LiteFold/DisProt huggingface dataset:
Protein: DP00435 (UniProt Q01853)
Region: residues 736	to 806
Annotation: disorder (Structural state)
Evidence: X-ray crystallography-based structural model with missing residue coordinates used in manual assertion
Supporting statements:
Our crystal structure of murine p97 comprises residues 17–700 and consists of: complete models for the N terminal substrate binding domain and the D1 AAA domain, and a poly-alanine partial model for the D2 AAA domain, in which the α-helical and C-terminal regions are highly disordered (see representative densities in Fig. 1).
The PDB shows that this region lacks electron density, indicating that it is disordered.
Cross-references: PDB:1R7R
Protein: DP00435 (UniProt Q01853)
Region: residues 703	to 726
Annotation: disorder (Structural state)
Evidence: X-ray crystallography-based structural model with missing residue coordinates used in manual assertion
Supporting statements:
Our crystal structure of murine p97 comprises residues 17–700 and consists of: complete models for the N terminal substrate binding domain and the D1 AAA domain, and a poly-alanine partial model for the D2 AAA domain, in which the α-helical and C-terminal regions are highly disordered (see representative densities in Fig. 1).
The PDB shows that this region lacks electron density, indicating that it is disordered.
Cross-references: PDB:1R7R
Protein: DP00435 (UniProt Q01853)
Region: residues 708	to 727
Annotation: disorder (Structural state)
Evidence: X-ray crystallography-based structural model with missing residue coordinates used in manual assertion
Supporting statements:
The refined model consists of residues 463–707 and 728–763. Electron density was not well defined for the first two and last 42 residues, as well as the loop from 708 to 727.
Cross-references: PDB:3CF0
Protein: DP00435 (UniProt Q01853)
Region: residues 708	to 727
Annotation: flexible linker (Disorder function)
Evidence: X-ray crystallography-based structural model with missing residue coordinates used in manual assertion
Supporting statements:
The refined model consists of residues 463–707 and 728–763. Electron density was not well defined for the first two and last 42 residues, as well as the loop from 708 to 727.
Cross-references: PDB:3CF0
Protein: DP00435 (UniProt Q01853)
Region: residues 1	to 20
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 PDB shows that this region lacks electron density, indicating that it is disordered.
Cross-references: PDB:3CF2
Protein: DP00435 (UniProt Q01853)
Region: residues 1	to 20
Annotation: disorder (Structural state)
Evidence: X-ray crystallography-based structural model with missing residue coordinates used in manual assertion
Supporting statements:
The PDB shows that this region lacks electron density, indicating that it is disordered.
Cross-references: PDB:3CF2
Protein: DP00435 (UniProt Q01853)
Region: residues 583	to 596
Annotation: disorder (Structural state)
Evidence: X-ray crystallography-based structural model with missing residue coordinates used in manual assertion
Supporting statements:
The PDB shows that this region lacks electron density, indicating that it is disordered.
Cross-references: PDB:3CF2
Protein: DP00435 (UniProt Q01853)
Region: residues 583	to 596
Annotation: flexible linker (Disorder function)
Evidence: X-ray crystallography-based structural model with missing residue coordinates used in manual assertion
Supporting statements:
The PDB shows that this region lacks electron density, indicating that it is disordered.
Resides R586 and R599 are located on a loop at the entrance to the D2 pore, and have been proposed to participate in the denaturing of substrate proteins.
Cross-references: PDB:3CF2
Protein: DP00435 (UniProt Q01853)
Region: residues 665	to 685
Annotation: disorder (Structural state)
Evidence: X-ray crystallography-based structural model with missing residue coordinates used in manual assertion
Supporting statements:
The PDB shows that this region lacks electron density, indicating that it is disordered.
Cross-references: PDB:3CF2
Protein: DP00435 (UniProt Q01853)
Region: residues 705	to 806
Annotation: disorder (Structural state)
Evidence: X-ray crystallography-based structural model with missing residue coordinates used in manual assertion
Supporting statements:
The PDB shows that this region lacks electron density, indicating that it is disordered.
Cross-references: PDB:3CF2
Protein: DP00437 (UniProt P43351)
Region: residues 1	to 23
Annotation: disorder (Structural state)
Evidence: X-ray crystallography-based structural model with missing residue coordinates used in manual assertion
Supporting statements:
Domain 1 (residues 24–177, the N-terminal 23 residues of the protein are disordered) forms the core of the structure and has a mixed α/β structure.
Cross-references: PDB:1H2I
Protein: DP00443 (UniProt Q14191)
Region: residues 1064	to 1092
Annotation: disorder (Structural state)
Evidence: nuclear magnetic resonance spectroscopy evidence used in manual assertion
Supporting statements:
The solution structure of the DPBD, the first of a WRN fragment, has been solved by NMR. DPBD consists of a winged helix-like motif and an unstructured C-terminal region of approximately 20 aa.
The ensemble within the box displays all 144 residues and illustrates the disordered N and C termini.
The C-terminal 24 residues are largely unstructured (Fig. 2). The unstructured C terminus contains two cysteine residues, C1070 and C1090, which most likely contribute to the oligomerization of the protein.
The significance of the unstructured C terminus in the DPBD in the DNA and protein binding remains to be determined.
Cross-references: PDB:2AXL
Protein: DP00445 (UniProt P02511)
Region: residues 166	to 175
Annotation: flexible C-terminal tail (Disorder function)
Evidence: nuclear magnetic resonance spectroscopy evidence used in manual assertion
Supporting statements:
The heterogeneous region 1 (HR1), the IXI motif, the flexible C-terminal residues Lys166–Lys175 and three disease-related mutations involved in cataract and myopathy (R120G, D140N and Gln151-stop) are indicated.
Protein: DP00445 (UniProt P02511)
Region: residues 153	to 175
Annotation: disorder (Structural state)
Evidence: nuclear magnetic resonance spectroscopy evidence used in manual assertion
Supporting statements:
The C-terminal residues of αB are highly dynamic and yielded narrow
resonances in solution-state 1H-15N correlation experiments (Fig. 2a).
In contrast to previous studies, in which only residues E164–K175
have been observed36,37, in our study we assigned 11 additional
residues, thus yielding assignments for the entire C-terminal stretch
S153–K175 (Supplementary Table 2)
Cross-references: BMRB:26640
Protein: DP00445 (UniProt P02511)
Region: residues 166	to 175
Annotation: disorder (Structural state)
Evidence: small-angle X-ray scattering evidence used in manual assertion
Supporting statements:
The individual bead models (Supplementary Fig. 6b) generated using the program GASBOR38 have extrusions emanating from the central body, which we interpret as flexible C-terminal residues 166–175 of the oligomer39.
We consider this solution as one species in a heterogeneous ensemble of oligomers. Variable conformations of the flexible C-terminal extensions (residues Lys166–Lys175) and variable intermolecular interactions may contribute to the observed heterogeneity.
Protein: DP00445 (UniProt P02511)
Region: residues 151	to 175
Annotation: disorder (Structural state)
Evidence: nuclear magnetic resonance evidence used in manual assertion
Supporting statements:
At pH 6.5, the involved isoleucines and threonines (Thr132 and Thr134 in β8 and Thr158 and Thr162 of the C terminus) show chemical-shift perturbations or doubling of intraresidual cross-peaks (for example, at ∼59–63 p.p.m., ∼36–39 p.p.m. or 26 p.p.m. in F1 and at 69–72.5 p.p.m. or 9.5–27 p.p.m. in F2), indicating a pH-dependent change in the substrate binding groove (Figs. 3a and 5a). 
Residues 151-175 are unmodeled in PDB entry 2KLR 
NMR spectra collected at pH 7.5 reveal a structurally homogeneous part of the protein comprising α-crystallin domain residues 71–150, with the exception of Ser76, Val77 and Asn78 in the β3 strand, which each show two backbone 15N signals.
Cross-references: ELM:LIG_sHSP_IxI_1
PDB:2KLR
Protein: DP00446 (UniProt O35718)
Region: residues 128	to 163
Annotation: disorder (Structural state)
Evidence: nuclear magnetic resonance spectroscopy evidence used in manual assertion
Supporting statements:
Significantly, there was a large unstructured region between Met128 and Arg163 that contained a high proportion of proline residues (12 out of 35).
Cross-references: BMRB:6580
Protein: DP00446 (UniProt O35718)
Region: residues 129	to 163
Annotation: disorder (Structural state)
Evidence: nuclear magnetic resonance spectroscopy evidence used in manual assertion
Supporting statements:
The SH2 domain is formed by residues Gly45-Asn185, excluding an unstructured insert of 35 residues (Pro129-Arg163).
Following helix B, there is a 35 residue insert, a PEST motif (Rogers et al., 1986). This displays no evidence of structure, and backbone amide NMR relaxation data suggest a high degree of flexibility (see Figures S1 and S2 in the Supplemental Data available with this article online).
Cross-references: PDB:2BBU
Protein: DP00446 (UniProt O35718)
Region: residues 129	to 163
Annotation: limited proteolysis display site (Disorder function)
Evidence: co-immunoprecipitation evidence used in manual assertion
Supporting statements:
Intracellular levels of SOCS3 are strongly regulated by proteolysis. As PEST motifs are known to be signals for protein degradation in vivo, we measured the half-life of SOCS3 proteins that lacked the PEST motif, as well as constructs lacking both the SOCS box and the N-terminal region.
Pulse-chase experiments show that removing the PEST motif decreases SOCS3 turnover (Figure 5A) in both full-length SOCS3 (Figure 5A, left panel) and SOCS3(22-185) (Figure 5A, right panel). Removing the PEST motif had a greater effect on SOCS3 stability than did removing both the SOCS box and N-terminal domain.
The PEST motif consists of the Pro129-Arg163 residues.
Protein: DP00446 (UniProt O35718)
Region: residues 186	to 225
Annotation: disorder (Structural state)
Evidence: nuclear magnetic resonance spectroscopy evidence used in manual assertion
Supporting statements:
A 42-residue 15N-labelled recombinant SOCS box peptide was produced; the 1H–15N HSQC spectrum of this isolated peptide is characteristic of that of an unstructured protein (Fig. 4a).
Overhauser enhancement spectroscopy (NOESY) experiments of unlabelled SOCS box domain also suggested that the peptide was completely unstructured in solution (data not shown).
The SOCS box is unstructured in isolation but becomes structured upon elonginBC association
These data imply that the C-terminal half of the SOCS box undergoes significant conformational exchange in the absence of bound cullin5 whether as an isolated domain or as part of full-length SOCS3.
Protein: DP00446 (UniProt O35718)
Region: residues 186	to 197
Annotation: disorder to order (Structural transition)
Evidence: nuclear magnetic resonance spectroscopy evidence used in manual assertion
Supporting statements:
Resonances that could be assigned in this region showed α-helical chemical shifts but were significantly broadened and displayed NOEs only to adjacent residues. In contrast, the N-terminal half of the SOCS box, which contains the elonginBC-binding motif (the BC box, residues 1–12) was completely assigned and well structured.
The SOCS box is unstructured in isolation but becomes structured upon elonginBC association
These data imply that the C-terminal half of the SOCS box undergoes significant conformational exchange in the absence of bound cullin5 whether as an isolated domain or as part of full-length SOCS3.
This region, the SOCS3 elonginBC binding motif (termed the BC box), which is completely unstructured as an isolated peptide and only adopts structure upon binding, exists as a nine-residue α-helix with a three-residue N-terminal extension.
Cross-references: PDB:2JZ3
Protein: DP00446 (UniProt O35718)
Region: residues 186	to 197
Annotation: protein binding (Molecular function)
Evidence: nuclear magnetic resonance spectroscopy evidence used in manual assertion
Supporting statements:
Resonances that could be assigned in this region showed α-helical chemical shifts but were significantly broadened and displayed NOEs only to adjacent residues. In contrast, the N-terminal half of the SOCS box, which contains the elonginBC-binding motif (the BC box, residues 1–12) was completely assigned and well structured.
The SOCS box is unstructured in isolation but becomes structured upon elonginBC association
These data imply that the C-terminal half of the SOCS box undergoes significant conformational exchange in the absence of bound cullin5 whether as an isolated domain or as part of full-length SOCS3.
This region, the SOCS3 elonginBC binding motif (termed the BC box), which is completely unstructured as an isolated peptide and only adopts structure upon binding, exists as a nine-residue α-helix with a three-residue N-terminal extension.
Cross-references: PDB:2JZ3
Protein: DP00446 (UniProt O35718)
Region: residues 186	to 197
Annotation: protein binding (Molecular function)
Evidence: isothermal titration calorimetry evidence used in manual assertion
Supporting statements:
Therefore, the minimal high-affinity binding epitope for elonginBC on SOCS3 is VATLQHLCRKTV 197, corresponding to residues 1–12 of the SOCS box domain.
Protein: DP00446 (UniProt O35718)
Region: residues 15	to 28
Annotation: disorder (Structural state)
Evidence: X-ray crystallography-based structural model with missing residue coordinates used in manual assertion
Supporting statements:
Residues 15–28, which include residues 22–28 of the kinase inhibitory region, are disordered.
Cross-references: PDB:2HMH
Protein: DP00447 (UniProt P12579)
Region: residues 164	to 241
Annotation: disorder (Structural state)
Evidence: cleavage assay evidence used in manual assertion
Supporting statements:
N-terminal sequencing and MS set the limits of the trypsin-resistant fragment (X) between aa 104 and 163.
Protein: DP00447 (UniProt P12579)
Region: residues 1	to 103
Annotation: disorder (Structural state)
Evidence: cleavage assay evidence used in manual assertion
Supporting statements:
N-terminal sequencing and MS set the limits of the trypsin-resistant fragment (X) between aa 104 and 163.
Protein: DP00461 (UniProt P08083)
Region: residues 67	to 90
Annotation: disorder (Structural state)
Evidence: X-ray crystallography-based structural model with missing residue coordinates used in manual assertion
Supporting statements:
Here, we present the crystal structure, at 3.1 å resolution, of a large fragment of colicin N (missing the first 66 residues) that contains the pore-forming and the receptor-binding domains.
The translocation domain, located between residues 17 and 66 [44], has a glycine/proline/serine/asparagine-rich sequence, which is likely to have poorly defined secondary structure. The translocation domain is absent in the 3.1 å resolution structure, but the majority of it is present in the initial crystal form (see the Materials and methods section), which comprises residues 37–387.
There is no evidence of any density for the translocation domain; this is in complete accord with circular dichroism and fluorescence results, which demonstrate that this domain does not adopt any regular secondary structure.
The residue boundaries differ from the ones reported by the authors, because they did not use the UniProt sequence (the latter contains a signal peptide).
Cross-references: PDB:1A87
Protein: DP00461 (UniProt P08083)
Region: residues 1	to 90
Annotation: disorder to order (Structural transition)
Evidence: far-UV circular dichroism evidence used in manual assertion
Supporting statements:
By expressing the far-UV CD spectra in units of dE where concentration is in moles of protein/liter rather than the more conventional moles of residues/liter we can generate the expected spectrum of a 1:1 mixture of TolA-(296 – 421) and T-domain (Fig. 1B). This can be compared with the measured far-UV CD spectrum of the 1:1 complex. The spectra are different, indicating that changes in secondary structure occur upon binding. The difference between TolA-(296 – 421) and the complex is also shown (Fig. 1A). This may correspond to the new structure of the T-domain with a reduction in the unstructured component and its replacement by a secondary structure signal (210–225 nm).
The CD data suggest large scale changes in the secondary structure of the T-domain during TolA binding. The measured spectrum of the complex differs significantly from the summed spectra of the two individual components, and subtraction of the TolA-(296 – 421) spectrum from the complex reveals a “T- domain like” signal, which, however, contains less random and more secondary structure.
Protein: DP00461 (UniProt P08083)
Region: residues 2	to 90
Annotation: disorder (Structural state)
Evidence: nuclear magnetic resonance spectroscopy evidence used in manual assertion
Supporting statements:
The 1H– 15N HSQC spectrum of N-labelled intact colicin N confirms that the protein contains a largely unstructured and flexible region (Fig. 1), as indicated by the numerous sharp amide NH resonances with a narrow 1H chemical shift dispersion, between 7.5 and 9 ppm, seen in the spectrum at a high threshold where broad peaks from the folded domains are not visible (Fig. 1). Sequential assignment of these resonances revealed that they belong to the 90 residue T-domain.
resonances for T-domain 2–90 are sharp signals with a relatively narrow 1H chemical shift dispersion as expected for a disordered protein
Cross-references: BMRB:15506
Protein: DP00461 (UniProt P08083)
Region: residues 2	to 90
Annotation: protein binding (Molecular function)
Evidence: nuclear magnetic resonance spectroscopy evidence used in manual assertion
Supporting statements:
All of the 85 expected backbone NH resonances of T-domain 2–90 could be assigned unambiguously (Fig. 3) consistent with an intra-molecular interaction of the T-domain of intact colicin N with one of its folded domains.
Protein: DP00461 (UniProt P08083)
Region: residues 1	to 90
Annotation: disorder (Structural state)
Evidence: far-UV circular dichroism evidence used in manual assertion
Supporting statements:
The isolated colicin N N-terminal domain appears to be unstructured in circular dichroism 
The isolated T-domain is unstructured. The circular dichroism (CD) spectrum of the isolated T- domain shows a random coil conformation, although the negative signal between 210 and 240nm may indicate some ordered secondary structure
Protein: DP00461 (UniProt P08083)
Region: residues 1	to 90
Annotation: disorder (Structural state)
Evidence: fluorescence evidence used in manual assertion
Supporting statements:
The isolated colicin N N-terminal domain appears to be unstructured in circular dichroism and fluorescence studies.
Consistent with the random coil CD data, the two tryptophans of the isolated T-domain are exposed to the aqueous phase
The aqueous exposure of the tryptophans is further evidence of the unfolded state of the isolated T-domain
Protein: DP00461 (UniProt P08083)
Region: residues 1	to 90
Annotation: protein binding (Molecular function)
Evidence: isothermal titration calorimetry evidence used in manual assertion
Supporting statements:
We have measured the binding of colicin N to TolA by isothermal titration microcalorimetry (ITC)
The isolated N-terminal domain exhibits a higher affinity for TolA (Kd = 1 uM) than does the whole colicin (18 uM)

Isolated T-domain has a higher TolA binding affinity than colicin N
the isolated T-domain shows more than a 10-fold increase in affinity in ITC experiments
The isolated T-domain has a dissociation constant of 1uM for TolA
Protein: DP00461 (UniProt P08083)
Region: residues 1	to 90
Annotation: protein binding (Molecular function)
Evidence: dynamic fluorescence quenching evidence used in manual assertion
Supporting statements:
We have measured the binding of colicin N to TolA by isothermal titration microcalorimetry (ITC) and tryptophan fluorescence
On complex formation with TolA, the tryptophans of the T-domain become buried with a Stern–Volmer constant of 0.8 M-1.
Protein: DP00461 (UniProt P08083)
Region: residues 40	to 76
Annotation: pre-molten globule (Structural state)
Evidence: nuclear magnetic resonance spectroscopy evidence used in manual assertion
Supporting statements:
T-domain does not exist as an extended strand in solution, but rather adopts a compact average conformation without forming long stretches of secondary structure.
The initial 1H-15N HSQC spectrum of the T-domain 40–76 peptide in solution showed at least 35 peaks, excluding side chain signals, suggesting that all the backbone NH resonances were detected between 7.7 and 8.7 ppm (1H). NOESY data collected on the peptide showed very few cross-peaks, presumably owing to its flexibility. The 1H-15N HSQC peaks of the T-domain 40–76 are clearly not clustered in the narrow region (~0.45 ppm 1H) to be expected for a random coil, but are more dispersed, covering a range of 1 ppm (1H), which indicates that the peptide has at least some regions of non-random structure. However, if the peptide were rigidly structured the NOESY spectrum would be expected to show considerably more cross-peaks than were observed.
Protein: DP00461 (UniProt P08083)
Region: residues 1	to 90
Annotation: protein binding (Molecular function)
Evidence: fluorescence evidence used in manual assertion
Supporting statements:
The binding to TolA-II,III was measured by tryptophan fluorescence and SPR (Fig. 2 and Table I). S58C, S61C, N70C, and N71C exhibit binding comparable to the wild-type T-domain.
Protein: DP00461 (UniProt P08083)
Region: residues 1	to 90
Annotation: protein binding (Molecular function)
Evidence: surface plasmon resonance evidence used in manual assertion
Supporting statements:
The binding to TolA-II,III was measured by tryptophan fluorescence and SPR (Fig. 2 and Table I). S58C, S61C, N70C, and N71C exhibit binding comparable to the wild-type T-domain.
Protein: DP00461 (UniProt P08083)
Region: residues 1	to 90
Annotation: protein binding (Molecular function)
Evidence: fluorescence resonance energy transfer evidence used in manual assertion
Supporting statements:
For labeled sample k-1 was five times higher (0.051 +/- 0.037 s-1) than for the unlabeled one (0.011 +/- 0.012 s-1). This gives Kd values of 0.5 uM for N71C and 0.1 uM for N71C-AEDANS. The k1 values are similar to those obtained by the 90-residue wild-type T-domain (1.6 * 10^5 M-1 s-1) in the same system (13), while the k-1 value for the wild-type was higher (0.37 s-1).
Protein: DP00461 (UniProt P08083)
Region: residues 1	to 90
Annotation: protein binding (Molecular function)
Evidence: fluorescence evidence used in manual assertion
Supporting statements:
Fluorescence and surface plasmon resonance confirm that the new unfolding transition accompanies dissociation of ColN-(1–90). Hence upon binding the disordered structure of ColN-(1–90) converts to a cooperatively folded domain without altering the TolA-(296–421) structure.
The binding of full-length (ColN-(1–90)) T-domain to these TolA variants was measured using fluorescence spectroscopy and gel filtration chromatography. The T-domain contains two tryptophans that become buried upon TolA binding causing both an increase and a blue shift of their fluorescence emission (32–34). Both TolA variants with natural C termini bound to T-domain with similar affinity.