LiteFold/DisProt huggingface dataset:
Protein: DP03874 (UniProt P42345)
Region: residues 904	to 926
Annotation: disorder (Structural state)
Evidence: cryogenic electron microscopy-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:6ZWO
PDB:6ZWM
Protein: DP03874 (UniProt P42345)
Region: residues 1239	to 1262
Annotation: disorder (Structural state)
Evidence: cryogenic electron microscopy-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:6ZWO
PDB:6ZWM
Protein: DP03874 (UniProt P42345)
Region: residues 1811	to 1872
Annotation: disorder (Structural state)
Evidence: cryogenic electron microscopy-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:6ZWO
PDB:6ZWM
Protein: DP03874 (UniProt P42345)
Region: residues 2434	to 2491
Annotation: disorder (Structural state)
Evidence: cryogenic electron microscopy-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:6ZWO
PDB:6ZWM
Protein: DP03875 (UniProt Q92913-2)
Region: residues 159	to 192
Annotation: disorder (Structural state)
Evidence: X-ray crystallography-based structural model with missing residue coordinates used in manual assertion
Supporting statements:
The PDB evidence shows this region lacks electron density, indicating it is disordered.
Cross-references: PDB:4DCK
Protein: DP03875 (UniProt Q92913-2)
Region: residues 159	to 192
Annotation: disorder (Structural state)
Evidence: X-ray crystallography-based structural model with missing residue coordinates used in manual assertion
Supporting statements:
The PDB evidence shows this region lacks electron density, indicating it is disordered.
Cross-references: PDB:4JPZ
Protein: DP03876 (UniProt Q9UBK8)
Region: residues 165	to 216
Annotation: disorder (Structural state)
Evidence: X-ray crystallography-based structural model with missing residue coordinates used in manual assertion
Supporting statements:
The first 54 residues are disordered, as are flexible regions Leu258−Asp271, Gln502−Ala515, and Val615−Ala620.
Cross-references: PDB:2QTL
PDB:2QTZ
Protein: DP03876 (UniProt Q9UBK8)
Region: residues 258	to 271
Annotation: disorder (Structural state)
Evidence: X-ray crystallography-based structural model with missing residue coordinates used in manual assertion
Supporting statements:
The first 54 residues are disordered, as are flexible regions Leu258−Asp271, Gln502−Ala515, and Val615−Ala620.
Cross-references: PDB:2QTL
PDB:2QTZ
Protein: DP03876 (UniProt Q9UBK8)
Region: residues 502	to 515
Annotation: disorder (Structural state)
Evidence: X-ray crystallography-based structural model with missing residue coordinates used in manual assertion
Supporting statements:
The first 54 residues are disordered, as are flexible regions Leu258−Asp271, Gln502−Ala515, and Val615−Ala620.
Cross-references: PDB:2QTL
PDB:2QTZ
Protein: DP03877 (UniProt O43776)
Region: residues 98	to 110
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:5XIX
Protein: DP03878 (UniProt Q15233)
Region: residues 54	to 65
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:7PU5
Protein: DP03878 (UniProt Q15233)
Region: residues 53	to 65
Annotation: disorder (Structural state)
Evidence: X-ray crystallography-based structural model with missing residue coordinates used in manual assertion
Supporting statements:
The asymmetric unit contains a single heterodimer, residues 66–320 of PSPC1 and residues 66–304 of NONO (494 aa), 470 waters, and 11 ethylene glycol molecules.
Cross-references: PDB:3SDE
Protein: DP03879 (UniProt E9AE57)
Region: residues 1	to 21
Annotation: disorder (Structural state)
Evidence: X-ray crystallography-based structural model with missing residue coordinates used in manual assertion
Supporting statements:
The residues visualized in each structure, of 568 residues, are listed in Table S5. 
Cross-references: PDB:6UNZ
PDB:6UO0
PDB:6UOI
PDB:6UOJ
Protein: DP03880 (UniProt P27913)
Region: residues 14	to 23
Annotation: disorder (Structural state)
Evidence: far-UV circular dichroism evidence used in manual assertion
Supporting statements:
As the corresponding DENV C domain, the peptide is intrinsically disordered in aqueous solution (Figure 2C) but gains structure upon binding to the DPC micelles (Figure 3A), forming an α-helix spanning from Met2 to Ala6.
Protein: DP03880 (UniProt P27913)
Region: residues 15	to 19
Annotation: lipid binding (Molecular function)
Evidence: nuclear magnetic resonance spectroscopy evidence used in manual assertion
Supporting statements:
As the corresponding DENV C domain, the peptide is intrinsically disordered in aqueous solution (Figure 2C) but gains structure upon binding to the DPC micelles (Figure 3A), forming an α-helix spanning from Met2 to Ala6.
Protein: DP03880 (UniProt P27913)
Region: residues 14	to 23
Annotation: lipid binding (Molecular function)
Evidence: field potential recording evidence used in manual assertion
Supporting statements:
Both ΔΠ and zeta potential show that pep14-23 interacts with POPG-containing lipid systems (Figure 2A and B).
Protein: DP03880 (UniProt P27913)
Region: residues 14	to 23
Annotation: lipid binding (Molecular function)
Evidence: far-UV circular dichroism evidence used in manual assertion
Supporting statements:
It was observed that the most negatively charged pure POPG vesicles induce a small α-helical conformational switch at that concentration.
The data shows that electrostatic forces play a significant role in the positively charged pep14-23 (net charge +5) interaction with negatively charged POPG vesicles.
Protein: DP03880 (UniProt P27913)
Region: residues 14	to 23
Annotation: disorder to order (Structural transition)
Evidence: far-UV circular dichroism evidence used in manual assertion
Supporting statements:
It was observed that the most negatively charged pure POPG vesicles induce a small α-helical conformational switch at that concentration.
The data shows that electrostatic forces play a significant role in the positively charged pep14-23 (net charge +5) interaction with negatively charged POPG vesicles.
Protein: DP03881 (UniProt O15118)
Region: residues 605	to 620
Annotation: disorder (Structural state)
Evidence: X-ray crystallography-based structural model with missing residue coordinates used in manual assertion
Supporting statements:
In our crystal structure, only residues 384 to 624 are visible, and the secondary structures are labeled. We cannot see the electron density for the N-terminal 12 amino acids and C-terminal 16 amino acids, indicating these disordered regions might be flexible loops.
Cross-references: PDB:5F18
PDB:5F1B
Protein: DP03881 (UniProt O15118)
Region: residues 374	to 383
Annotation: disorder (Structural state)
Evidence: X-ray crystallography-based structural model with missing residue coordinates used in manual assertion
Supporting statements:
In our crystal structure, only residues 384 to 624 are visible, and the secondary structures are labeled. We cannot see the electron density for the N-terminal 12 amino acids and C-terminal 16 amino acids, indicating these disordered regions might be flexible loops.
Cross-references: PDB:5F18
PDB:5F1B
Protein: DP03881 (UniProt O15118)
Region: residues 288	to 333
Annotation: disorder (Structural state)
Evidence: X-ray crystallography-based structural model with missing residue coordinates used in manual assertion
Supporting statements:
The densities of residues 23, 288–333, 642–649, 797–813, and 1256–1278 of NPC1 were not resolved nor built.
Cross-references: PDB:6UOX
Protein: DP03881 (UniProt O15118)
Region: residues 797	to 813
Annotation: disorder (Structural state)
Evidence: X-ray crystallography-based structural model with missing residue coordinates used in manual assertion
Supporting statements:
The densities of residues 23, 288–333, 642–649, 797–813, and 1256–1278 of NPC1 were not resolved nor built.
Cross-references: PDB:6UOX
Protein: DP03881 (UniProt O15118)
Region: residues 1256	to 1278
Annotation: disorder (Structural state)
Evidence: X-ray crystallography-based structural model with missing residue coordinates used in manual assertion
Supporting statements:
The densities of residues 23, 288–333, 642–649, 797–813, and 1256–1278 of NPC1 were not resolved nor built.
Cross-references: PDB:6UOX
Protein: DP03881 (UniProt O15118)
Region: residues 289	to 329
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:5JNX
Protein: DP03881 (UniProt O15118)
Region: residues 773	to 803
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:5JNX
Protein: DP03881 (UniProt O15118)
Region: residues 960	to 983
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:5JNX
Protein: DP03881 (UniProt O15118)
Region: residues 1252	to 1278
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:5JNX
Protein: DP03882 (UniProt P01111)
Region: residues 59	to 70
Annotation: disorder (Structural state)
Evidence: X-ray crystallography-based structural model with missing residue coordinates used in manual assertion
Supporting statements:
However, in Ka13GNP, there is significant adjustment of ϕ,ψ torsions associated with P loop residues, the γ-phosphate of GppNHp is shifted toward switch I, and switch II is disordered from residue 59 to 70. 
Cross-references: PDB:6E6H
Protein: DP03884 (UniProt O96028)
Region: residues 661	to 986
Annotation: disorder (Structural state)
Evidence: cryogenic electron microscopy-based structural model with missing residue coordinates used in manual assertion
Supporting statements:
The PDB shows the protein lacks electron density in this region when in complex with 187-bp nucleosome core particles, indicating it is disordered.
Cross-references: PDB:7CRO
Protein: DP03884 (UniProt O96028)
Region: residues 1206	to 1365
Annotation: disorder (Structural state)
Evidence: cryogenic electron microscopy-based structural model with missing residue coordinates used in manual assertion
Supporting statements:
The PDB shows the protein lacks electron density in this region when in complex with 187-bp nucleosome core particles, indicating it is disordered.
Cross-references: PDB:7CRO
Protein: DP03884 (UniProt O96028)
Region: residues 1221	to 1226
Annotation: histone methyltransferase activity (H3-K36 specific) (Molecular function)
Evidence: loss-of-function mutant phenotype evidence used in manual assertion
Supporting statements:
The essential sequence was further narrowed down for NSD2 to residues 1221 to 1226 (TKKKTR), the deletion of which abolished the ability of NSD2 to methylate nucleosome.
Protein: DP03885 (UniProt P49902)
Region: residues 489	to 536
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:2XCW
PDB:2XJD
PDB:2XJF
PDB:2XCV
PDB:2XJE
PDB:2XJB
PDB:2XJC
Protein: DP03885 (UniProt P49902)
Region: residues 399	to 419
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:2XCW
PDB:2XJD
PDB:2XJF
PDB:2XCX
PDB:2XCV
PDB:2XJE
PDB:2XJB
PDB:2XJC
Protein: DP03885 (UniProt P49902)
Region: residues 1	to 23
Annotation: disorder (Structural state)
Evidence: X-ray crystallography-based structural model with missing residue coordinates used in manual assertion
Supporting statements:
The Crystal structure of the NT5C2 protein in the active state shows this region lacks electron density, indicating it is disordered.
Cross-references: PDB:6DDQ
PDB:6DDK
PDB:6DDC
PDB:6DDO
PDB:6DDB
PDB:6DDL
Protein: DP03885 (UniProt P49902)
Region: residues 489	to 561
Annotation: disorder (Structural state)
Evidence: X-ray crystallography-based structural model with missing residue coordinates used in manual assertion
Supporting statements:
The N- and C-termini amino acids (L24 and D552), and the termini amino acids (T510 and P541) of the disordered region in the C segment are also labeled.
Of note, this tightly closed conformation is released in the allosterically activated structure of NT5C2 in which the C-terminal is no longer visible at the dimer interface and is also displaced from the surface of the neighboring subunit by the N-terminal segment (Figure S5B).
Cross-references: PDB:6DE3
PDB:6DE1
PDB:6DE2
Protein: DP03885 (UniProt P49902)
Region: residues 403	to 419
Annotation: disorder (Structural state)
Evidence: X-ray crystallography-based structural model with missing residue coordinates used in manual assertion
Supporting statements:
The N- and C-termini amino acids (S4 and S488), and the termini amino acids (L402 and R421) of the disordered region in the arm segment are also labeled.
Specifically, the loop at the tip of the helical arm segment of NT5C2 establishes intimate contacts with the other monomer in the basal structure, yet these contacts are lost upon activation with the helical arm pivoting away from the other monomer and the tip region becoming disordered upon allosteric activation supporting a role for this element in NT5C2 regulation (Figure 2A–F).
Cross-references: PDB:6DE1
PDB:6DD3
PDB:6DE0
PDB:6DDY
Protein: DP03885 (UniProt P49902)
Region: residues 403	to 419
Annotation: order to disorder (Structural transition)
Evidence: X-ray crystallography-based structural model with missing residue coordinates used in manual assertion
Supporting statements:
The N- and C-termini amino acids (S4 and S488), and the termini amino acids (L402 and R421) of the disordered region in the arm segment are also labeled.
Specifically, the loop at the tip of the helical arm segment of NT5C2 establishes intimate contacts with the other monomer in the basal structure, yet these contacts are lost upon activation with the helical arm pivoting away from the other monomer and the tip region becoming disordered upon allosteric activation supporting a role for this element in NT5C2 regulation (Figure 2A–F).
Cross-references: PDB:6DDL
PDB:6DE1
PDB:6DD3
PDB:6DE0
PDB:6DDY
PDB:6DDO
PDB:6DDC
PDB:6DDB
PDB:6DDQ
PDB:6DDK
Protein: DP03885 (UniProt P49902)
Region: residues 1	to 23
Annotation: disorder to order (Structural transition)
Evidence: X-ray crystallography-based structural model with missing residue coordinates used in manual assertion
Supporting statements:
As a result, NT5C2 must undergo structural rearrangement in order to switch to an active configuration. This transition to an active state, involves the organization of the N-terminal segment of the protein in a helical configuration.
Cross-references: PDB:6DD3
PDB:6DDX
PDB:6DE1
PDB:6DDZ
PDB:6DE3
PDB:6DDY
PDB:6DDB
PDB:6DDH
PDB:6DE2
PDB:6DDY
PDB:6DE0
PDB:6DDQ
PDB:6DDK
PDB:6DDC
PDB:6DDO
PDB:6DDL
Protein: DP03885 (UniProt P49902)
Region: residues 489	to 510
Annotation: order to disorder (Structural transition)
Evidence: X-ray crystallography-based structural model with missing residue coordinates used in manual assertion
Supporting statements:
In the absence of an allosteric regulator, the C-terminal segment of one NT5C2 subunit (residues 479–510 and 537–553) folds over the base of the arm segment of the neighboring protomer so that the acidic C-terminal tail introduces itself into the positively charged inter-subunit pocket promoting a compact dimer and a tightly-associated NT5C2 tetramer conformation (Figure 6C, 6D and Figure S5A). Of note, this tightly closed conformation is released in the allosterically activated structure of NT5C2 in which the C-terminal is no longer visible at the dimer interface and is also displaced from the surface of the neighboring subunit by the N-terminal segment (Figure S5B).
Cross-references: PDB:6DE2
PDB:6DE3
PDB:6DE1
PDB:6DDO
PDB:6DDQ
PDB:6DDK
Protein: DP03885 (UniProt P49902)
Region: residues 537	to 553
Annotation: order to disorder (Structural transition)
Evidence: X-ray crystallography-based structural model with missing residue coordinates used in manual assertion
Supporting statements:
In the absence of an allosteric regulator, the C-terminal segment of one NT5C2 subunit (residues 479–510 and 537–553) folds over the base of the arm segment of the neighboring protomer so that the acidic C-terminal tail introduces itself into the positively charged inter-subunit pocket promoting a compact dimer and a tightly-associated NT5C2 tetramer conformation (Figure 6C, 6D and Figure S5A). Of note, this tightly closed conformation is released in the allosterically activated structure of NT5C2 in which the C-terminal is no longer visible at the dimer interface and is also displaced from the surface of the neighboring subunit by the N-terminal segment (Figure S5B).
Cross-references: PDB:6DE2
PDB:6DE3
PDB:6DE1
PDB:6DDO
PDB:6DDQ
PDB:6DDK
Protein: DP03886 (UniProt Q4Q159)
Region: residues 214	to 240
Annotation: disorder (Structural state)
Evidence: X-ray crystallography-based structural model with missing residue coordinates used in manual assertion
Supporting statements:
A surface loop from residues 214 to 241 is disordered and is therefore missing from the model. 
Cross-references: PDB:4AIR
Protein: DP03887 (UniProt Q01782)
Region: residues 120	to 132
Annotation: disorder (Structural state)
Evidence: X-ray crystallography-based structural model with missing residue coordinates used in manual assertion
Supporting statements:
Missing electron density corresponding to a loop region.
Cross-references: PDB:1E7W
Protein: DP03887 (UniProt Q01782)
Region: residues 121	to 133
Annotation: disorder (Structural state)
Evidence: X-ray crystallography-based structural model with missing residue coordinates used in manual assertion
Supporting statements:
Missing electron density corresponding to a loop region.
We assume that a combination of static and conformational disorder is present and that the R-work and R-free values likely contain a significant contribution from the density that we have been unable to model.
Cross-references: PDB:2QHX
Protein: DP03888 (UniProt P61956)
Region: residues 1	to 14
Annotation: disorder (Structural state)
Evidence: gel-filtration evidence used in manual assertion
Supporting statements:
 As expected, SUMO2 elutes first than ΔNt-SUMO2 (Figure 4). However, the calculated difference in apparent molecular weight between the two proteins is ∼10 kDa, which is much higher than the one expected for a tail of only 14 residues (∼1.5 kDa). This suggests that the large difference in hydrodynamic volume between the two proteins can be attributed to the disordered nature of SUMO2 N-terminal extension.
Protein: DP03889 (UniProt Q16625)
Region: residues 383	to 415
Annotation: disorder (Structural state)
Evidence: X-ray crystallography-based structural model with missing residue coordinates used in manual assertion
Supporting statements:
Crystals grown using an occludin fragment that contains the C-terminal ∼140 amino acid residues that traditionally have defined this domain (383–522) reveal that only the last 106 residues form an ordered structure. The 34 N-terminal residues had no observable electron density, implying a disordered region. 
Cross-references: PDB:1XAW
Protein: DP03890 (UniProt Q01968)
Region: residues 697	to 729
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:3QIS
Protein: DP03891 (UniProt O15294)
Region: residues 757	to 771
Annotation: disorder (Structural state)
Evidence: cryogenic electron microscopy-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:6MA1
PDB:6MA2
PDB:6MA3
PDB:6MA4
PDB:6MA5
Protein: DP03892 (UniProt P00439)
Region: residues 1	to 20
Annotation: disorder (Structural state)
Evidence: X-ray crystallography-based structural model with missing residue coordinates used in manual assertion
Supporting statements:
Mammalian PAH is tetrameric, and its 52 kDa subunits are composed of a regulatory domain (RD, residues 1–110) with an unstructured N-terminal tail (N term; residues 1–29), a catalytic domain (CD, residues 111–410), and an oligomerization domain (OD, residues 411–452) responsible for dimerization and subsequent tetramerization (SI Appendix, Fig. S1).
The PDB shows the protein lacks electron density in this region, indicating it is disordered.
Cross-references: PDB:6HYC
Protein: DP03894 (UniProt O75151)
Region: residues 60	to 79
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:3PU3
PDB:3PUA
PDB:3PTR
PDB:3PU8
PDB:3PUS
Protein: DP03896 (UniProt Q13635)
Region: residues 1	to 75
Annotation: disorder (Structural state)
Evidence: cryogenic electron microscopy-based structural model with missing residue coordinates used in manual assertion
Supporting statements:
The density of residues 1–75 (N-terminal domain), 608–618 and 721–729 (TM6-TM7 linker), 888–901 (in ECD-II) and 1177–1188 (C-terminus) is not resolved nor built.
Cross-references: PDB:6OEV
PDB:6OEU
Protein: DP03896 (UniProt Q13635)
Region: residues 608	to 730
Annotation: disorder (Structural state)
Evidence: cryogenic electron microscopy-based structural model with missing residue coordinates used in manual assertion
Supporting statements:
The density of residues 1–75 (N-terminal domain), 608–618 and 721–729 (TM6-TM7 linker), 888–901 (in ECD-II) and 1177–1188 (C-terminus) is not resolved nor built.
Cross-references: PDB:6OEV
PDB:6OEU
Protein: DP03896 (UniProt Q13635)
Region: residues 888	to 901
Annotation: disorder (Structural state)
Evidence: cryogenic electron microscopy-based structural model with missing residue coordinates used in manual assertion
Supporting statements:
The density of residues 1–75 (N-terminal domain), 608–618 and 721–729 (TM6-TM7 linker), 888–901 (in ECD-II) and 1177–1188 (C-terminus) is not resolved nor built.
Cross-references: PDB:6OEV
PDB:6OEU