LiteFold/DisProt huggingface dataset:
Protein: DP03647 (UniProt Q9M2T2)
Region: residues 111	to 156
Annotation: disorder (Structural state)
Evidence: nuclear magnetic resonance evidence used in manual assertion
Supporting statements:
In the solution structure of the protein, secondary structural elements are formed by residues 3–9 (β1), 56–62 (β2), 133–135 (β3), and 96–110 (α-helix). Most of the rest of the chain segments are disordered.
Cross-references: PDB:5YQ3
Protein: DP03648 (UniProt Q9SL42)
Region: residues 20	to 37
Annotation: disorder (Structural state)
Evidence: nuclear magnetic resonance evidence used in manual assertion
Supporting statements:
The coordinates of residues in disordered regions 1–6 and 20–37 were not considered.
Cross-references: PDB:1J6Y
BMRB:4670
Protein: DP03648 (UniProt Q9SL42)
Region: residues 20	to 37
Annotation: flexible linker (Disorder function)
Evidence: nuclear magnetic resonance evidence used in manual assertion
Supporting statements:
The PIN1At fold could be superimposed on that of the catalytic domain of hPIN1 and had a 19 residue flexible loop located between strand β1 and helix α1.
Cross-references: BMRB:4670
PDB:1J6Y
Protein: DP03649 (UniProt Q9UQ80)
Region: residues 363	to 394
Annotation: disorder (Structural state)
Evidence: X-ray crystallography-based structural model with missing residue coordinates used in manual assertion
Supporting statements:
In addition to the human MAP2 fold, Ebp1 contains a C-terminal elongation of 57 residues. Part of it is ordered in the crystal structure (residues 340–362) and attaches a short amphipathic α-helix (α10) to the outer face of the second half of the pita-bread fold (1, 4 ).
Cross-references: PDB:2Q8K
Protein: DP03649 (UniProt Q9UQ80)
Region: residues 364	to 368
Annotation: phosphorylation display site (Disorder function)
Evidence: mutant phenotype evidence used in manual assertion
Supporting statements:
Substitution of Ala at 366Thr resulted in a 90% decrease in phosphorylation.
Our in vitro data indicate that a peptide corresponding to amino acids 361–371 was phosphorylated in vitro, and that mutation of 366Thr, but not 363Ser, decreased phosphorylation. This finding suggests that 366Thr, present in the C-terminal end of the protein necessary for ErbB3 binding and upstream of a putative nuclear localization signal (KKKK) (Lamartine et al., 1997,) may be phosphorylated in vivo by PKC.
Protein: DP03650 (UniProt Q01484)
Region: residues 1113	to 1122
Annotation: disorder (Structural state)
Evidence: X-ray crystallography-based structural model with missing residue coordinates used in manual assertion
Supporting statements:
The final structural model contains most of residues from ankyrin-B ZZUD except for a few flexible loops (Fig. 1A).
The Ankyrin-2 fragment used in this publication was derived from the UniProtKB: A0A5F9ZHA, IDR is 100% identical.
Cross-references: PDB:4D8O
Protein: DP03650 (UniProt Q01484)
Region: residues 1113	to 1122
Annotation: flexible linker (Disorder function)
Evidence: X-ray crystallography-based structural model with missing residue coordinates used in manual assertion
Supporting statements:
The final structural model contains most of residues from ankyrin-B ZZUD except for a few flexible loops (Fig. 1A).
The Ankyrin-2 fragment used in this publication was derived from the UniProtKB: A0A5F9ZHA, IDR is 100% identical.
Cross-references: PDB:4D8O
Protein: DP03650 (UniProt Q01484)
Region: residues 1457	to 1476
Annotation: flexible linker (Disorder function)
Evidence: X-ray crystallography-based structural model with missing residue coordinates used in manual assertion
Supporting statements:
The final structural model contains most of residues from ankyrin-B ZZUD except for a few flexible loops (Fig. 1A).
The Ankyrin-2 fragment used in this publication was derived from the UniProtKB: A0A5F9ZHA, IDR is 100% identical.
Cross-references: PDB:4D8O
Protein: DP03650 (UniProt Q01484)
Region: residues 1457	to 1476
Annotation: disorder (Structural state)
Evidence: X-ray crystallography-based structural model with missing residue coordinates used in manual assertion
Supporting statements:
The final structural model contains most of residues from ankyrin-B ZZUD except for a few flexible loops (Fig. 1A).
The Ankyrin-2 fragment used in this publication was derived from the UniProtKB: A0A5F9ZHA, IDR is 100% identical.
Cross-references: PDB:4D8O
Protein: DP03650 (UniProt Q01484)
Region: residues 817	to 873
Annotation: disorder (Structural state)
Evidence: X-ray crystallography-based structural model with missing residue coordinates used in manual assertion
Supporting statements:
The lack of electron density in this region, as show in the PDB, indicates a disorder region.
Cross-references: PDB:4RLV
Protein: DP03650 (UniProt Q01484)
Region: residues 846	to 873
Annotation: disorder (Structural state)
Evidence: X-ray crystallography-based structural model with missing residue coordinates used in manual assertion
Supporting statements:
The lack of electron density in this region, shown in the PDB, indicates a disorder region.
Cross-references: PDB:5Y4F
Protein: DP03650 (UniProt Q01484)
Region: residues 683	to 693
Annotation: disorder (Structural state)
Evidence: X-ray crystallography-based structural model with missing residue coordinates used in manual assertion
Supporting statements:
The lack of electron density in this region, shown in the PDB, indicates a disorder region.
Cross-references: PDB:5Y4D
Protein: DP03650 (UniProt Q01484)
Region: residues 1243	to 1255
Annotation: disorder (Structural state)
Evidence: X-ray crystallography-based structural model with missing residue coordinates used in manual assertion
Supporting statements:
The lack of electron density in this region, shown in the PDB, indicates a disorder region.
Cross-references: PDB:6M3Q
Protein: DP03651 (UniProt Q9MBH1)
Region: residues 148	to 165
Annotation: disorder (Structural state)
Evidence: nuclear magnetic resonance evidence used in manual assertion
Supporting statements:
Heteronuclear 15N-1H NOE values shown in Figure 1(E) reflect the relative rigidity of the secondary structure elements and disorder in the C-terminus, specifically beyond the untethered C-terminal α-helix. 
Cross-references: PDB:2JQV
BMRB:15295
Protein: DP03651 (UniProt Q9MBH1)
Region: residues 110	to 121
Annotation: disorder (Structural state)
Evidence: nuclear magnetic resonance evidence used in manual assertion
Supporting statements:
Residue ranges for secondary structure elements include: α1(19–27), α2(71–81), α3(122–147), α4(152–157), β1(9–13), β2(32–39), β3(42–43), β4(54–55), β5(61–70), β6(86–95) and β7(101–109).
Cross-references: PDB:2JQV
BMRB:15295
Protein: DP03652 (UniProt Q9LTJ1)
Region: residues 128	to 140
Annotation: disorder (Structural state)
Evidence: nuclear magnetic resonance evidence used in manual assertion
Supporting statements:
The obtained 20 minimum energy structures were well defined, as indicated by the root-mean-square deviation (RMSD) for the backbone of 0.6 ± 0.2 Å except for a loop region (residues 93–98) and a disordered C-terminal region (residues 128–140) (Figure2A and Table 2).
Cross-references: PDB:7D8K
Protein: DP03652 (UniProt Q9LTJ1)
Region: residues 67	to 78
Annotation: disorder (Structural state)
Evidence: X-ray crystallography-based structural model with missing residue coordinates used in manual assertion
Supporting statements:
The PDB structure of AtMBD6 with methylated DNA shows this region lacks electron density, indicating it is disordered. 
Cross-references: PDB:7FEF
Protein: DP03652 (UniProt Q9LTJ1)
Region: residues 127	to 137
Annotation: disorder (Structural state)
Evidence: X-ray crystallography-based structural model with missing residue coordinates used in manual assertion
Supporting statements:
The PDB structure of AtMBD6 with methylated DNA shows this region lacks electron density, indicating it is disordered. 
Cross-references: PDB:7FEF
Protein: DP03653 (UniProt Q1ECR9)
Region: residues 27	to 82
Annotation: disorder (Structural state)
Evidence: nuclear magnetic resonance evidence used in manual assertion
Supporting statements:
The protein is dynamically disordered with the exception of two ordered loops that are held together by disulfide bridges. The C21–C29 loop (red) is more ordered than the C41–C47 loop (magenta), and the two ordered regions are independently ordered.
Cross-references: PDB:6NU4
Protein: DP03653 (UniProt Q1ECR9)
Region: residues 27	to 82
Annotation: positive regulation of cytosolic calcium ion concentration (Biological process)
Evidence: nuclear magnetic resonance evidence used in manual assertion
Supporting statements:
Purified samples of the native sequence of RALF8 exhibited well-resolved nuclear magnetic resonance (NMR) spectra and also biological activity through interaction with a plant receptor kinase, cytoplasmic calcium mobilization, and in vivo root growth suppression.
RALF8 samples were shown to be active by a cytoplasmic calcium mobilization assay [Fig.4(a)] and by a root growth inhibition assay [Fig.4(b,c)].
Protein: DP03653 (UniProt Q1ECR9)
Region: residues 27	to 82
Annotation: regulation of root meristem growth (Biological process)
Evidence: in vivo assay evidence used in manual assertion
Supporting statements:
Purified samples of the native sequence of RALF8 exhibited well-resolved nuclear magnetic resonance (NMR) spectra and also biological activity through interaction with a plant receptor kinase, cytoplasmic calcium mobilization, and in vivo root growth suppression.
Wild‐type roots showed 75% growth inhibition at 1μM RALF8 concentration compared with the control condition, whereas fer knockout mutant roots were completely insensitive to RALF8‐caused suppression up to 5μM RALF8, with the highest concentration examined in this study.
Protein: DP03654 (UniProt P63104)
Region: residues 234	to 245
Annotation: disorder (Structural state)
Evidence: nuclear magnetic resonance spectroscopy evidence used in manual assertion
Supporting statements:
NMR spectroscopy of 14-3-3ζ reveals a flexible C-terminal extension: differentiation of the chaperone and phosphoserine-binding activities of 14-3-3ζ
1H-NMR spectroscopy revealed the presence of a flexible and unstructured C-terminal extension, 12 amino acids in length, which protrudes from the domain core of 14-3-3ζ and is similar in structure and length to the C-terminal extension of mammalian sHsps. 
It is concluded that, like sHsps, 14-3-3ζ has a short C-terminal extension that is flexible, polar and unstructured. Its function is to stabilize and solubilize the protein, and it has no direct role in its chaperone action.
Taken together these results indicated that the strongest cross-peaks in the two-dimensional NMR spectra of full-length 14-3-3ζ were attributable to the 12 amino acid residues at the extreme C-terminus of the 14-3-3ζ dimer (i.e. from Gly234 to Asn245), with no cross-peaks being observed for residues preceding Gly234.
From this, it can be inferred that the amino acids from Trp228 to Gln233 (inclusive) form a ‘hinge’ which has decreased conformational flexibility, spanning the region between the domain core of the protein and the 12 amino acids (Gly234–Asn245) at the extreme C-terminus of 14-3-3ζ which have significantly enhanced flexibility. 
The significant overlap of cross-peaks in the TOCSY spectra of 14-3-3ζ from Gly234 to Asn245 with the peptide corresponding to the last 16 amino acids of the protein, the close similarity of α-CH chemical shifts to random coil values [32] and the presence of strong sequential NHi+ 1 to α-CHi nuclear Overhauser effects show that the C-terminus of 14-3-3ζ has an extended conformation with little or no preferred secondary structure, and a much greater degree of conformational flexibility than the rest of the protein. Thus 14-3-3ζ has a flexible C-terminal extension encompassing its last 12 amino acids that is directly comparable with the C-terminal extension of mammalian sHsps in terms of its polar nature and conformational flexibility.
Consistent with folding prediction algorithms, the NMR data indicate that the last 12 C-terminal amino acids of 14-3-3ζ (Gly234–Asp245) are solvent-exposed and exhibit flexibility that is independent of the domain core of the protein, while adopting no preferred secondary structure.
Therefore it is concluded that 14-3-3ζ, and by analogy all other 14-3-3 proteins, have a flexible C-terminal extension.
Protein: DP03654 (UniProt P63104)
Region: residues 234	to 245
Annotation: regulation of protein stability (Biological process)
Evidence: far-UV circular dichroism evidence used in manual assertion
Supporting statements:
The extension stabilizes 14-3-3ζ, but has no direct role in chaperone action.
It is concluded that, like sHsps, 14-3-3ζ has a short C-terminal extension that is flexible, polar and unstructured. Its function is to stabilize and solubilize the protein, and it has no direct role in its chaperone action.
Truncation of 14-3-3ζ resulted in a slight decrease in the mean residue elipticity at 208 and 222 nm relative to the WT protein, implying reduced α-helical content for the truncated mutant relative to the WT protein. As our NMR studies indicate that the C-terminal extension of 14-3-3ζ adopts a disordered solvent-exposed structure in solution with no preferred secondary structure, the decreased CD minima observed for truncated 14-3- 3ζ relative to WT suggest that this extension stabilizes the domain core and α-helical content of the 14-3-3ζ dimer.
The far-UV CD spectra of WT (continuous line) and 15C (broken line) 14-3-3ζ illustrating the decreased α-helical structure of the truncated protein at 37◦C, as denoted by the decreased minima at 208 and 222 nm relative to that of WT 14-3-3ζ.
Thus, on the basis of the yeast two-hybrid studies, SEC, MALLS, CD and DLS analysis, it is concluded that although truncation of 14-3-3ζ does not affect the ability of the protein to form dimers at 25 ◦C, the C-terminal extension is important in maintaining the overall shape, secondary structure and dimeric state of the protein at 37 ◦C.
However, although C-terminal truncation of 14-3-3ζ did not significantly alter the average diameter of the dimer at 25 ◦C, at physiological temperature, the truncated protein aggregated progressively with time. C-terminal truncation also slightly decreased the α-helical content of 14-3-3ζ. Thus the C-terminal extension of 14-3-3ζ is important in maintaining the overall structural integrity of the protein without directly being involved in dimer formation. Consistent with this, C-terminal truncation resulted in a significant decrease in the thermostability of the protein, and enhanced its susceptibility to denaturant.
Protein: DP03654 (UniProt P63104)
Region: residues 234	to 245
Annotation: regulation of protein stability (Biological process)
Evidence: dynamic light scattering assay evidence used in manual assertion
Supporting statements:
The extension stabilizes 14-3-3ζ, but has no direct role in chaperone action.
It is concluded that, like sHsps, 14-3-3ζ has a short C-terminal extension that is flexible, polar and unstructured. Its function is to stabilize and solubilize the protein, and it has no direct role in its chaperone action.
Thus the truncated mutant has a tendency to aggregate at physiological temperature (Figure 3D, right-hand panel).
DLS profiles of WT (left-hand panel) and 15C (right-hand panel) 14-3-3ζ at 25◦C and 37◦C, where the eluted particle size distribution is shown by number and demonstrates the propensity of 15C 14-3-3ζ to aggregate with time at 37◦C.
Thus, on the basis of the yeast two-hybrid studies, SEC, MALLS, CD and DLS analysis, it is concluded that although truncation of 14-3-3ζ does not affect the ability of the protein to form dimers at 25 ◦C, the C-terminal extension is important in maintaining the overall shape, secondary structure and dimeric state of the protein at 37 ◦C.
These data are also consistent with the DLS data in Figure 3(D) which highlight the greater tendency for 15C 14-3-3ζ to aggregate compared with the full-length protein.
However, although C-terminal truncation of 14-3-3ζ did not significantly alter the average diameter of the dimer at 25 ◦C, at physiological temperature, the truncated protein aggregated progressively with time. C-terminal truncation also slightly decreased the α-helical content of 14-3-3ζ. Thus the C-terminal extension of 14-3-3ζ is important in maintaining the overall structural integrity of the protein without directly being involved in dimer formation. Consistent with this, C-terminal truncation resulted in a significant decrease in the thermostability of the protein, and enhanced its susceptibility to denaturant.
Protein: DP03654 (UniProt P63104)
Region: residues 234	to 245
Annotation: regulation of protein stability (Biological process)
Evidence: temperature-induced protein unfolding evidence used in manual assertion
Supporting statements:
The extension stabilizes 14-3-3ζ, but has no direct role in chaperone action.
It is concluded that, like sHsps, 14-3-3ζ has a short C-terminal extension that is flexible, polar and unstructured. Its function is to stabilize and solubilize the protein, and it has no direct role in its chaperone action.
The light-scattering data suggest that C-terminal truncation of 14-3-3ζ decreases its thermostability and hence its C-terminal extension contributes to the stability of the protein. In agreement with this, the far-UV CD-melting profiles also indicated that the truncated protein had decreased thermostability relative to the WT protein, as quantified by a decrease in α-helical content of both proteins at 222 nm with increasing temperature due to unfolding and aggregation (Figure 4B). These data indicated that 15C 14-3-3ζ began to lose α-helical content at 32 ◦C, whereas this did not occur until approximately 37 ◦C for the WT protein.
The melting curve of 15C relative toWT 14-3-3ζ illustrates a decrease from 60◦C to 56◦C at which the mid-point of protein denaturation/unfolding occurs due to C-terminal truncation.
Thus truncation of the C-terminal extension led to decreased stability of 14-3-3ζ to denaturant. It is therefore concluded that the C-terminal extension of 14-3-3ζ has a role in maintaining the structural integrity of the domain core of the protein.
Thus the C-terminal extension of 14-3-3ζ is important in maintaining the overall structural integrity of the protein without directly being involved in dimer formation. Consistent with this, C-terminal truncation resulted in a significant decrease in the thermostability of the protein, and enhanced its susceptibility to denaturant.
Protein: DP03654 (UniProt P63104)
Region: residues 234	to 245
Annotation: regulation of protein stability (Biological process)
Evidence: urea-induced protein unfolding evidence used in manual assertion
Supporting statements:
The extension stabilizes 14-3-3ζ, but has no direct role in chaperone action.
It is concluded that, like sHsps, 14-3-3ζ has a short C-terminal extension that is flexible, polar and unstructured. Its function is to stabilize and solubilize the protein, and it has no direct role in its chaperone action.
C-terminal truncation of 14-3-3ζ reduces the half-point of unfolding by 0.33 M urea relative to the full-length protein.
Thus truncation of the C-terminal extension led to decreased stability of 14-3-3ζ to denaturant. It is
therefore concluded that the C-terminal extension of 14-3-3ζ has a role in maintaining the structural integrity of the domain core of the protein.
Thus the C-terminal extension of 14-3-3ζ is important in maintaining the overall structural integrity of the protein without directly being involved in dimer formation. Consistent with this, C-terminal truncation resulted in a significant decrease in the thermostability of the protein, and enhanced its susceptibility to denaturant.
Protein: DP03655 (UniProt Q9SSK9)
Region: residues 45	to 65
Annotation: disorder (Structural state)
Evidence: nuclear magnetic resonance evidence used in manual assertion
Supporting statements:
The MLP28 structure deviates significantly from the conserved Bet v 1 fold in that the β2 strand and the second short α-helix between strands β1 and β2 of the Bet v 1 fold are replaced by a long, flexible loop comprising residues 45–65.
Cross-references: PDB:2I9Y
Protein: DP03656 (UniProt Q9SN73)
Region: residues 57	to 67
Annotation: disorder (Structural state)
Evidence: x-ray crystallography evidence used in manual assertion
Supporting statements:
The chain termini (residues 56 to 67 and 130
to 136) are disordered.
Disordered boundaries are 57-67 since the first residue of the PDB structure reported by the authors (metionine) does not overlap with the first amino acid of UniProt sequence (lysine).
Cross-references: PDB:6EKB
Protein: DP03657 (UniProt Q9SSA5)
Region: residues 297	to 336
Annotation: disorder (Structural state)
Evidence: x-ray crystallography evidence used in manual assertion
Supporting statements:
The loops in the cyclophilin domain are quite disordered.
Cross-references: PDB:3RFY
Protein: DP03657 (UniProt Q9SSA5)
Region: residues 350	to 377
Annotation: disorder (Structural state)
Evidence: x-ray crystallography evidence used in manual assertion
Supporting statements:
The loops in the cyclophilin domain are quite disordered.
Cross-references: PDB:3RFY
Protein: DP03659 (UniProt Q14318)
Region: residues 1	to 32
Annotation: disorder (Structural state)
Evidence: heteronuclear single quantum coherence spectroscopy evidence used in manual assertion
Supporting statements:
The N-terminal tail (residues 1–32) exhibits negative or near zero {1H}-15N hetNOE values, suggesting the unstructured characteristic of this region.
The N-terminal extension (residues 1–32) is not presented for clarity as it is highly flexible and only a restricted number of NOEs were observed in this region.
Comparable low heteronuclear NOE values are observed for residues 1–32 in the N-terminal extension for both the free and CaM/Ca2+-bound NTD indicating that this region exhibits increased conformational mobility on (sub)-nanosecond time scales.
Protein: DP03659 (UniProt Q14318)
Region: residues 1	to 32
Annotation: calmodulin binding (Molecular function)
Evidence: nuclear magnetic resonance spectroscopy evidence used in manual assertion
Supporting statements:
However, striking differences are observed for the local tumbling correlation times (τc, Fig. 2b) and T2 values (Supplementary Fig. S1) values for residues 11–26 in the N-terminal extension upon binding of the NTD to CaM/Ca2+. This indicates the presence of conformational exchange processes at μs-ms timescales that are linked to the interaction with CaM/Ca2+.
In the reciprocal experiment, addition of unlabeled CaM/Ca2+ to the 15N-labeled NTD generated noticeable changes in the 1H-15N HSQC spectrum, which were mapped primarily to the N-terminal extension of the NTD, mainly for residues Ala16, Arg17 and Phe19 – Glu24 (Fig. 4b,c).
Taken together, these data suggest that the N-terminal extension of FKBP38 is directly involved in a molecular interaction with CaM/Ca2+.
Protein: DP03659 (UniProt Q14318)
Region: residues 1	to 32
Annotation: protein binding (Molecular function)
Evidence: heteronuclear single quantum coherence spectroscopy evidence used in manual assertion
Supporting statements:
A comparison of the 2D 1H- 15N HSQC spectra of the NTD (residues 1–149) and the FKBD38 (residues 33–149) (Fig. 3a) confirmed the structural similarity of the NTD and the FKDB38. However, differences in chemical shifts are observed for residues in the core domain, consistent with autoinhibitory interactions between the N-terminal extension and the core domain. As summarized in Figs. 3b and 3c, most of these perturbed residues were localized in a defined region, including residues Ser58, Lys62, Gly63 and Gln64 in the β1/β2-loop; Val65 in strand β2; Phe88 and Thr89 in β4; and Asp92, Cys93, Asp94, Val95 and Ile96 in the β4/α1-loop and close to the putative isomerase active site.