LiteFold/DisProt huggingface dataset:
Protein: DP02870 (UniProt P22893)
Region: residues 129	to 163
Annotation: disorder (Structural state)
Evidence: nuclear magnetic resonance spectroscopy evidence used in manual assertion
Supporting statements:
The solution structure of Nup475(Y143K) was solved with use of a combination of 2D and 3D experiments on nonlabeled, 15N-labeled, and 15N/13C-labeled protein samples. Although the fragment was 77 amino acids in length, intraresidue NOEs were observed only for residues 9−42, and resonance assignments are reported for residues 5−42. This region has the amino acid sequence -T5TSSRYKTELC15RTYSESGRC24RYGAKC30QFAH34GLGELRQA42- and corresponds to residues 91−128 in the murine protein. The assigned 15N HSQC of the peptide demonstrates that nearly all of the shifted resonances correspond to the well-structured domain, while the unassigned resonances are sharp, poorly dispersed, and occur in the region of the spectrum normally associated with unstructured elements (Figure 1).
The overlap introduced by the peaks due to the unstructured domain made the 13C/15N HSQC-NOESY and TOCSY spectra difficult to assign unambiguously.
Cross-references: PDB:1M9O
Protein: DP02871 (UniProt Q5D1E7)
Region: residues 296	to 339
Annotation: disorder (Structural state)
Evidence: X-ray crystallography-based structural model with missing residue coordinates used in manual assertion
Supporting statements:
We analyzed Rengase-1 derived from Mus musculus and solved the structures of the four domains; NTD, PIN, ZF, and CTD individually by X-ray crystallography or NMR (Fig. 1a–e). X-ray crystallography was attempted for the fragment containing both the PIN and ZF domains, however, electron density was observed only for the PIN domain (Fig. 1c), consistent with a previous report on Regnase-1 derived from Homo sapiens11.
A Regnase-1 construct consisting of PIN and ZF domains derived from Mus musculus was crystallized; however, the electron density of the ZF domain was low, indicating that the ZF domain is highly mobile in the absence of target mRNA or possibly other protein-protein interactions.
Cross-references: PDB:5H9W
Protein: DP02871 (UniProt Q5D1E7)
Region: residues 301	to 326
Annotation: mRNA binding (Molecular function)
Evidence: electrophoretic mobility shift assay evidence used in manual assertion
Supporting statements:
Our NMR experiments confirmed direct binding of the ZF domain to IL-6 mRNA with a Kd of 10 ± 1.1 μM. Furthermore, an in vitro gel shift assay indicated that Regnase-1 containing the ZF domain enhanced target mRNA-binding, but the protein-RNA complex remained in the bottom of the well without entering into the polyacrylamide gel. These results indicate that Regnase-1 directly binds to RNA and precipitates under such experimental conditions.
Protein: DP02871 (UniProt Q5D1E7)
Region: residues 301	to 326
Annotation: mRNA binding (Molecular function)
Evidence: nuclear magnetic resonance spectroscopy evidence used in manual assertion
Supporting statements:
Our NMR experiments confirmed direct binding of the ZF domain to IL-6 mRNA with a Kd of 10 ± 1.1 μM. Furthermore, an in vitro gel shift assay indicated that Regnase-1 containing the ZF domain enhanced target mRNA-binding, but the protein-RNA complex remained in the bottom of the well without entering into the polyacrylamide gel. These results indicate that Regnase-1 directly binds to RNA and precipitates under such experimental conditions.
Protein: DP02871 (UniProt Q5D1E7)
Region: residues 306	to 322
Annotation: zinc ion binding (Molecular function)
Evidence: nuclear magnetic resonance spectroscopy evidence used in manual assertion
Supporting statements:
Three Cys residues and one His residue responsible for Zn2+-binding were shown in sticks.
NMR data shows the residues Cys306, Cys312, Cys318 and His322 bind to a Zn+2 ion. 
Cross-references: BMRB:25719
PDB:2N5K
Protein: DP02872 (UniProt Q8N5H7)
Region: residues 756	to 769
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.
Cross-references: PDB:3T6G
Protein: DP02873 (UniProt P97465)
Region: residues 257	to 266
Annotation: disorder (Structural state)
Evidence: X-ray crystallography-based structural model with missing residue coordinates used in manual assertion
Supporting statements:
The electron density was of good quality and well defined for most of the structure. The final model consists of residues 154-256 of mouse Dok1 in chain A, residues 154-254 in chain B, and 16 water molecules.
Cross-references: PDB:1UEF
PDB:1P5T
Protein: DP02874 (UniProt Q61033)
Region: residues 472	to 491
Annotation: disorder (Structural state)
Evidence: X-ray crystallography-based structural model with missing residue coordinates used in manual assertion
Supporting statements:
LAP2α-CTD forms an elongated dimer that is ∼94 Å long and 54 Å wide (Figure 3). In one monomer (orange in Figure 3), the current model contains amino acid residues His465–Gly471 and Pro492–Arg689. In the other monomer (green in Figure 3), the model contains residues His465–Glu473, Pro489–Ser544, and Ser556–Val685. The missing parts were disordered and did not have interpretable electron density.
Cross-references: PDB:2V0X
Protein: DP02874 (UniProt Q61033)
Region: residues 51	to 110
Annotation: disorder (Structural state)
Evidence: author statement used in manual assertion
Supporting statements:
The constant region (residues 1–186) consists of a LEM-like domain (residues 1–50) connected by a flexible tether to a LEM domain between residues 111 and 153 (Cai et al., 2001).
Protein: DP02874 (UniProt Q61033)
Region: residues 51	to 110
Annotation: flexible linker (Disorder function)
Evidence: author statement used in manual assertion
Supporting statements:
The constant region (residues 1–186) consists of a LEM-like domain (residues 1–50) connected by a flexible tether to a LEM domain between residues 111 and 153 (Cai et al., 2001).
Protein: DP02875 (UniProt P55789)
Region: residues 81	to 93
Annotation: disorder (Structural state)
Evidence: X-ray crystallography-based structural model with missing residue coordinates used in manual assertion
Supporting statements:
The N-terminus of each subunit was disordered, with the final model including residues 94–205 from each subunit.
In all subunits, the first 27 N-terminal residues of the sfALR construct (Figure S1; comprising 14 residues of the tag and linker, followed by 13 residues from the N-terminus of the cytokine form of ALR) were disordered.
Cross-references: PDB:3MBG
Protein: DP02876 (UniProt Q8N884)
Region: residues 289	to 305
Annotation: disorder (Structural state)
Evidence: X-ray crystallography-based structural model with missing residue coordinates used in manual assertion
Supporting statements:
The final model of human cGAS, except for the disordered regions (residues 218-222, 255-260, 289-305, 363-370 and 426-427), was refined to an R-factor of 20.6% (R free = 25.2%).
Cross-references: PDB:4MKP
Protein: DP02878 (UniProt Q8XAD5)
Region: residues 1	to 63
Annotation: disorder (Structural state)
Evidence: small-angle X-ray scattering evidence used in manual assertion
Supporting statements:
Here, we present a combination of SAXS and NMR data to describe the conformational ensemble of the PaaA2 antitoxin from the human pathogen E. coli O157
We show that the conformational ensemble of PaaA2 is highly compact and that the protein exists in solution as two preformed helices, connected by a flexible linker, that probably act as molecular recognition elements for toxin inhibition.
The structural properties of PaaA2 in solution were further investigated by SAXS measurements (Figure 3A and Table S2). The SAXS data also indicate that PaaA2 is an IDP-like protein as the normalized Kratky plot displays the behavior of a highly flexible biomolecule (Figure 3A, inset).
comparison of the experimentally determined Rg of PaaA2 with the values expected for an IDP of similar length (63 amino acids) or a globular protein with a similar molecular mass (∼8.5 kDa) suggests that the behavior of PaaA2 in solution most resembles that of an IDP and not of a globular protein (Figure 3B).
Altogether, these findings reveal that, in the absence of its cognate binding partner ParE2, the PaaA2 antitoxin in solution harbors two α helices connected by a flexible linker
Although PaaA2 may assume a certain level of compactness, it is clear that the protein neither adopts a globular conformation nor contains a hydrophobic core. Although the former is supported by the analytical SEC and DLS experiments, the latter is evidenced by the thermal unfolding data
 Second, the structural study of PaaA2 reveals that the antitoxin is a monomer composed of two α helices connected by a highly flexible linker. Interestingly, these pre-existing α helices align well with the toxin-binding elements of the archetypal RelB antitoxins. Therefore, we hypothesize that these helices act as molecular recognition elements that allow PaaA2 to efficiently bind the ParE2 toxin. Given that the helices are preformed, PaaA2 probably interacts with its cognate toxin through the mechanism of conformational selection
Cross-references: PDB:3ZBE
Protein: DP02878 (UniProt Q8XAD5)
Region: residues 1	to 63
Annotation: disorder (Structural state)
Evidence: far-UV circular dichroism evidence used in manual assertion
Supporting statements:
Here, we present a combination of SAXS and NMR data to describe the conformational ensemble of the PaaA2 antitoxin from the human pathogen E. coli O157

We show that the conformational ensemble of PaaA2 is highly compact and that the protein exists in solution as two preformed helices, connected by a flexible linker, that probably act as molecular recognition elements for toxin inhibition.
Estimation of the antitoxin’s secondary structure content based on the analysis of the CD spectrum reveals that PaaA2 consists of random coil with a significant amount of α helices (∼35% α helicity; Figure 2A and Table S1)
it is noteworthy that the denaturation is fully reversible (Figure S2) and that the thermal profile is not sigmoidal, suggesting that the unfolding event occurs through a noncooperative process.

Altogether, these findings reveal that, in the absence of its cognate binding partner ParE2, the PaaA2 antitoxin in solution harbors two α helices connected by a flexible linker
Although PaaA2 may assume a certain level of compactness, it is clear that the protein neither adopts a globular conformation nor contains a hydrophobic core. Although the former is supported by the analytical SEC and DLS experiments, the latter is evidenced by the thermal unfolding data
Second, the structural study of PaaA2 reveals that the antitoxin is a monomer composed of two α helices connected by a highly flexible linker. Interestingly, these pre-existing α helices align well with the toxin-binding elements of the archetypal RelB antitoxins. Therefore, we hypothesize that these helices act as molecular recognition elements that allow PaaA2 to efficiently bind the ParE2 toxin. Given that the helices are preformed, PaaA2 probably interacts with its cognate toxin through the mechanism of conformational selection
Although the whole protein is overall disordered, NMR reveals that regions 16-28 and 42-57 are preformed helices
Protein: DP02878 (UniProt Q8XAD5)
Region: residues 1	to 63
Annotation: disorder (Structural state)
Evidence: chromatography evidence used in manual assertion
Supporting statements:
Here, we present a combination of SAXS and NMR data to describe the conformational ensemble of the PaaA2 antitoxin from the human pathogen E. coli O157

We show that the conformational ensemble of PaaA2 is highly compact and that the protein exists in solution as two preformed helices, connected by a flexible linker, that probably act as molecular recognition elements for toxin inhibition.
The analytical SEC and DLS experiments indicate that PaaA2 displays IDP-like features and adopts an extended, nonglobular conformation (Figures 2B and 2C). The ratios between the apparent and theoretical values for molecular mass (Mr,app/Mr,theor) and hydrodynamic radius (Rh,app/Rh,theor) are 2.2–2.8 and 1.3–1.6, respectively, which is a typical trait for IDPs
Altogether, these findings reveal that, in the absence of its cognate binding partner ParE2, the PaaA2 antitoxin in solution harbors two α helices connected by a flexible linker

Although PaaA2 may assume a certain level of compactness, it is clear that the protein neither adopts a globular conformation nor contains a hydrophobic core. Although the former is supported by the analytical SEC and DLS experiments, the latter is evidenced by the thermal unfolding data.

econd, the structural study of PaaA2 reveals that the antitoxin is a monomer composed of two α helices connected by a highly flexible linker. Interestingly, these pre-existing α helices align well with the toxin-binding elements of the archetypal RelB antitoxins. Therefore, we hypothesize that these helices act as molecular recognition elements that allow PaaA2 to efficiently bind the ParE2 toxin. Given that the helices are preformed, PaaA2 probably interacts with its cognate toxin through the mechanism of conformational selection
Protein: DP02878 (UniProt Q8XAD5)
Region: residues 1	to 63
Annotation: disorder (Structural state)
Evidence: dynamic light scattering assay evidence used in manual assertion
Supporting statements:
Here, we present a combination of SAXS and NMR data to describe the conformational ensemble of the PaaA2 antitoxin from the human pathogen E. coli O157.
We show that the conformational ensemble of PaaA2 is highly compact and that the protein exists in solution as two preformed helices, connected by a flexible linker, that probably act as molecular recognition elements for toxin inhibition.

The analytical SEC and DLS experiments indicate that PaaA2 displays IDP-like features and adopts an extended, nonglobular conformation (Figures 2B and 2C). The ratios between the apparent and theoretical values for molecular mass (Mr,app/Mr,theor) and hydrodynamic radius (Rh,app/Rh,theor) are 2.2–2.8 and 1.3–1.6, respectively, which is a typical trait for IDPs

Altogether, these findings reveal that, in the absence of its cognate binding partner ParE2, the PaaA2 antitoxin in solution harbors two α helices connected by a flexible linker
Although PaaA2 may assume a certain level of compactness, it is clear that the protein neither adopts a globular conformation nor contains a hydrophobic core. Although the former is supported by the analytical SEC and DLS experiments, the latter is evidenced by the thermal unfolding data.
Second, the structural study of PaaA2 reveals that the antitoxin is a monomer composed of two α helices connected by a highly flexible linker. Interestingly, these pre-existing α helices align well with the toxin-binding elements of the archetypal RelB antitoxins. Therefore, we hypothesize that these helices act as molecular recognition elements that allow PaaA2 to efficiently bind the ParE2 toxin. Given that the helices are preformed, PaaA2 probably interacts with its cognate toxin through the mechanism of conformational selection
Protein: DP02878 (UniProt Q8XAD5)
Region: residues 29	to 41
Annotation: flexible linker (Disorder function)
Evidence: nuclear magnetic resonance spectroscopy evidence used in manual assertion
Supporting statements:
Here, we present a combination of SAXS and NMR data to describe the conformational ensemble of the PaaA2 antitoxin from the human pathogen E. coli O157

We show that the conformational ensemble of PaaA2 is highly compact and that the protein exists in solution as two preformed helices, connected by a flexible linker, that probably act as molecular recognition elements for toxin inhibition.
The fully assigned 1H-15N HSQC spectrum of PaaA2 shows that most of the backbone amide resonances are confined to a narrow spectral region (Figure 4A), typical for IDPs or proteins with a high α-helical content (Wüthrich, 1986,  Wishart et al., 1991). On the other hand, δ2D (Camilloni et al., 2012), which is benchmarked for IDPs, identifies two stable cores existing in an α-helical conformation for more than 80% of the time: residues Asn22 to Arg26 and Glu46 to Glu51 for helices 1 and 2, respectively (Figure 4C). These core regions coincide with the predicted α helices and contain flanking regions with percentages of α helicity between 15% and 80% (Figure 4C), which is overall in agreement with the CD data (Table S1). All of the other residues are predicted to adopt a coil-like conformation. In agreement with these predictions, the NOE spectroscopy (NOESY) spectra indicate the absence of β sheet signatures and contain peaks characteristic of α helices.
Altogether, these findings reveal that, in the absence of its cognate binding partner ParE2, the PaaA2 antitoxin in solution harbors two α helices connected by a flexible linker
Although PaaA2 may assume a certain level of compactness, it is clear that the protein neither adopts a globular conformation nor contains a hydrophobic core. Although the former is supported by the analytical SEC and DLS experiments, the latter is evidenced by the thermal unfolding data.
Second, the structural study of PaaA2 reveals that the antitoxin is a monomer composed of two α helices connected by a highly flexible linker. Interestingly, these pre-existing α helices align well with the toxin-binding elements of the archetypal RelB antitoxins. Therefore, we hypothesize that these helices act as molecular recognition elements that allow PaaA2 to efficiently bind the ParE2 toxin. Given that the helices are preformed, PaaA2 probably interacts with its cognate toxin through the mechanism of conformational selection
Protein: DP02878 (UniProt Q8XAD5)
Region: residues 15	to 34
Annotation: protein binding (Molecular function)
Evidence: x-ray crystallography evidence used in manual assertion
Supporting statements:
The antitoxin EcPaaA2 is characterized by tha helices (H1 ans H2) that serve as molecular recognition elements to wrap itself around EcParE2
In this antitoxin-toxin heterodimer, the EcPaaA2 completely wraps itself around EcParE2 in an all alpha helical conformation and covers an accessible surface area of around 1500 A2 on EcParE2
The EcPaaA2 antitoxin was recently found to be an intrinsically disordered protein with a broad conformational ensemble but containing two alpha helices. When bound to its cognate toxin these two transient helices stabilize and extend to encompass residues I15-A34 and H42-S61 (H1 and H2), the remaining aminoacids adopt defined loop conformations
Cross-references: PDB:5CW7
PDB:5CZF
Protein: DP02878 (UniProt Q8XAD5)
Region: residues 15	to 34
Annotation: molecular function regulator (Molecular function)
Evidence: x-ray crystallography evidence used in manual assertion
Supporting statements:
The antitoxin EcPaaA2 is characterized by tha helices (H1 ans H2) that serve as molecular recognition elements to wrap itself around EcParE2
In this antitoxin-toxin heterodimer, the EcPaaA2 completely wraps itself around EcParE2 in an all alpha helical conformation and covers an accessible surface area of around 1500 A2 on EcParE2
The EcPaaA2 antitoxin was recently found to be an intrinsically disordered protein with a broad conformational ensemble but containing two alpha helices. When bound to its cognate toxin these two transient helices stabilize and extend to encompass residues I15-A34 and H42-S61 (H1 and H2), the remaining aminoacids adopt defined loop conformations
Cross-references: PDB:5CW7
PDB:5CZF
Protein: DP02878 (UniProt Q8XAD5)
Region: residues 42	to 61
Annotation: molecular function regulator (Molecular function)
Evidence: x-ray crystallography evidence used in manual assertion
Supporting statements:
The antitoxin EcPaaA2 is characterized by tha helices (H1 ans H2) that serve as molecular recognition elements to wrap itself around EcParE2
In this antitoxin-toxin heterodimer, the EcPaaA2 completely wraps itself around EcParE2 in an all alpha helical conformation and covers an accessible surface area of around 1500 A2 on EcParE2
The EcPaaA2 antitoxin was recently found to be an intrinsically disordered protein with a broad conformational ensemble but containing two alpha helices. When bound to its cognate toxin these two transient helices stabilize and extend to encompass residues I15-A34 and H42-S61 (H1 and H2), the remaining aminoacids adopt defined loop conformations
Cross-references: PDB:5CW7
PDB:5CZF
Protein: DP02878 (UniProt Q8XAD5)
Region: residues 42	to 61
Annotation: protein binding (Molecular function)
Evidence: x-ray crystallography evidence used in manual assertion
Supporting statements:
The antitoxin EcPaaA2 is characterized by tha helices (H1 ans H2) that serve as molecular recognition elements to wrap itself around EcParE2
In this antitoxin-toxin heterodimer, the EcPaaA2 completely wraps itself around EcParE2 in an all alpha helical conformation and covers an accessible surface area of around 1500 A2 on EcParE2
The EcPaaA2 antitoxin was recently found to be an intrinsically disordered protein with a broad conformational ensemble but containing two alpha helices. When bound to its cognate toxin these two transient helices stabilize and extend to encompass residues I15-A34 and H42-S61 (H1 and H2), the remaining aminoacids adopt defined loop conformations
Cross-references: PDB:5CW7
PDB:5CZF
Protein: DP02878 (UniProt Q8XAD5)
Region: residues 5	to 49
Annotation: disorder to order (Structural transition)
Evidence: x-ray crystallography evidence used in manual assertion
Supporting statements:
The antitoxin EcPaaA2 is characterized by tha helices (H1 ans H2) that serve as molecular recognition elements to wrap itself around EcParE2
In this antitoxin-toxin heterodimer, the EcPaaA2 completely wraps itself around EcParE2 in an all alpha helical conformation and covers an accessible surface area of around 1500 A2 on EcParE2
The EcPaaA2 antitoxin was recently found to be an intrinsically disordered protein with a broad conformational ensemble but containing two alpha helices. When bound to its cognate toxin these two transient helices stabilize and extend to encompass residues I15-A34 and H42-S61 (H1 and H2), the remaining aminoacids adopt defined loop conformations
Cross-references: PDB:5CW7
PDB:5CZF
Protein: DP02878 (UniProt Q8XAD5)
Region: residues 1	to 12
Annotation: molecular adaptor activity (Molecular function)
Evidence: x-ray crystallography evidence used in manual assertion
Supporting statements:
The antitoxin EcPaaA2 is characterized by tha helices (H1 ans H2) that serve as molecular recognition elements to wrap itself around EcParE2
The N-terminus of EcxPaaA2 is important for the assembly of the hetero-hexadecamer
Solution studies reveal that the removal of the first 12 residues  of the EcPaaA2 antitoxin generates a toxin-antitoxin complex which has all the hallmarks of a heterodimer
The N terminal region is neccessary for formation of the higher order hetero-hexadecamer assembly
Cross-references: PDB:5CW7
PDB:5CZF
Protein: DP02879 (UniProt P59594)
Region: residues 1	to 17
Annotation: disorder (Structural state)
Evidence: cryogenic electron microscopy-based structural model with missing residue coordinates used in manual assertion
Supporting statements:
Flexible region in the structrures of ACE2-free SARS-CoV spike glycoprotein with three RBD in down conformation (PDB:6ACC) and with one RBD in up conformation (PDB:6ACD), and in the SARS-CoV spike glycoprotein and ACE2 complex, ACE2-bound conformation 1 (PDB:6acg), conformation 2 (PDB:6acj) and conformation 3 (PDB:6ack).
Cross-references: PDB:6ACC
PDB:6ACD