated for 44K (42.3-41.6 Å) (Table 4) are in good agreement with the values derived from SEC (47.7-39.6 Å). 10 mM of calcium ions was enough to decrease the RS of 44K from 46.7 to 42.3 Å. The frictional coefficient f/f0 decreased from 2.331 to 2.192, while the sedimentation coefficient s20,w increased from 1.686 to 1.794 S. There was no signif-icant change in the MW. These results clearly indicate that 44K becomes more compact in the presence of calcium ions. Increasing the concentration of calcium ions above 10 mM did not result in significant changes.
Protein: DP03323 (UniProt Q13316)
Region: residues 218	to 513
Annotation: calcium ion binding (Molecular function)
Evidence: chromatography evidence used in manual assertion
Supporting statements:
In contrast, a series of SEC experiments  revealed that calcium ions influenced the conformations of  both fragments. Concomitantly to the increase of concentration of calcium ions, the RS of 44K and 56K fragments decreased from 47.8 to 39.6 Å and from 62.0 to 53.3 Å, respectively (Figure 7D).
Protein: DP03323 (UniProt Q13316)
Region: residues 17	to 217
Annotation: calcium ion binding (Molecular function)
Evidence: chromatography evidence used in manual assertion
Supporting statements:
Concomitantly to the increase of concentration of calcium ions, the RS of 44K and 56K fragments decreased from 47.8 to 39.6 Å and from 62.0 to 53.3 Å, respectively (Figure 7D).
Protein: DP03323 (UniProt Q13316)
Region: residues 218	to 513
Annotation: calcium ion binding (Molecular function)
Evidence: analytical ultracentrifugation evidence used in manual assertion
Supporting statements:
The RS values calculated for 44K (42.3-41.6 Å) (Table 4) are in good agreement with the values derived from SEC (47.7-39.6 Å). 10 mM of calcium ions was enough to decrease the RS of 44K from 46.7 to 42.3 Å. The frictional coefficient f/f0 decreased from 2.331 to 2.192, while the sedimentation coefficient s20,w increased from 1.686 to 1.794 S. There was no signif-icant change in the MW. These results clearly indicate that 44K becomes more compact in the presence of calcium ions. Increasing the concentration of calcium ions above 10 mM did not result in significant changes.
Protein: DP03324 (UniProt P35052)
Region: residues 350	to 361
Annotation: disorder (Structural state)
Evidence: X-ray crystallography-based structural model with missing residue coordinates used in manual assertion
Supporting statements:
As noted, some parts of the structure (PDB entry 4acr) were partially disordered and were not visible in the initial electron-density map.
Cross-references: PDB:4ACR
Protein: DP03325 (UniProt Q9SZF7)
Region: residues 59	to 120
Annotation: disorder (Structural state)
Evidence: X-ray crystallography-based structural model with missing residue coordinates used in manual assertion
Supporting statements:
Most of the N-terminal extensions were not observed in the current electron density map, whereas the short N-terminal segment of SHR, the N-terminal strap, was observed to extend towards SCR.
The N-terminal 6 residues of SCR (residues 275-280) and 61 residues of SHR (residues 59-119) were not observed in the current map.
The boundaries of the N-terminal region are 59 to 120 according the PDB 5B3G.
Cross-references: PDB:5B3G