LiteFold/DisProt huggingface dataset:
Protein: DP03924 (UniProt P78352)
Region: residues 1	to 71
Annotation: disorder (Structural state)
Evidence: nuclear magnetic resonance spectroscopy evidence used in manual assertion
Supporting statements:
The amide proton chemical shifts exhibited very narrow chemical shift dispersion (within 8.0–8.7 ppm), suggesting a solvent exposed random coil conformation for the entire 71-residue peptide chain, which is consistent with a lack of any ring-current shifted amide or methyl resonances.
The secondary structure of PSD95-NT in the absence of calmodulin (calculated by chemical shift index (Wishart et al. 1992)) indicates a random coil conformation for the entire 71-residue peptide (Fig. 2) that we suggest may increase the exposure and availability of Cys3 and Cys5 for palmitoylation by palmitoyl transferase enzymes.
Cross-references: BMRB:50752
Protein: DP03925 (UniProt Q4Q5U3)
Region: residues 602	to 617
Annotation: disorder (Structural state)
Evidence: nuclear magnetic resonance spectroscopy evidence used in manual assertion
Supporting statements:
However, of the 87 non proline residues expressed, only 66 amide peaks were visible in the HSQC spectrum, (Fig. 2), suggesting that the first 16 residues are not structured. Consequently, the backbone amides for the first 16 residues, 3 prolines (namely Pro 22, Pro 24, and Pro 55) could not be observed in the 15N HSQC.
Interestingly, the first 16 residues predicted to form a helix in LmMCCC BCCP were not visible in the 1H15N HSQC spectrum, at pH 8.0, which led us to speculate that the region is probably not folded.
Moreover, the amino acid sequence of LmMCCC BCCP domain (2LTDGFGDASMAGGTSA16) also suggests that the region should be unstructured, as there are numerous glycines present, that are established helix breakers.
The authors used a construct where the residues 602-687 of the protein are preceded by a single Met residue. Their numbering is valid for their construct, so it has to be shifted by 600 to get the corresponding UniProt positions.
Cross-references: BMRB:50309
Protein: DP03926 (UniProt P81274)
Region: residues 355	to 421
Annotation: disorder (Structural state)
Evidence: X-ray crystallography-based structural model with missing residue coordinates used in manual assertion
Supporting statements:
Apart from the capping helix next to TPR8, which is visible in the LGN–mInsc complex (Yuzawa et al., 2011 ) but not in the LGN–Frmpd4 complex (Fig. 5 a), they share a similar TPR structure, with r.m.s.d.s of 0.87 Å for TPR2–6 (204 Cα atoms) and 2.38 Å for TPR1–8 (320 Cα atoms).
Cross-references: PDB:4WNG
PDB:4WNE
PDB:4WND
Protein: DP03926 (UniProt P81274)
Region: residues 275	to 421
Annotation: disorder (Structural state)
Evidence: X-ray crystallography-based structural model with missing residue coordinates used in manual assertion
Supporting statements:
The PDB shows the protein lacks electron density in this region, indicating it is disordered. Furthermore, it should be noted the crystal structure describes the protein in oxidized form. 
Cross-references: PDB:4WNF
Protein: DP03927 (UniProt W1J0W9)
Region: residues 982	to 1027
Annotation: disorder (Structural state)
Evidence: nuclear magnetic resonance spectroscopy evidence used in manual assertion
Supporting statements:
No backbone amide signals were detectable for residues H982 and S1027 most likely due to fast exchange of the respective amide protons with the solvent or due to conformational exchange.
The backbone resonances of PaxA T1-CDD bound to the PaxB NDD could be assigned with the same degree of completeness as for the free protein. All expected backbone amide signals except those for H982 and S1027 (99/101, 98.0%; Fig. ​Fig.2a,2a, top) and all Cα (104/104), 99% of all Cβ (99/100), 95% of all CO (99/104), all Hα (104/104) and 99% of all Hβ (99/100) chemical shifts were assigned.
Cross-references: BMRB:50594
BMRB:34575
Protein: DP03927 (UniProt W1J0W9)
Region: residues 1070	to 1084
Annotation: disorder (Structural state)
Evidence: nuclear magnetic resonance spectroscopy evidence used in manual assertion
Supporting statements:
According to TALOS-N the C-terminus including the predicted CDD of the PaxA T1-CDD construct is unstructured.
The authors do not write down exact boundaries for the disordered C-terminus, but from figure 1a it can be clearly seen that helical propensity drops down at residue 1070 and there are no stable secondary structure elements following it.
Cross-references: BMRB:50594
Protein: DP03927 (UniProt W1J0W9)
Region: residues 1073	to 1082
Annotation: disorder to order (Structural transition)
Evidence: nuclear magnetic resonance spectroscopy evidence used in manual assertion
Supporting statements:
According to TALOS-N the C-terminus including the predicted CDD of the PaxA T1-CDD construct is unstructured.
The authors do not write down exact boundaries for the disordered C-terminus, but from figure 1a it can be clearly seen that helical propensity drops down at residue 1070 and there are no stable secondary structure elements following it.
The analysis of the backbone chemical shifts of the PaxA T1-CDD with TALOS-N in its bound state suggests that its secondary structure is very similar to that in its free state but that there is now an additional α-helix present at the very C-terminus suggesting that the predicted docking domain becomes structured upon binding (Fig. ​(Fig.2a,2a, bottom).
In figure 2a that depics the structural properties of the protein in the complex, a new helix is formed between residues 1073-1082 that was not present in the unbound form (Figure 1a).
Cross-references: BMRB:50594
BMRB:34575
Protein: DP03927 (UniProt W1J0W9)
Region: residues 1073	to 1082
Annotation: protein binding (Molecular function)
Evidence: nuclear magnetic resonance spectroscopy evidence used in manual assertion
Supporting statements:
PaxA T1-CDD and PaxB NDD form a stable 1:1 complex according to analytical gel filtration and NMR titration experiments which is in slow exchange on the NMR time scale. 
The analysis of the backbone chemical shifts of the PaxA T1-CDD with TALOS-N in its bound state suggests that its secondary structure is very similar to that in its free state but that there is now an additional α-helix present at the very C-terminus suggesting that the predicted docking domain becomes structured upon binding (Fig. ​(Fig.2a,2a, bottom).
In figure 2a that depics the structural properties of the protein in the complex, a new helix is formed between residues 1073-1082 that was not present in the unbound form (Figure 1a).
Cross-references: BMRB:34575
Protein: DP03928 (UniProt Q7RTN6)
Region: residues 292	to 347
Annotation: disorder (Structural state)
Evidence: X-ray crystallography-based structural model with missing residue coordinates used in manual assertion
Supporting statements:
STRADα residues 292–347, 383–385, and 402–424, and MO25α residues 337–341 were not associated with clear electron density and were not included in the model.
Cross-references: PDB:3GNI
Protein: DP03928 (UniProt Q7RTN6)
Region: residues 300	to 347
Annotation: disorder (Structural state)
Evidence: X-ray crystallography-based structural model with missing residue coordinates used in manual assertion
Supporting statements:
The PDB shows the protein lacks electron density in this region, indicating it is disordered.
Cross-references: PDB:2WTK
Protein: DP03928 (UniProt Q7RTN6)
Region: residues 402	to 424
Annotation: disorder (Structural state)
Evidence: X-ray crystallography-based structural model with missing residue coordinates used in manual assertion
Supporting statements:
STRADα residues 292–347, 383–385, and 402–424, and MO25α residues 337–341 were not associated with clear electron density and were not included in the model.
Whereas clear electron density is present for the last six amino acids of STRADα (residues 426–431, including the WEF motif that interacts with MO25α, Figure S3A), residues 402–425 of STRADα were not visible in the electron density maps, and it was thus not possible to directly identify the appropriate symmetry mates of STRADα and MO25α that make up the biologically relevant binary complex.
Cross-references: PDB:3GNI
Protein: DP03929 (UniProt Q9U1W1)
Region: residues 195	to 486
Annotation: disorder (Structural state)
Evidence: far-UV circular dichroism evidence used in manual assertion
Supporting statements:
Circular dichroism spectroscopy was used to characterize the carboxyl-terminus of C. elegans TFG (amino acids 195-486). Samples were analyzed at different concentrations, and the data were normalized relative to one another. CD spectra were collected at 25°C in 25 mM sodium phosphate (pH 7.2) using a 1 mm path length quartz cell. The spectra are characteristic of an intrinsically disordered protein.
Protein: DP03930 (UniProt Q811T9)
Region: residues 728	to 852
Annotation: disorder (Structural state)
Evidence: nuclear magnetic resonance spectroscopy evidence used in manual assertion
Supporting statements:
The nuclear magnetic resonance (NMR) spectra of 15N-labeled DISC1 728–852 also revealed that this fragment is largely unstructured in solution (Figure S3G).
Protein: DP03930 (UniProt Q811T9)
Region: residues 774	to 829
Annotation: protein binding (Molecular function)
Evidence: nuclear magnetic resonance spectroscopy evidence used in manual assertion
Supporting statements:
We next determined the high-resolution complex structure of DISC1 765–852/Ndel1 CT-CC by NMR spectroscopy (Figures S2C and S2E; Table S1).
Cross-references: PDB:5YI4
Protein: DP03930 (UniProt Q811T9)
Region: residues 765	to 835
Annotation: disorder to order (Structural transition)
Evidence: nuclear magnetic resonance spectroscopy evidence used in manual assertion
Supporting statements:
In the complex, DISC1 765–835 contained two helices that formed an antiparallel hairpin, and Ndel1 CT-CC adopted a single α helix that packed with the DISC1 helix hairpin to form a three-helix bundle through canonical coiled-coil interactions (Figures 2A and 2B). The extension sequence (DISC1 835–852) used to link Ndel1 CT-CC adopted a random coil structure, showing that the covalent linking does not alter the structure of the complex.
Cross-references: PDB:5YI4
Protein: DP03931 (UniProt Q9NRI5)
Region: residues 718	to 771
Annotation: disorder (Structural state)
Evidence: far-UV circular dichroism evidence used in manual assertion
Supporting statements:
An additional construct lies within the N-terminal half of the C region, representing AA 718–771 of DISC1. This fragment is also predicted as monomeric by SEC (Fig. 3G), whereas CD revealed a lack of regular secondary structure (Fig. 3H).
Protein: DP03933 (UniProt Q9TU17)
Region: residues 98	to 141
Annotation: disorder (Structural state)
Evidence: cryogenic electron microscopy-based structural model with missing residue coordinates used in manual assertion
Supporting statements:
Density for Met1 is not observed in the cryo-EM maps and was shown, by tandem mass spectrometry (MS/MS), to be removed in both Cx46 and Cx50. The resulting N-terminal glycine (G2) is partially acetylated (Extended Data Fig. 1), as shown for the bovine isoforms15,16. The intracellular loop (ICL) connecting TM2–TM3 and the cytoplasmic C-terminal domain (CTD) containing the native cleavage sites of Cx46 and Cx50 are also not resolved16. 
Cross-references: PDB:6MHQ
EMDB:9116
Protein: DP03933 (UniProt Q9TU17)
Region: residues 223	to 348
Annotation: disorder (Structural state)
Evidence: cryogenic electron microscopy-based structural model with missing residue coordinates used in manual assertion
Supporting statements:
Density for Met1 is not observed in the cryo-EM maps and was shown, by tandem mass spectrometry (MS/MS), to be removed in both Cx46 and Cx50. The resulting N-terminal glycine (G2) is partially acetylated (Extended Data Fig. 1), as shown for the bovine isoforms15,16. The intracellular loop (ICL) connecting TM2–TM3 and the cytoplasmic C-terminal domain (CTD) containing the native cleavage sites of Cx46 and Cx50 are also not resolved16. 
Cross-references: PDB:6MHQ
EMDB:9116
Protein: DP03933 (UniProt Q9TU17)
Region: residues 110	to 136
Annotation: disorder (Structural state)
Evidence: cryogenic electron microscopy-based structural model with missing residue coordinates used in manual assertion
Supporting statements:
The intracellular loop (ICL) and C-terminal domain (CTD) remain unresolved, presumably due to intrinsic disorder of these regulatory domains16,18,19.
Cross-references: PDB:7JN0
PDB:7JKC
PDB:7JMD
PDB:7JN1
Protein: DP03933 (UniProt Q9TU17)
Region: residues 225	to 413
Annotation: disorder (Structural state)
Evidence: cryogenic electron microscopy-based structural model with missing residue coordinates used in manual assertion
Supporting statements:
The intracellular loop (ICL) and C-terminal domain (CTD) remain unresolved, presumably due to intrinsic disorder of these regulatory domains16,18,19.
Cross-references: PDB:7JN0
PDB:7JKC
PDB:7JMD
PDB:7JN1
Protein: DP03934 (UniProt P55917)
Region: residues 98	to 153
Annotation: disorder (Structural state)
Evidence: cryogenic electron microscopy-based structural model with missing residue coordinates used in manual assertion
Supporting statements:
Density for Met1 is not observed in the cryo-EM maps and was shown, by tandem mass spectrometry (MS/MS), to be removed in both Cx46 and Cx50. The resulting N-terminal glycine (G2) is partially acetylated (Extended Data Fig. 1), as shown for the bovine isoforms15,16. The intracellular loop (ICL) connecting TM2–TM3 and the cytoplasmic C-terminal domain (CTD) containing the native cleavage sites of Cx46 and Cx50 are also not resolved16. 
Cross-references: PDB:6MHY
EMDB:9116
Protein: DP03934 (UniProt P55917)
Region: residues 235	to 440
Annotation: disorder (Structural state)
Evidence: cryogenic electron microscopy-based structural model with missing residue coordinates used in manual assertion
Supporting statements:
Density for Met1 is not observed in the cryo-EM maps and was shown, by tandem mass spectrometry (MS/MS), to be removed in both Cx46 and Cx50. The resulting N-terminal glycine (G2) is partially acetylated (Extended Data Fig. 1), as shown for the bovine isoforms15,16. The intracellular loop (ICL) connecting TM2–TM3 and the cytoplasmic C-terminal domain (CTD) containing the native cleavage sites of Cx46 and Cx50 are also not resolved16. 
Cross-references: PDB:6MHY
EMDB:9116
Protein: DP03934 (UniProt P55917)
Region: residues 110	to 148
Annotation: disorder (Structural state)
Evidence: cryogenic electron microscopy-based structural model with missing residue coordinates used in manual assertion
Supporting statements:
The intracellular loop (ICL) and C-terminal domain (CTD) remain unresolved, presumably due to intrinsic disorder of these regulatory domains16,18,19.
Cross-references: PDB:7JMC
PDB:7JM9
PDB:7JJP
PDB:7JLW
Protein: DP03934 (UniProt P55917)
Region: residues 237	to 440
Annotation: disorder (Structural state)
Evidence: cryogenic electron microscopy-based structural model with missing residue coordinates used in manual assertion
Supporting statements:
The intracellular loop (ICL) and C-terminal domain (CTD) remain unresolved, presumably due to intrinsic disorder of these regulatory domains16,18,19.
Cross-references: PDB:7JMC
PDB:7JM9
PDB:7JJP
PDB:7JLW
Protein: DP03935 (UniProt P28234)
Region: residues 252	to 356
Annotation: disorder (Structural state)
Evidence: nuclear magnetic resonance spectroscopy evidence used in manual assertion
Supporting statements:
The overall structure of the Cx40CT (Ser-251–Val-355), as calculated from using 1123 NOE restraints, is intrinsically disordered or random-coiled.
Cross-references: PDB:2K7M
Protein: DP03935 (UniProt P28234)
Region: residues 252	to 356
Annotation: disorder (Structural state)
Evidence: Fourier-transform infrared spectroscopy evidence used in manual assertion
Supporting statements:
A major band appears at 1643 cm−1, which is consistent with random coil structure. A weaker absorption at 1659 cm−1 may correspond to a very dynamic α-helix accessible to the solvent. Also, a very broad band at 1670 cm−1 corresponds to turns typically present in dynamic and unfolded proteins.
Protein: DP03935 (UniProt P28234)
Region: residues 252	to 356
Annotation: disorder (Structural state)
Evidence: far-UV circular dichroism evidence used in manual assertion
Supporting statements:
As expected from the NMR data, Cx40CT and Cx43CT at pH 6.0 present a high proportion of random-coiled structure (major absorption at 200 nm for Cx40CT and 201 nm for Cx43CT) (Fig. 3A).
Protein: DP03937 (UniProt Q03190)
Region: residues 270	to 333
Annotation: disorder (Structural state)
Evidence: far-UV circular dichroism evidence used in manual assertion
Supporting statements:
B: circular dichroism shows Cx37-CT is disordered at both pH 7.4 and 5.8.
Protein: DP03938 (UniProt P29353-2)
Region: residues 1	to 41
Annotation: disorder (Structural state)
Evidence: nuclear magnetic resonance spectroscopy evidence used in manual assertion
Supporting statements:
As expected, the residues 1–41 were structurally disordered and did not appear to have any effect on the structured core region of the domain.
No NOEs were observed between the N- and C-terminal residues 17–41 and 192–207, and the core region of the domain in the free form of the Shc PTB domain.
The structure of PTB domain from the construct 1–207 was virtually superimposable with that obtained from the construct 17–207 in the free form.
Cross-references: PDB:1N3H
PDB:1OY2
Protein: DP03938 (UniProt P29353-2)
Region: residues 192	to 207
Annotation: disorder (Structural state)
Evidence: nuclear magnetic resonance spectroscopy evidence used in manual assertion
Supporting statements:
No NOEs were observed between the N- and C-terminal residues 17–41 and 192–207, and the core region of the domain in the free form of the Shc PTB domain.
The structure of PTB domain from the construct 1–207 was virtually superimposable with that obtained from the construct 17–207 in the free form.
Cross-references: PDB:1N3H
PDB:1OY2
Protein: DP03938 (UniProt P29353-2)
Region: residues 17	to 34
Annotation: disorder (Structural state)
Evidence: nuclear magnetic resonance spectroscopy evidence used in manual assertion
Supporting statements:
For clarity, the Nterminal residues of the PTB domain (17-34) that were illdefined by the NMR data are not shown. These residues do not exhibit any long-range NOEs to the rest of the protein and are probably not part of the PTB domain. 
Cross-references: PDB:1SHC
Protein: DP03939 (UniProt B0JEU3)
Region: residues 418	to 450
Annotation: disorder (Structural state)
Evidence: x-ray crystallography evidence used in manual assertion
Supporting statements:
Two regions, one from residue number 201 to 209
and another from 282 to 316 were found to be disordered with poor
electron density in the case of SL80.1.
Cross-references: PDB:6L4M
Protein: DP03939 (UniProt B0JEU3)
Region: residues 543	to 569
Annotation: disorder (Structural state)
Evidence: X-ray crystallography-based structural model with missing residue coordinates used in manual assertion
Supporting statements:
Nine residues from N-terminal and 27 residues from C-terminal could not be traced in the crystal structure as the electron density for these residues was missing.
Protein: DP03940 (UniProt Q8S4P9)
Region: residues 25	to 59
Annotation: disorder (Structural state)
Evidence: X-ray crystallography-based structural model with missing residue coordinates used in manual assertion
Supporting statements:
All the three independent monomers in the case of HZ.1 had 12 residues missing from the N-terminal end and 16 residues missing from the C-terminal end.
Cross-references: PDB:6L4C
Protein: DP03940 (UniProt Q8S4P9)
Region: residues 433	to 448
Annotation: disorder (Structural state)
Evidence: X-ray crystallography-based structural model with missing residue coordinates used in manual assertion
Supporting statements:
All the three independent monomers in the case of HZ.1 had 12 residues missing from the N-terminal end and 16 residues missing from the C-terminal end.
Cross-references: PDB:6L4C
Protein: DP03941 (UniProt Q20010)
Region: residues 2	to 122
Annotation: disorder (Structural state)
Evidence: far-UV circular dichroism evidence used in manual assertion
Supporting statements:
The SAS-5 N- and C-terminal segments are unstructured in isolation.
Overlaid CD spectra of SAS-5 N-terminal (residues 2–122) and C-terminal (residues 269–404) fragments recorded at 10°C. The semi-quantitative contribution of secondary structure elements in each spectrum is deconvoluted in the bar chart left. Grey colour corresponds to random coil, green to β-strand and red to α-helical segments.
Protein: DP03941 (UniProt Q20010)
Region: residues 269	to 404
Annotation: disorder (Structural state)
Evidence: far-UV circular dichroism evidence used in manual assertion
Supporting statements:
The SAS-5 N- and C-terminal segments are unstructured in isolation.
Overlaid CD spectra of SAS-5 N-terminal (residues 2–122) and C-terminal (residues 269–404) fragments recorded at 10°C. The semi-quantitative contribution of secondary structure elements in each spectrum is deconvoluted in the bar chart left. Grey colour corresponds to random coil, green to β-strand and red to α-helical segments.
Protein: DP03942 (UniProt P34413)
Region: residues 1	to 22
Annotation: disorder (Structural state)
Evidence: cryogenic electron microscopy-based structural model with missing residue coordinates used in manual assertion
Supporting statements:
Regions that were disordered in the structures are indicated with dashed lines.
The cryo-EM structure of C-mannosyltransferase CeDPY19, in complex with Dol25-P-Man and bound to CMT2-Fab and anti-Fab nanobody (whether alone or with Dol25-P-C-Man and/or an acceptor peptide, shows this region is disordered. 
Cross-references: PDB:14782
EMDB:14779
EMDB:14781
PDB:7ZLI
PDB:7ZLH
PDB:7ZLG
PDB:7ZLJ
EMDB:14780
Protein: DP03943 (UniProt A7M6E7)
Region: residues 80	to 89
Annotation: disorder (Structural state)
Evidence: x-ray crystallography evidence used in manual assertion
Supporting statements:
The region under positive selection (T79–D112; shown in red in Fig. 1B) forms part of the Tm-1 surface and contains α3 and residues L80–A89, which, because this sequence has no interpretable electron density, may be a disordered loop.
Cross-references: PDB:3WRW
Protein: DP03943 (UniProt A7M6E7)
Region: residues 80	to 89
Annotation: disorder to order (Structural transition)
Evidence: x-ray crystallography evidence used in manual assertion
Supporting statements:
No dramatic structural differences were found for free and ToMV-Hel–bound Tm-1(431) (Cα rmsd, 1.004 Å), although a disorder-to-order transition involving residues L80–A89 and changes in the orientations of the side chains involved in ATPγS binding were observed (Fig. 4A). 
Cross-references: PDB:3WRW
PDB:3WRY
PDB:3WRX
Protein: DP03944 (UniProt P19525)
Region: residues 229	to 255
Annotation: disorder (Structural state)
Evidence: X-ray crystallography-based structural model with missing residue coordinates used in manual assertion
Supporting statements:
Residues 256–257, 441–450, and 335–355 from chain A, 255, 334–355, and 439–451 from chain B, and 334–356, 441–444, and 449 from chain C were inserted and Prime version 1 (Schrödinger, LLC)44 was used to generate a configuration of the missing loops.
Cross-references: PDB:6D3K
PDB:6D3L
Protein: DP03944 (UniProt P19525)
Region: residues 337	to 355
Annotation: disorder (Structural state)
Evidence: X-ray crystallography-based structural model with missing residue coordinates used in manual assertion
Supporting statements:
Residues 256–257, 441–450, and 335–355 from chain A, 255, 334–355, and 439–451 from chain B, and 334–356, 441–444, and 449 from chain C were inserted and Prime version 1 (Schrödinger, LLC)44 was used to generate a configuration of the missing loops.
Cross-references: PDB:6D3K
PDB:6D3L