LiteFold/DisProt huggingface dataset:
Protein: DP03537 (UniProt Q05320)
Region: residues 524	to 539
Annotation: lipid binding (Molecular function)
Evidence: fluorescence evidence used in manual assertion
Supporting statements:
In fact, when EBO16 was incubated with SDS micelles, the spectral peak was blue-shifted from 337 to 324 nm (Fig. 1B). The shift of about 13 nm suggests that tryptophan enters a hydrophobic environment in the SDS micelles.
Protein: DP03537 (UniProt Q05320)
Region: residues 524	to 539
Annotation: lipid binding (Molecular function)
Evidence: static fluorescence quenching evidence used in manual assertion
Supporting statements:
In the absence of SDS micelles, a steep slope is observed (Ksv = 15.8 m-1), whereas in the presence of SDS micelles a reduced slope is obtained (Ksv = 10.2 m-1). The fluorescence data clearly indicate that the single Trp of EBO16 is protected by the micelle from quenching. EBO16 in the micellar environment undergoes structural modifications including intramolecular rearrangements and acquisition of helical structure, showing a tendency to self-associate.
Protein: DP03537 (UniProt Q05320)
Region: residues 524	to 539
Annotation: lipid binding (Molecular function)
Evidence: nuclear magnetic resonance spectroscopy evidence used in manual assertion
Supporting statements:
Taken together, the NOE connectivities and chemical shift deviation data support the presence of a helix from Leu-6 to Phe-12 (Fig. 2, A and B). This was also observed in 40, 100, and 200 mm SDS, which confirms a stable interaction between the peptide and SDS at concentrations above the critical micellar concentration (data not shown).
Cross-references: BMRB:11004
PDB:2RLJ
Protein: DP03537 (UniProt Q05320)
Region: residues 524	to 539
Annotation: disorder (Structural state)
Evidence: nuclear magnetic resonance spectroscopy evidence used in manual assertion
Supporting statements:
Because EBO16 is very flexible when free in solution, it did not show NOEs during the 80 ms of mixing time.
Protein: DP03537 (UniProt Q05320)
Region: residues 529	to 535
Annotation: lipid binding (Molecular function)
Evidence: nuclear magnetic resonance spectroscopy evidence used in manual assertion
Supporting statements:
The NOESY spectrum of EBO16 in the presence of DRMs showed transfer NOEs for all residues ranging from Leu-6 to Phe-12 (Fig. 4A). We also observed transferred NOEs for the residues ranging from Leu-6 to Ile-9 for EBO16 in the presence of LUVs containing PC/PE/PI/Cho.
LUV stands for large unilamellar vesicle, while DRM stands for detergent-resistant membrane fraction, which where obtained from cells.
Protein: DP03537 (UniProt Q05320)
Region: residues 524	to 539
Annotation: viral entry into host cell (Biological process)
Evidence: nuclear magnetic resonance spectroscopy evidence used in manual assertion
Supporting statements:
The NOESY spectrum of EBO16 in the presence of DRMs showed transfer NOEs for all residues ranging from Leu-6 to Phe-12 (Fig. 4A). We also observed transferred NOEs for the residues ranging from Leu-6 to Ile-9 for EBO16 in the presence of LUVs containing PC/PE/PI/Cho.
LUV stands for large unilamellar vesicle, while DRM stands for detergent-resistant membrane fraction, which where obtained from cells.
 These data are the first indication that EBO16 can interact with DRMs in an early stage of infection.
Protein: DP03537 (UniProt Q05320)
Region: residues 190	to 212
Annotation: disorder (Structural state)
Evidence: X-ray crystallography-based structural model with missing residue coordinates used in manual assertion
Supporting statements:
No electron density is observed for residues 190-213, 311-312, 464-501 and 600-632. Weak or discontinuous electron density is seen in the loop containing the GP1-GP2 disulfide bridge (residues 49-56) and the outer regions of the GP1 glycan cap (residues 268-278 and 299-310); these regions are modeled as poly-alanine fragments.
Chain O shown in the PDB, lacks electron density up to the 212 residue, for this reason the disorder region is describe in the 190-212 region.
Cross-references: PDB:3CSY
Protein: DP03537 (UniProt Q05320)
Region: residues 279	to 298
Annotation: disorder (Structural state)
Evidence: X-ray crystallography-based structural model with missing residue coordinates used in manual assertion
Supporting statements:
No electron density is observed for residues 190-213, 311-312, 464-501 and 600-632. Weak or discontinuous electron density is seen in the loop containing the GP1-GP2 disulfide bridge (residues 49-56) and the outer regions of the GP1 glycan cap (residues 268-278 and 299-310); these regions are modeled as poly-alanine fragments.
As shown in the PDB, the region 279-298 lacks electron density.
Cross-references: PDB:3CSY
Protein: DP03537 (UniProt Q05320)
Region: residues 465	to 501
Annotation: disorder (Structural state)
Evidence: X-ray crystallography-based structural model with missing residue coordinates used in manual assertion
Supporting statements:
No electron density is observed for residues 190-213, 311-312, 464-501 and 600-632. Weak or discontinuous electron density is seen in the loop containing the GP1-GP2 disulfide bridge (residues 49-56) and the outer regions of the GP1 glycan cap (residues 268-278 and 299-310); these regions are modeled as poly-alanine fragments.
As shown in the PDB, the region 465-501 lacks electron density.
Cross-references: PDB:3CSY
Protein: DP03537 (UniProt Q05320)
Region: residues 524	to 539
Annotation: viral entry into host cell (Biological process)
Evidence: fluorescence evidence used in manual assertion
Supporting statements:
In fact, when EBO16 was incubated with SDS micelles, the spectral peak was blue-shifted from 337 to 324 nm (Fig. 1B). The shift of about 13 nm suggests that tryptophan enters a hydrophobic environment in the SDS micelles.
Protein: DP03537 (UniProt Q05320)
Region: residues 632	to 641
Annotation: disorder (Structural state)
Evidence: nuclear magnetic resonance spectroscopy evidence used in manual assertion
Supporting statements:
IDR is 100% identical to the Zaire ebolavirus Kikwit-95 strain (DP035378) assessed in this publication.
Cross-references: PDB:5T42
DisProt:DP03538r001
Protein: DP03538 (UniProt P87666)
Region: residues 632	to 641
Annotation: disorder (Structural state)
Evidence: nuclear magnetic resonance spectroscopy evidence used in manual assertion
Supporting statements:
We found that, independent of pH, EBOV MPER/TM consists of an unstructured N-terminal region and a short helix in the MPER region that is followed by a turn and the TM helix: i.e., MPER/TM forms a helix-turn-helix motif.
The ensemble is characterized by an unstructured N-terminal region (residues D632 to N641), a helical MPER region (D642 to Q650), a turn (W651 to I656), and a TM helical region (G657 to F676).
Cross-references: PDB:5T42
Protein: DP03538 (UniProt P87666)
Region: residues 524	to 539
Annotation: disorder (Structural state)
Evidence: nuclear magnetic resonance spectroscopy evidence used in manual assertion
Supporting statements:
IDR is 100% identical to the Zaire ebolavirus 
Mayinga-76 strain (DP03537) assessed in this publication.
Cross-references: DisProt:DP03537r009
Protein: DP03538 (UniProt P87666)
Region: residues 524	to 539
Annotation: disorder (Structural state)
Evidence: fluorescence evidence used in manual assertion
Supporting statements:
IDR is 100% identical to the Zaire ebolavirus 
Mayinga-76 strain (DP03537) assessed in this publication.
Cross-references: DisProt:DP03537r005
Protein: DP03538 (UniProt P87666)
Region: residues 524	to 539
Annotation: order (Structural state)
Evidence: far-UV circular dichroism evidence used in manual assertion
Supporting statements:
IDR is 100% identical to the Zaire ebolavirus 
Mayinga-76 strain (DP03537) assessed in this publication.
Cross-references: DisProt:DP03537r002
Protein: DP03538 (UniProt P87666)
Region: residues 524	to 539
Annotation: disorder (Structural state)
Evidence: far-UV circular dichroism evidence used in manual assertion
Supporting statements:
IDR is 100% identical to the Zaire ebolavirus 
Mayinga-76 strain (DP03537) assessed in this publication.
Cross-references: DisProt:DP03537r001
Protein: DP03538 (UniProt P87666)
Region: residues 524	to 539
Annotation: disorder to order (Structural transition)
Evidence: far-UV circular dichroism evidence used in manual assertion
Supporting statements:
IDR is 100% identical to the Zaire ebolavirus 
Mayinga-76 strain (DP03537) assessed in this publication.
Cross-references: DisProt:DP03537r003
Protein: DP03538 (UniProt P87666)
Region: residues 524	to 539
Annotation: lipid binding (Molecular function)
Evidence: curator inference from database used in manual assertion
Supporting statements:
IDR is 100% identical to the Zaire ebolavirus 
Mayinga-76 strain (DP03537) assessed in this publication.
Cross-references: PDB:2RLJ
BMRB:11004
DisProt:DP03537r004
DisProt:DP03537r006
DisProt:DP03537r007
DisProt:DP03537r008
Protein: DP03538 (UniProt P87666)
Region: residues 529	to 535
Annotation: lipid binding (Molecular function)
Evidence: nuclear magnetic resonance spectroscopy evidence used in manual assertion
Supporting statements:
IDR is 100% identical to the Zaire ebolavirus Mayinga-76 strain (DP03537) assessed in this publication.
Cross-references: DisProt:DP03537r010
Protein: DP03538 (UniProt P87666)
Region: residues 524	to 539
Annotation: viral entry into host cell (Biological process)
Evidence: curator inference from database used in manual assertion
Supporting statements:
IDR is 100% identical to the Zaire ebolavirus Mayinga-76 strain (DP03537) assessed in this publication.
Cross-references: DisProt:DP03537r016
DisProt:DP03537r015
DisProt:DP03537r011
Protein: DP03538 (UniProt P87666)
Region: residues 190	to 212
Annotation: disorder (Structural state)
Evidence: X-ray crystallography-based structural model with missing residue coordinates used in manual assertion
Supporting statements:
IDR is 100% identical to the Zaire ebolavirus Mayinga-76 strain (DP03537) assessed in this publication.
Cross-references: DisProt:DP03537r012
PDB:3CSY
Protein: DP03538 (UniProt P87666)
Region: residues 279	to 298
Annotation: disorder (Structural state)
Evidence: X-ray crystallography-based structural model with missing residue coordinates used in manual assertion
Supporting statements:
IDR is 100% identical to the Zaire ebolavirus Mayinga-76 strain (DP03537) assessed in this publication.
Cross-references: DisProt:DP03537r013
PDB:3CSY
Protein: DP03539 (UniProt A0A097F4I8)
Region: residues 1	to 24
Annotation: disorder (Structural state)
Evidence: cryogenic electron microscopy-based structural model with missing residue coordinates used in manual assertion
Supporting statements:
Importantly, both the N- and C-terminal arms of the Z protein remain highly flexible when bound to the L polymerase, which offers an opportunity for the Z protein to simultaneously interact with multiple binding partners.
The Z protein consists of a stable central RING domain and two flexible arms in the amino (N) and C termini
Cross-references: PDB:7ELA
EMDB:EMD-31178
Protein: DP03539 (UniProt A0A097F4I8)
Region: residues 74	to 99
Annotation: disorder (Structural state)
Evidence: cryogenic electron microscopy-based structural model with missing residue coordinates used in manual assertion
Supporting statements:
Importantly, both the N- and C-terminal arms of the Z protein remain highly flexible when bound to the L polymerase, which offers an opportunity for the Z protein to simultaneously interact with multiple binding partners.
The Z protein consists of a stable central RING domain and two flexible arms in the amino (N) and C termini
Cross-references: PDB:7ELA
EMDB:EMD-31178
Protein: DP03541 (UniProt Q9DQX7)
Region: residues 147	to 157
Annotation: disorder (Structural state)
Evidence: X-ray crystallography-based structural model with missing residue coordinates used in manual assertion
Supporting statements:
The final model included 513 of the 569 residues (excluding FLAG and His tags) of LASV NP. The regions comprising residues 1–7, 147–157, 339–363, 517–521, and 562–569 were disordered and could not be identified in the electron density.
Cross-references: PDB:3R3L
Protein: DP03541 (UniProt Q9DQX7)
Region: residues 339	to 363
Annotation: disorder (Structural state)
Evidence: X-ray crystallography-based structural model with missing residue coordinates used in manual assertion
Supporting statements:
The final model included 513 of the 569 residues (excluding FLAG and His tags) of LASV NP. The regions comprising residues 1–7, 147–157, 339–363, 517–521, and 562–569 were disordered and could not be identified in the electron density.
Cross-references: PDB:3R3L
Protein: DP03541 (UniProt Q9DQX7)
Region: residues 339	to 363
Annotation: flexible linker (Disorder function)
Evidence: X-ray crystallography-based structural model with missing residue coordinates used in manual assertion
Supporting statements:
The final model included 513 of the 569 residues (excluding FLAG and His tags) of LASV NP. The regions comprising residues 1–7, 147–157, 339–363, 517–521, and 562–569 were disordered and could not be identified in the electron density.
Cross-references: PDB:3R3L
Protein: DP03542 (UniProt P13699)
Region: residues 147	to 157
Annotation: disorder (Structural state)
Evidence: X-ray crystallography-based structural model with missing residue coordinates used in manual assertion
Supporting statements:
In the NP protomer structure, 514 residues of the 569-residue LASV NP protein were built into the model (Fig. 1a). The electron densities for residues 1 to 6, 147 to 157, 339 to 363, 518 to 521, 562 to 569 were not well defined.
Cross-references: PDB:3MWP
PDB:3MWT
PDB:3MX2
PDB:3MX5
Protein: DP03542 (UniProt P13699)
Region: residues 339	to 363
Annotation: disorder (Structural state)
Evidence: X-ray crystallography-based structural model with missing residue coordinates used in manual assertion
Supporting statements:
In the NP protomer structure, 514 residues of the 569-residue LASV NP protein were built into the model (Fig. 1a). The electron densities for residues 1 to 6, 147 to 157, 339 to 363, 518 to 521, 562 to 569 were not well defined.
Cross-references: PDB:3MWP
PDB:3MWT
PDB:3MX2
PDB:3MX5
Protein: DP03542 (UniProt P13699)
Region: residues 339	to 363
Annotation: flexible linker (Disorder function)
Evidence: X-ray crystallography-based structural model with missing residue coordinates used in manual assertion
Supporting statements:
In the NP protomer structure, 514 residues of the 569-residue LASV NP protein were built into the model (Fig. 1a). The electron densities for residues 1 to 6, 147 to 157, 339 to 363, 518 to 521, 562 to 569 were not well defined.
Flexible linker connecting the N domain (7-338) and C domain (364-561).
Protein: DP03543 (UniProt Q72500)
Region: residues 1	to 96
Annotation: disorder (Structural state)
Evidence: nuclear magnetic resonance spectroscopy evidence used in manual assertion
Supporting statements:
Vpr is unstructured at neutral pH, whereas under acidic conditions or upon addition of trifluorethanol it adopts alpha-helical structures.
The one- and two-dimensional NMR spectra (Figs. 5 and6) show a further phenomenon; in both pure aqueous as well as 50% TFE solutions the protein has some regions that show particularly broad lines, whereas at least several parts of the molecule appear to be relatively flexible resulting in sharper lines.
Protein: DP03543 (UniProt Q72500)
Region: residues 1	to 96
Annotation: disorder (Structural state)
Evidence: far-UV circular dichroism evidence used in manual assertion
Supporting statements:
Vpr is unstructured at neutral pH, whereas under acidic conditions or upon addition of trifluorethanol it adopts alpha-helical structures.
The peptide is completely unstructured at neutral pH, whereas lowering the pH to a critical threshold of pH 5.0 or adding a membrane mimetic, such as TFE, stabilizes secondary structure that is mainly α-helical in character.
Protein: DP03543 (UniProt Q72500)
Region: residues 1	to 96
Annotation: symbiont-mediated perturbation of host cell cycle progression (Biological process)
Evidence: flow cytometry evidence used in manual assertion
Supporting statements:
sVpr Is Transduced Efficiently and Induces G2Cell Cycle Arrest
HeLa cells were incubated with sVpr labeled with a Cy3-like fluorophor that allows effective sorting of the transduced cells. WhensVpr-Cy3 was added at concentrations of 2, 5, and 10 μg ml−1, flow cytometric studies revealed dose-dependent uptake of sVpr-Cy3 from the medium (71, 92, and 97% of the cells, respectively) (Fig.9 A). When cells were incubated with sVpr-Cy3 at 2 μg ml−1 and sorted based on fluorescence, 30% of the positive cells were arrested in the G2/M phase of the cell cycle. In contrast, only 13% of cells of the non-transduced cell population were present in G2/M (Fig. 9 B). These data strongly suggest that sVpr is biologically active and is able to induce G2 cell cycle arrest in susceptible cells.
Protein: DP03543 (UniProt Q72500)
Region: residues 1	to 96
Annotation: viral penetration into host nucleus (Biological process)
Evidence: epifluorescence microscopy evidence used in manual assertion
Supporting statements:
These studies revealed that sVpr-488 effectively entered cells following its addition in the extracellular medium (in a process termed as protein transduction) and further accumulated in the nucleus of these transduced cells (Fig.7).
Confocal microscopy revealed that in HeLa cells the transduced peptide sVpr-488 appears to be occasionally concentrated in cytosolic spots, whereas the majority of the peptide was clearly localized in the nucleus (Fig. 7,C and D). These data, together with our preliminary observation that sVpr activates HIV-1 replication and is specifically incorporated into budding HIV-1 virions (data not shown), provide evidence that sVpr possesses biological activities similar to those of viral Vpr.
Protein: DP03543 (UniProt Q72500)
Region: residues 1	to 96
Annotation: release from viral latency (Biological process)
Evidence: enzyme-linked immunoabsorbent assay evidence used in manual assertion
Supporting statements:
Extracellular Vpr protein increases cellular permissiveness to human immunodeficiency virus replication and reactivates virus from latency
In addition, extracellular Vpr reactivated HIV-1 expression in five latently infected cell lines of T-cell, B-cell, and promonocytic origin which normally express very low levels of HIV RNA and protein, indicating an activation of translational or pretranslational events in the virus life cycle.
Protein: DP03543 (UniProt Q72500)
Region: residues 1	to 96
Annotation: viral genome replication (Biological process)
Evidence: enzyme-linked immunoabsorbent assay evidence used in manual assertion
Supporting statements:
Extracellular Vpr protein increases cellular permissiveness to human immunodeficiency virus replication and reactivates virus from latency
Extracellular Vpr also induced efficient HIV-1 replication in newly infected resting peripheral blood mononuclear cells.
Protein: DP03544 (UniProt P08669)
Region: residues 1	to 58
Annotation: disorder (Structural state)
Evidence: X-ray crystallography-based structural model with missing residue coordinates used in manual assertion
Supporting statements:
The final model contains residues 59-416 of GP  monomer A, with disordered regions from 171-179, 209-210, 256-259 and 329-330; residues 59- 418 of GP monomer B, with disordered regions from 170-179, 209-210, and 256-259; residues  59-418 of GP monomer C, with disordered regions from 170-179, 209-210, and 256-259 and  329-330 and Fab 37.7H residues 2-225 of the heavy chain (chains D, F and H), with a disordered  region from 159-165 and residues 3-213 of the light chain (chains E, G and L).
Cross-references: PDB:5VK2
Protein: DP03545 (UniProt P35256)
Region: residues 242	to 253
Annotation: disorder (Structural state)
Evidence: X-ray crystallography-based structural model with missing residue coordinates used in manual assertion
Supporting statements:
Missing electron density region in the C-terminus of Marburgvirus VP24.
Cross-references: PDB:4OR8
Protein: DP03546 (UniProt P35260)
Region: residues 1	to 35
Annotation: disorder (Structural state)
Evidence: X-ray crystallography-based structural model with missing residue coordinates used in manual assertion
Supporting statements:
The construct crystallized was the complete mVP40, containing residues 1 to 303 (Fig. 1 and ​and2).2). Of these, the N terminus (residues 1 to 37 in molecule 1 and 1 to 35 in molecule 2) and a few short loops (residues 71 to 72, 156 to 157, and 264 to 267 in molecule 1 and residues 216 to 218, 259 to 260, 264 to 269, and 302 to 303 in molecule 2) were disordered.
Cross-references: PDB:5B0V
Protein: DP03547 (UniProt P89522)
Region: residues 183	to 193
Annotation: disorder (Structural state)
Evidence: X-ray crystallography-based structural model with missing residue coordinates used in manual assertion
Supporting statements:
Of the three molecules of CCHFV N in the asymmetric unit, we were able to observe clear electron density only of the flexible linker residues 181 to 195 connecting the stalk domain and the globular body domain in molecule B (see Fig. S2 in the supplemental material). The linker is not visible in molecules B and C, and unobserved disordered residues include 181 to 194 in molecule A and 181 to 195 in molecule C.
Cross-references: PDB:4AQG
Protein: DP03547 (UniProt P89522)
Region: residues 183	to 193
Annotation: flexible linker (Disorder function)
Evidence: X-ray crystallography-based structural model with missing residue coordinates used in manual assertion
Supporting statements:
Of the three molecules of CCHFV N in the asymmetric unit, we were able to observe clear electron density only of the flexible linker residues 181 to 195 connecting the stalk domain and the globular body domain in molecule B (see Fig. S2 in the supplemental material). The linker is not visible in molecules B and C, and unobserved disordered residues include 181 to 194 in molecule A and 181 to 195 in molecule C.
Cross-references: PDB:4AQG
Protein: DP03548 (UniProt P05453)
Region: residues 1	to 250
Annotation: pre-molten globule (Structural state)
Evidence: fluorescence resonance energy transfer evidence used in manual assertion
Supporting statements:
A natively unfolded yeast prion monomer adopts an ensemble of collapsed and rapidly fluctuating structures
These results establish that the monomeric form of NM adopts an ensemble of relatively unordered states with rapid conformational fluctuations.
We have used single-molecule and small-ensemble techniques to directly study the conformational properties of NM in physiological buffers in the non-prion monomeric state. Our results demonstrate that natively unfolded NM is not a completely denatured random coil under these conditions. Instead, it occupies an ensemble of rapidly interconverting compact conformations.
Our finding that the N region of native NM is significantly more compact than a corresponding denatured protein (40) then identifies it with the premolten globule class of natively unfolded proteins. It has been noted that a combination of low mean hydrophobicity and high charge is a prerequisite for maintaining a flexible, unstructured state under physiological conditions (49). The amyloid core of Sup35 (N region) contains only 8% hydrophobic and 4% charged amino acids. Our results indicate that the core N region remains compact and flexible despite lacking both hydrophobic and charged residues.
Protein: DP03549 (UniProt Q91H74)
Region: residues 2898	to 2909
Annotation: disorder (Structural state)
Evidence: X-ray crystallography-based structural model with missing residue coordinates used in manual assertion
Supporting statements:
This region lacks electron density in both form 1 and 2 of the crystals, indicating this residues are unstructured.
Cross-references: PDB:6KR3
PDB:6KR2
Protein: DP03549 (UniProt Q91H74)
Region: residues 3377	to 3391
Annotation: disorder (Structural state)
Evidence: X-ray crystallography-based structural model with missing residue coordinates used in manual assertion
Supporting statements:
This region lacks electron density in both form 1 and 2 of the crystals, indicating this residues are unstructured.
Cross-references: PDB:6KR3
PDB:6KR2