LiteFold/DisProt huggingface dataset:
Protein: DP03766 (UniProt A4IDD0)
Region: residues 242	to 264
Annotation: disorder (Structural state)
Evidence: cryogenic electron microscopy-based structural model with missing residue coordinates used in manual assertion
Supporting statements:
The electron microscopy evidences of the proteasome 20S subunit complexed with a imidazo[1,2-a]pyrimidine and the proteasome 20S subunit apo structures, shows this region lacks electron density, indicating it is disordered.
Cross-references: PDB:6QM8
PDB:6QM7
Protein: DP03766 (UniProt A4IDD0)
Region: residues 242	to 264
Annotation: disorder (Structural state)
Evidence: cryogenic electron microscopy-based structural model with missing residue coordinates used in manual assertion
Supporting statements:
The electron microscopy evidences of the proteasome 20S subunit complexed with the inhibitory compounds LXE408 and bortezomib shows this region lacks electron density, indicating it is disordered.
Cross-references: EMDB:10462
PDB:6TCZ
Protein: DP03767 (UniProt A4HV47)
Region: residues 1	to 54
Annotation: disorder (Structural state)
Evidence: electron microscopy evidence used in manual assertion
Supporting statements:
The electron microscopy evidences of the proteasome 20S subunit complexed with a imidazo[1,2-a]pyrimidine and the proteasome 20S subunit apo structures, shows this region lacks electron density, indicating it is disordered.
Cross-references: PDB:6QM7
PDB:6QM8
Protein: DP03768 (UniProt A4IDD6)
Region: residues 1	to 99
Annotation: disorder (Structural state)
Evidence: electron microscopy evidence used in manual assertion
Supporting statements:
The electron microscopy evidences of the proteasome 20S subunit complexed with a imidazo[1,2-a]pyrimidine and the proteasome 20S subunit apo structures, shows this region lacks electron density, indicating it is disordered.
Cross-references: PDB:6QM7
PDB:6QM8
Protein: DP03768 (UniProt A4IDD6)
Region: residues 1	to 99
Annotation: disorder (Structural state)
Evidence: cryogenic electron microscopy-based structural model with missing residue coordinates used in manual assertion
Supporting statements:
The electron microscopy evidences of the proteasome 20S subunit complexed with an inhibitory compound (LXE408) shows this region lacks electron density, indicating it is disordered.
Cross-references: EMDB:10462
PDB:6TCZ
Protein: DP03769 (UniProt A4HSQ5)
Region: residues 1	to 33
Annotation: disorder (Structural state)
Evidence: electron microscopy evidence used in manual assertion
Supporting statements:
The electron microscopy evidences of the proteasome 20S subunit complexed with a imidazo[1,2-a]pyrimidine and the proteasome 20S subunit apo structures, shows this region lacks electron density, indicating it is disordered.
Cross-references: PDB:6QM7
PDB:6QM8
Protein: DP03770 (UniProt A4IBS2)
Region: residues 1	to 29
Annotation: disorder (Structural state)
Evidence: electron microscopy evidence used in manual assertion
Supporting statements:
The electron microscopy evidences of the proteasome 20S subunit apo structure shows this region lacks electron density, indicating it is disordered.
Cross-references: PDB:6QM8
Protein: DP03770 (UniProt A4IBS2)
Region: residues 1	to 29
Annotation: disorder (Structural state)
Evidence: cryogenic electron microscopy-based structural model with missing residue coordinates used in manual assertion
Supporting statements:
The electron microscopy evidences of the proteasome 20S subunit complexed with an inhibitory compound (LXE408) shows this region lacks electron density, indicating it is disordered.
Cross-references: PDB:6TCZ
EMDB:10462
Protein: DP03771 (UniProt Q8WQM6)
Region: residues 201	to 210
Annotation: disorder (Structural state)
Evidence: X-ray crystallography-based structural model with missing residue coordinates used in manual assertion
Supporting statements:
The LdTOP1S(201-262) model extends from Lys211 to Phe262, with 11 disordered side-chains.
Cross-references: PDB:2B9S
Protein: DP03772 (UniProt D0AB09)
Region: residues 1	to 10
Annotation: disorder (Structural state)
Evidence: X-ray crystallography-based structural model with missing residue coordinates used in manual assertion
Supporting statements:
There is a single LdNMT molecule in the asymmetric unit and the chain is well defined in the electron density maps, with the exception of residues 1–10 at the amino terminus and residues 83–85 and 334–339, which are not defined by the maps and assumed to be disordered.
Cross-references: PDB:2WUU
Protein: DP03773 (UniProt A0A024B7W1)
Region: residues 2396	to 2434
Annotation: disorder (Structural state)
Evidence: far-UV circular dichroism evidence used in manual assertion
Supporting statements:
Further, using a series of circular dichroism spectroscopic experiments, we validate the cytosolic region as an intrinsically disordered protein region. 
We experimentally validated NS4B-CR peptide to remain in disordered conformation in buffered conditions. Far-UV CD spectrum where negative ellipticity near 198 nm is indicative of its flexible nature is shown in Fig. 8A.
The cytosolic region NS4B-CR (residues 131–169) of Zika virus NS4B protein corresponds to residues 2396-2434 of Zika virus Genome polyprotein.
Protein: DP03773 (UniProt A0A024B7W1)
Region: residues 2396	to 2434
Annotation: pre-molten globule (Structural state)
Evidence: far-UV circular dichroism evidence used in manual assertion
Supporting statements:
To analyze the ability of NS4B-CR peptide to interact with cellular lipid molecules, we studied its behavior in the presence of lipids and artiﬁcial membrane forming SDS micelles (Tulumello and Deber, 2009). As shown in Fig. 9A and B, the maximum negative ellipticity of CD spectra of NS4B-CR peptide under the influence of SDS micelles shifts from wavelength 198.5 nm to 201.6 nm. This indicates the formation of a pre-molten globule structure in SDS.
The cytosolic region NS4B-CR (residues 131–169) of Zika virus NS4B protein corresponds to residues 2396-2434 of Zika virus Genome polyprotein.
Protein: DP03773 (UniProt A0A024B7W1)
Region: residues 2396	to 2434
Annotation: disorder to pre-molten globule (Structural transition)
Evidence: far-UV circular dichroism evidence used in manual assertion
Supporting statements:
To analyze the ability of NS4B-CR peptide to interact with cellular lipid molecules, we studied its behavior in the presence of lipids and artiﬁcial membrane forming SDS micelles (Tulumello and Deber, 2009). As shown in Fig. 9A and B, the maximum negative ellipticity of CD spectra of NS4B-CR peptide under the influence of SDS micelles shifts from wavelength 198.5 nm to 201.6 nm. This indicates the formation of a pre-molten globule structure in SDS.
Protein: DP03773 (UniProt A0A024B7W1)
Region: residues 2396	to 2434
Annotation: lipid binding (Molecular function)
Evidence: far-UV circular dichroism evidence used in manual assertion
Supporting statements:
To analyze the ability of NS4B-CR peptide to interact with cellular lipid molecules, we studied its behavior in the presence of lipids and artiﬁcial membrane forming SDS micelles (Tulumello and Deber, 2009). As shown in Fig. 9A and B, the maximum negative ellipticity of CD spectra of NS4B-CR peptide under the influence of SDS micelles shifts from wavelength 198.5 nm to 201.6 nm. This indicates the formation of a pre-molten globule structure in SDS.
Protein: DP03773 (UniProt A0A024B7W1)
Region: residues 2927	to 2941
Annotation: disorder (Structural state)
Evidence: X-ray crystallography-based structural model with missing residue coordinates used in manual assertion
Supporting statements:
The PDB evidence of the free Zika NS5 polymerase domain shows this region lacks electron density, indicating it is disordered.
Cross-references: PDB:6LD1
Protein: DP03773 (UniProt A0A024B7W1)
Region: residues 2979	to 2992
Annotation: disorder (Structural state)
Evidence: X-ray crystallography-based structural model with missing residue coordinates used in manual assertion
Supporting statements:
The PDB evidence of the free Zika NS5 polymerase domain shows this region lacks electron density, indicating it is disordered.
Cross-references: PDB:6LD1
Protein: DP03773 (UniProt A0A024B7W1)
Region: residues 966	to 1065
Annotation: disorder (Structural state)
Evidence: X-ray crystallography-based structural model with missing residue coordinates used in manual assertion
Supporting statements:
For ZIKV, the first half of NS1c and the terminal residues beyond 339 were not resolved (Fig. 1C).
Cross-references: PDB:7BSD
Protein: DP03774 (UniProt A0A504X6A3)
Region: residues 1	to 54
Annotation: disorder (Structural state)
Evidence: cryogenic electron microscopy-based structural model with missing residue coordinates used in manual assertion
Supporting statements:
The electron microscopy evidences of the proteasome 20S subunit complexed with an inhibitory compound (LXE408) shows this region lacks electron density, indicating it is disordered.
Cross-references: EMDB:10462
PDB:6TCZ
Protein: DP03775 (UniProt A0A3S7WPD8)
Region: residues 1	to 33
Annotation: disorder (Structural state)
Evidence: cryogenic electron microscopy-based structural model with missing residue coordinates used in manual assertion
Supporting statements:
The electron microscopy evidences of the proteasome 20S subunit complexed with the inhibitory compounds LXE408 and bortezomib shows this region lacks electron density, indicating it is disordered.
Cross-references: PDB:6TD5
PDB:6TCZ
EMDB:10462
Protein: DP03776 (UniProt A0A504Y5E1)
Region: residues 274	to 285
Annotation: disorder (Structural state)
Evidence: cryogenic electron microscopy-based structural model with missing residue coordinates used in manual assertion
Supporting statements:
The electron microscopy evidences of the proteasome 20S subunit complexed with the inhibitory compounds LXE408 and bortezomib shows this region lacks electron density, indicating it is disordered.
Cross-references: PDB:6TD5
PDB:6TCZ
EMDB:10462
Protein: DP03777 (UniProt Q9TXA6)
Region: residues 129	to 141
Annotation: disorder (Structural state)
Evidence: cryogenic electron microscopy-based structural model with missing residue coordinates used in manual assertion
Supporting statements:
The electron microscopy evidences of the small subunit of Leishmania ribosome bound to paromomycin shows this region lacks electron density, indicating it is disordered.
Cross-references: EMDB:7024
PDB:6AZ1
Protein: DP03778 (UniProt O44012)
Region: residues 239	to 249
Annotation: disorder (Structural state)
Evidence: cryogenic electron microscopy-based structural model with missing residue coordinates used in manual assertion
Supporting statements:
The electron microscopy evidences of the small subunit of Leishmania ribosome bound to paromomycin shows this region lacks electron density, indicating it is disordered.
Cross-references: EMDB:7024
PDB:6AZ1
Protein: DP03779 (UniProt A4IDS4)
Region: residues 212	to 246
Annotation: disorder (Structural state)
Evidence: cryogenic electron microscopy-based structural model with missing residue coordinates used in manual assertion
Supporting statements:
The electron microscopy evidences of the small subunit of Leishmania ribosome bound to paromomycin shows this region lacks electron density, indicating it is disordered.
Cross-references: EMDB:7024
PDB:6AZ1
Protein: DP03780 (UniProt D1M863)
Region: residues 1	to 25
Annotation: disorder (Structural state)
Evidence: cryogenic electron microscopy-based structural model with missing residue coordinates used in manual assertion
Supporting statements:
The electron microscopy evidences of the small subunit of the Leishmania donovani 80S ribosome shows this region lacks electron density, indicating it is disordered.
Cross-references: EMDB:8343
PDB:5T2A
Protein: DP03781 (UniProt Q6QDB5)
Region: residues 70	to 80
Annotation: disorder (Structural state)
Evidence: X-ray crystallography-based structural model with missing residue coordinates used in manual assertion
Supporting statements:
Missing segments include residues 70–80 (the loop linking β3 and α3), 112–132 (the β4–α4 loop) and 227–254 (the β6–α6 loop).
Cross-references: PDB:2XOX
Protein: DP03781 (UniProt Q6QDB5)
Region: residues 112	to 132
Annotation: disorder (Structural state)
Evidence: X-ray crystallography-based structural model with missing residue coordinates used in manual assertion
Supporting statements:
Missing segments include residues 70–80 (the loop linking β3 and α3), 112–132 (the β4–α4 loop) and 227–254 (the β6–α6 loop).
Cross-references: PDB:2XOX
Protein: DP03781 (UniProt Q6QDB5)
Region: residues 227	to 254
Annotation: disorder (Structural state)
Evidence: X-ray crystallography-based structural model with missing residue coordinates used in manual assertion
Supporting statements:
Missing segments include residues 70–80 (the loop linking β3 and α3), 112–132 (the β4–α4 loop) and 227–254 (the β6–α6 loop).
Cross-references: PDB:2XOX
Protein: DP03782 (UniProt B5TV91)
Region: residues 186	to 226
Annotation: disorder (Structural state)
Evidence: X-ray crystallography-based structural model with missing residue coordinates used in manual assertion
Supporting statements:
The whole molecule was traced with help of electron density map but there was a poor electron density for 41-residue long segment (186–226) and hence it could not be defined.
Cross-references: PDB:5H0T
Protein: DP03782 (UniProt B5TV91)
Region: residues 118	to 134
Annotation: disorder (Structural state)
Evidence: X-ray crystallography-based structural model with high relative B-factor values used in manual assertion
Supporting statements:
The average value of the B-factor for the atoms of the IDCL loop in LdPCNA is 114 Å2 whereas as the average B-factor for rest of the protein atoms is 74 Å2 indicating that the IDCL loop is a highly flexible structure.
Cross-references: PDB:5H0T
Protein: DP03782 (UniProt B5TV91)
Region: residues 118	to 134
Annotation: flexible linker (Disorder function)
Evidence: X-ray crystallography-based structural model with high relative B-factor values used in manual assertion
Supporting statements:
The average value of the B-factor for the atoms of the IDCL loop in LdPCNA is 114 Å2 whereas as the average B-factor for rest of the protein atoms is 74 Å2 indicating that the IDCL loop is a highly flexible structure.
Domain-1 and Domain-2 are connected by a flexible 17-residue loop known as inter-domain connecting loop (IDCL) (residues, Leu118-Arg134).
Cross-references: PDB:5H0T
Protein: DP03783 (UniProt Q4Q5S8)
Region: residues 1	to 10
Annotation: disorder (Structural state)
Evidence: X-ray crystallography-based structural model with missing residue coordinates used in manual assertion
Supporting statements:
The PDBs structures of the major N-myristoyltransferase in complex with a variety of inhibitors show this region lacks electron density, indicating it is disordered.
Cross-references: PDB:6QDE
PDB:6QDA
PDB:6QDB
PDB:6QD9
PDB:6QDH
PDB:6QDF
PDB:6QDD
PDB:6QDC
PDB:6QDG
Protein: DP03784 (UniProt Q4QCD2)
Region: residues 737	to 747
Annotation: disorder (Structural state)
Evidence: X-ray crystallography-based structural model with missing residue coordinates used in manual assertion
Supporting statements:
Residues 207 to 736 are well defined in the electron density map; only the 22 amino acid N-terminal expression tag, residue 206, and the final 11 residues at the C-terminus, Thr737-Gln747, are absent from the structure.
Cross-references: PDB:3KFL
Protein: DP03786 (UniProt A0A175WC91)
Region: residues 118	to 132
Annotation: disorder (Structural state)
Evidence: X-ray crystallography-based structural model with missing residue coordinates used in manual assertion
Supporting statements:
The main difference arises from an additional flexible, 17 residue-loop between β-strands β4 and β5 of PPP2, which had no associated electron density in the crystal structure.
The star indicates the equivalent position of the additional flexible loop in PPP2, with missing electron density.
Cross-references: PDB:7JMR
Protein: DP03786 (UniProt A0A175WC91)
Region: residues 118	to 132
Annotation: flexible linker (Disorder function)
Evidence: X-ray crystallography-based structural model with missing residue coordinates used in manual assertion
Supporting statements:
The main difference arises from an additional flexible, 17 residue-loop between β-strands β4 and β5 of PPP2, which had no associated electron density in the crystal structure.
The star indicates the equivalent position of the additional flexible loop in PPP2, with missing electron density.
Cross-references: PDB:7JMR
Protein: DP03786 (UniProt A0A175WC91)
Region: residues 118	to 133
Annotation: flexible linker (Disorder function)
Evidence: X-ray crystallography-based structural model with missing residue coordinates used in manual assertion
Supporting statements:
The main difference arises from an additional flexible, 17 residue-loop between β-strands β4 and β5 of PPP2, which had no associated electron density in the crystal structure.
The star indicates the equivalent position of the additional flexible loop in PPP2, with missing electron density.
Cross-references: PDB:7JMV
Protein: DP03786 (UniProt A0A175WC91)
Region: residues 118	to 133
Annotation: disorder (Structural state)
Evidence: X-ray crystallography-based structural model with missing residue coordinates used in manual assertion
Supporting statements:
The main difference arises from an additional flexible, 17 residue-loop between β-strands β4 and β5 of PPP2, which had no associated electron density in the crystal structure.
The star indicates the equivalent position of the additional flexible loop in PPP2, with missing electron density.
Cross-references: PDB:7JMV
Protein: DP03787 (UniProt A0A1B0XTC8)
Region: residues 437	to 451
Annotation: disorder (Structural state)
Evidence: X-ray crystallography-based structural model with missing residue coordinates used in manual assertion
Supporting statements:
The PDB structure of the Zika envelope protein bound to a neutralizing antibody shows this region lacks electron density, indicating it is disordered.
Cross-references: PDB:5GZO
Protein: DP03788 (UniProt A0A109PRQ3)
Region: residues 2927	to 2944
Annotation: disorder (Structural state)
Evidence: X-ray crystallography-based structural model with missing residue coordinates used in manual assertion
Supporting statements:
There are four flexible loops in the fingers subdomain (β1‐α2 loop, α3‐α4 loop, α6‐α7 loop and α7‐α8 loop), which are disordered in our structure and other flavivirus RdRp structures.
Cross-references: PDB:5WZ3
Protein: DP03788 (UniProt A0A109PRQ3)
Region: residues 2976	to 2995
Annotation: disorder (Structural state)
Evidence: X-ray crystallography-based structural model with missing residue coordinates used in manual assertion
Supporting statements:
There are four flexible loops in the fingers subdomain (β1‐α2 loop, α3‐α4 loop, α6‐α7 loop and α7‐α8 loop), which are disordered in our structure and other flavivirus RdRp structures.
Cross-references: PDB:5WZ3
Protein: DP03788 (UniProt A0A109PRQ3)
Region: residues 2785	to 2794
Annotation: disorder (Structural state)
Evidence: X-ray crystallography-based structural model with missing residue coordinates used in manual assertion
Supporting statements:
The PDB structure of theZika virus NS5 methyltransferase bound to s-adenosylmethionine and a RNA analogue (m7GpppA) shows this region lacks electron density, indicating it is disordered.
Cross-references: PDB:5WZ1
PDB:5WZ2
Protein: DP03789 (UniProt A0A1V0E2H9)
Region: residues 1	to 23
Annotation: disorder (Structural state)
Evidence: nuclear magnetic resonance spectroscopy evidence used in manual assertion
Supporting statements:
We measured the 15N relaxation parameters (Figure S2), which is typical of a dimer and allowed us to distinguish different dynamic regions: (i) a highly flexible disordered region observed for residues 1–23, (ii) a transition disordered region from residue 24 to 35, (iii) a globular ordered region from residue 36 to 98, and (iv) a flexible C-terminus (residues 99–104).
Cross-references: BMRB:30397
PDB:6C44
Protein: DP03790 (UniProt A9LID6)
Region: residues 674	to 773
Annotation: disorder (Structural state)
Evidence: cryogenic electron microscopy-based structural model with missing residue coordinates used in manual assertion
Supporting statements:
The electron microscopy evidences of the Immature Dengue virus serotype 3 enveloprotein in complex with human antibody 1H10 Fab at pH 5.0 shows this region lacks electron density, indicating it is disordered.
Cross-references: PDB:6IDK
PDB:6IDL
Protein: DP03790 (UniProt A9LID6)
Region: residues 194	to 280
Annotation: disorder (Structural state)
Evidence: cryogenic electron microscopy-based structural model with missing residue coordinates used in manual assertion
Supporting statements:
The electron microscopy evidences of the Immature Dengue virus serotype 3 premembrane protein in complex with human antibody 1H10 Fab at pH 5.0 shows this region lacks electron density, indicating it is disordered.
Cross-references: PDB:6IDK
PDB:6IDL
Protein: DP03791 (UniProt Q26502)
Region: residues 1	to 15
Annotation: disorder (Structural state)
Evidence: X-ray crystallography-based structural model with missing residue coordinates used in manual assertion
Supporting statements:
Several portions of the structure were not traceable owing to poor observed electron density; in addition to the extreme termini (residues 1–15 and 404–406, respectively), this also applies to loop segments 108–110 and 173–180.
Cross-references: PDB:3STO
Protein: DP03792 (UniProt G4VQX9)
Region: residues 280	to 289
Annotation: disorder (Structural state)
Evidence: X-ray crystallography-based structural model with missing residue coordinates used in manual assertion
Supporting statements:
Furthermore, the domain II carries unresolved portion of the structure: residues 281QIGSSA286 (SmADSL-AMP) and 281QIGSSAMPY289 (SmADSL-Apo) are on a disordered loop. This loop contains the signature sequence 281Q*GSS*MP*K*NP293 unique to the β-elimination superfamily [12].
The PDB shows the region 280-289 lacks electron density, indicating it is disordered.
Cross-references: PDB:5EYV
Protein: DP03792 (UniProt G4VQX9)
Region: residues 280	to 289
Annotation: flexible linker (Disorder function)
Evidence: X-ray crystallography-based structural model with missing residue coordinates used in manual assertion
Supporting statements:
Furthermore, the domain II carries unresolved portion of the structure: residues 281QIGSSA286 (SmADSL-AMP) and 281QIGSSAMPY289 (SmADSL-Apo) are on a disordered loop. This loop contains the signature sequence 281Q*GSS*MP*K*NP293 unique to the β-elimination superfamily [12].
The PDB shows the region 280-289 lacks electron density, indicating it is disordered.
Cross-references: PDB:5EYV
Protein: DP03793 (UniProt Q6WVP6)
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:
Disordered segments excluded from the final models include the N-terminal hexahistidine tag and its linker segment, residues M1–P17, surface loop K111–S119, and T362–Q364 at the C-terminus.
The N-terminal extension (17 residues with the hexahistidine tag and its linker segment) and the inserted loop lack clearly defined electron density and are presumed to be disordered.
Cross-references: PDB:4Q3P
Protein: DP03794 (UniProt Q5SBG8)
Region: residues 900	to 920
Annotation: disorder (Structural state)
Evidence: X-ray crystallography-based structural model with missing residue coordinates used in manual assertion
Supporting statements:
The NS1 structure is complete with the exception of one internal 20-residue disordered loop.
Cross-references: PDB:4TPL
Protein: DP03794 (UniProt Q5SBG8)
Region: residues 900	to 920
Annotation: flexible linker (Disorder function)
Evidence: X-ray crystallography-based structural model with missing residue coordinates used in manual assertion
Supporting statements:
The NS1 structure is complete with the exception of one internal 20-residue disordered loop.
Cross-references: PDB:4TPL