LiteFold/DisProt huggingface dataset:
Protein: DP01379 (UniProt P0CU44)
Region: residues 1	to 224
Annotation: disorder (Structural state)
Evidence: nuclear magnetic resonance spectroscopy-based hydrogen-deuterium exchange evidence used in manual assertion
Supporting statements:
For the disordered proteins tested (α-synuclein and CAHS proteins), nearly all the amide protons were exchanged for deuterons within 20 min, as shown by the decrease in intensity of the one-dimensional proton spectrum (Figure 2).
Protein: DP01379 (UniProt P0CU44)
Region: residues 1	to 224
Annotation: response to desiccation (Biological process)
Evidence: small interfering RNA knockdown evidence used in manual assertion
Supporting statements:
Tardigrade-Specific IDPs Are Required for Desiccation Tolerance
However, targeting two of four highly induced (13- to 22-fold) CAHS genes significantly (p < 0.01) reduced survival after desiccation compared with a control treatment, GFP RNAi (Figure 4B). 
Tardigrades Use Intrinsically Disordered Proteins to Survive Desiccation.
Protein: DP01380 (UniProt P0CU45)
Region: residues 1	to 227
Annotation: disorder (Structural state)
Evidence: nuclear magnetic resonance spectroscopy-based hydrogen-deuterium exchange evidence used in manual assertion
Supporting statements:
For the disordered proteins tested (α-synuclein and CAHS proteins), nearly all the amide protons were exchanged for deuterons within 20 min, as shown by the decrease in intensity of the one-dimensional proton spectrum (Figure 2).
Protein: DP01380 (UniProt P0CU45)
Region: residues 1	to 227
Annotation: disorder (Structural state)
Evidence: nuclear magnetic resonance spectroscopy evidence used in manual assertion
Supporting statements:
IDPs lack persistent secondary structure (Theillet et al., 2014; Yamaguchi et al., 2012), which we confirmed for CAHS proteins using nuclear magnetic resonance spectroscopy (NMR).
For α-synuclein, a known disordered protein, and for CAHS proteins, the crosspeaks occur over a narrower window (Figure 2, top), from ~8.0 to ~8.6 ppm, which coincides with the range for amide protons in the central residue of unstructured tripeptides (Schwarzinger et al., 2000).
Protein: DP01380 (UniProt P0CU45)
Region: residues 3	to 227
Annotation: response to desiccation (Biological process)
Evidence: small interfering RNA knockdown evidence used in manual assertion
Supporting statements:
Tardigrades Use Intrinsically Disordered Proteins to Survive Desiccation.
Tardigrade-Specific IDPs Are Required for Desiccation Tolerance
However, targeting two of four highly induced (13- to 22-fold) CAHS genes significantly (p < 0.01) reduced survival after desiccation compared with a control treatment, GFP RNAi (Figure 4B).
Protein: DP01381 (UniProt P0CU46)
Region: residues 1	to 237
Annotation: disorder (Structural state)
Evidence: nuclear magnetic resonance spectroscopy evidence used in manual assertion
Supporting statements:
IDPs lack persistent secondary structure (Theillet et al., 2014; Yamaguchi et al., 2012), which we confirmed for CAHS proteins using nuclear magnetic resonance spectroscopy (NMR)
For α-synuclein, a known disordered protein, and for CAHS proteins, the crosspeaks occur over a narrower window (Figure 2, top), from ~8.0 to ~8.6 ppm, which coincides with the range for amide protons in the central residue of unstructured tripeptides (Schwarzinger et al., 2000).
Protein: DP01381 (UniProt P0CU46)
Region: residues 1	to 237
Annotation: disorder (Structural state)
Evidence: nuclear magnetic resonance spectroscopy-based hydrogen-deuterium exchange evidence used in manual assertion
Supporting statements:
For the disordered proteins tested (α-synuclein and CAHS proteins), nearly all the amide protons were exchanged for deuterons within 20 min, as shown by the decrease in intensity of the one-dimensional proton spectrum (Figure 2).
Protein: DP01381 (UniProt P0CU46)
Region: residues 1	to 237
Annotation: response to desiccation (Biological process)
Evidence: small interfering RNA knockdown evidence used in manual assertion
Supporting statements:
Tardigrades Use Intrinsically Disordered Proteins to Survive Desiccation.
Tardigrade-Specific IDPs Are Required for Desiccation Tolerance
However, targeting two of four highly induced (13- to 22-fold) CAHS genes significantly (p < 0.01) reduced survival after desiccation compared with a control treatment, GFP RNAi (Figure 4B).
Protein: DP01382 (UniProt P0CU47)
Region: residues 1	to 414
Annotation: disorder (Structural state)
Evidence: nuclear magnetic resonance spectroscopy evidence used in manual assertion
Supporting statements:
IDPs lack persistent secondary structure (Theillet et al., 2014; Yamaguchi et al., 2012), which we confirmed for CAHS proteins using nuclear magnetic resonance spectroscopy (NMR).
For α-synuclein, a known disordered protein, and for CAHS proteins, the crosspeaks occur over a narrower window (Figure 2, top), from ~8.0 to ~8.6 ppm, which coincides with the range for amide protons in the central residue of unstructured tripeptides (Schwarzinger et al., 2000).
Protein: DP01382 (UniProt P0CU47)
Region: residues 1	to 414
Annotation: disorder (Structural state)
Evidence: nuclear magnetic resonance spectroscopy-based hydrogen-deuterium exchange evidence used in manual assertion
Supporting statements:
For the disordered proteins tested (α-synuclein and CAHS proteins), nearly all the amide protons were exchanged for deuterons within 20 min, as shown by the decrease in intensity of the one-dimensional proton spectrum (Figure 2).
Protein: DP01383 (UniProt P0CU51)
Region: residues 1	to 229
Annotation: disorder (Structural state)
Evidence: nuclear magnetic resonance spectroscopy evidence used in manual assertion
Supporting statements:
IDPs lack persistent secondary structure (Theillet et al., 2014; Yamaguchi et al., 2012), which we confirmed for CAHS proteins using nuclear magnetic resonance spectroscopy (NMR).
For α-synuclein, a known disordered protein, and for CAHS proteins, the crosspeaks occur over a narrower window (Figure 2, top), from ~8.0 to ~8.6 ppm, which coincides with the range for amide protons in the central residue of unstructured tripeptides (Schwarzinger et al., 2000).
Protein: DP01383 (UniProt P0CU51)
Region: residues 1	to 229
Annotation: disorder (Structural state)
Evidence: nuclear magnetic resonance spectroscopy-based hydrogen-deuterium exchange evidence used in manual assertion
Supporting statements:
For the disordered proteins tested (α-synuclein and CAHS proteins), nearly all the amide protons were exchanged for deuterons within 20 min, as shown by the decrease in intensity of the one-dimensional proton spectrum (Figure 2).
Protein: DP01383 (UniProt P0CU51)
Region: residues 1	to 229
Annotation: response to desiccation (Biological process)
Evidence: mutant physiological response evidence used in manual assertion
Supporting statements:
Similar results were obtained in bacteria, with exogenous expression of some CAHS proteins resulting in increases of more than 2 orders of magnitude in desiccation tolerance (Figure 6B). Importantly, α-synuclein, a protein that exists as a disordered monomer in cells (Fauvet et al., 2012; Theillet et al., 2016) and has no known connection to stress tolerance (Drescher et al., 2012; Theillet et al., 2014), did not increase survival under drying conditions (Figure 6B), demonstrating that something beyond intrinsic disorder of TDPs is essential for their protective capabilities.
Tardigrade-Specific IDPs Increase Desiccation Tolerance in Heterologous Systems and In Vitro
Protein: DP01384 (UniProt P0CU50)
Region: residues 1	to 94
Annotation: disorder (Structural state)
Evidence: nuclear magnetic resonance spectroscopy evidence used in manual assertion
Supporting statements:
Here, we characterize the conformational and physical behaviour of CAHS‐8 from Hypsibius exemplaris. NMR spectroscopy reveals that the protein comprises an extended central helical domain flanked by disordered termini.
By using high‐field NMR spectroscopy, we reveal that the protein comprises an extended central helical domain, with apparent coiled‐coil propensity, flanked by long, highly disordered N‐ and C‐terminal domains.
The 15N‐1H HSQC spectrum of CAHS‐8 (Figure 1 A) is typical of an intrinsically disordered protein, with low dispersion in the 1HN dimension.
Protein: DP01384 (UniProt P0CU50)
Region: residues 195	to 227
Annotation: disorder (Structural state)
Evidence: nuclear magnetic resonance spectroscopy evidence used in manual assertion
Supporting statements:
Here, we characterize the conformational and physical behaviour of CAHS‐8 from Hypsibius exemplaris. NMR spectroscopy reveals that the protein comprises an extended central helical domain flanked by disordered termini.
By using high‐field NMR spectroscopy, we reveal that the protein comprises an extended central helical domain, with apparent coiled‐coil propensity, flanked by long, highly disordered N‐ and C‐terminal domains.
The 15N‐1H HSQC spectrum of CAHS‐8 (Figure 1 A) is typical of an intrinsically disordered protein, with low dispersion in the 1HN dimension.
Protein: DP01384 (UniProt P0CU50)
Region: residues 1	to 227
Annotation: disorder (Structural state)
Evidence: heteronuclear single quantum coherence spectroscopy evidence used in manual assertion
Supporting statements:
For α-synuclein, a known disordered protein, and for CAHS proteins, the crosspeaks occur over a narrower window (Figure 2, top), from ~8.0 to ~8.6 ppm, which coincides with the range for amide protons in the central residue of unstructured tripeptides (Schwarzinger et al., 2000).
Protein: DP01384 (UniProt P0CU50)
Region: residues 1	to 227
Annotation: response to desiccation (Biological process)
Evidence: mutant physiological response evidence used in manual assertion
Supporting statements:
Several CAHS proteins were sufficient to increase the desiccation tolerance of yeast nearly 100-fold (Figure 6A). Similar results were obtained in bacteria, with exogenous expression of some CAHS proteins resulting in increases of more than 2 orders of magnitude in desiccation tolerance (Figure 6B). Importantly, α-synuclein, a protein that exists as a disordered monomer in cells (Fauvet et al., 2012; Theillet et al., 2016) and has no known connection to stress tolerance (Drescher et al., 2012; Theillet et al., 2014), did not increase survival under drying conditions (Figure 6B), demonstrating that something beyond intrinsic disorder of TDPs is essential for their protective capabilities.
Tardigrade-Specific IDPs Increase Desiccation Tolerance in Heterologous Systems and In Vitro
Protein: DP01385 (UniProt P0CU48)
Region: residues 1	to 227
Annotation: disorder (Structural state)
Evidence: nuclear magnetic resonance spectroscopy evidence used in manual assertion
Supporting statements:
IDPs lack persistent secondary structure (Theillet et al., 2014; Yamaguchi et al., 2012), which we confirmed for CAHS proteins using nuclear magnetic resonance spectroscopy (NMR).
For α-synuclein, a known disordered protein, and for CAHS proteins, the crosspeaks occur over a narrower window (Figure 2, top), from ~8.0 to ~8.6 ppm, which coincides with the range for amide protons in the central residue of unstructured tripeptides (Schwarzinger et al., 2000).
Protein: DP01385 (UniProt P0CU48)
Region: residues 1	to 227
Annotation: disorder (Structural state)
Evidence: nuclear magnetic resonance spectroscopy-based hydrogen-deuterium exchange evidence used in manual assertion
Supporting statements:
For the disordered proteins tested (α-synuclein and CAHS proteins), nearly all the amide protons were exchanged for deuterons within 20 min, as shown by the decrease in intensity of the one-dimensional proton spectrum (Figure 2).
Protein: DP01385 (UniProt P0CU48)
Region: residues 1	to 227
Annotation: response to desiccation (Biological process)
Evidence: small interfering RNA knockdown evidence used in manual assertion
Supporting statements:
Tardigrades Use Intrinsically Disordered Proteins to Survive Desiccation.
Tardigrade-Specific IDPs Are Required for Desiccation Tolerance
However, targeting two of four highly induced (13- to 22-fold) CAHS genes significantly (p < 0.01) reduced survival after desiccation compared with a control treatment, GFP RNAi (Figure 4B).
Protein: DP01386 (UniProt P0CU49)
Region: residues 1	to 238
Annotation: disorder (Structural state)
Evidence: nuclear magnetic resonance spectroscopy evidence used in manual assertion
Supporting statements:
For α-synuclein, a known disordered protein, and for CAHS proteins, the crosspeaks occur over a narrower window (Figure 2, top), from ~8.0 to ~8.6 ppm, which coincides with the range for amide protons in the central residue of unstructured tripeptides (Schwarzinger et al., 2000).
IDPs lack persistent secondary structure (Theillet et al., 2014; Yamaguchi et al., 2012), which we confirmed for CAHS proteins using nuclear magnetic resonance spectroscopy (NMR).
Protein: DP01386 (UniProt P0CU49)
Region: residues 1	to 238
Annotation: disorder (Structural state)
Evidence: nuclear magnetic resonance spectroscopy-based hydrogen-deuterium exchange evidence used in manual assertion
Supporting statements:
For the disordered proteins tested (α-synuclein and CAHS proteins), nearly all the amide protons were exchanged for deuterons within 20 min, as shown by the decrease in intensity of the one-dimensional proton spectrum (Figure 2).
Protein: DP01386 (UniProt P0CU49)
Region: residues 1	to 238
Annotation: response to desiccation (Biological process)
Evidence: mutant physiological response evidence used in manual assertion
Supporting statements:
Several CAHS proteins were sufficient to increase the desiccation tolerance of yeast nearly 100-fold (Figure 6A). 
Tardigrade-Specific IDPs Increase Desiccation Tolerance in Heterologous Systems and In Vitro
Protein: DP01388 (UniProt P0CU52)
Region: residues 1	to 227
Annotation: disorder (Structural state)
Evidence: nuclear magnetic resonance spectroscopy-based hydrogen-deuterium exchange evidence used in manual assertion
Supporting statements:
For the disordered proteins tested (α-synuclein and CAHS proteins), nearly all the amide protons were exchanged for deuterons within 20 min, as shown by the decrease in intensity of the one-dimensional proton spectrum (Figure 2).
Protein: DP01388 (UniProt P0CU52)
Region: residues 1	to 227
Annotation: disorder (Structural state)
Evidence: nuclear magnetic resonance spectroscopy evidence used in manual assertion
Supporting statements:
IDPs lack persistent secondary structure (Theillet et al., 2014; Yamaguchi et al., 2012), which we confirmed for CAHS proteins using nuclear magnetic resonance spectroscopy (NMR).
For α-synuclein, a known disordered protein, and for CAHS proteins, the crosspeaks occur over a narrower window (Figure 2, top), from ~8.0 to ~8.6 ppm, which coincides with the range for amide protons in the central residue of unstructured tripeptides (Schwarzinger et al., 2000).
Protein: DP01388 (UniProt P0CU52)
Region: residues 1	to 227
Annotation: response to desiccation (Biological process)
Evidence: mutant physiological response evidence used in manual assertion
Supporting statements:
Several CAHS proteins were sufficient to increase the desiccation tolerance of yeast nearly 100-fold (Figure 6A). Similar results were obtained in bacteria, with exogenous expression of some CAHS proteins resulting in increases of more than 2 orders of magnitude in desiccation tolerance (Figure 6B). Importantly, α-synuclein, a protein that exists as a disordered monomer in cells (Fauvet et al., 2012; Theillet et al., 2016) and has no known connection to stress tolerance (Drescher et al., 2012; Theillet et al., 2014), did not increase survival under drying conditions (Figure 6B), demonstrating that something beyond intrinsic disorder of TDPs is essential for their protective capabilities.
Tardigrade-Specific IDPs Increase Desiccation Tolerance in Heterologous Systems and In Vitro
Protein: DP01389 (UniProt P84233)
Region: residues 1	to 35
Annotation: disorder (Structural state)
Evidence: nuclear magnetic resonance spectroscopy evidence used in manual assertion
Supporting statements:
A strong correlation exists between the most dynamic histone residues identified in the current study, amino acids 1–35 in H3 and 1–21 in H4, and the crystal structure of the nucleosome core particle which reveals the same residues as being largely unstructured.
Cross-references: PDB:1KX5
Protein: DP01389 (UniProt P84233)
Region: residues 2	to 37
Annotation: disorder (Structural state)
Evidence: cryogenic electron microscopy-based structural model with missing residue coordinates used in manual assertion
Supporting statements:
This region is not visible in the structure.
Cross-references: PDB:8SIY
Protein: DP01389 (UniProt P84233)
Region: residues 1	to 37
Annotation: flexible N-terminal tail (Disorder function)
Evidence: cryogenic electron microscopy-based structural model with missing residue coordinates used in manual assertion
Supporting statements:
This region is not visible in the structure indicating it is disordered.
Protein: DP01390 (UniProt P62799)
Region: residues 1	to 21
Annotation: disorder (Structural state)
Evidence: nuclear magnetic resonance spectroscopy evidence used in manual assertion
Supporting statements:
A strong correlation exists between the most dynamic histone residues identified in the current study, amino acids 1–35 in H3 and 1–21 in H4, and the crystal structure of the nucleosome core particle which reveals the same residues as being largely unstructured.
Cross-references: PDB:1KX5
Protein: DP01390 (UniProt P62799)
Region: residues 2	to 24
Annotation: disorder (Structural state)
Evidence: cryogenic electron microscopy-based structural model with missing residue coordinates used in manual assertion
Supporting statements:
This region is not visible in the structure.
Cross-references: PDB:8SIY
Protein: DP01391 (UniProt P03520)
Region: residues 1	to 60
Annotation: disorder (Structural state)
Evidence: nuclear magnetic resonance spectroscopy evidence used in manual assertion
Supporting statements:
The N(0)-binding region of the vesicular stomatitis virus phosphoprotein is globally disordered but contains transient α-helices.
Here, using nuclear magnetic resonance (NMR) spectroscopy and small-angle X-ray scattering (SAXS), we show that an isolated peptide corresponding to the 60 first N-terminal residues of VSV P (P(60)) and encompassing P(NTR) has overall molecular dimensions and a dynamic behavior characteristic of a disordered protein but transiently populates conformers containing α-helices.
Isolated VSV P60 is intrinsically disordered but exhibits transient secondary structures
The 2D 1H-15N-HSQC NMR spectrum of P60 exhibited narrow line widths and poor dispersion of the amide proton chemical shifts (Fig. 3), in agreement with structural disorder in solution. These results indicate that VSV P60 has overall molecular dimensions and NMR spectroscopic properties of a disordered protein, as shown previously for RV P68.
Protein: DP01391 (UniProt P03520)
Region: residues 1	to 60
Annotation: disorder (Structural state)
Evidence: small-angle X-ray scattering evidence used in manual assertion
Supporting statements:
The N(0)-binding region of the vesicular stomatitis virus phosphoprotein is globally disordered but contains transient α-helices.
Here, using nuclear magnetic resonance (NMR) spectroscopy and small-angle X-ray scattering (SAXS), we show that an isolated peptide corresponding to the 60 first N-terminal residues of VSV P (P(60)) and encompassing P(NTR) has overall molecular dimensions and a dynamic behavior characteristic of a disordered protein but transiently populates conformers containing α-helices.
Protein: DP01391 (UniProt P03520)
Region: residues 1	to 60
Annotation: disorder (Structural state)
Evidence: far-UV circular dichroism evidence used in manual assertion
Supporting statements:
The N(0)-binding region of the vesicular stomatitis virus phosphoprotein is globally disordered but contains transient α-helices.
Here, using nuclear magnetic resonance (NMR) spectroscopy and small-angle X-ray scattering (SAXS), we show that an isolated peptide corresponding to the 60 first N-terminal residues of VSV P (P(60)) and encompassing P(NTR) has overall molecular dimensions and a dynamic behavior characteristic of a disordered protein but transiently populates conformers containing α-helices.
Isolated VSV P60 is intrinsically disordered but exhibits transient secondary structures
The far-UV CD spectrum exhibited a prominent shoulder near 222 nm and a minimum near 205 nm, suggesting the presence of α-helical structure (Fig. 4). Assuming that the molar ellipticity value at 222 nm reports only on the presence of α-helix, the average helical content of P60 was estimated to be 7%.12,42 NMR spectroscopy is highly sensitive to local structure and therefore provides information about the location and population of fluctuating secondary structures within an otherwise flexible protein.
Protein: DP01391 (UniProt P03520)
Region: residues 1	to 60
Annotation: disorder (Structural state)
Evidence: light scattering evidence used in manual assertion
Supporting statements:
The N(0)-binding region of the vesicular stomatitis virus phosphoprotein is globally disordered but contains transient α-helices.
Here, using nuclear magnetic resonance (NMR) spectroscopy and small-angle X-ray scattering (SAXS), we show that an isolated peptide corresponding to the 60 first N-terminal residues of VSV P (P(60)) and encompassing P(NTR) has overall molecular dimensions and a dynamic behavior characteristic of a disordered protein but transiently populates conformers containing α-helices.
Isolated VSV P60 is intrinsically disordered but exhibits transient secondary structures
The N-terminal domain of VSV P (P60, aa 1–60) was produced in Escherichia coli as a recombinant protein containing a C-terminal His-tag (8 aa). The long-term stability of P60 was significantly improved in the presence of a mixture of 50 mMl-Arg and 50 mMl-Glu.39 Under these conditions, an average molecular mass of 7.2 ± 0.7 kDa was determined by SEC combined with detection by multiangle laser light scattering and refractometry (SEC/MALLS/RI), indicating that P60 was monomeric (MM calculated from the sequence = 8054 Da) and well behaved in solution up to concentrations of 2 mM (Fig. 1). Its Stokes' radius of 2.3 ± 0.1 nm indicated an extended conformation, closer to that expected for an unfolded protein of the same molecular mass (RS = 2.5 nm) than to that expected for a globular protein (RS = 1.5 nm).
Protein: DP01391 (UniProt P03520)
Region: residues 6	to 33
Annotation: disorder to order (Structural transition)
Evidence: x-ray crystallography evidence used in manual assertion
Supporting statements:
Replication of non-segmented negative-strand RNA viruses requires the continuous supply of the nucleoprotein (N) in the form of a complex with the phosphoprotein (P). Here, we present the structural characterization of a soluble, heterodimeric complex between a variant of vesicular stomatitis virus N lacking its 21 N-terminal residues (NΔ21) and a peptide of 60 amino acids (P60) encompassing the molecular recognition element (MoRE) of P that binds RNA-free N (N0). The complex crystallized in a decameric circular form, which was solved at 3.0 Å resolution, reveals how the MoRE folds upon binding to N and competes with RNA binding and N polymerization.
The authors describe a structure of the vesicular stomatitis virus N⁰-P complex (PDB:3PMK), using a recombinant phosphoprotein (UniProt ACC: B7UCZ3) whose N-terminal region is identical to the phosphoprotein here annotated.
Cross-references: PDB:3PMK