LiteFold/DisProt huggingface dataset:
Protein: DP02004 (UniProt Q92793)
Region: residues 674	to 1080
Annotation: protein binding (Molecular function)
Evidence: qualitative western immunoblotting evidence used in manual assertion
Supporting statements:
We observed on SDS-PAGE the formation of high-Mw complexes in which the presence (and thus interaction) of both protein partners was proven by two consecutive Western blots (with a membrane stripping step in between) with anti-His and anti-GST antibody to visualize high-Mw overlapping bands (box).
Protein: DP02004 (UniProt Q92793)
Region: residues 1852	to 2057
Annotation: flexible linker (Disorder function)
Evidence: nuclear magnetic resonance spectroscopy evidence used in manual assertion
Supporting statements:
The 1H-15N correlation spectrum exhibits all of the peculiar NMR features of an IDP, namely, a reduced chemical-shift dispersion that is particularly pronounced in the 1H dimension, and a high degree of signal crowding.
Protein: DP02005 (UniProt P47710)
Region: residues 1	to 185
Annotation: disorder (Structural state)
Evidence: cleavage assay evidence used in manual assertion
Supporting statements:
Lipid raft LUVs did not prevent the degradation of α-casein, a protein with an open conformation that is susceptible to proteolysisat all temperatures.
Protein: DP02006 (UniProt P04183)
Region: residues 64	to 73
Annotation: disorder (Structural state)
Evidence: X-ray crystallography-based structural model with missing residue coordinates used in manual assertion
Supporting statements:
Owing to flexible parts, none of the subunits display electron density before amino acid 18 and after amino acid 192. Density is also absent for the loop between amino acids 64 and 73.
Cross-references: PDB:2WVJ
Protein: DP02006 (UniProt P04183)
Region: residues 1	to 17
Annotation: disorder (Structural state)
Evidence: X-ray crystallography-based structural model with missing residue coordinates used in manual assertion
Supporting statements:
Owing to flexible parts, none of the subunits display electron density before amino acid 18 and after amino acid 192. Density is also absent for the loop between amino acids 64 and 73.
Cross-references: PDB:2WVJ
Protein: DP02006 (UniProt P04183)
Region: residues 193	to 234
Annotation: disorder (Structural state)
Evidence: X-ray crystallography-based structural model with missing residue coordinates used in manual assertion
Supporting statements:
Owing to flexible parts, none of the subunits display electron density before amino acid 18 and after amino acid 192. Density is also absent for the loop between amino acids 64 and 73.
Cross-references: PDB:2WVJ
Protein: DP02007 (UniProt Q9H2Y7)
Region: residues 1265	to 1521
Annotation: disorder (Structural state)
Evidence: far-UV circular dichroism evidence used in manual assertion
Supporting statements:
In silico analysis and circular dichroism experiments (Fig. 5) showed that ZFP106-f is also largely disordered, which suggests a rather transient binding between the two IDRs that can occur either via a mutual (synergistic) folding39 or a “fuzzy” interaction31, in which both IDRs remain largely disordered.
Protein: DP02007 (UniProt Q9H2Y7)
Region: residues 1265	to 1521
Annotation: protein binding (Molecular function)
Evidence: qualitative western immunoblotting evidence used in manual assertion
Supporting statements:
We observed on SDS-PAGE the formation of high-Mw complexes in which the presence (and thus interaction) of both protein partners was proven by two consecutive Western blots (with a membrane stripping step in between) with anti-His and anti-GST antibody to visualize high-Mw overlapping bands (box).
Protein: DP02007 (UniProt Q9H2Y7)
Region: residues 1256	to 1521
Annotation: protein binding (Molecular function)
Evidence: competitive binding evidence used in manual assertion
Supporting statements:
The free ID3 was found to compete with the ID3 of full-length CBP for binding the substrate, ZFP106-f, causing a significant concentration-dependent decrease in the acetylation of ZFP106-f (Fig. 4a).
Overall, these results show that ID3 specifically binds to ZFP106-f via defined sequence features.
Protein: DP02007 (UniProt Q9H2Y7)
Region: residues 1300	to 1400
Annotation: protein binding (Molecular function)
Evidence: site-directed spin-labelling electron paramagnetic resonance evidence used in manual assertion
Supporting statements:
Moreover, the interacting region(s) of ZFP106-f can be delineated from the different effects the presence of the three ZFP106-f constructs has on ID3 signal intensities in the 2D 1H-15N NMR spectra (Fig. 6b). A strong signal decrease was observed with the ZFP106-f-M2, and much weaker effect with ZFP106-f-M1. The paramagnetic tag sites M1 and M2 are in relative close proximity to each other (Fig. 6a). In contrast, ZFP106-f-M3 caused no change in signal intensity in the CTR of ID3, suggesting an interaction site between residues 1300–1400 of ZFP106 (Fig. 6).
Protein: DP02008 (UniProt Q9M4V2)
Region: residues 1	to 80
Annotation: disorder (Structural state)
Evidence: far-UV circular dichroism evidence used in manual assertion
Supporting statements:
Figure 4. CD spectra of BnaDGAT11-80 and BnaDGAT181-113. Residues 1 to 80 are highly disordered
Protein: DP02008 (UniProt Q9M4V2)
Region: residues 1	to 80
Annotation: protein binding (Molecular function)
Evidence: far-UV circular dichroism evidence used in manual assertion
Supporting statements:
The highly disordered region of BnaDGAT1, residues 1 to 80, was found to facilitate dimerization, as evident from cross-linking studies (Fig. 7).
Protein: DP02008 (UniProt Q9M4V2)
Region: residues 1	to 80
Annotation: disorder (Structural state)
Evidence: sodium dodecyl sulfate polyacrylamide gel electrophoresis evidence used in manual assertion
Supporting statements:
The mobility of these recombinant proteins on SDS-PAGE was atypical as they migrated slower than expected, based on their expected molecular masses (16 kDa and 9 kDa, respectively) (Fig. 2 inset). This lower mobility, specifically observed with the recombinant N-terminal domains of BnaDGAT11-80, is often observed in IDPs (eg. Juxtanodin) and attributed to the lack of hydrophobic amino acid residues and anomalous interaction with SDS.
Disorder is also claimed for the longer segment 1-113, but in the previous paper they have shown that the segment 81-113 is folded.
Protein: DP02008 (UniProt Q9M4V2)
Region: residues 1	to 80
Annotation: disorder (Structural state)
Evidence: cleavage assay evidence used in manual assertion
Supporting statements:
Additionally, these purified constructs were susceptible to proteolysis despite the addition of protease inhibitors.
Disorder is also claimed for the longer segment 1-113, but in the previous paper they have shown that the segment 81-113 is folded.
Protein: DP02008 (UniProt Q9M4V2)
Region: residues 1	to 80
Annotation: disorder (Structural state)
Evidence: chromatography evidence used in manual assertion
Supporting statements:
These studies confirmed the molecular masses 13.9 kDa (BnaDGAT11-113) and 8.6 kDa (BnaDGAT11-80). The apparent molecular mass calculated from SEC-MALLS were lower than that calculated using SEC standards demonstrating the nonglobular and monomeric nature of the purified constructs.
Disorder is also claimed for the longer segment 1-113, but in the previous paper they have shown that the segment 81-113 is folded.
Protein: DP02008 (UniProt Q9M4V2)
Region: residues 1	to 80
Annotation: disorder (Structural state)
Evidence: far-UV circular dichroism evidence used in manual assertion
Supporting statements:
In the absence of ligand, both proteins exhibited a negative minimum close to 200 nm, a typical observation for disordered proteins37 (Fig. 4A,B).
Disorder is also claimed for the longer segment 1-113, but in the previous paper they have shown that the segment 81-113 is folded.
Protein: DP02008 (UniProt Q9M4V2)
Region: residues 1	to 113
Annotation: disorder (Structural state)
Evidence: small-angle X-ray scattering evidence used in manual assertion
Supporting statements:
The scattering profiles, for the various forms of BnaDGAT11-113, exhibited a typical profile of IDRs (Fig. 5A).
Here, with the low-resolution techniques disorder is claimed for the longer segment 1-113, but in the previous paper they have shown that the segment 81-113 is folded.
The Kratky plots do not have maxima, but instead have a short plateau followed by a monotonic increase at higher value of [q]. This indicates the presence of a highly extended particle for BnaDGAT11-113, thus confirming the intrinsically disordered nature of the N-terminal region of BnaDGAT11-113 (Fig. 5B).
Protein: DP02008 (UniProt Q9M4V2)
Region: residues 1	to 80
Annotation: small molecule binding (Molecular function)
Evidence: isothermal titration calorimetry evidence used in manual assertion
Supporting statements:
ITC was performed to investigate the interaction thermodynamics of BnaDGAT1 N-terminal domain with acyl-CoA and CoA. Four independent systems were analyzed: BnaDGAT11-113 or BnaDGAT11-80 in combination with oleoyl-CoA or CoA.
Interestingly, BnaDGAT11-80 also interacted with both ligands but with lower affinity (Kd of 117 μM for oleoyl-CoA and Kd of 178 μM for CoA) (Fig. 3C, D).
Protein: DP02008 (UniProt Q9M4V2)
Region: residues 1	to 80
Annotation: small molecule binding (Molecular function)
Evidence: far-UV circular dichroism evidence used in manual assertion
Supporting statements:
Contrary to the above, BnaDGAT11-80 showed a decreased helicity upon ligand binding, along with a decrease in random coil nature as demonstrated by the decrease in negative ellipticity at ~200 nm (Fig. 4B). Overall, these observations suggest that there is some gain in helical structure for the entire segment (1-113) and reduction in the random coil nature of the shorter segment upon ligand binding.
Protein: DP02009 (UniProt O75683)
Region: residues 1	to 182
Annotation: disorder (Structural state)
Evidence: nuclear magnetic resonance spectroscopy evidence used in manual assertion
Supporting statements:
Here, we compared spectral resolution and sensitivity for 2D 1H-15N and 13C-15N correlation spectra recorded through direct detection of each of the two correlated nuclei for two protein regions that are entirely disordered (Hdm2-ABD and Surf6-N) and 2D 1H-15N correlation spectra for a ~73 kDa folded, pentameric protein with two short IDRs (N130).
Protein: DP02009 (UniProt O75683)
Region: residues 1	to 195
Annotation: disorder (Structural state)
Evidence: cryogenic electron microscopy-based structural model with missing residue coordinates used in manual assertion
Supporting statements:
The Cryo-EM structures of human pre-60S particles as they matured in the nucleolus and nucleus show this region of the Surfeit locus protein 6 lacks electron density, indicating it is disordered. 
Cross-references: PDB:8FKQ
PDB:8FKP
PDB:8FKR
PDB:8FKS
EMDB:29252
EMDB:29253
EMDB:29254
EMDB:29255
Protein: DP02009 (UniProt O75683)
Region: residues 1	to 182
Annotation: molecular condensate scaffold activity (Molecular function)
Evidence: fluorescence microscopy evidence used in manual assertion
Supporting statements:
To these pre-equilibrated homotypic NPM1 droplets, which incorporated client S6N, we added an extra 3.5 mole equivalents of S6N and monitored their composition using time-lapse imaging. Upon addition of this extra amount, S6N was slowly incorporated within the scaffold, as demonstrated by an increase in the S6N-A647:NPM1-A488 fluorescence intensity ratio over time (Fig. 5c, d). Furthermore, S6N competed for pre-existing NPM1-NPM1 interactions, resulting in a decrease in NPM1-Alexa Fluor 488 intensity within droplets (Fig. 5d). This S6N-dependent, partial expulsion of NPM1 from the NPM1-S6N droplets concomitantly triggered formation of de novo, heterotypic droplets with S6N molecules in the light phase (Supplementary Fig. 12).
Together, the results of these scaffold rearrangement experiments suggest that the homotypic (NPM1-NPM1) and heterotypic (NPM1-S6N) scaffolds form miscible, co-existing liquid phases that dynamically interconvert in response to changes in the protein composition of the surrounding milieu.
Protein: DP02010 (UniProt Q9NRJ3)
Region: residues 1	to 10
Annotation: disorder (Structural state)
Evidence: nuclear magnetic resonance spectroscopy evidence used in manual assertion
Supporting statements:
The tertiary fold of chemokines is largely stabilized by two characteristic disulfide bonds which link the flexible N-terminus to the chemokine core.
Protein: DP02010 (UniProt Q9NRJ3)
Region: residues 1	to 108
Annotation: disorder (Structural state)
Evidence: nuclear magnetic resonance spectroscopy evidence used in manual assertion
Supporting statements:
We propose that the pH-dependent structural lability of CCL28 is important for its role as both a chemoattractant and antimicrobial agent
Protein: DP02010 (UniProt Q9NRJ3)
Region: residues 99	to 127
Annotation: disorder (Structural state)
Evidence: nuclear magnetic resonance spectroscopy evidence used in manual assertion
Supporting statements:
In addition to having a third, non-canonical disulfide bond, CCL28 has an extended C-terminal domain of 28 residues which follows the most C-terminal cysteine residue (cysteine 80). Our structural and functional analyses revealed that the extended C-terminal domain of CCL28 is unstructured and dynamic
The last cysteine in the sequence is Cys99, referred to as "cysteine 80" in the paper since the authors cloned the human CCL28 gene lacking its signal peptide (19 amino acids)"
Cross-references: PDB:6CWS
Protein: DP02011 (UniProt P32684)
Region: residues 253	to 290
Annotation: disorder (Structural state)
Evidence: X-ray crystallography-based structural model with missing residue coordinates used in manual assertion
Supporting statements:
Only residues corresponding to the N-terminal and central domains are visible in our RluF–RNA electron density maps. The C-terminal domain, shown by limited proteolysis to comprise residues Thr253–Arg290, is disordered.
Cross-references: PDB:3DH3
Protein: DP02012 (UniProt Q9Z8L4)
Region: residues 1	to 95
Annotation: disorder (Structural state)
Evidence: X-ray crystallography-based structural model with missing residue coordinates used in manual assertion
Supporting statements:
The N-terminal region, corresponding to the first ∼95 residues in FL_pCopN, and the last ∼15 C-terminal residues were disordered both in FL_pCopN and in D29.
Cross-references: PDB:4P40
Protein: DP02012 (UniProt Q9Z8L4)
Region: residues 384	to 399
Annotation: disorder (Structural state)
Evidence: X-ray crystallography-based structural model with missing residue coordinates used in manual assertion
Supporting statements:
The N-terminal region, corresponding to the first ∼95 residues in FL_pCopN, and the last ∼15 C-terminal residues were disordered both in FL_pCopN and in D29.
Cross-references: PDB:4P40
Protein: DP02013 (UniProt P0DP23)
Region: residues 76	to 85
Annotation: disorder (Structural state)
Evidence: nuclear magnetic resonance spectroscopy evidence used in manual assertion
Supporting statements:
Upon interaction with the RalA-HVR, the central helix of CaM undergoes extensive unfolding between residues Lys75 and Glu84. Melting of this helix to this extent, although uncommon in CaM structures, is consistent with previous observations that helical content decreases upon complex formation with the RalA HVR (23). This unfolded linker, coupled with the partial disorder of the HVR, results in the lack of fixed orientation of the N-lobe with respect to the C-lobe (Fig. 3A). There is a notable absence of interlobe NOEs, and residues of the central linker show only short-range, mostly intraresidue NOEs, which are not indicative of secondary structure.
Cross-references: BMRB:34608
PDB:7NQC
Protein: DP02013 (UniProt P0DP23)
Region: residues 76	to 85
Annotation: order to disorder (Structural transition)
Evidence: nuclear magnetic resonance spectroscopy evidence used in manual assertion
Supporting statements:
Upon interaction with the RalA-HVR, the central helix of CaM undergoes extensive unfolding between residues Lys75 and Glu84. Melting of this helix to this extent, although uncommon in CaM structures, is consistent with previous observations that helical content decreases upon complex formation with the RalA HVR (23). This unfolded linker, coupled with the partial disorder of the HVR, results in the lack of fixed orientation of the N-lobe with respect to the C-lobe (Fig. 3A). There is a notable absence of interlobe NOEs, and residues of the central linker show only short-range, mostly intraresidue NOEs, which are not indicative of secondary structure.
Cross-references: BMRB:34608
PDB:7NQC
Protein: DP02013 (UniProt P0DP23)
Region: residues 76	to 85
Annotation: flexible linker (Disorder function)
Evidence: nuclear magnetic resonance spectroscopy evidence used in manual assertion
Supporting statements:
Upon interaction with the RalA-HVR, the central helix of CaM undergoes extensive unfolding between residues Lys75 and Glu84. Melting of this helix to this extent, although uncommon in CaM structures, is consistent with previous observations that helical content decreases upon complex formation with the RalA HVR (23). This unfolded linker, coupled with the partial disorder of the HVR, results in the lack of fixed orientation of the N-lobe with respect to the C-lobe (Fig. 3A). There is a notable absence of interlobe NOEs, and residues of the central linker show only short-range, mostly intraresidue NOEs, which are not indicative of secondary structure.
Cross-references: BMRB:34608
PDB:7NQC
Protein: DP02015 (UniProt P52272)
Region: residues 41	to 70
Annotation: protein binding (Molecular function)
Evidence: X-ray crystallography-based structural model with missing residue coordinates used in manual assertion
Supporting statements:
both bPY-NLSs and hPY-NLSs bind Kapβ2 in an extended conformation, with structural conservation at the arginine and proline-tyrosine residues of their C-terminal R/K/Hx2–5PY motifs and at their N-terminal basic or hydrophobic motifs.
Cross-references: PDB:2OT8
Protein: DP02017 (UniProt A0A0H3LBR3)
Region: residues 90	to 99
Annotation: disorder (Structural state)
Evidence: X-ray crystallography-based structural model with missing residue coordinates used in manual assertion
Supporting statements:
This region lacks electron density, indicating it is disordered.
Cross-references: PDB:4W4K
Protein: DP02025 (UniProt P30429-1)
Region: residues 1	to 108
Annotation: disorder (Structural state)
Evidence: X-ray crystallography-based structural model with missing residue coordinates used in manual assertion
Supporting statements:
CED-4b exhibits a similar structure, except that its CARD domain is flexible and disordered in the crystals.
Cross-references: PDB:2A5Y
Protein: DP02027 (UniProt P17405)
Region: residues 49	to 85
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 structure are grey
Cross-references: PDB:5I81
Protein: DP02027 (UniProt P17405)
Region: residues 614	to 631
Annotation: disorder (Structural state)
Evidence: X-ray crystallography-based structural model with missing residue coordinates used in manual assertion
Supporting statements:
The same residue range is visible in the olipudase alfa structure, suggesting ASM N and C termini are inherently disordered and flexible. The structure includes an N-terminal saposin domain (residues 84–167), a proline-rich linker (168–195), a catalytic metallophosphatase domain (196–538), and a helical C-terminal domain (539–611) (Fig. 1).
Cross-references: PDB:5I81
Protein: DP02030 (UniProt P09546)
Region: residues 611	to 669
Annotation: disorder (Structural state)
Evidence: X-ray crystallography-based structural model with missing residue coordinates used in manual assertion
Supporting statements:
Although residues 611–669 were not observed in any of the structures, the protein had not been degraded by proteolysis. Mass spectroscopy of a PutA86-669 crystal returned an unambiguous result of 66.8 kDa. Thus, residues 611–669 appear to be disordered in the PutA86-669 structures.
Cross-references: PDB:1TIW
PDB:1TJ2
PDB:1TJ0
PDB:1TJ1
Protein: DP02030 (UniProt P09546)
Region: residues 185	to 243
Annotation: disorder (Structural state)
Evidence: X-ray crystallography-based structural model with missing residue coordinates used in manual assertion
Supporting statements:
The electron density was quite strong and unambiguous for residues 88–144, 162–184, and 244–610 in all four of the PutA86-669 structures.
 In full-length PutA, residues 188–241 are probably stabilized by interactions with a domain not present in the PutA86-669 construct, and, in the absence of these contacts, residues 188–241 are not properly folded.
Cross-references: PDB:1TJ0
PDB:1TJ2
PDB:1TIW
PDB:1TJ1
Protein: DP02033 (UniProt P32504)
Region: residues 1	to 43
Annotation: disorder (Structural state)
Evidence: X-ray crystallography-based structural model with missing residue coordinates used in manual assertion
Supporting statements:
No clear electron density was seen for residues 1–43 or 538–551, and loops between residues 65–72, 97–108, 168–182, 257–264, and 414–423 were also disordered and not included in the final model.
Cross-references: PDB:4ACO
Protein: DP02033 (UniProt P32504)
Region: residues 97	to 108
Annotation: disorder (Structural state)
Evidence: X-ray crystallography-based structural model with missing residue coordinates used in manual assertion
Supporting statements:
No clear electron density was seen for residues 1–43 or 538–551, and loops between residues 65–72, 97–108, 168–182, 257–264, and 414–423 were also disordered and not included in the final model.
Cross-references: PDB:4ACO
Protein: DP02033 (UniProt P32504)
Region: residues 168	to 182
Annotation: disorder (Structural state)
Evidence: X-ray crystallography-based structural model with missing residue coordinates used in manual assertion
Supporting statements:
No clear electron density was seen for residues 1–43 or 538–551, and loops between residues 65–72, 97–108, 168–182, 257–264, and 414–423 were also disordered and not included in the final model.
Cross-references: PDB:4ACO
Protein: DP02033 (UniProt P32504)
Region: residues 414	to 423
Annotation: disorder (Structural state)
Evidence: X-ray crystallography-based structural model with missing residue coordinates used in manual assertion
Supporting statements:
No clear electron density was seen for residues 1–43 or 538–551, and loops between residues 65–72, 97–108, 168–182, 257–264, and 414–423 were also disordered and not included in the final model.
Cross-references: PDB:4ACO
Protein: DP02033 (UniProt P32504)
Region: residues 538	to 551
Annotation: disorder (Structural state)
Evidence: X-ray crystallography-based structural model with missing residue coordinates used in manual assertion
Supporting statements:
No clear electron density was seen for residues 1–43 or 538–551, and loops between residues 65–72, 97–108, 168–182, 257–264, and 414–423 were also disordered and not included in the final model.
Cross-references: PDB:4ACO
Protein: DP02033 (UniProt P32504)
Region: residues 538	to 956
Annotation: disorder (Structural state)
Evidence: X-ray crystallography-based structural model with missing residue coordinates used in manual assertion
Supporting statements:
Residues 538-956 are unobserved in the crystal structure of yeast Ndc10.
Cross-references: PDB:4ACO
Protein: DP02033 (UniProt P32504)
Region: residues 552	to 956
Annotation: disorder (Structural state)
Evidence: cleavage assay evidence used in manual assertion
Supporting statements:
During purifications of the full-length protein, we identified a 64.6-kDa proteolytically derived fragment of Ndc10, which was determined to contain residues 1–551 of the N-terminal.
Residues 538-956 are unobserved in the crystal structure of yeast Ndc10.
Cross-references: PDB:4ACO