LiteFold/DisProt huggingface dataset:
Protein: DP02951 (UniProt P01501)
Region: residues 44	to 69
Annotation: protein binding (Molecular function)
Evidence: isothermal titration calorimetry evidence used in manual assertion
Supporting statements:
We characterized the thermodynamic parameters of the binding process between melittin and HAA through isothermal titration calorimetry (ITC), and found the binding tobe endothermic and entropy-driven.
Protein: DP02951 (UniProt P01501)
Region: residues 63	to 68
Annotation: lipid binding (Molecular function)
Evidence: enzymatic activity assay evidence used in manual assertion
Supporting statements:
To assess the functional role of the positive (K21RKR24) sequence in the C-terminus of melittin, we designed a negatively charged melittin peptide (D21EDE24-melittin). These negative residues were predicted to disrupt the binding of melittin with the plasma membrane.
These data demonstrate that residues required for melittin activity include those residing in the C-terminal α-helix, comprising several key positively charged residues necessary for interaction with the plasma membrane.
Protein: DP02951 (UniProt P01501)
Region: residues 63	to 68
Annotation: localization (Biological process)
Evidence: enzymatic activity assay evidence used in manual assertion
Supporting statements:
To assess the functional role of the positive (K21RKR24) sequence in the C-terminus of melittin, we designed a negatively charged melittin peptide (D21EDE24-melittin). These negative residues were predicted to disrupt the binding of melittin with the plasma membrane.
These data demonstrate that residues required for melittin activity include those residing in the C-terminal α-helix, comprising several key positively charged residues necessary for interaction with the plasma membrane.
Protein: DP02951 (UniProt P01501)
Region: residues 44	to 70
Annotation: molecular function inhibitor activity (Molecular function)
Evidence: qualitative western immunoblotting evidence used in manual assertion
Supporting statements:
Honeybee venom and melittin suppress the activation of EGFR and HER2 by interfering with the phosphorylation of these receptors in the plasma membrane of breast carcinoma cells.
Honeybee venom and melittin suppress the phosphorylation of EGFR and HER2.
Here, we show that honeybee venom and melittin suppress the ligand-induced phosphorylation of EGFR and HER2, dynamically modulating downstream signaling pathways in breast cancer cells.
Protein: DP02953 (UniProt P08572)
Region: residues 1629	to 1638
Annotation: disorder (Structural state)
Evidence: X-ray crystallography-based structural model with missing residue coordinates used in manual assertion
Supporting statements:
These hairpins (residues 37–45 in the case of SM1 and
residues 144–154 in the case of SM1') were not visible in the
structure of a2NC1 homo (Fig. 3), as would be expected if they
were disordered in this noncanonical homo-octamer.
Cross-references: PDB:5NB2
Protein: DP02953 (UniProt P08572)
Region: residues 1680	to 1696
Annotation: disorder (Structural state)
Evidence: X-ray crystallography-based structural model with missing residue coordinates used in manual assertion
Supporting statements:
SM3' was disordered and was not visible in either a2NC1 homo
or a4NC1 homo (Fig. 3)
a2NC1 domain is crystallized in 5NB2 while a4NC1 is crystallized in 5NB1 (however such PDB is not associated to this UniprotID)
Cross-references: PDB:5NB2
Protein: DP02953 (UniProt P08572)
Region: residues 1680	to 1696
Annotation: disorder to order (Structural transition)
Evidence: x-ray crystallography evidence used in manual assertion
Supporting statements:
Here, we define three structural motifs in sheet II (Fig. 3), SM1 (hairpin b3–b4), SM2 (hairpin b6–b7) and SM3 (b9 and the preceding loop), and their homologous counterparts in sheet II0, SM1’ (hairpin b3’–b4’), SM2’ (hairpin b6’–b7’) and SM3’ (b9’ and the preceding loop) (Figs. 3a and 3b).
The comparison between the structure of the a2NC1 domain in its noncanonical homohexamer and the same domain in a121NC1 (a2NC1a121) revealed that there are conformational differences that might explain the greater number of subunits (Fig. 2, Supplementary Fig. S6).
Overall, a comparison of noncanonical and canonical oligomers (Figs. 3a and 3b) revealed that the SM1, SM1’ and SM2 flexible regions are key determinants in protomer formation, while the loops connecting these motifs, Lb7b8 (motif ClA), Lb70b80 and SM3’, are needed to establish the protomer–protomer interactions that generate the hexamer.
Indeed, previous work with the natural a121NC1 heterohexamer has reported structural inter-chain variability in the conformations of these loops (Sundaramoorthy et al., 2002; Than et al., 2002).
Proposed model for canonical hexamer assembly. Individual monomers (a) start to nucleate a protomer via

b-sheets I/I0 (b). Next, the SM1/1’ and SM2/SM2’ flexible regions from b-sheets II/II0 are stabilized in the nascent protomer, resulting in favoured additional intersubunit interactions within the protomer (c). Final stabilization is attained with the proper folding of SM3’ and of the ClA and ClB motifs that allow the binding of chloride ions (green spheres) (d). The two protomers in the hexamer are now ready to be joined by sulfilimine bonds (red lines).
Our findings of noncanonical assemblies for a2NC1 and a4NC1 homo-oligomers and the structural changes observed in the chains forming these noncanonical protomers in comparison to a2NC1_121 and to the chains in a1NC1homo, a3NC1homo and a5NC1homo could imply that chain folding is closely related to protomer assembly. It is unlikely that a2NC1homo and a4NC1homo could represent stable physiological assemblies, but the structures of the individual chains in these noncanonical oligomers might provide a frozen glimpse of transient conformational states in the process of NC1 folding and hexamer building.
The disordered loops are present in the noncanonical octamer (5NB2_B), while the same loops are ordered when the a2NC1 chain is assembled into the canonical a2NC1_121 hexamer (5NAX).
Cross-references: PDB:5NB2
PDB:5NAX
Protein: DP02953 (UniProt P08572)
Region: residues 1629	to 1638
Annotation: self-assembly (Disorder function)
Evidence: x-ray crystallography evidence used in manual assertion
Supporting statements:
Overall, a comparison of noncanonical and canonical oligomers (Figs. 3a and 3b) revealed that the SM1, SM1’ and SM2 flexible regions are key determinants in protomer formation, while the loops connecting these motifs, Lb7b8 (motif ClA), Lb70b80 and SM3’, are needed to establish the protomer–protomer interactions that generate the hexamer.
Proposed model for canonical hexamer assembly. Individual monomers (a) start to nucleate a protomer via

b-sheets I/I0 (b). Next, the SM1/1’ and SM2/SM2’ flexible regions from b-sheets II/II0 are stabilized in the nascent protomer, resulting in favoured additional intersubunit interactions within the protomer (c). Final stabilization is attained with the proper folding of SM3’ and of the ClA and ClB motifs that allow the binding of chloride ions (green spheres) (d). The two protomers in the hexamer are now ready to be joined by sulfilimine bonds (red lines).
Our findings of noncanonical assemblies for a2NC1 and a4NC1 homo-oligomers and the structural changes observed in the chains forming these noncanonical protomers in comparison to a2NC1_121 and to the chains in a1NC1homo, a3NC1homo and a5NC1homo could imply that chain folding is closely related to protomer assembly. It is unlikely that a2NC1homo and a4NC1homo could represent stable physiological assemblies, but the structures of the individual chains in these noncanonical oligomers might provide a frozen glimpse of transient conformational states in the process of NC1 folding and hexamer building.
The disordered loops are present in the noncanonical octamer (5NB2_B), while the same loops are ordered when the a2NC1 chain is assembled into the canonical a2NC1_121 hexamer (5NAX).
Cross-references: PDB:5NB2
PDB:5NAX
Protein: DP02953 (UniProt P08572)
Region: residues 1680	to 1696
Annotation: molecular adaptor activity (Molecular function)
Evidence: x-ray crystallography evidence used in manual assertion
Supporting statements:
Overall, a comparison of noncanonical and canonical oligomers (Figs. 3a and 3b) revealed that the SM1, SM1’ and SM2 flexible regions are key determinants in protomer formation, while the loops connecting these motifs, Lb7b8 (motif ClA), Lb70b80 and SM3’, are needed to establish the protomer–protomer interactions that generate the hexamer.
Proposed model for canonical hexamer assembly. Individual monomers (a) start to nucleate a protomer via

b-sheets I/I0 (b). Next, the SM1/1’ and SM2/SM2’ flexible regions from b-sheets II/II0 are stabilized in the nascent protomer, resulting in favoured additional intersubunit interactions within the protomer (c). Final stabilization is attained with the proper folding of SM3’ and of the ClA and ClB motifs that allow the binding of chloride ions (green spheres) (d). The two protomers in the hexamer are now ready to be joined by sulfilimine bonds (red lines).
Our findings of noncanonical assemblies for a2NC1 and a4NC1 homo-oligomers and the structural changes observed in the chains forming these noncanonical protomers in comparison to a2NC1_121 and to the chains in a1NC1homo, a3NC1homo and a5NC1homo could imply that chain folding is closely related to protomer assembly. It is unlikely that a2NC1homo and a4NC1homo could represent stable physiological assemblies, but the structures of the individual chains in these noncanonical oligomers might provide a frozen glimpse of transient conformational states in the process of NC1 folding and hexamer building.
The disordered loops are present in the noncanonical octamer (5NB2_B), while the same loops are ordered when the a2NC1 chain is assembled into the canonical a2NC1_121 hexamer (5NAX).
Cross-references: PDB:5NB2
PDB:5NAX
Protein: DP02954 (UniProt Q12888)
Region: residues 1750	to 1768
Annotation: disorder (Structural state)
Evidence: X-ray crystallography-based structural model with missing residue coordinates used in manual assertion
Supporting statements:
The N-terminal BRCT domain of BP1 contains a unique large insertion of 29 residues (1741-1769) rich in polar and charged residues between b1 and a1 that are not found in BRCA1 or other BRCTs. In our structure, this region is very disordered, probably indicating that it is highly fexible. However, in the first copy of BP1, some broken electron density is interpretable for residues 1741-1750 and there is good indication from model
building that these residues form an a-helical structure (a-I) that extends from the surface of the N-terminal BRCT domain into the solvent (Figure 1).
Cross-references: PDB:1GZH
Protein: DP02954 (UniProt Q12888)
Region: residues 1741	to 1767
Annotation: disorder (Structural state)
Evidence: X-ray crystallography-based structural model with missing residue coordinates used in manual assertion
Supporting statements:
An N-terminal fragment (residues 1702–1713) and the region between β1A and α1A (residues 1741–1769) do not have interpretable electron density, and we presume are disordered. Residues 1741–1769 correspond to a 29 amino acid insertion that is not found in other BRCT repeats and is rich in polar and charged residues.
Cross-references: PDB:1KZY
Protein: DP02954 (UniProt Q12888)
Region: residues 1	to 1483
Annotation: disorder (Structural state)
Evidence: author statement used in manual assertion
Supporting statements:
(B) Diagram of the domain structure of 53BP1. The N-terminal region of 53BP1 is a disordered region containing multiple ATM phosphorylation sites while the C-terminal half contains the following domains: dynein light chain 8 (LC8) binding, oligomerization, glycine–arginine rich (GAR), tandem Tudor (recognizes methylated residues), ubiquitination-dependent recruitment (UDR), nuclear localization signal (NLS), and tandem BRCT.
The unstructured N-terminal half of 53BP1 contains 28 S/TQ sites that are phosphorylated by ATM following DNA damage and are required for its recruitment of NHEJ-promoting factors.
Following the unstructured region the first structured region is the tudor-like domain, which spans the 1484-1603 region according to UniProt.
Protein: DP02954 (UniProt Q12888)
Region: residues 1140	to 1225
Annotation: disorder (Structural state)
Evidence: far-UV circular dichroism evidence used in manual assertion
Supporting statements:
Far-UV circular dichroism shows a spectrum with a strong negative ellipticity at 200 nm, which is consistent with a primarily disordered structure (Fig. 2 A).
Protein: DP02954 (UniProt Q12888)
Region: residues 1140	to 1225
Annotation: disorder (Structural state)
Evidence: nuclear magnetic resonance spectroscopy evidence used in manual assertion
Supporting statements:
The lack of contiguous regions with deviation from Cα-Cβ shifts from expected values indicates that the 53BP1 LBD is dynamic and disordered, consistent with the prediction. 15N relaxation experiments confirm that the 53BP1 LBD is disordered with little evidence of restricted motion across the chain (Fig. 2 C).
Protein: DP02954 (UniProt Q12888)
Region: residues 1150	to 1157
Annotation: protein binding (Molecular function)
Evidence: nuclear magnetic resonance spectroscopy evidence used in manual assertion
Supporting statements:
The presence of three LC8 binding sites in 53BP1 is supported by the loss of resonances for residues between 1144 and 1211.
Protein: DP02954 (UniProt Q12888)
Region: residues 1167	to 1174
Annotation: protein binding (Molecular function)
Evidence: nuclear magnetic resonance spectroscopy evidence used in manual assertion
Supporting statements:
The presence of three LC8 binding sites in 53BP1 is supported by the loss of resonances for residues between 1144 and 1211.
Protein: DP02954 (UniProt Q12888)
Region: residues 1192	to 1199
Annotation: protein binding (Molecular function)
Evidence: nuclear magnetic resonance spectroscopy evidence used in manual assertion
Supporting statements:
The presence of three LC8 binding sites in 53BP1 is supported by the loss of resonances for residues between 1144 and 1211.
Protein: DP02956 (UniProt O70200)
Region: residues 1	to 16
Annotation: disorder (Structural state)
Evidence: X-ray crystallography-based structural model with missing residue coordinates used in manual assertion
Supporting statements:
The residues invisible in electron density are indicated by gray shading
The residues Met1 to Leu16 and Tyr124 to Pro147 in HIba1, and Met1 to Leu16 and Asn128 to Pro147 inMIba1 were invisible in the final electron density map, as indicated by gray in Figure1
The mass spectrum of purified samples showed that there are truncated proteins with molecular masses of 13,234 Da for H-Iba1 (VM=1.82 Å3/Da) and 14,486 Da for M-Iba1 (VM=1.92 Å3/Da), respectively, suggesting that from eight to 13 amino acid residues are possibly disorderd in crystals 
Both of the highly mobile N-terminal and C-terminal regions protrude from the upper surface, as labeled in Figure 6 (middle)
Cross-references: PDB:1WY9
Protein: DP02956 (UniProt O70200)
Region: residues 124	to 147
Annotation: disorder (Structural state)
Evidence: X-ray crystallography-based structural model with missing residue coordinates used in manual assertion
Supporting statements:
The residues invisible in electron density are indicated by gray shading
The residues Met1 to Leu16 and Tyr124 to Pro147 in HIba1, and Met1 to Leu16 and Asn128 to Pro147 inMIba1 were invisible in the final electron density map, as indicated by gray in Figure1
The mass spectrum of purified samples showed that there are truncated proteins with molecular masses of 13,234 Da for H-Iba1 (VM=1.82 Å3/Da) and 14,486 Da for M-Iba1 (VM=1.92 Å3/Da), respectively, suggesting that from eight to 13 amino acid residues are possibly disorderd in crystals
Both of the highly mobile N-terminal and C-terminal regions protrude from the upper surface, as labeled in Figure 6 (middle)
Cross-references: PDB:1WY9
Protein: DP02957 (UniProt P47992)
Region: residues 90	to 114
Annotation: disorder (Structural state)
Evidence: nuclear magnetic resonance spectroscopy evidence used in manual assertion
Supporting statements:
Two regions are dynamically disordered as evidenced by 1H and 13C chemical shifts and {15N}-1H NOEs: residues 1–9 of the amino terminus and residues 69-93 of the C-terminal extension.
A steady decline is seen in the heteronuclear NOE values for the unstructured residues approaching the ends of the N- and C-termini with negative NOE values observed for residues near each terminus; these values are consistent with large-amplitude motions on the picosecond to nanosecond time scale and a complete lack of stable secondary or tertiary structure.
No long-range NOEs were observed for the 9 N-terminal and 26 C-terminal residues.
Residues 1–8 and 69–93 are highly disordered.
Residues comprising the unique C-terminal sequence of hLtn are entirely disordered in solution (Figures 4 and 5), but residues 9–68 adopt the conserved fold observed for all other chemokines (Figure 6).
The IDR characterized in the publication and spanning residues 69-93 corresponds to region 90-114 of the amino acid sequence, since the natural precursor form of the protein contains a signal peptide (1-21) that is cleaved in the mature secreted protein.
Cross-references: PDB:1J8I
PDB:1J9O
Protein: DP02957 (UniProt P47992)
Region: residues 90	to 114
Annotation: disorder (Structural state)
Evidence: nuclear magnetic resonance spectroscopy evidence used in manual assertion
Supporting statements:
The IDR characterized in the publication and spanning residues 69-93 corresponds to region 90-114 of the amino acid sequence, since the natural precursor form of the protein contains a signal peptide (1-21) that is cleaved in the mature secreted protein.
The C-terminal α-helix observed at 10 °C and 200 mM NaCl, which is conserved in other chemokines, is absent at 45 °C and no salt, and the last 38 residues of the protein are completely disordered, as indicated by heteronuclear 15N-1H NOEs. 
Under these conditions, hLtn adopted the conserved chemokine fold consisting of three antiparallel β-strands and a C-terminal α-helix with unstructured N- (1–9) and C-terminal (69–93) residues.
Cross-references: BMRB:5251
Protein: DP02957 (UniProt P47992)
Region: residues 97	to 114
Annotation: disorder (Structural state)
Evidence: nuclear magnetic resonance spectroscopy evidence used in manual assertion
Supporting statements:
The IDR characterized in the publication and spanning residues 76-93 corresponds to region 97-114  of the amino acid sequence, since the the Ltn expression construct described in the paper lacks the N-terminal Val-1 residue and the resulting protein therefore corresponds to Ltn (2–93). In addition the natural precursor form of the protein contains a signal peptide (1-21) that is cleaved in the mature secreted protein.
Completely disordered residues 76–93 were not included in water refinement calculations, thus the ensemble of CC3 NMR structures deposited in the PDB contains only residues 1–75.
Backbone r.m.s.d. (Figure 3B) and 15N-1H heteronuclear NOE (Figure 3C) values confirm that residues 1–10 and 69–93 are dynamically disordered in solution, as observed with the Ltn10 structure (4). 
Cross-references: PDB:2HDM
Protein: DP02957 (UniProt P47992)
Region: residues 82	to 114
Annotation: disorder (Structural state)
Evidence: nuclear magnetic resonance spectroscopy evidence used in manual assertion
Supporting statements:
The IDR characterized in the publication and spanning residues 61-93 corresponds to region 82-114 of the amino acid sequence, since the natural precursor form of the protein contains a signal peptide (1-21) that is cleaved in the mature secreted protein.
Disordered N- and C-terminal residues (residues 1–7 and 53–93) are not shown.
Completely disordered residues 61–93 were not included in water refinement calculations, thus the ensemble of Ltn40 NMR structures deposited in the Protein Data Bank contains only residues 1–60. NMR structure refinement statistics are provided in Table S1.
Cross-references: PDB:2JP1
Protein: DP02958 (UniProt Q55DL0)
Region: residues 491	to 503
Annotation: disorder (Structural state)
Evidence: X-ray crystallography-based structural model with missing residue coordinates used in manual assertion
Supporting statements:
Only residues 7–490 could be traced; 5 amino acids at the N terminus, the 13C-terminal residues, and the polyhistidine tag are not visible in the electron density map because of structural flexibility.
Cross-references: PDB:2FTW
Protein: DP02959 (UniProt P42527)
Region: residues 810	to 841
Annotation: disorder (Structural state)
Evidence: X-ray crystallography-based structural model with missing residue coordinates used in manual assertion
Supporting statements:
An intramolecular ligand for the Pi-pocket can be generated by the auto-phosphorylation of a conserved threonine residue (Thr825 in MHCK-A; Thr348 in eEF2K) in the unstructured linker C-terminal to the α -kinase domain.
Region 810-841 is a flexible linker connecting the α-kinase domain and the WD repeat domain.
Cross-references: PDB:5E4H
Protein: DP02959 (UniProt P42527)
Region: residues 810	to 841
Annotation: flexible linker (Disorder function)
Evidence: x-ray crystallography evidence used in manual assertion
Supporting statements:
An intramolecular ligand for the Pi-pocket can be generated by the auto-phosphorylation of a conserved threonine residue (Thr825 in MHCK-A; Thr348 in eEF2K) in the unstructured linker C-terminal to the α -kinase domain.
Region 810-841 is a flexible linker connecting the α-kinase domain and the WD repeat domain.
Protein: DP02959 (UniProt P42527)
Region: residues 806	to 841
Annotation: phosphorylation display site (Disorder function)
Evidence: x-ray crystallography evidence used in manual assertion
Supporting statements:
The key residue in the C-tail was identified as Thr825, which was found to be constitutively autophosphorylated.
The residue in the C-tail which regulates autophosphorylation is found within the disorder region
Protein: DP02959 (UniProt P42527)
Region: residues 822	to 830
Annotation: molecular function regulator (Molecular function)
Evidence: enzymatic activity assay evidence used in manual assertion
Supporting statements:
Similar to results reported previously, the QQG(p)TMVMPD peptide restored ~60% of kinase activity with a Kd of 38 ± 12 μM29. The QQG(p)TMSMPD peptide was less effective, yielding a Kd of 98 ± 20 μM and a maximal kinase activity of ~50%. The results are consistent with the conclusion that a hydrophobic residue at the +2 position following the phosphothreonine enhances binding to the Pi-pocket.
Protein: DP02959 (UniProt P42527)
Region: residues 823	to 827
Annotation: phosphorylation display site (Disorder function)
Evidence: enzymatic activity assay evidence used in manual assertion
Supporting statements:
Incubation of A-CAT-5xA with [γ-32P]ATP resulted in the incorporation of less than 0.1 mol of phosphate/mol (Fig. 3A). The amount of phosphate incorporated into A-CAT-5xA increased to 0.2 mol/mol after a 1-h treatment with calf intestinal alkaline phosphatase and to 0.33 mol/mol after a 5-h treatment with SAP (Fig. 3A). We interpret these results to indicate that Thr825 is nearly fully phosphorylated in bacterially expressed A-CAT-5xA and that it is only partially dephosphorylated even after extensive phosphatase treatment.
Protein: DP02959 (UniProt P42527)
Region: residues 823	to 831
Annotation: self-activation (Disorder function)
Evidence: enzymatic activity assay evidence used in manual assertion
Supporting statements:
In contrast, mutation of Thr825 to alanine decreased kinase and ATPase activities by 95% (Fig. 2B). This result suggests that autophosphorylation of Thr825 is critical for the activity of A-CAT.