LiteFold/DisProt huggingface dataset:
Protein: DP01642 (UniProt P06492)
Region: residues 412	to 490
Annotation: protein binding (Molecular function)
Evidence: nuclear magnetic resonance spectroscopy evidence used in manual assertion
Supporting statements:
PC4ntd specifically stimulates the VP16−PC4 interaction for most residues in the 444−448 and 474−484 regions in VP16ad as we observe 2−3-fold increased chemical shift changes in these regions for the VP16ad−PC4 versus the VP16ad−PC4ctd interaction.
For the titrations of 15N-labeled VP16 with PC4 (Figures 1 and 2), we observed broadening and disappearance of peaks due to the formation of a larger complex and exchange between the PC4-bound and free VP16ad.
HSV-1 VP16 amino acid sequences of the KOS and F strains are identical for all 490 residues and differ from strain 17 by only two amino acid substitutions (Asp-Asn at position 13 and Ala-Thr at position 124).
Cross-references: PDB:2PHE
Protein: DP01642 (UniProt P06492)
Region: residues 412	to 490
Annotation: protein binding (Molecular function)
Evidence: glutathione S-transferase pull-down assay evidence used in manual assertion
Supporting statements:
As shown in Figure 3A, wild-type PC4 can interact with full-length VP16 (Kd = 0.7 ± 0.2 μM), and both regions are mostly indispensable for the interaction. The VP16ad/n subdomain failed to interact with PC4, while the VP16ad/c region binds at least 20 times weaker (Kd = 15 ± 6 μM).
HSV-1 VP16 amino acid sequences of the KOS and F strains are identical for all 490 residues and differ from strain 17 by only two amino acid substitutions (Asp-Asn at position 13 and Ala-Thr at position 124).
Protein: DP01642 (UniProt P06492)
Region: residues 454	to 490
Annotation: protein binding (Molecular function)
Evidence: glutathione S-transferase pull-down assay evidence used in manual assertion
Supporting statements:
As shown in Figure 3A, wild-type PC4 can interact with full-length VP16 (Kd = 0.7 ± 0.2 μM), and both regions are mostly indispensable for the interaction. The VP16ad/n subdomain failed to interact with PC4, while the VP16ad/c region binds at least 20 times weaker (Kd = 15 ± 6 μM).
HSV-1 VP16 amino acid sequences of the KOS and F strains are identical for all 490 residues and differ from strain 17 by only two amino acid substitutions (Asp-Asn at position 13 and Ala-Thr at position 124).
Protein: DP01642 (UniProt P06492)
Region: residues 412	to 490
Annotation: molecular function activator activity (Molecular function)
Evidence: glutathione S-transferase pull-down assay evidence used in manual assertion
Supporting statements:
As shown in Figure 3A, wild-type PC4 can interact with full-length VP16 (Kd = 0.7 ± 0.2 μM), and both regions are mostly indispensable for the interaction. The VP16ad/n subdomain failed to interact with PC4, while the VP16ad/c region binds at least 20 times weaker (Kd = 15 ± 6 μM).
HSV-1 VP16 amino acid sequences of the KOS and F strains are identical for all 490 residues and differ from strain 17 by only two amino acid substitutions (Asp-Asn at position 13 and Ala-Thr at position 124).
Protein: DP01642 (UniProt P06492)
Region: residues 412	to 490
Annotation: molecular function activator activity (Molecular function)
Evidence: nuclear magnetic resonance spectroscopy evidence used in manual assertion
Supporting statements:
NMR titration experiments (Figures 1 and 2) indicate that both VP16 activation subdomains are involved in the interaction with PC4 and TFIIBc. Deletion analysis shows that the VP16ad/n region fails to interact while VP16ad/c has a reduced binding affinity (>20 times compared to the full VP16ad) for PC4 (Figure 3A), indicating that both VP16 activation subdomains are required for high-affinity cooperative binding. 
HSV-1 VP16 amino acid sequences of the KOS and F strains are identical for all 490 residues and differ from strain 17 by only two amino acid substitutions (Asp-Asn at position 13 and Ala-Thr at position 124).
Cross-references: PDB:2PHG
PDB:2PHE
Protein: DP01642 (UniProt P06492)
Region: residues 350	to 394
Annotation: disorder (Structural state)
Evidence: X-ray crystallography-based structural model with missing residue coordinates used in manual assertion
Supporting statements:
Residues 350–394 (45 residues) and 403–412 (10 residues) are missing and apparently disordered in the crystal (see Fig. ​Fig.1A,1A, bottom). The model was refined to 2.1 Å resolution with a crystallographic R factor of 0.19 and Rfree value of 0.26 (Table ​2).
Cross-references: PDB:16VP
Protein: DP01642 (UniProt P06492)
Region: residues 403	to 412
Annotation: disorder (Structural state)
Evidence: X-ray crystallography-based structural model with missing residue coordinates used in manual assertion
Supporting statements:
Residues 350–394 (45 residues) and 403–412 (10 residues) are missing and apparently disordered in the crystal (see Fig. ​Fig.1A,1A, bottom). The model was refined to 2.1 Å resolution with a crystallographic R factor of 0.19 and Rfree value of 0.26 (Table ​2).
Cross-references: PDB:16VP
Protein: DP01643 (UniProt O75506)
Region: residues 1	to 10
Annotation: disorder (Structural state)
Evidence: nuclear magnetic resonance spectroscopy evidence used in manual assertion
Supporting statements:
The spectrum is contoured at a high threshold to emphasize intense correlations from flexible regions. These correlations belong to residues at the NH2 and COOH termini.
Protein: DP01643 (UniProt O75506)
Region: residues 60	to 76
Annotation: disorder (Structural state)
Evidence: cleavage assay evidence used in manual assertion
Supporting statements:
V8 proteolysis produces two fragments of 6984.8 and 7227.4 daltons, whereas trypsin digestion yields a single proteolytic product of 7682.7 daltons. These fragments mapped the proteolytic cleavage sites immediately carboxyl-terminal to residues Glu-63 and Glu-65 (in the case of V8), and Lys-69 (in the case of trypsin) in the intact protein (Fig. 2).
Protein: DP01643 (UniProt O75506)
Region: residues 60	to 76
Annotation: protein binding (Molecular function)
Evidence: cleavage assay evidence used in manual assertion
Supporting statements:
Collectively, our analyses suggest three alternative structural models for HSBP1 (Fig. 1 C): 1) a single continuous helix, 2) two noninteracting helices separated by a linker region (residues 35–40), and 3) two interacting helices arranged in an anti-parallel orientation. In each of the models, the helical regions or portions thereof can engage in intermolecular interactions, giving rise to a higher order oligomer.
Protein: DP01643 (UniProt O75506)
Region: residues 60	to 76
Annotation: disorder (Structural state)
Evidence: nuclear magnetic resonance spectroscopy evidence used in manual assertion
Supporting statements:
Most of the intense resonances correspond to residues at the less conserved carboxyl terminus extending approximately from Gly-60 to Ser-76. The Hα secondary chemical shifts and the pattern of1H-1H NOEs (data not shown) further indicate the absence of regular secondary structure in this region. Thus, NMR analyses and limited proteolysis both establish that the carboxyl terminus of HSBP1 is unstructured and flexible.
Protein: DP01643 (UniProt O75506)
Region: residues 60	to 76
Annotation: protein binding (Molecular function)
Evidence: nuclear magnetic resonance spectroscopy evidence used in manual assertion
Supporting statements:
Collectively, our analyses suggest three alternative structural models for HSBP1 (Fig. 1 C): 1) a single continuous helix, 2) two noninteracting helices separated by a linker region (residues 35–40), and 3) two interacting helices arranged in an anti-parallel orientation. In each of the models, the helical regions or portions thereof can engage in intermolecular interactions, giving rise to a higher order oligomer.
Protein: DP01644 (UniProt P09038)
Region: residues 143	to 160
Annotation: disorder (Structural state)
Evidence: X-ray crystallography-based structural model with missing residue coordinates used in manual assertion
Supporting statements:
the PDB structure shows this region lacks electron density, indicating it is disordered.
Cross-references: PDB:1BFG
Protein: DP01645 (UniProt P20239)
Region: residues 463	to 484
Annotation: disorder (Structural state)
Evidence: X-ray crystallography-based structural model with missing residue coordinates used in manual assertion
Supporting statements:
The PDB shows this region lacks electron density, indicating it is disordered.
Protein: DP01646 (UniProt P35236)
Region: residues 37	to 52
Annotation: protein binding (Molecular function)
Evidence: X-ray crystallography-based structural model with missing residue coordinates used in manual assertion
Supporting statements:
a 1.9 A crystallographic analysis of inactive ERK2 bound to a "D motif" docking peptide (pepHePTP) derived from hematopoietic tyrosine phosphatase, a negative regulator of ERK2.
Cross-references: DIBS:DI1010079
Protein: DP01647 (UniProt P51449)
Region: residues 479	to 518
Annotation: disorder (Structural state)
Evidence: X-ray crystallography-based structural model with missing residue coordinates used in manual assertion
Supporting statements:
Whereas the electron densities are excellent quality from residue 265 to residue 479 or residue 481, residues from a C-terminal part of H11 to H12 could not be modeled because no clear electron density was observed for this region.
Cross-references: PDB:3B0W
Protein: DP01647 (UniProt P51449)
Region: residues 500	to 518
Annotation: disorder (Structural state)
Evidence: X-ray crystallography-based structural model with missing residue coordinates used in manual assertion
Supporting statements:
For the co-crystallization of inverse agonists or antagonists acting via steric clash resulting in flexible/disordered
helix 12, we report a method using optimal constructs which have helix 12 deleted.
Cross-references: PDB:5NU1
Protein: DP01648 (UniProt P84022)
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 N-terminal nine residues, which are not conserved in Smads, and the C-terminal thirteen residues, which are rich in proline, are disordered in the crystals.
Cross-references: PDB:1MHD
Protein: DP01648 (UniProt P84022)
Region: residues 133	to 144
Annotation: disorder (Structural state)
Evidence: X-ray crystallography-based structural model with missing residue coordinates used in manual assertion
Supporting statements:
The final refined model contains two molecules of Smad3 MH1 (residues 7–132 and 9–132, respectively), a 15-bp DNA duplex, 47 well ordered water molecules, and two zinc atoms. Residues at the N and C termini have no electron density in the maps, and we presume that these regions are disordered in the crystals.
Cross-references: PDB:1OZJ
Protein: DP01649 (UniProt P0C1H4)
Region: residues 1	to 35
Annotation: disorder (Structural state)
Evidence: cryogenic electron microscopy-based structural model with missing residue coordinates used in manual assertion
Supporting statements:
The density is missing for residues 1-35 and fact that the histone tails are disordered is well-established (eg.Potoyan et al 2010)
Cross-references: PDB:2XQL
Protein: DP01650 (UniProt P0A7K2)
Region: residues 33	to 43
Annotation: disorder (Structural state)
Evidence: nuclear magnetic resonance spectroscopy evidence used in manual assertion
Supporting statements:
There is an indirect evidence of the existence of transitory helical structures at least in the first part (residues 33-43) of the hinge region.
Cross-references: PDB:1RQU
Protein: DP01651 (UniProt Q96T88)
Region: residues 165	to 181
Annotation: disorder (Structural state)
Evidence: nuclear magnetic resonance spectroscopy evidence used in manual assertion
Supporting statements:
the lowercase sequences are flexible regions in the liganded x-ray structure
Cross-references: PDB:2L3R
Protein: DP01651 (UniProt Q96T88)
Region: residues 286	to 301
Annotation: phosphorylation display site (Disorder function)
Evidence: nuclear magnetic resonance spectroscopy evidence used in manual assertion
Supporting statements:
Our data also suggest that phosphorylation of a linker residue can modulate the relative position of the reader modules, thereby altering the histone H3–binding mode.
Protein: DP01651 (UniProt Q96T88)
Region: residues 490	to 501
Annotation: nucleic acid binding (Molecular function)
Evidence: X-ray crystallography-based structural model with missing residue coordinates used in manual assertion
Supporting statements:
the resulting hole in the DNA is partially filled by the NKR finger
Protein: DP01651 (UniProt Q96T88)
Region: residues 646	to 678
Annotation: protein binding (Molecular function)
Evidence: X-ray crystallography-based structural model with missing residue coordinates used in manual assertion
Supporting statements:
An Allosteric Interaction Links USP7 to Deubiquitination and Chromatin Targeting of UHRF1.
Protein: DP01653 (UniProt Q3E840)
Region: residues 70	to 82
Annotation: disorder (Structural state)
Evidence: nuclear magnetic resonance spectroscopy evidence used in manual assertion
Supporting statements:
Unlike the well-structured region (residues 5−70), the N- and C-terminal regions (residues 1−4 and 71−83) are disordered.
Cross-references: PDB:1YOP
Protein: DP01654 (UniProt P36578)
Region: residues 46	to 63
Annotation: disorder (Structural state)
Evidence: X-ray crystallography-based structural model with missing residue coordinates used in manual assertion
Supporting statements:
From PDB structure
Cross-references: PDB:5LKS
Protein: DP01654 (UniProt P36578)
Region: residues 80	to 114
Annotation: disorder (Structural state)
Evidence: X-ray crystallography-based structural model with missing residue coordinates used in manual assertion
Supporting statements:
From PDB structure
Cross-references: PDB:5LKS
Protein: DP01654 (UniProt P36578)
Region: residues 301	to 320
Annotation: disorder (Structural state)
Evidence: X-ray crystallography-based structural model with missing residue coordinates used in manual assertion
Supporting statements:
From PDB structure
Cross-references: PDB:5LKS
Protein: DP01654 (UniProt P36578)
Region: residues 369	to 427
Annotation: disorder (Structural state)
Evidence: X-ray crystallography-based structural model with missing residue coordinates used in manual assertion
Supporting statements:
From PDB structure
Cross-references: PDB:5LKS
Protein: DP01657 (UniProt Q5XJY5)
Region: residues 166	to 232
Annotation: disorder (Structural state)
Evidence: cryogenic electron microscopy-based structural model with missing residue coordinates used in manual assertion
Supporting statements:
Each of the large adaptor subunits β- and γ-COP contains an α-solenoid ‘trunk’ domain, connected by an unstructured linker region to a small appendage domain.
Note, that the C-terminal domain of α-COP, ε-COP, and the δ-COP MHD, are not visualized in the leaf structure, since they compose the inter-triad linkages.
Cross-references: PDB:5NZU
PDB:5NZR
PDB:5NZV
PDB:5NZT
PDB:5NZS
EMDB:EMD-3724
EMDB:EMD-3723
EMDB:EMD-3722
EMDB:EMD-3721
EMDB:EMD-3720
Protein: DP01657 (UniProt Q5XJY5)
Region: residues 245	to 261
Annotation: disorder (Structural state)
Evidence: cryogenic electron microscopy-based structural model with missing residue coordinates used in manual assertion
Supporting statements:
The region lack electron density in the COPI coat linkage II and IV. These structures allowed the correct visualization of the δ-COP MHD and definition of the IDR boundaries, between the c’ α-helice and the MHD.
Cross-references: PDB:5NZU
PDB:5NZV
EMDB:EMD-3724
EMDB:EMD-3723
Protein: DP01658 (UniProt Q09882)
Region: residues 100	to 315
Annotation: disorder to order (Structural transition)
Evidence: cryogenic electron microscopy evidence used in manual assertion
Supporting statements:
These proteins adopt extended but defined conformations upon binding to their interacting partners.
Cross-references: PDB:3JB9
Protein: DP01658 (UniProt Q09882)
Region: residues 100	to 315
Annotation: RNA binding (Molecular function)
Evidence: cryogenic electron microscopy evidence used in manual assertion
Supporting statements:
Prp45 also directly interacts with U2 and U6 snRNAs at the catalytic center.
Cross-references: PDB:3JB9
Protein: DP01658 (UniProt Q09882)
Region: residues 100	to 315
Annotation: protein binding (Molecular function)
Evidence: cryogenic electron microscopy evidence used in manual assertion
Supporting statements:
Prp45 appears to promote spliceosome assembly by directly interacting with, and thus linking together, at least nine distinct proteins, including Spp42, Cwf17, and Cwf4/Syf3
Prp45 interacts with at least nine protein components and two snRNAs
Cross-references: PDB:3JB9
Protein: DP01658 (UniProt Q09882)
Region: residues 100	to 315
Annotation: molecular adaptor activity (Molecular function)
Evidence: cryogenic electron microscopy evidence used in manual assertion
Supporting statements:
Prp45 appears to promote spliceosome assembly by directly interacting with, and thus linking together, at least nine distinct proteins, including Spp42, Cwf17, and Cwf4/Syf3
Cross-references: PDB:3JB9
Protein: DP01659 (UniProt P05434)
Region: residues 1	to 23
Annotation: disorder (Structural state)
Evidence: nuclear magnetic resonance spectroscopy evidence used in manual assertion
Supporting statements:
Initial analysis of the NOE data indicated that the first 23 residues (Gly(2) through Gly21) of the 96-residue CRC-N construct were highly disordered.
Cross-references: PDB:2AMI
BMRB:6820
Protein: DP01660 (UniProt P12301)
Region: residues 97	to 116
Annotation: disorder (Structural state)
Evidence: X-ray crystallography-based structural model with missing residue coordinates used in manual assertion
Supporting statements:
Thirdly, residues 14–33 are not visible in the electron density map, suggesting that this loop might be very flexible and presumably extended when PsbQ is free in solution
Cross-references: PDB:1VYK
Protein: DP01660 (UniProt P12301)
Region: residues 84	to 119
Annotation: disorder (Structural state)
Evidence: nuclear magnetic resonance spectroscopy evidence used in manual assertion
Supporting statements:
The heteronuclear NOEs and relaxation rates corroborate the first 35 residues of the N‐terminal region and the residues between helix 0 and helix 1 to be highly flexible and intrinsically disordered.
Cross-references: PDB:2MWQ
BMRB:25350
Protein: DP01660 (UniProt P12301)
Region: residues 1	to 83
Annotation: disorder (Structural state)
Evidence: cryogenic electron microscopy-based structural model with missing residue coordinates used in manual assertion
Supporting statements:
In the Cryo-EM structure of spinach PSII-LHCII supercomplex portrayed in the PDB this region lacks electron density, indicating it is disordered.
Cross-references: EMDB:EMD-6617
PDB:3JCU
Protein: DP01662 (UniProt P55957)
Region: residues 1	to 12
Annotation: disorder (Structural state)
Evidence: nuclear magnetic resonance spectroscopy evidence used in manual assertion
Supporting statements:
Loops 1–12 and 43–77 are not displayed in the figure because they are completely disordered.
Cross-references: PDB:2BID
Protein: DP01662 (UniProt P55957)
Region: residues 43	to 77
Annotation: disorder (Structural state)
Evidence: nuclear magnetic resonance spectroscopy evidence used in manual assertion
Supporting statements:
Loops 1–12 and 43–77 are not displayed in the figure because they are completely disordered.
Cross-references: PDB:2BID
Protein: DP01662 (UniProt P55957)
Region: residues 76	to 106
Annotation: disorder (Structural state)
Evidence: nuclear magnetic resonance evidence used in manual assertion
Supporting statements:
The signals in the free peptide spectrum (black) fall in the center of the spectrum, which is indicative of an unstructured conformation.
Protein: DP01662 (UniProt P55957)
Region: residues 76	to 106
Annotation: order (Structural state)
Evidence: nuclear magnetic resonance evidence used in manual assertion
Supporting statements:
When bound, most of the peaks (colored) dispersed reflecting conformational changes and folding of the peptide.
Cross-references: PDB:2KBW
Protein: DP01662 (UniProt P55957)
Region: residues 76	to 106
Annotation: disorder to order (Structural transition)
Evidence: nuclear magnetic resonance evidence used in manual assertion
Supporting statements:
The signals in the free peptide spectrum (black) fall in the center of the spectrum, which is indicative of an unstructured conformation. When bound, most of the peaks (colored) dispersed reflecting conformational changes and folding of the peptide.
Protein: DP01662 (UniProt P55957)
Region: residues 76	to 106
Annotation: protein binding (Molecular function)
Evidence: nuclear magnetic resonance evidence used in manual assertion
Supporting statements:
Chemical shift perturbations in cMCL-1 upon peptide binding were very similar (data not shown); the BID-BH3 titration spectra were selected as representative to analyze in more detail.
Cross-references: PDB:2KBW
Protein: DP01663 (UniProt P27177)
Region: residues 25	to 134
Annotation: disorder (Structural state)
Evidence: nuclear magnetic resonance spectroscopy evidence used in manual assertion
Supporting statements:
N-terminal to this structured domain there is a flexibly disordered tail of 110 residues for chPrP(23–225), 118 residues for tPrP(23–225), and 69 residues for mature xlPrP (Fig. 1).
Cross-references: PDB:1U3M
Protein: DP01663 (UniProt P27177)
Region: residues 200	to 217
Annotation: disorder (Structural state)
Evidence: nuclear magnetic resonance spectroscopy evidence used in manual assertion
Supporting statements:
An additional “structural signature” for chPrP is provided by an insertion between the helices α2 and α3 ​(Figs.11 and ​and2), which forms a flexibly disordered loop and an N-terminal elongation of helix α3 in chPrP(121–225) (Fig. 3). This insertion is conserved in all known avian PrP sequences (4).
Cross-references: PDB:1U3M
Protein: DP01663 (UniProt P27177)
Region: residues 200	to 217
Annotation: flexible linker (Disorder function)
Evidence: nuclear magnetic resonance spectroscopy evidence used in manual assertion
Supporting statements:
 An additional “structural signature” for chPrP is provided by an insertion between the helices α2 and α3 (Figs.11 and ​and2), which forms a flexibly disordered loop and an N-terminal elongation of helix α3 in chPrP(121–225) (Fig. 3). This insertion is conserved in all known avian PrP sequences (4).
Protein: DP01664 (UniProt Q9I9C0)
Region: residues 25	to 142
Annotation: disorder (Structural state)
Evidence: nuclear magnetic resonance spectroscopy evidence used in manual assertion
Supporting statements:
N-terminal to this structured domain there is a flexibly disordered tail of 110 residues for chPrP(23–225), 118 residues for tPrP(23–225), and 69 residues for mature xlPrP (Fig. 1).
Cross-references: PDB:1U5L
Protein: DP01665 (UniProt Q5S1W7)
Region: residues 1	to 69
Annotation: disorder (Structural state)
Evidence: nuclear magnetic resonance spectroscopy evidence used in manual assertion
Supporting statements:
N-terminal to this structured domain there is a flexibly disordered tail of 110 residues for chPrP(23–225), 118 residues for tPrP(23–225), and 69 residues for mature xlPrP (Fig. 1).
Cross-references: PDB:1XU0
Protein: DP01668 (UniProt P12081)
Region: residues 344	to 355
Annotation: disorder (Structural state)
Evidence: X-ray crystallography-based structural model with missing residue coordinates used in manual assertion
Supporting statements:
Well-defined electron density is present for most parts of the protein in all four chains of Hs-cHisRS except the N-terminal WHEP domains (52 residues). In addition, in all four chains, five residues at the C-termini, and between eight to twelve residues in two internal loops (Pro344 to Gly355; Glu401 to Glu402), are disordered. These loops are not directly involved in histidine or ATP binding.
Cross-references: PDB:4PHC