LiteFold/DisProt huggingface dataset:
Protein: DP02197 (UniProt P0ADV9)
Region: residues 24	to 58
Annotation: disorder (Structural state)
Evidence: X-ray crystallography-based structural model with missing residue coordinates used in manual assertion
Supporting statements:
Residues 59–184 were observed in the electron density map, but two regions (residues 24–58 and 185–191) were disordered.
Protein: DP02201 (UniProt P0A9A6)
Region: residues 317	to 383
Annotation: disorder (Structural state)
Evidence: far-UV circular dichroism evidence used in manual assertion
Supporting statements:
The CD spectra of both Ct tails are similar to each other and to those of other intrinsically disordered peptides
Protein: DP02201 (UniProt P0A9A6)
Region: residues 317	to 383
Annotation: disorder (Structural state)
Evidence: nuclear magnetic resonance spectroscopy evidence used in manual assertion
Supporting statements:
NMR of the monomeric FtsZ C-terminus demonstrates that it is intrinsically disordered
Here, we used solution NMR spectroscopy to elucidate the secondary structure of the monomeric FtsZ CTR. The two-dimensional 1H-15N (heteronuclear single-quantum coherence—HSQC) NMR correlation spectra of FtsZ CTR exhibits narrow chemical shift dispersion, typical of a disordered protein, suggesting a lack of structural order consistent with sequence-based predictions (Figure 1a). Furthermore, we assigned the 13Cα and 13Cβ chemical shifts for FtsZ CTR and computed the secondary chemical shifts (ΔδCα–ΔδCβ), obtained by measuring the difference in the observed 13Cα and 13Cβ chemical shifts and those predicted for a completely disordered structure. These secondary chemical shifts are mostly near zero for all residues, consistent with intrinsic disorder.
Taken together, our data suggest that FtsZ CTR is monomeric and remains mostly intrinsically disordered, although we observe two consecutive residues with strong signatures of partial α-helical conformations and prediction of a short, partially helical motif, amino acids 375 through 379, near the multiprotein interaction site that overlaps the C-terminal ClpX recognition site (amino acids 375–383).
1H-15N HSQC spectrum of FtsZ CTR is consistent with intrinsic disorder.
Secondary structure populations derived from the observed chemical shifts using the δ2D algorithm confirms the dominance of random coil (i.e., disordered) conformations
Protein: DP02202 (UniProt P17865)
Region: residues 317	to 382
Annotation: disorder (Structural state)
Evidence: far-UV circular dichroism evidence used in manual assertion
Supporting statements:
The CD spectra of both Ct tails are similar to each other and to those of other intrinsically disordered peptides, such as the adducin tail (Hughes & Bennett, 1995), prothymosin alpha (Gast et al., 1995), and p21 (Kriwacki et al., 1996), suggesting the lack of any prominent secondary structure (Fig. 6a).
Protein: DP02202 (UniProt P17865)
Region: residues 315	to 382
Annotation: disorder (Structural state)
Evidence: far-UV circular dichroism evidence used in manual assertion
Supporting statements:
Consistent with the predictions from simulations, ultraviolet circular dichroism (UV-CD) measurements for the isolated CTT peptide indicate that it is conformationally heterogeneous
Protein: DP02202 (UniProt P17865)
Region: residues 315	to 382
Annotation: disorder to order (Structural transition)
Evidence: far-UV circular dichroism evidence used in manual assertion
Supporting statements:
The spectrum of full-length FtsZ closely resembles that of the ΔCTT construct with a mixture of structures. The sum of the spectra for the core domain and the CTT does not reproduce the spectrum of a full-length protein. This suggests that the CTT likely undergoes conformational changes when it is tethered to the core domain by forming intermodule interactions with the core.
Protein: DP02202 (UniProt P17865)
Region: residues 377	to 382
Annotation: self-assembly (Disorder function)
Evidence: far-UV circular dichroism evidence used in manual assertion
Supporting statements:
Swapping the 6-residue CTV from B. subtilis FtsZ with the 4-residue CTV from Escherichia coli FtsZ completely abolished lateral interactions between chimeric B. subtilis FtsZ polymers.
EM images of Bs FtsZ ΔC17 assembled in the presence of GTP indicate that it is almost exclusively in single-stranded protofilaments.
Under standard polymerization conditions, Bs FtsZ CTVE was able to form single-stranded polymers; however, no FtsZ filament bundles were observed (Fig. 3A). 
Data from Ec FtsZ CTVB indicates that the CTV from B. subtilis is sufficient to promote lateral interactions between single-stranded FtsZ polymers.
Our data suggest that CTV charge is the primary determinant of Bs FtsZ lateral interaction potential.
Protein: DP02202 (UniProt P17865)
Region: residues 377	to 382
Annotation: cell division (Biological process)
Evidence: far-UV circular dichroism evidence used in manual assertion
Supporting statements:
Analysis of Bs ftsZ CTVE mutants suggests that the lateral interactions we observed in vitro are critical for FtsZ ring integrity in vivo and support a role for the CTV in stabilizing FtsZ polymers within the cytokinetic ring. Although B. subtilis cells expressing Bs ftsZ CTVE grew normally and exhibited exclusively medial FtsZ rings (Fig. 5A), they were on average ∼85% longer than congenic wild-type cells (Fig. 5D). ∼31% (90 of 290) of Bs ftsZ CTVE mutants were filamentous (>5 cell lengths), suggesting that cells expressing the chimera failed to divide at a relatively high frequency.
Comparisons of cell length (L) with the number of FtsZ rings (R) indicated that the L/R ratio of the Bs ftsZ CTVE mutants was nearly 75% greater than wild-type cells.
Protein: DP02203 (UniProt Q9Q6P4)
Region: residues 899	to 919
Annotation: disorder (Structural state)
Evidence: X-ray crystallography-based structural model with missing residue coordinates used in manual assertion
Supporting statements:
Flexible region in the West Nile Virus NS1 protein, corresponds to a disordered loop which is also disordered in the DENV2 NS1 protein. Corresponds to an antigenic region containing a conserved hydrophobic WKxW motif
Each “wing” domain contains two glycosylation sites (Asn130, Asn175), an internal disulfide (Cys55-Cys143), and two discreet subdomains. An α/β subdomain (amino acids 38 – 151) comprises a four-stranded β-sheet, two α-helices and a disordered distal tip (amino acids 108 – 128; Fig. 1A, dotted line).
A 20-residue disordered region is indicated with dotted lines.
Ns1 disordered distal tip (amino acids 108 – 128) corresponds to 899-919 region of the West Nile virus (strain NY-99) polyprotein.
Cross-references: PDB:4O6C
PDB:4O6D
Protein: DP02204 (UniProt Q5UB51)
Region: residues 1413	to 1438
Annotation: disorder (Structural state)
Evidence: X-ray crystallography-based structural model with missing residue coordinates used in manual assertion
Supporting statements:
The region corresponds to a flexible and disordered region of the NS2B protein, which is an NS3 protease cofactor. This region can be crystallized in different conformations, or be missing from the electron densities
Cross-references: PDB:3U1J
Protein: DP02204 (UniProt Q5UB51)
Region: residues 1413	to 1419
Annotation: protein binding (Molecular function)
Evidence: X-ray crystallography-based structural model with missing residue coordinates used in manual assertion
Supporting statements:
Residues 50 to 61 of NS2B form a tight complex with NS3, and it has been proposed that W61 is the last residue that is tightly bound to NS3, after which the rest of the residues (residues 62 to 88) are flexible and able to adopt multiple conformations (1). However, the structures of both DENV-1 protease and DENV-3 protease-aprotinin show that more residues (beyond W61) from NS2B are interacting with NS3 (up to T68 and E66 of NS2B, respectively). These results suggest that the conformational change to the closed form is a dynamic and iterative process.
Cross-references: PDB:3U1J
Protein: DP02204 (UniProt Q5UB51)
Region: residues 1645	to 1655
Annotation: disorder (Structural state)
Evidence: X-ray crystallography-based structural model with missing residue coordinates used in manual assertion
Supporting statements:
The PDB shows the disorder region from 1645-1655 (NS3).
Cross-references: PDB:3U1J
PDB:3U1I
Protein: DP02205 (UniProt Q2TUW1)
Region: residues 1	to 238
Annotation: disorder (Structural state)
Evidence: far-UV circular dichroism evidence used in manual assertion
Supporting statements:
The protein was disordered in aqueous solution, as indicated by a single minimum at about 198 nm in the CD spectra.
Protein: DP02205 (UniProt Q2TUW1)
Region: residues 1	to 238
Annotation: zinc ion binding (Molecular function)
Evidence: far-UV circular dichroism evidence used in manual assertion
Supporting statements:
In contrast, the CD signal decayed sharply when various concentrations of Zn2þ (4–40 mM) were added (Fig. 3B), indicating that the structures of GmASR changed in the presence of Zn2þ.
Protein: DP02205 (UniProt Q2TUW1)
Region: residues 1	to 238
Annotation: nickel cation binding (Molecular function)
Evidence: affinity chromatography evidence used in manual assertion
Supporting statements:
Since the GmASR protein itself bound to the Ni beads in the purification column, there was no need to add His tags, usually a necessary step in this method.
However, it did remain in the columns immobilizing Fe3þ, Ni2þ, Cu2þ, and Zn2þ ions. The proteins retained in these columns were eluted by EDTA, indicating that GmASR was retained in the columns due to binding to Fe3þ, Ni2þ, Cu2þ, and Zn2þ (Fig. 1B).
Protein: DP02205 (UniProt Q2TUW1)
Region: residues 1	to 238
Annotation: iron ion binding (Molecular function)
Evidence: affinity chromatography evidence used in manual assertion
Supporting statements:
However, it did remain in the columns immobilizing Fe3þ, Ni2þ, Cu2þ,
and Zn2þ ions. The proteins retained in these columns were eluted by EDTA, indicating that GmASR was retained in the columns due to binding to Fe3þ, Ni2þ, Cu2þ, and Zn2þ (Fig. 1B).
Protein: DP02205 (UniProt Q2TUW1)
Region: residues 1	to 238
Annotation: copper ion binding (Molecular function)
Evidence: affinity chromatography evidence used in manual assertion
Supporting statements:
However, it did remain in the columns immobilizing Fe3þ, Ni2þ, Cu2þ,
and Zn2þ ions. The proteins retained in these columns were eluted by EDTA, indicating that GmASR was retained in the columns due to binding to Fe3þ, Ni2þ, Cu2þ, and Zn2þ (Fig. 1B).
Protein: DP02205 (UniProt Q2TUW1)
Region: residues 1	to 238
Annotation: zinc ion binding (Molecular function)
Evidence: affinity chromatography evidence used in manual assertion
Supporting statements:
However, it did remain in the columns immobilizing Fe3þ, Ni2þ, Cu2þ,
and Zn2þ ions. The proteins retained in these columns were eluted by EDTA, indicating that GmASR was retained in the columns due to binding to Fe3þ, Ni2þ, Cu2þ, and Zn2þ (Fig. 1B).
Protein: DP02205 (UniProt Q2TUW1)
Region: residues 1	to 238
Annotation: zinc ion binding (Molecular function)
Evidence: static fluorescence quenching evidence used in manual assertion
Supporting statements:
The results showed that the addition of Fe3þ or Zn2þ quenched the fluorescence of the GmASR protein markedly (Fig. 1C and D), providing further evidence that the protein does indeed bind directly to Fe3þ and Zn2þ ions.
Protein: DP02205 (UniProt Q2TUW1)
Region: residues 1	to 238
Annotation: iron ion binding (Molecular function)
Evidence: static fluorescence quenching evidence used in manual assertion
Supporting statements:
The results showed that the addition of Fe3þ or Zn2þ quenched the fluorescence of the GmASR protein markedly (Fig. 1C and D), providing further evidence that the protein does indeed bind directly to Fe3þ and Zn2þ ions.
Protein: DP02205 (UniProt Q2TUW1)
Region: residues 1	to 238
Annotation: iron ion binding (Molecular function)
Evidence: isothermal titration calorimetry evidence used in manual assertion
Supporting statements:
The calorimetric data for Fe3þ titration into a GmASR solution were fitted to a sequential three-site binding model, while the corresponding data for Zn2þ titration were fitted to a sequential two-site binding
model (Fig. 2, Table 1).
Protein: DP02205 (UniProt Q2TUW1)
Region: residues 1	to 238
Annotation: zinc ion binding (Molecular function)
Evidence: isothermal titration calorimetry evidence used in manual assertion
Supporting statements:
The calorimetric data for Fe3þ titration into a GmASR solution were fitted to a sequential three-site binding model, while the corresponding data for Zn2þ titration were fitted to a sequential two-site binding
model (Fig. 2, Table 1).
Protein: DP02205 (UniProt Q2TUW1)
Region: residues 1	to 238
Annotation: iron ion sequestering activity (Molecular function)
Evidence: isothermal titration calorimetry evidence used in manual assertion
Supporting statements:
Hydroxyl radicals in particular are highly reactive, and can be generated by the Fe-promoted Fenton reaction.13,18,21) To determine whether the GmASR protein can inhibit hydroxyl radical
generation, the effect of GmASR on hydroxyl radicals generated by Fe3þ was analyzed by measuring the degree of deoxyribose degradation.
The results showed that GmASR protein caused concentration-dependent inhibition of deoxyribose degradation under conditions consistent with a site-specific mechanism (Fig. 4A and B), but no
evidence was found of non-site-specific scavenging by GmASR of hydroxyl radicals (data not shown).
These results indicate that the GmASR protein blocks the generation of hydroxyl radicals by chelating Fe3þ ions (the site-specific mechanism) rather than by directly scavenging generated hydroxyl radicals (the non-sitespecific mechanism).
Protein: DP02205 (UniProt Q2TUW1)
Region: residues 1	to 238
Annotation: antioxidant activity (Molecular function)
Evidence: spectrophotometry evidence used in manual assertion
Supporting statements:
The anti-oxidative activity of the GmASR protein was found to be much higher than that of BSA, a standard protective agent against the hydroxyl radical (Fig. 4B). These results indicate that GmASR protein can reduce the levels of hydroxyl radical generated by the Fe3þ/H2O2 system via a site-specific mechanism, thereby inhibiting deoxyribose degradation as a consequence of its Fe3þ binding capability.
A common index of DNA damage is the conversion of the supercoiled form (SC) of plasmid DNA to the open circular (OC) and the linear form (LC).17) The inhibitory effect of the GmASR protein against oxidative DNA damage was investigated by a DNA cleavage assay using pET15b plasmid DNA. As Fig. 4C shows, in the absence of the protein, most of the supercoiled DNA was cut by the hydroxyl radicals generated by the
Fenton reaction (Fig. 4C, lanes 2–3). The GmASR protein protected DNA from oxidative damage in the absence of EDTA.
These results indicate that the GmASR protein blocks the generation of hydroxyl radicals by chelating Fe3þ ions (the site-specific mechanism) rather than by directly scavenging generated hydroxyl radicals (the non-sitespecific mechanism).
Protein: DP02206 (UniProt P15516)
Region: residues 20	to 51
Annotation: disorder (Structural state)
Evidence: nuclear magnetic resonance spectroscopy evidence used in manual assertion
Supporting statements:
However, H3 remains essentially unordered as suggested by the lack of longer range nuclear Overhauser effects (NOEs) in the NOESY spectrum.
Protein: DP02206 (UniProt P15516)
Region: residues 20	to 43
Annotation: disorder (Structural state)
Evidence: nuclear magnetic resonance spectroscopy evidence used in manual assertion
Supporting statements:
Col- lectively, the nmr data provide evidence that histatin 5 molecules are unstructured in aqueous solution.
Histatin 5 is a truncated form of Histatin 3.
Protein: DP02206 (UniProt P15516)
Region: residues 20	to 43
Annotation: disorder (Structural state)
Evidence: small-angle X-ray scattering evidence used in manual assertion
Supporting statements:
The plot enhances the large q region and reveals the flexibility/rigidity of the peptide. His5 shows a characteristic representation, typical for an IDP, indicated by the lack of a clear maximum in the curve. 
Histatin 5 is a truncated form of Histatin 3.
Protein: DP02206 (UniProt P15516)
Region: residues 20	to 51
Annotation: disorder (Structural state)
Evidence: far-UV circular dichroism evidence used in manual assertion
Supporting statements:
CD analysis of H3 indicated that H3 also has no well-defined secondary structure
in aqueous solution at pH 7.4.
Protein: DP02206 (UniProt P15516)
Region: residues 20	to 43
Annotation: disorder to order (Structural transition)
Evidence: nuclear magnetic resonance spectroscopy evidence used in manual assertion
Supporting statements:
However, histatin 5 prefers largelya-helical confor- mation  in  polar  aprotic  ( CD3)2SO  solution  that mimics the membrane environment.
Histatin 5 is a truncated form of Histatin 3.
Protein: DP02207 (UniProt P02808)
Region: residues 20	to 62
Annotation: disorder (Structural state)
Evidence: small-angle X-ray scattering evidence used in manual assertion
Supporting statements:
Fig. 6a shows the dimensionless Kratky plot, and as clearly visible, the profiles from the experiment and the simulation agree very well and display a random coil behavior, that is, a linear rise to a plateau at higher scattering angles.
Protein: DP02208 (UniProt A0A140GKJ0)
Region: residues 56	to 88
Annotation: disorder (Structural state)
Evidence: cryogenic electron microscopy-based structural model with missing residue coordinates used in manual assertion
Supporting statements:
The N-terminal 55 residues of ICP47 form a helical hairpin structure, which inserts into the opening between the two TM bundles. No density was observed for either the C-terminal 33 residues of ICP47 or the two TMD0s, indicating these regions are flexible in this conformation.
Cross-references: PDB:5U1D
Protein: DP02209 (UniProt O82132)
Region: residues 255	to 272
Annotation: disorder (Structural state)
Evidence: nuclear magnetic resonance spectroscopy evidence used in manual assertion
Supporting statements:
The 1H,15N HSQC spectrum of free DREB2A(255–272) showed limited dispersion in the proton dimension, indicating a lack of structure (Fig. 7A, black spectrum) (35). Consistent with this and with its far-UV CD spectrum (Fig. 6A), most residues have near-random coil secondary Cα chemical shifts (ΔδCα ≈0, Fig. 7D, top figure)
Protein: DP02209 (UniProt O82132)
Region: residues 255	to 272
Annotation: disorder (Structural state)
Evidence: far-UV circular dichroism evidence used in manual assertion
Supporting statements:
Experimental analysis for secondary structure content by far-UV CD indicated low α-helical contents of 12, 18, 10, and 13% in the ANAC013(254–274), DREB2A(255–272), COL10(175–208), and bZIP23(15–36) peptides, respectively
Protein: DP02209 (UniProt O82132)
Region: residues 168	to 335
Annotation: disorder (Structural state)
Evidence: far-UV circular dichroism evidence used in manual assertion
Supporting statements:
Using Far-UV CD, we found that the spectrum of the Dreb2a168–335 domain indicated a lack of secondary structure for this domain in solution. The negative maximum ∼200 nm implies an unstructured random coil conformation (Figure 1D).
Protein: DP02209 (UniProt O82132)
Region: residues 168	to 335
Annotation: protein binding (Molecular function)
Evidence: surface plasmon resonance evidence used in manual assertion
Supporting statements:
We found that only the extended C-terminal domain, Dreb2a 168–335 which includes both the BD and the AD, interacted with Med25 551–680 with significant affinity.
Protein: DP02209 (UniProt O82132)
Region: residues 255	to 272
Annotation: protein binding (Molecular function)
Evidence: far-UV circular dichroism evidence used in manual assertion
Supporting statements:
The spectrum of RCD1-RST(499–572) in complex with DREB2A(255–272) showed an absolute minimum shifted toward a higher wavelength compared with the theoretical spectrum. Moreover, the overall α-helical content in the complex was calculated to 39% compared with 31% in the theoretical complex. This indicated induction of structure upon complex formation (Fig. 6B).
Protein: DP02209 (UniProt O82132)
Region: residues 255	to 272
Annotation: disorder to order (Structural transition)
Evidence: far-UV circular dichroism evidence used in manual assertion
Supporting statements:
The spectrum of RCD1-RST(499–572) in complex with DREB2A(255–272) showed an absolute minimum shifted toward a higher wavelength compared with the theoretical spectrum. Moreover, the overall α-helical content in the complex was calculated to 39% compared with 31% in the theoretical complex. This indicated induction of structure upon complex formation (Fig. 6B).
Protein: DP02209 (UniProt O82132)
Region: residues 255	to 272
Annotation: disorder to order (Structural transition)
Evidence: nuclear magnetic resonance spectroscopy evidence used in manual assertion
Supporting statements:
The 1H,15N HSQC was dramatically changed upon addition of RCD1-RST(499–572) with a substantial increase in the 1H resonance dispersion (Fig. 7A, red spectrum). Furthermore, the Cα resonances for residues Val-261–Asp-267 experienced a significant downfield shift (ΔδCα >0), thus confirming the formation of an almost fully formed helical structure in this region (Fig. 7D, bottom figure) (34). Notably, the HSQC as well as the different triple resonance spectra lacked peaks for Phe-259 and Asp-260. This is consistent with the abolished binding of the F259A mutant (Fig. 2D; Table 3) and suggests that these residues are involved in the interaction.
Protein: DP02209 (UniProt O82132)
Region: residues 255	to 272
Annotation: protein binding (Molecular function)
Evidence: nuclear magnetic resonance spectroscopy evidence used in manual assertion
Supporting statements:
The 1H,15N HSQC was dramatically changed upon addition of RCD1-RST(499–572) with a substantial increase in the 1H resonance dispersion (Fig. 7A, red spectrum). Furthermore, the Cα resonances for residues Val-261–Asp-267 experienced a significant downfield shift (ΔδCα >0), thus confirming the formation of an almost fully formed helical structure in this region (Fig. 7D, bottom figure) (34). Notably, the HSQC as well as the different triple resonance spectra lacked peaks for Phe-259 and Asp-260. This is consistent with the abolished binding of the F259A mutant (Fig. 2D; Table 3) and suggests that these residues are involved in the interaction.
Protein: DP02209 (UniProt O82132)
Region: residues 255	to 272
Annotation: protein binding (Molecular function)
Evidence: isothermal titration calorimetry evidence used in manual assertion
Supporting statements:
The affinity of the interaction between RCD1-RST(499–572) and a short peptide of DREB2A, DREB2A(255–272), containing a predicted α-helix, was significantly lower, corresponding to a Kd of 117 nm, but with a large enthalpic contribution to binding of −51 kJ/mol (Fig. 2C).
Protein: DP02209 (UniProt O82132)
Region: residues 259	to 270
Annotation: disorder to order (Structural transition)
Evidence: nuclear magnetic resonance spectroscopy evidence used in manual assertion
Supporting statements:
When bound to RCD1-RST, DREB2A255-272 formed an a helix from V261-G270, with D260 forming an N-cap supported by the interaction between the residues in the N0-(F259) and N4-(L264) positions of the hydrophobic staple motif (Munoz et al., 1995) (Figure 2F).
Cross-references: BMRB:34152
PDB:5OAP
Protein: DP02209 (UniProt O82132)
Region: residues 259	to 270
Annotation: protein binding (Molecular function)
Evidence: nuclear magnetic resonance spectroscopy evidence used in manual assertion
Supporting statements:
The structure of bound DREB2A255-272 was solved using NMR data acquired with only DREB2A isotope labeled.
When bound to RCD1-RST, DREB2A255-272 formed an a helix from V261-G270, with D260 forming an N-cap supported by the interaction between the residues in the N0-(F259) and N4-(L264) positions of the hydrophobic staple motif (Munoz et al., 1995) (Figure 2F).
Cross-references: BMRB:34152
PDB:5OAP