LiteFold/DisProt huggingface dataset:
Protein: DP03072 (UniProt P53420)
Region: residues 1656	to 1671
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.
Cross-references: PDB:5NB1
Protein: DP03073 (UniProt P26285)
Region: residues 1	to 27
Annotation: disorder (Structural state)
Evidence: X-ray crystallography-based structural model with missing residue coordinates used in manual assertion
Supporting statements:
The missing residues are all from both the N- and C-terminal regulatory domains and are considered disordered, based on the results from mass spectroscopy of melt crystals (data not shown).
Cross-references: PDB:5HR5
Protein: DP03073 (UniProt P26285)
Region: residues 452	to 531
Annotation: disorder (Structural state)
Evidence: X-ray crystallography-based structural model with missing residue coordinates used in manual assertion
Supporting statements:
The missing residues are all from both the N- and C-terminal regulatory domains and are considered disordered, based on the results from mass spectroscopy of melt crystals (data not shown).
Cross-references: PDB:5HR5
Protein: DP03074 (UniProt O60825)
Region: residues 1	to 30
Annotation: disorder (Structural state)
Evidence: X-ray crystallography-based structural model with missing residue coordinates used in manual assertion
Supporting statements:
The final models revealed the residues 31–450 out of 505 of hPFKFB2 and those of 28–450 of bPFKFB2. The missing residues are all from both the N- and C-terminal regulatory domains and are considered disordered, based on the results from mass spectroscopy of melt crystals (data not shown).
Cross-references: PDB:5HTK
Protein: DP03074 (UniProt O60825)
Region: residues 451	to 505
Annotation: disorder (Structural state)
Evidence: X-ray crystallography-based structural model with missing residue coordinates used in manual assertion
Supporting statements:
The final models revealed the residues 31–450 out of 505 of hPFKFB2 and those of 28–450 of bPFKFB2. The missing residues are all from both the N- and C-terminal regulatory domains and are considered disordered, based on the results from mass spectroscopy of melt crystals (data not shown).
Cross-references: PDB:5HTK
Protein: DP03075 (UniProt Q9H3M7)
Region: residues 300	to 317
Annotation: disorder (Structural state)
Evidence: X-ray crystallography-based structural model with missing residue coordinates used in manual assertion
Supporting statements:
The electron density map of T–TXNIP presented here was not visible beyond residue 299, suggesting the presence of a flexible region.
Cross-references: PDB:4LL1
PDB:4LL4
Protein: DP03076 (UniProt P0A910)
Region: residues 39	to 51
Annotation: disorder (Structural state)
Evidence: X-ray crystallography-based structural model with missing residue coordinates used in manual assertion
Supporting statements:
The rms deviation between the common Ca atoms of both models (1-17, 31-63, 71-145 and 160-171) is 0.42 AÊ, and thus only slightly higher than expected from the coordinate errors. The largest deviations occur in the loop regions and smaller ones in turns T1 through to T3, and they correlate with the chain mobilities (Figure 2).
Loops L1, L2 and L4 have no density, indicating that they are extremely mobile.
Please, notice that residue numbering in the author statements refer to a construct lacking the N-terminal signal peptide. This entry refers to extracellular loop L1. Extracellular loop L2 is not listed due to its short length (<10 AAs).
The membrane domain of OmpA consists of an eight-stranded all-next-neighbor antiparallel beta-barrel with short turns at the periplasmic barrel end and long flexible loops at the external end. The structure analysis has been extended from medium resolution to 1.65 A (1 A=0.1 nm), and the molecular model has been refined anisotropically to show oriented mobilities of the structural elements.
The analysis indicates that the beta-barrel constitutes a solid scaffold such that the long external loops need not contribute to stability. These loops are highly mobile and thus cause a major problem during the crystallization process.
Cross-references: PDB:1QJP
Protein: DP03076 (UniProt P0A910)
Region: residues 167	to 180
Annotation: disorder (Structural state)
Evidence: X-ray crystallography-based structural model with missing residue coordinates used in manual assertion
Supporting statements:
The rms deviation between the common Ca atoms of both models (1-17, 31-63, 71-145 and 160-171) is 0.42 AÊ, and thus only slightly higher than expected from the coordinate errors. The largest deviations occur in the loop regions and smaller ones in turns T1 through to T3, and they correlate with the chain mobilities (Figure 2).
Loops L1, L2 and L4 have no density, indicating that they are extremely mobile.
Please, notice that residue numbering in the author statements refer to a construct lacking the N-terminal signal peptide. This entry refers to extracellular loop L3. Extracellular loop L2 is not listed due to its short length (<10 AAs).
he membrane domain of OmpA consists of an eight-stranded all-next-neighbor antiparallel beta-barrel with short turns at the periplasmic barrel end and long flexible loops at the external end. The structure analysis has been extended from medium resolution to 1.65 A (1 A=0.1 nm), and the molecular model has been refined anisotropically to show oriented mobilities of the structural elements.
The analysis indicates that the beta-barrel constitutes a solid scaffold such that the long external loops need not contribute to stability. These loops are highly mobile and thus cause a major problem during the crystallization process.
Cross-references: PDB:1QJP
Protein: DP03078 (UniProt P76045)
Region: residues 241	to 252
Annotation: disorder (Structural state)
Evidence: X-ray crystallography-based structural model with missing residue coordinates used in manual assertion
Supporting statements:
The final OmpG model includes ∼90% of the residues of the mature protein; the residues 20–27 in loop L1, 59-60 in L2, 220–231 in L6 and 261–266 in L7 are not visible in the electron density maps, presumably because they are disordered.
Please, notice that residue numbering in the author statements refer to the mature protein form lacking the N-terminal signal peptide. This entry refers to part of the extracellular loop L6. Other regions not visible in the electron density maps are not reported here due to their short length (<10 AAs)."
Cross-references: PDB:2F1C
Protein: DP03080 (UniProt Q9Z214)
Region: residues 144	to 163
Annotation: disorder (Structural state)
Evidence: X-ray crystallography-based structural model with missing residue coordinates used in manual assertion
Supporting statements:
Only residues 1 – 143 were clearly modelled into the experimental map (Figure 3) with a final R-factor of 19.5% and good stereochemistry (Table 1), while we could find a suitable space for about 20 residues from 144–163 in the electron density map. We concluded, therefore, that removal of the 12  residues from the original was essential for crystallization and that the 20 remaining C-terminal residues of the fragment in the crystal are disordered.
Cross-references: PDB:1I2H
Protein: DP03081 (UniProt P0DJI8)
Region: residues 74	to 85
Annotation: disorder (Structural state)
Evidence: cryogenic electron microscopy-based structural model with missing residue coordinates used in manual assertion
Supporting statements:
The IDR characterized in the publication and spanning residues 56-67 in the experimental construct corresponds to region 74-85 of the amino acid sequence.
Adjacent to the C-terminal ends of their ordered parts, both fibril reconstructions show diffuse density (Supplementary Figure 5), indicating that C-terminal tails of the fibril proteins, corresponding to residues 70–83 in the murine and 56–67 in the human fibril proteins, are structurally disordered.
Cross-references: PDB:6MST
Protein: DP03082 (UniProt P05367)
Region: residues 89	to 102
Annotation: disorder (Structural state)
Evidence: cryogenic electron microscopy-based structural model with missing residue coordinates used in manual assertion
Supporting statements:
The IDR characterized in the publication and spanning residues 70–83 in the experimental construct corresponds to region 89-102 of the amino acid sequence.
Adjacent to the C-terminal ends of their ordered parts, both fibril reconstructions show diffuse density (Supplementary Figure 5), indicating that C-terminal tails of the fibril proteins, corresponding to residues 70–83 in the murine and 56–67 in the human fibril proteins, are structurally disordered.
Cross-references: PDB:6DSO
Protein: DP03083 (UniProt Q9VNE4)
Region: residues 21	to 60
Annotation: disorder (Structural state)
Evidence: far-UV circular dichroism evidence used in manual assertion
Supporting statements:
Far-UV circular dichroism (CD) spectra of recombinant acidic regions: CeSPD-2 (aa 11-44), DmAsl (aa 21-60), MmAsl (aa 1-47), and MmSPD-2 (aa 168-256). All acidic regions demonstrated a classical random coil structure with maximum below 0 and minimum at ~200 nm.
Protein: DP03085 (UniProt Q0PF16)
Region: residues 40	to 54
Annotation: disorder (Structural state)
Evidence: X-ray crystallography-based structural model with missing residue coordinates used in manual assertion
Supporting statements:
A segment of the RING domain (amino acids 40–54) that includes most of the central helix is disordered in the crystal and is shown in the figure as a grey backbone trace modeled using the NMR structure of the human TRIM5α RING.
Cross-references: PDB:4TKP
Protein: DP03088 (UniProt Q9BV68)
Region: residues 41	to 66
Annotation: disorder (Structural state)
Evidence: nuclear magnetic resonance spectroscopy evidence used in manual assertion
Supporting statements:
Backbone assignment of residues 1–66 shows that residues 1–40 constitute the structured region while the remainder presents the chemical shift dispersion typical of disordered proteins.
Cross-references: PDB:2N9O
Protein: DP03090 (UniProt Q20363)
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:
Interestingly, the flexible N- and C-terminal regions of Sip1 are resolved to a large extent in the equatorial monomers with only 7 C- and 17 N-terminal residues missing, respectively (Figures 4C and 4D). 
Cross-references: PDB:4YDZ
Protein: DP03091 (UniProt P0AG86)
Region: residues 143	to 155
Annotation: disorder (Structural state)
Evidence: proton-based nuclear magnetic resonance evidence used in manual assertion
Supporting statements:
In this study, the C-terminal thirteen amino acid residues of SecB were shown to be highly mobile.
The 1H NMR resonances of these thirteen C-terminal amino acid residues (Q143QAGEGTEEHQDA155) had narrow linewidths, and appeared at positions corresponding to random chemical shift values (Wuthrich, 1986). Therefore, these amino acid residues represent a mobile C-terminal tail of SecB.
In this study, it was demonstrated that SecB contains a highly mobile C-terminal region and that deletion of the C-terminal tail produced a stable truncated protein that was defective in its function under certain conditions. The 1H NMR spectrum of wild type SecB contained narrow resonances most of which could be assigned to the C-terminal thirteen amino acid residues of SecB.
In this study, we demonstrate that the C-terminal 13 residues of SecB were highly mobile using 1H NMR spectroscopy.
Protein: DP03091 (UniProt P0AG86)
Region: residues 143	to 155
Annotation: localization (Biological process)
Evidence: fluorescence evidence used in manual assertion
Supporting statements:
A protein lacking the C-terminal 13 amino acids of wild-type SecB was found to retain the ability to bind unfolded maltose-binding protein (MBP) in vitro but to interfere with the normal kinetics of pre-MBP export when overexpressed in vivo.
Deletion of the C-terminal mobile region of SecB was found to alter the function of SecB when the mutant protein was overproduced and overproduction of SecA reversed this defect.
When SecB142 lacking the C-terminal mobile region was expressed at high levels, a kinetic defect in the export of pre-MBP was observed, demonstrating that removal of the mobile region altered the function of SecB. Despite the truncation, SecB142 was capable of binding pre-MBP as demonstrated by its ability to block the refolding of unfolded MBP.
In vitro experiments (intrinsic tryptophan fluorescence), monitoring MBP(Y283D) refolding in the presence of SecB (wt or SecB142). Results displayed in Figure 2.
Protein: DP03091 (UniProt P0AG86)
Region: residues 143	to 155
Annotation: localization (Biological process)
Evidence: sodium dodecyl sulfate polyacrylamide gel electrophoresis evidence used in manual assertion
Supporting statements:
Deletion of the C-terminal mobile region of SecB was found to alter the function of SecB when the mutant protein was overproduced and overproduction of SecA reversed this defect.
As shown in Fig. 3A, pre-MBP export was severely defective in secB- strains containing vector only. In contrast, export was rapid in the same strain transformed with wild type secB on the overproducing plasmid. When the strain was transformed with the plasmid containing the secB142op mutation, a moderate export defect was observed. Pre-MBP export in the psecB142op containing strain exhibited the kinetics typically seen for other secB missense mutations (36, 37).
In Fig. 3B, the same set of plasmids were transformed into a strain containing a chromosomal secB+ allele. As expected, export was rapid in the strains containing wild type secB and a mild defect was evident in the strain containing secB+ on the overproducing plasmid. When the plasmid containing the secB142op mutation was transformed into the secB+ strain, a dominant negative export defect was observed. 
As seen in Fig. 3C, when SecA was overexpressed in a secB1- strain both the mild export defect due to wild type SecB overproduction, and the moderate defect of the secB142op mutation were suppressed. This result suggests that SecA levels were limiting in the presence of excess SecB and that this effect was more pronounced with the secB142op mutation.
In vivo experiments to determine whether SecB142 was functional: "pre- maltose binding protein (pre-MBP) export was analyzed by pulse-chase labeling of cells with Tran[35S]- label (ICN), extraction and immunoprecipitation with anti-MBP anti-serum. MBP species were analyzed by SDS polyacrylamide gel electrophoresis and fluorography."
Protein: DP03091 (UniProt P0AG86)
Region: residues 143	to 153
Annotation: disorder (Structural state)
Evidence: X-ray crystallography-based structural model with missing residue coordinates used in manual assertion
Supporting statements:
The model is not complete, as 8N-terminal residues and 11 C-terminal residues are not visible in the electron density maps. 
Cross-references: PDB:1QYN
Protein: DP03092 (UniProt O00308)
Region: residues 662	to 702
Annotation: disorder (Structural state)
Evidence: X-ray crystallography-based structural model with missing residue coordinates used in manual assertion
Supporting statements:
Notably, residues 661–702 of WWP2 were not built in the model owing to a lack of electron density, which might be the result of intrinsic flexibility
Cross-references: PDB:4Y07
Protein: DP03093 (UniProt Q9SSN3)
Region: residues 45	to 58
Annotation: disorder (Structural state)
Evidence: X-ray crystallography-based structural model with missing residue coordinates used in manual assertion
Supporting statements:
The electron density for the region between residues 45 and 58 was not observed and therefore not modeled.
Electron density between residues 45 and 58, comprising the BB‐loop and αB‐helix, was not observed and therefore not modeled. 
 Incidentally, the electron density corresponding to the BB‐loop residues of AtTIR was not visible, probably because of the intrinsic flexibility of this particular sequence.
Cross-references: PDB:3JRN
Protein: DP03094 (UniProt Q9SEL7)
Region: residues 111	to 127
Annotation: disorder (Structural state)
Evidence: X-ray crystallography-based structural model with missing residue coordinates used in manual assertion
Supporting statements:
In Deg5 (S266A), residues 111–125 from loop LA, 155–159 from loop LB and 287–295 from loop L2 cannot be traced in the electron-density map. These loops, together with loop L3 (241–251), which has significantly high B-factor values, are flexible in the crystal.
A few additional residues are invisible in the electron density map
Cross-references: PDB:4IC5
Protein: DP03094 (UniProt Q9SEL7)
Region: residues 286	to 295
Annotation: disorder (Structural state)
Evidence: X-ray crystallography-based structural model with missing residue coordinates used in manual assertion
Supporting statements:
In Deg5 (S266A), residues 111–125 from loop LA, 155–159 from loop LB and 287–295 from loop L2 cannot be traced in the electron-density map. These loops, together with loop L3 (241–251), which has significantly high B-factor values, are flexible in the crystal.
Cross-references: PDB:4IC5
Protein: DP03096 (UniProt O04147)
Region: residues 103	to 113
Annotation: disorder (Structural state)
Evidence: X-ray crystallography-based structural model with missing residue coordinates used in manual assertion
Supporting statements:
It is noteworthy that an exposed surface loop connecting α3 and β5 (residues 101–115) is positioned in the immediate vicinity of the active site. The loop is poorly defined in the present structure, most likely due to the inherent flexibility of this region. It is highly disordered and could not be traced at all in molecules 2 and 3. 
The averaged density allowed building of all three molecules in the asymmetric unit, with the exception of a surface loop constituted by residues 100–115.
A solvent-exposed surface loop (residues 100–115) is very likely to play a flap-like role, opening and closing the active site.
Cross-references: PDB:1FSI
Protein: DP03098 (UniProt P02774)
Region: residues 107	to 125
Annotation: disorder (Structural state)
Evidence: X-ray crystallography-based structural model with missing residue coordinates used in manual assertion
Supporting statements:
The IDR characterized in the PDB and spanning residues 91-109 corresponds to region 107-125 of the amino acid sequence, since the natural precursor form of the protein contains a signal peptide (1-16) that is missing in the mature protein.
Not included in the final model are a few flexible regions that are poorly defined in the electron density maps, which include actin residues Asp-1–Asp-3, His-40–Asp-51, and Ala-365–Ala-375, DBP residues Gly-107–Ala-125, and the C-terminal Leu-474.
Limited Structural Changes After Formation of the Actin–DBP Complex. 
The structure of DBP shows only minor changes after formation of the actin–DBP complex.
Formation of the strong actin–DBP complex proceeds with limited conformational changes to both proteins, demonstrating how DBP has evolved to become an effective actin-scavenger protein.
Cross-references: PDB:1KW2
PDB:1KXP
Protein: DP03098 (UniProt P02774)
Region: residues 107	to 127
Annotation: disorder (Structural state)
Evidence: X-ray crystallography-based structural model with missing residue coordinates used in manual assertion
Supporting statements:
The IDR characterized in the publication and spanning residues 91-111 corresponds to region 107-127 of the amino acid sequence, since the natural precursor form of the protein contains a signal peptide (1-16) that is missing in the mature protein.
DBP residues 91-111 and actin residues 1, 2, 40-50, 374, and 375 appear to be disordered in this structure and are absent from the model.
Cross-references: PDB:1LOT
Protein: DP03099 (UniProt P68135)
Region: residues 41	to 53
Annotation: disorder (Structural state)
Evidence: X-ray crystallography-based structural model with missing residue coordinates used in manual assertion
Supporting statements:
The IDR characterized in the publication and spanning residues 40–51 corresponds to region 41-53 of the amino acid sequence, as it includes a few more residues invisible in the electron density map.
Not included in the final model are a few flexible regions that are poorly defined in the electron density maps, which include actin residues Asp-1–Asp-3, His-40–Asp-51, and Ala-365–Ala-375, DBP residues Gly-107–Ala-125, and the C-terminal Leu-474.
Cross-references: PDB:1KXP
Protein: DP03099 (UniProt P68135)
Region: residues 367	to 377
Annotation: disorder (Structural state)
Evidence: X-ray crystallography-based structural model with missing residue coordinates used in manual assertion
Supporting statements:
The IDR characterized in the publication and spanning residues 365-375 corresponds to region 367-377 of the amino acid sequence, as it includes a few more residues invisible in the electron density map.
Not included in the final model are a few flexible regions that are poorly defined in the electron density maps, which include actin residues Asp-1–Asp-3, His-40–Asp-51, and Ala-365–Ala-375, DBP residues Gly-107–Ala-125, and the C-terminal Leu-474.
Cross-references: PDB:1KXP
Protein: DP03099 (UniProt P68135)
Region: residues 42	to 52
Annotation: disorder (Structural state)
Evidence: X-ray crystallography-based structural model with missing residue coordinates used in manual assertion
Supporting statements:
The IDR characterized in the publication and spanning residues 40-50 corresponds to region 42-52 of the amino acid sequence, as it includes a few more residues invisible in the electron density map.
DBP residues 91-111 and actin residues 1, 2, 40-50, 374, and 375 appear to be disordered in this structure and are absent from the model.
Cross-references: PDB:1LOT
Protein: DP03100 (UniProt Q14258)
Region: residues 361	to 433
Annotation: disorder (Structural state)
Evidence: X-ray crystallography-based structural model with missing residue coordinates used in manual assertion
Supporting statements:
The 73-residue long linker (residues 361–433) connecting the CC and PRYSPRY domain is not visible in the electron density so the exact connectivity is uncertain
Cross-references: PDB:6FLN
Protein: DP03100 (UniProt Q14258)
Region: residues 361	to 433
Annotation: flexible linker (Disorder function)
Evidence: x-ray crystallography evidence used in manual assertion
Supporting statements:
The 73-residue long linker (residues 361–433) connecting the CC and PRYSPRY domain is not visible in the electron density so the exact connectivity is uncertain
Cross-references: PDB:6FLN