LiteFold/DisProt huggingface dataset:
Protein: DP03101 (UniProt O15344)
Region: residues 87	to 116
Annotation: disorder (Structural state)
Evidence: nuclear magnetic resonance spectroscopy evidence used in manual assertion
Supporting statements:
The NH signals for the first 30 amino acid residues were less dispersed and located centrally within the spectrum with less than 1 ppm and 5 ppm signal dispersion in the 1H and 15N resonances, respectively. This indicated that these residues were most likely unstructured.
Cross-references: PDB:2FFW
BMRB:6920
Protein: DP03101 (UniProt O15344)
Region: residues 87	to 116
Annotation: flexible linker (Disorder function)
Evidence: nuclear magnetic resonance spectroscopy evidence used in manual assertion
Supporting statements:
The 78 native amino acid residues comprised the 48 amino acid region defining the B-box1 motif and an additional 30 residues from the N-terminal linker that joined the RING and B-box1 sequences
Protein: DP03102 (UniProt O44326)
Region: residues 613	to 678
Annotation: disorder (Structural state)
Evidence: X-ray crystallography-based structural model with missing residue coordinates used in manual assertion
Supporting statements:
Although the C-terminal tail (residues 613–678) is part of the crystallized construct, it was  not visible in the structure; in particular, the extra  α helix (“helix C”) found just after the  arm repeats in crystals of full-length zebrafish  β-catenin (Xing et al., 2008) and in  plakoglobin (Choi et al., 2009) is absent.
Cross-references: PDB:4R0Z
Protein: DP03102 (UniProt O44326)
Region: residues 613	to 678
Annotation: molecular function inhibitor activity (Molecular function)
Evidence: isothermal titration calorimetry evidence used in manual assertion
Supporting statements:
To test whether the tails of HMP-2 affect the  affinity for pHMR-1  cyto80  , ITC experiments were performed using HMP-2  13end   and  HMP-2  54end  . The presence of the C-terminal tail of HMP-2 weakens the affinity  approximately 7-fold (23 nM vs. 3.1 nM), whereas the presence of the N-terminal tail did  not significantly affect binding to phosphorylated HMR-1 (Figs. 1A, S2, Table S2).
Protein: DP03102 (UniProt O44326)
Region: residues 613	to 678
Annotation: protein binding (Molecular function)
Evidence: isothermal titration calorimetry evidence used in manual assertion
Supporting statements:
To test whether the tails of HMP-2 affect the  affinity for pHMR-1  cyto80  , ITC experiments were performed using HMP-2  13end   and  HMP-2  54end. The presence of the C-terminal tail of HMP-2 weakens the affinity  approximately 7-fold (23 nM vs. 3.1 nM), whereas the presence of the N-terminal tail did  not significantly affect binding to phosphorylated HMR-1 (Figs. 1A, S2, Table S2).
Protein: DP03104 (UniProt P29590)
Region: residues 94	to 104
Annotation: disorder (Structural state)
Evidence: nuclear magnetic resonance spectroscopy evidence used in manual assertion
Supporting statements:
The N terminal segment from Glu49 to Phe54 and the C-terminal segment from Pro94 to Ile104 are disordered.
Cross-references: PDB:2MWX
Protein: DP03105 (UniProt Q967F4)
Region: residues 2850	to 2875
Annotation: disorder (Structural state)
Evidence: X-ray crystallography-based structural model with missing residue coordinates used in manual assertion
Supporting statements:
Region I interacts with side  chains from arm repeats 7, 8 and 9 (Fig. 3B). Residues 1153–1178, which connect regions I  and II, are disordered.
Cross-references: PDB:4R10
PDB:4R11
Protein: DP03105 (UniProt Q967F4)
Region: residues 2850	to 2875
Annotation: protein binding (Molecular function)
Evidence: x-ray crystallography evidence used in manual assertion
Supporting statements:
Region I interacts with side  chains from arm repeats 7, 8 and 9 (Fig. 3B). Residues 1153–1178, which connect regions I  and II, are disordered. Hydrophobic residues on the amphipathic helix in region II pack  against HMP-2 residues located on arm repeats 11 and 12, including Tyr599 (see below)  (Fig. 3C). 
Cross-references: PDB:4R10
PDB:4R11
Protein: DP03105 (UniProt Q967F4)
Region: residues 2910	to 2920
Annotation: disorder (Structural state)
Evidence: X-ray crystallography-based structural model with missing residue coordinates used in manual assertion
Supporting statements:
The mass spectrometry analysis of in vitro  phosphorylated HMR-1 suggested that four  residues in region IV are sequentially phosphorylated by CKI. In pHMR-1 conformation A,  only the first phosphorylated residue, Ser1212, is observed; all of the HMR-1 residues Cterminal to this position are disordered (Fig. 4A,B).
Cross-references: PDB:4R10
PDB:4R11
Protein: DP03105 (UniProt Q967F4)
Region: residues 2841	to 2920
Annotation: disorder (Structural state)
Evidence: chromatography evidence used in manual assertion
Supporting statements:
The purified HMR-1 cytoplasmic tail runs about 3x larger than its predicted size on a gel filtration column, similar to the  behavior of the unstructured E-cadherin cytoplasmic domain (  Huber et al., 2001  ), consistent  with its being an intrinsically unstructured protein.
Protein: DP03105 (UniProt Q967F4)
Region: residues 2841	to 2920
Annotation: disorder to order (Structural transition)
Evidence: x-ray crystallography evidence used in manual assertion
Supporting statements:
The purified HMR-1 cytoplasmic tail runs about 3x larger than its predicted size on a gel filtration column, similar to the  behavior of the unstructured E-cadherin cytoplasmic domain (  Huber et al., 2001  ), consistent  with its being an intrinsically unstructured protein. Thus it is likely that the region around  HMR-1 S1212 is disordered unless it is phosphorylated and bound to HMP-2.
From the experimental information (SEC evidence of disorder state and crystallography evidence of order state) it can be concluded a structural transition.
Cross-references: PDB:4R10
PDB:4R11
Protein: DP03106 (UniProt P34369)
Region: residues 2308	to 2329
Annotation: disorder (Structural state)
Evidence: X-ray crystallography-based structural model with missing residue coordinates used in manual assertion
Supporting statements:
The  extreme  N-terminal  five  residues  and  Cterminal 22 residues of cC273 are disordered and cannot be seen in the crystal structure.
The  remaining  five  frameshift  and  one missense  RP13  mutations  are  downstream  from  c-F2307 (h-R2314)  and  fall  within  the  terminal  peptide  that  is disordered in the cC273 structure. 
Although the peptide downstream  from  c-F2307  (h-F2314)  is  disordered  in  our crystal structure, it may  take on a  defined conformation upon  interaction  with  its  partner. 
Figure 2. Multiple  sequence  alignment  among  cC273,  hC273,  y C273,  and  Af2198.  The  three  Prp8  sequences  are  aligned  using MultAlin (Corpet 1988). Af2198 is aligned with cC273 based on structural superimposition. Secondary structures as they are observed in  the crystal  structures of  cC273 and Af2198 are  labeled on top of  the cC273 sequence and the bottom of  the  Af2198 sequence, respectively.  3 10 helices  are  not  differentiated  from a helices  and  are  both  labeled  as  helices  with  prefixafor  simplicity. Gray represents residues that are disordered in the crystal structure.
Cross-references: PDB:2P87
Protein: DP03107 (UniProt Q23229)
Region: residues 29	to 38
Annotation: disorder (Structural state)
Evidence: X-ray crystallography-based structural model with missing residue coordinates used in manual assertion
Supporting statements:
The following regions were omitted from the final model for lack of interpretable density: residues 1–7, 29–38, and 190–195 in monomer 1 and residues 1–7, 29–38, and 190–194 in monomer 2.
Cross-references: PDB:1MG7
Protein: DP03108 (UniProt P15374)
Region: residues 147	to 166
Annotation: disorder (Structural state)
Evidence: X-ray crystallography-based structural model with missing residue coordinates used in manual assertion
Supporting statements:
The UCH‐L3 structure includes a disordered 20 residue loop (residues 147‐166) that is positioned over the active site and may function in the definition of substrate specificity.
Two regions of UCH‐L3 lack defined electron density and have been omitted from the model (residues 1‐4 and 147‐166).
Access to the active site appears to be restricted futher by a 20 residue disordered loop consisting of residues 147‐166 which spans the active site cleft. 
The 20 residue loop between Thr147 and Val166 that is disordered in our crystals.
Cross-references: PDB:1UCH
Protein: DP03108 (UniProt P15374)
Region: residues 147	to 166
Annotation: molecular function regulator (Molecular function)
Evidence: x-ray crystallography evidence used in manual assertion
Supporting statements:
Access to the active site appears to be restricted futher by a 20 residue disordered loop consisting of residues 147‐166 which spans the active site cleft.
Cross-references: PDB:1UCH
Protein: DP03109 (UniProt Q9BYI3)
Region: residues 149	to 253
Annotation: disorder (Structural state)
Evidence: X-ray crystallography-based structural model with missing residue coordinates used in manual assertion
Supporting statements:
Ribbon diagrams for TTC7B and FAM126A-N colored from blue (N-terminus) to red (C-terminus). The “arm” in FAM126A is green. Disordered residues absent from the model are indicated by dotted lines.
Cross-references: PDB:5DSE
Protein: DP03110 (UniProt Q9FIX2)
Region: residues 151	to 165
Annotation: disorder (Structural state)
Evidence: nuclear magnetic resonance spectroscopy evidence used in manual assertion
Supporting statements:
 Residues of the N-terminal tag (1–9) and the disordered C-terminus (159–173) are omitted for clarity and were not included in the coordinates deposited in the PDB. 
Authors refered residues 159-173 correspond to annotated residues 151-165.
A long flexible α-helix protrudes from the structure at the C-terminal end.
Cross-references: PDB:2G0Q
Protein: DP03111 (UniProt O23813)
Region: residues 53	to 62
Annotation: disorder (Structural state)
Evidence: X-ray crystallography-based structural model with missing residue coordinates used in manual assertion
Supporting statements:
In the crystallographic asymmetric unit of Form-1 crystal, there were two SiRs, designated as molecules A and B, aligned face-to-face; the structures of the polypeptide chain and two prosthetic groups were clearly revealed except for those of a flexible loop (Ser240 and Ala241 for molecule A and Gly236 to Ala241 for molecule B) and the terminal regions (the N-terminal ten residues and the C-terminal nine residues).
The construct's C-terminal residues correspond to annotated 53-62 region. 
Cross-references: PDB:5H8V
PDB:5H92
PDB:5H8Y
Protein: DP03112 (UniProt P49235)
Region: residues 55	to 65
Annotation: disorder (Structural state)
Evidence: X-ray crystallography-based structural model with missing residue coordinates used in manual assertion
Supporting statements:
In both structures (ZMGlu1 and ZMGlu1–pNPTGlc complex), the extreme N-terminal 12 and C-terminal 11 residues were
not defined in the electron-density maps, suggesting that these
regions are disordered.
Cross-references: PDB:1E1F
Protein: DP03112 (UniProt P49235)
Region: residues 556	to 566
Annotation: disorder (Structural state)
Evidence: X-ray crystallography-based structural model with missing residue coordinates used in manual assertion
Supporting statements:
In both structures (ZMGlu1 and ZMGlu1–pNPTGlc complex), the extreme N-terminal 12 and C-terminal 11 residues were
not defined in the electron-density maps, suggesting that these
regions are disordered.
Cross-references: PDB:1E1E
PDB:1E1F
Protein: DP03113 (UniProt Q6ZNA4)
Region: residues 927	to 937
Annotation: disorder (Structural state)
Evidence: nuclear magnetic resonance spectroscopy evidence used in manual assertion
Supporting statements:
For the N- and C-terminal residues (Lys927–Asp937 and Gln989–Ser994, respectively) the average S2 order parameter is 0.29 +- 0.02, whereas S2 values are much higher for the RING core region (Thr938–Ala988; average S2 value of 0.85 +- 0.02) (Supporting Information Fig. S5). Thus, the core of the Arkadia RING domain exhibits a rather rigid structure, while the two termini are mobile on the sub-nanosecond time scale and show only few NOEs (Supporting Information Figs. S2 and S5). The 15N relaxation data and order parameters clearly show that the above-mentioned b1-strand Thr938-Glu940 separates the flexibly disordered N-terminus from the wellstructured rigid core of the RING-H2 domain.
Cross-references: PDB:2KIZ
Protein: DP03113 (UniProt Q6ZNA4)
Region: residues 300	to 386
Annotation: disorder (Structural state)
Evidence: author statement used in manual assertion
Supporting statements:
The free RNF111/Arkadia SIMs domain is also likely to be disordered and a similar poly-SUMO binding mechanism is employed.
By using NMR, SAXS and X-ray crystallography, the authors demonstrated that the SIMs domain in another related member of the family of SUMO-targeted ubiquitin ligases (RNF4) is largely unstructured. The region 300-386 encompass the SUMO interaction motif (SIM) 1, 2 and 3 present in the protein.
Protein: DP03114 (UniProt Q86TV6)
Region: residues 343	to 358
Annotation: disorder (Structural state)
Evidence: X-ray crystallography-based structural model with missing residue coordinates used in manual assertion
Supporting statements:
 Ribbon diagrams for TTC7B and FAM126A-N colored from blue (N-terminus) to red (C-terminus). The “arm” in FAM126A is green. Disordered residues absent from the model are indicated by dotted lines
Cross-references: PDB:5DSE
Protein: DP03114 (UniProt Q86TV6)
Region: residues 619	to 686
Annotation: disorder (Structural state)
Evidence: X-ray crystallography-based structural model with missing residue coordinates used in manual assertion
Supporting statements:
 Ribbon diagrams for TTC7B and FAM126A-N colored from blue (N-terminus) to red (C-terminus). The “arm” in FAM126A is green. Disordered residues absent from the model are indicated by dotted lines
Cross-references: PDB:5DSE
Protein: DP03114 (UniProt Q86TV6)
Region: residues 197	to 212
Annotation: disorder (Structural state)
Evidence: X-ray crystallography-based structural model with missing residue coordinates used in manual assertion
Supporting statements:
 Ribbon diagrams for TTC7B and FAM126A-N colored from blue (N-terminus) to red (C-terminus). The “arm” in FAM126A is green. Disordered residues absent from the model are indicated by dotted lines
Cross-references: PDB:5DSE
Protein: DP03114 (UniProt Q86TV6)
Region: residues 157	to 166
Annotation: disorder (Structural state)
Evidence: X-ray crystallography-based structural model with missing residue coordinates used in manual assertion
Supporting statements:
 Ribbon diagrams for TTC7B and FAM126A-N colored from blue (N-terminus) to red (C-terminus). The “arm” in FAM126A is green. Disordered residues absent from the model are indicated by dotted lines
Cross-references: PDB:5DSE
Protein: DP03115 (UniProt Q6P4R8)
Region: residues 483	to 495
Annotation: disorder (Structural state)
Evidence: X-ray crystallography-based structural model with missing residue coordinates used in manual assertion
Supporting statements:
The last 12 residues of the construct (residues 484–495) were disordered and were not modeled.
Region bundaries are updated according to PDB file
Cross-references: PDB:3U21
Protein: DP03116 (UniProt O95155)
Region: residues 1208	to 1227
Annotation: disorder (Structural state)
Evidence: nuclear magnetic resonance spectroscopy evidence used in manual assertion
Supporting statements:
The first 20 N-terminal amino acids of the E4B construct used for structure determination (aa 1208-1302) lack a defined conformation and connect to a long loop (L1: Ala1228 - Asp1243) that extends to a first β-strand (B1: Pro1244 - Leu1247).
Cross-references: PDB:2KRE
Protein: DP03116 (UniProt O95155)
Region: residues 1208	to 1225
Annotation: disorder (Structural state)
Evidence: X-ray crystallography-based structural model with missing residue coordinates used in manual assertion
Supporting statements:
The resulting electron density map has a good fit for most regions of E4B and UbcH5c, except for the first eighteen N-terminal residues (aa 1208-1225) and last two C-terminal residues (1301 and 1302) of E4B, which are not visible in the electron density.
The solved structure is the U-box Domain of Human E4B Ubiquitin Ligase
Cross-references: PDB:3L1X
Protein: DP03116 (UniProt O95155)
Region: residues 1208	to 1222
Annotation: disorder (Structural state)
Evidence: X-ray crystallography-based structural model with missing residue coordinates used in manual assertion
Supporting statements:
The resulting electron density map has a good fit for most regions of E4B and UbcH5c, except for the first eighteen N-terminal residues (aa 1208-1225) and last two C-terminal residues (1301 and 1302) of E4B, which are not visible in the electron density.
the solved structure is the the U-BOX domain of human E4B ubiquitin ligase in complex with UBCH5C E2 ubiquitin conjugating enzyme
Cross-references: PDB:3L1Z
Protein: DP03118 (UniProt P30793)
Region: residues 42	to 57
Annotation: disorder (Structural state)
Evidence: X-ray crystallography-based structural model with missing residue coordinates used in manual assertion
Supporting statements:
The region 42-57 is missing in the electron density in the PDB structures, indicating disorder.
Cross-references: PDB:7ALQ
Protein: DP03118 (UniProt P30793)
Region: residues 1	to 42
Annotation: disorder (Structural state)
Evidence: cleavage assay evidence used in manual assertion
Supporting statements:
All attempts to purify this protein yielded mixtures of partially proteolyzed polypeptides as shown by SDS/PAGE. N-terminal sequencing showed that different subunits had been proteolyzed at any one of eight Arg residues in the N-terminal stretch of 41 residues, affording a variety of cleavage products.
Protein: DP03120 (UniProt Q9HC77)
Region: residues 311	to 348
Annotation: disorder (Structural state)
Evidence: nuclear magnetic resonance spectroscopy evidence used in manual assertion
Supporting statements:
NMR data show that PN2-3 does not fold into a well defined tertiary structure but that a 23-residue region (from residues 29 to 51) is predominantly α-helical in agreement with CD measurements.
Protein: DP03120 (UniProt Q9HC77)
Region: residues 361	to 422
Annotation: disorder (Structural state)
Evidence: nuclear magnetic resonance spectroscopy evidence used in manual assertion
Supporting statements:
NMR data show that PN2-3 does not fold into a well defined tertiary structure but that a 23-residue region (from residues 29 to 51) is predominantly α-helical in agreement with CD measurements.
Protein: DP03121 (UniProt P11686)
Region: residues 151	to 182
Annotation: disorder (Structural state)
Evidence: X-ray crystallography-based structural model with missing residue coordinates used in manual assertion
Supporting statements:
Residues 149–180 and 82–88, corresponding to the disordered regions defined by HDX-MS of intact CTC (Fig. 1A) and encompassing the proteolyzed 161–167 segment, have little visible electron density in our maps and were not modeled (Fig. 1B).
IDR region boundaries were modified according to alignment of the PDB and UniProt sequences
Cross-references: PDB:2YAD
Protein: DP03121 (UniProt P11686)
Region: residues 59	to 89
Annotation: disorder (Structural state)
Evidence: X-ray crystallography-based structural model with missing residue coordinates used in manual assertion
Supporting statements:
The paper does not state this region is IDR, however atomic coordinates are missing from the PDB file. 3 Met residues present in this region were not included in the PDB protein construct.
Cross-references: PDB:2YAD
Protein: DP03121 (UniProt P11686)
Region: residues 59	to 89
Annotation: flexible linker (Disorder function)
Evidence: x-ray crystallography evidence used in manual assertion
Supporting statements:
 Surfactant protein C proprotein (proSP-C) contains four regions; a short N-terminal segment (residues 1–23) facing the cytosol and important for intracellular trafficking, a transmembrane (TM) region constituting the main part of mature SP-C (residues 24–58) eventually secreted with phospholipids into the alveoli, a linker region (residues 59–89), and a BRICHOS domain (residues 90–197), defined from the structure presented here and localized to the ER lumen (1) (Fig. 1A)
Cross-references: PDB:2YAD
Protein: DP03122 (UniProt Q14691)
Region: residues 146	to 196
Annotation: disorder (Structural state)
Evidence: X-ray crystallography-based structural model with missing residue coordinates used in manual assertion
Supporting statements:
Psf1 has only an α-domain (residues 1–145), whereas all of its C-terminal 51 residues are disordered.
Possibly not IDR? "Kamada et al. (13) reported that their GINS complex crystallized only when a Psf1 mutant lacking the C-terminal 47 residues (14) was used, suggesting that the presence of this β-domain inhibited crystal packing of the GINS complex. Kamada et al. (13) proposed that the deleted region of Psf1 folds into a β-domain structure and that the correct positioning of this domain on the surface of the GINS complex is critical for function."
Cross-references: PDB:2Q9Q
Protein: DP03122 (UniProt Q14691)
Region: residues 146	to 196
Annotation: protein binding (Molecular function)
Evidence: x-ray crystallography evidence used in manual assertion
Supporting statements:
The last visible C-terminal residue of Psf1 (S145) before the disordered C-terminal domain is adjacent to the disordered fragment of Sld5 (residue 65–71) and to the disordered C-terminal residues of Psf3 (residues 194–216); these disordered regions are shown as spheres in Fig. 3d. The colocalization of these disordered parts of three different subunits on the GINS surface suggests that this site may bind partner proteins in the replication complex.
Cross-references: PDB:2Q9Q
Protein: DP03123 (UniProt Q9BRX5)
Region: residues 194	to 216
Annotation: disorder (Structural state)
Evidence: X-ray crystallography-based structural model with missing residue coordinates used in manual assertion
Supporting statements:
The last visible C-terminal residue of Psf1 (S145) before the disordered C-terminal domain is adjacent to the disordered fragment of Sld5 (residue 65–71) and to the disordered C-terminal residues of Psf3 (residues 194–216); these disordered regions are shown as spheres in Fig. 3d. 
Cross-references: PDB:2Q9Q
Protein: DP03123 (UniProt Q9BRX5)
Region: residues 194	to 216
Annotation: protein binding (Molecular function)
Evidence: x-ray crystallography evidence used in manual assertion
Supporting statements:
The last visible C-terminal residue of Psf1 (S145) before the disordered C-terminal domain is adjacent to the disordered fragment of Sld5 (residue 65–71) and to the disordered C-terminal residues of Psf3 (residues 194–216); these disordered regions are shown as spheres in Fig. 3d. The colocalization of these disordered parts of three different subunits on the GINS surface suggests that this site may bind partner proteins in the replication complex.
Cross-references: PDB:2Q9Q
Protein: DP03124 (UniProt O95835)
Region: residues 622	to 635
Annotation: disorder (Structural state)
Evidence: X-ray crystallography-based structural model with missing residue coordinates used in manual assertion
Supporting statements:
The secondary structure elements of our structure are shown at the top with broken lines for residues undefined in the current electron density map. 
The N-terminal 14 residues and a short C-terminal segment comprising 5 residues are unstructured (broken lines). 
Cross-references: PDB:5B5W
Protein: DP03124 (UniProt O95835)
Region: residues 361	to 567
Annotation: disorder (Structural state)
Evidence: nuclear magnetic resonance spectroscopy evidence used in manual assertion
Supporting statements:
15N-labelled PY12 (containing both PPxY motifs; aa 361–567) was titrated against unlabeled WW12 (containing both WW domains; aa 163–266). The HSQCs of the free and bound PY12 were compared to observe changes in the peaks. The HSQC of free PY12 shows that the protein is unstructured, as most of the peaks are clustered together around the 1H chemical shift 8 ppm (Figure 6A green).