LiteFold/DisProt huggingface dataset:
Protein: DP01858 (UniProt Q96270)
Region: residues 1	to 169
Annotation: response to cold (Biological process)
Evidence: fluorescence evidence used in manual assertion
Supporting statements:
Therefore, we analyzed the stability of liposomes modeling the lipid composition of inner chloroplast membranes (ICMM) after a freeze/thaw cycle and a dehydration/rehydration cycle in the ethylene glycolpresence of all six LEA_4 proteins at different LEA protein: lipid mass ratios (Figure 13).
Protein: DP01859 (UniProt Q5NJL5)
Region: residues 1	to 358
Annotation: disorder (Structural state)
Evidence: far-UV circular dichroism evidence used in manual assertion
Supporting statements:
The CD spectrum of the protein in aqueous solution appeared typical of a random coil structure, with a 195-nm minimum of ellipticity. LEAM is thus a monomer that is natively unfolded in solution
Protein: DP01859 (UniProt Q5NJL5)
Region: residues 1	to 358
Annotation: disorder (Structural state)
Evidence: Fourier-transform infrared spectroscopy evidence used in manual assertion
Supporting statements:
In solution, the LEAM spectra revealed a maximum at 1649 cm−1, with a main peak at 1647.5 cm−1 surrounded by two other peaks at 1663 and 1630 cm−1. These values were assigned to random coil structures according to published data and in light of the CD observations
Protein: DP01860 (UniProt P17639)
Region: residues 1	to 92
Annotation: disorder (Structural state)
Evidence: nuclear magnetic resonance spectroscopy evidence used in manual assertion
Supporting statements:
The embryo-specific EMB-1 protein of Daucus carota is flexible and unstructured in solution
The NMR results reveal poor chemical shift dispersion, rapid chemical exchange of the amide backbone protons, unexpectedly narrow linewidths and the general absence of nuclear Overhauser effects. Together, these results indicate the EMB-1 protein has no defined secondary or tertiary structure in solution and the polypeptide backbone of the EMB-1 protein is flexible on a sub-nanosecond time scale.
In the spectrum of EMB-1 (Fig. 4a), the alpha proton resonances, aromatic proton resonances of the tyr and phe residues, and the methyl proton resonances of the val, leu and ile residues are found at chemical shift positions characteristic of a random coil structure (i.e., about 7 ppm, 4 ppm, and 1 - 1.5 ppm, respectively) [16] and exhibit low chemical shift dispersion. These data indicate the absence of secondary or environmental-dependent chemical shifts and hence the absence of ordered structure of EMB-1 in aqueous solution. 
In EMB-1, amide proton exchange is rapid, indicating the absence of a stably-folded structure (Fig. 4a).
Protein: DP01861 (UniProt P01042)
Region: residues 438	to 531
Annotation: disorder (Structural state)
Evidence: far-UV circular dichroism evidence used in manual assertion
Supporting statements:
What was observed were CD spectra consistent with a random coil structure and minimal α-helix or β sheet, which is demonstrated by the lack of negative peaks at 222 nm for α-helices and 215 nm for β-sheets
Protein: DP01861 (UniProt P01042)
Region: residues 438	to 531
Annotation: disorder (Structural state)
Evidence: nuclear magnetic resonance spectroscopy evidence used in manual assertion
Supporting statements:
The results suggest that under all measured conditions, HK5 has little secondary structure (Fig. 2), as exhibited by the lack of distinct peaks and the small 1H and 15N chemical shift ranges. Titration of Zn2+, Co2+, or Fe2+ up to 400 μM, did not induce any additional secondary structure. Taken together, these data suggest HK5 is likely an intrinsically unstructured protein.
Protein: DP01861 (UniProt P01042)
Region: residues 438	to 531
Annotation: protein binding (Molecular function)
Evidence: experimental evidence used in manual assertion
Supporting statements:
Here we demonstrate that HK5 is an intrinsically unstructured protein (IUP) and binds to ferritin in a metal-mediated interaction that occurs on the surface of ferritin and works independently of oxidized iron in its ferrihydrite core.
To test whether HK5 had a preference for interacting with one of the subunits in vitro, binding affinity for HK5 and ferritin H or ferritin L were measured individually. In the absence of metal ions, HK5 has similar binding affinities to ferritin L and ferritin H, with Kd values of 247 µM and 129 µM, respectively.
Protein: DP01863 (UniProt O75533)
Region: residues 1	to 462
Annotation: disorder (Structural state)
Evidence: X-ray crystallography-based structural model with missing residue coordinates used in manual assertion
Supporting statements:
On the basis of bioinformatics predictions and limited proteolysis, we removed intrinsically disordered regions from SF3b (Figure S1A, available online). The resulting SF3b core complex formed crystals and enabled de novo structure determination by combining single isomorphous replacement with anomalous scattering (SIRAS) and molecular replacement-single-wavelength anomalous dispersion (MR-SAD) (Figures S1B–S1E).
 One molecule is present in the asymmetric unit and comprises SF3b155 residues 463–1,304 (the HEAT domain), SF3b130 residues 1–1,217, SF3b14b residues 7–95, and SF3b10 residues 15–80 (Figures 1C–1F).
Cross-references: PDB:5IFE
Protein: DP01863 (UniProt O75533)
Region: residues 190	to 344
Annotation: disorder (Structural state)
Evidence: far-UV circular dichroism evidence used in manual assertion
Supporting statements:
Circular dichroism (CD) was used to investigate the secondary structural organization of the SF3b155r domain (Figure 4(b)). The pronounced negative band just below 200 nm of the SF3b155r CD spectrum is characteristic of a protein that is in a largely unstructured conformation33.
Protein: DP01863 (UniProt O75533)
Region: residues 190	to 344
Annotation: splicing factor binding (Molecular function)
Evidence: isothermal titration calorimetry evidence used in manual assertion
Supporting statements:
Assuming identical and independent (non-cooperative) binding sites, the best fit of the wild-type SF3b155r binding isotherm was obtained with a stoichiometry of three binding sites for U2AF65 within SF3b155r (Figure 5(a)).
Protein: DP01864 (UniProt Q9XTN4)
Region: residues 43	to 101
Annotation: disorder (Structural state)
Evidence: nuclear magnetic resonance spectroscopy evidence used in manual assertion
Supporting statements:
The finding that the N-terminal half of BrkNter remains unfolded upon DNA binding prompted us to design a smaller construct, BrkDBD (residues G43 to N101), restricted to the DNA-binding domain proper. Again, in the absence of DNA, BrkDBD is unfolded at 25 °C as judged from the weak spectral dispersion (see Figure 7(a), red resonances) and low {1H}-15N NOEs (not shown). 
Cross-references: BMRB:7134
Protein: DP01864 (UniProt Q9XTN4)
Region: residues 46	to 95
Annotation: nucleic acid binding (Molecular function)
Evidence: nuclear magnetic resonance spectroscopy evidence used in manual assertion
Supporting statements:
Thus, DNA binding induces partial folding of BrkNter. During the sequential assignment process by standard triple-resonance NMR techniques, it became clear that the folded amino acid residues belong to the C-terminal part of BrkNter (residues R46 to R95), which therefore constitutes the proper DNA-binding domain.
Spectra of BrkDBD in complex with the respective double-stranded 12-mer DNA, omb12T5, no longer showed this heterogeneity and had nearly identical chemical shifts to the BrkDBD–omb12 complex (data not shown).
The binding was confirmed to both Double-stranded DNA omb12 (5′d-TGAGGCGCCAAC) and omb12t5 (5′d-TGAGGCGTCAAC).
Cross-references: BMRB:7097
PDB:2GLO
Protein: DP01864 (UniProt Q9XTN4)
Region: residues 1	to 101
Annotation: disorder (Structural state)
Evidence: heteronuclear single quantum coherence spectroscopy evidence used in manual assertion
Supporting statements:
The 1H-15N-heteronuclear single quantum coherence (HSQC) spectrum of BrkNter in the absence of DNA (Figure 2(a)) at 25 °C reveals very limited dispersion, with chemical shifts for many of the 1H/15N resonances around 8 ppm/120 ppm. This indicates that the respective amino acid residues are in random coil conformation and therefore that apo-BrkNter is not folded at 25 °C.
Protein: DP01864 (UniProt Q9XTN4)
Region: residues 46	to 101
Annotation: disorder to order (Structural transition)
Evidence: heteronuclear single quantum coherence spectroscopy evidence used in manual assertion
Supporting statements:
In contrast, addition of an equimolar amount of omb12 DNA (which corresponds in sequence to an in vivo binding site of Brk6) induces a drastic change in the 1H-15N-HSQC spectrum (Figure 2(b), blue resonances): approximately half of the resonances shift strongly to widely dispersed spectral positions, indicative of a folded structure.
Assignment was completed only for residues K41 to N101, since the N-terminal part (before R46) remained unfolded and highly flexible, as indicated by unchanged random coil chemical shifts, strong overlap, and {1H}-15N NOE values below 0.3 (Figure 2(d), blue circles).
Spectra of BrkDBD in complex with the respective double-stranded 12-mer DNA, omb12T5, no longer showed this heterogeneity and had nearly identical chemical shifts to the BrkDBD–omb12 complex (data not shown).
Cross-references: BMRB:7097
PDB:2GLO
Protein: DP01864 (UniProt Q9XTN4)
Region: residues 43	to 101
Annotation: DNA binding (Molecular function)
Evidence: electrophoretic mobility shift assay evidence used in manual assertion
Supporting statements:
Gel mobility assays indicated that the affinities for all three complexes BrkNter–omb12, BrkDBD–omb12 and BrkDBD–omb12T5 are very similar (data not shown). Therefore, the smallest and most homogeneous complex, BrkDBD–omb12T5, appeared best suited for NMR analysis, and the subsequent structure determination was carried out on this complex.
The binding was confirmed to both Double-stranded DNA omb12 (5′d-TGAGGCGCCAAC) and omb12t5 (5′d-TGAGGCGTCAAC).
Protein: DP01867 (UniProt P47047)
Region: residues 1	to 85
Annotation: disorder (Structural state)
Evidence: X-ray crystallography-based structural model with missing residue coordinates used in manual assertion
Supporting statements:
Gaps in the current model include 85 residues of the native sequence at the N‐terminus and 11 loops of varying length throughout the rest of the sequence (Figure 1).
Protein: DP01867 (UniProt P47047)
Region: residues 361	to 389
Annotation: disorder (Structural state)
Evidence: X-ray crystallography-based structural model with missing residue coordinates used in manual assertion
Supporting statements:
Several large loops, which are disordered in the current structure, potentially interact with the incoming RNA. These loops include: a 15-residue loop (699–713) in the fist, a 29-residue region (361–389) in domain 2, and an 18-residue loop (943–961) in domain 4.
Cross-references: PDB:3L9O
Protein: DP01867 (UniProt P47047)
Region: residues 699	to 713
Annotation: disorder (Structural state)
Evidence: X-ray crystallography-based structural model with missing residue coordinates used in manual assertion
Supporting statements:
Several large loops, which are disordered in the current structure, potentially interact with the incoming RNA. These loops include: a 15-residue loop (699–713) in the fist, a 29-residue region (361–389) in domain 2, and an 18-residue loop (943–961) in domain 4.
Cross-references: PDB:3L9O
Protein: DP01867 (UniProt P47047)
Region: residues 943	to 961
Annotation: disorder (Structural state)
Evidence: X-ray crystallography-based structural model with missing residue coordinates used in manual assertion
Supporting statements:
Several large loops, which are disordered in the current structure, potentially interact with the incoming RNA. These loops include: a 15-residue loop (699–713) in the fist, a 29-residue region (361–389) in domain 2, and an 18-residue loop (943–961) in domain 4.
Cross-references: PDB:3L9O
Protein: DP01867 (UniProt P47047)
Region: residues 1	to 78
Annotation: disorder (Structural state)
Evidence: X-ray crystallography-based structural model with missing residue coordinates used in manual assertion
Supporting statements:
A dashed line in the secondary structure plot indicates regions
that are not observed in the electron density.
Cross-references: PDB:4QU4
Protein: DP01867 (UniProt P47047)
Region: residues 363	to 391
Annotation: disorder (Structural state)
Evidence: X-ray crystallography-based structural model with missing residue coordinates used in manual assertion
Supporting statements:
The crystal asymmetric unit contains two independent molecules. Molecule A includes most of the Mtr4 polypeptide chain, with the exception of residues 363–391. Molecule B has well-defined electron density for the DExH core, which is essentially identical to that of molecule A.
Cross-references: PDB:2XGJ
Protein: DP01867 (UniProt P47047)
Region: residues 943	to 958
Annotation: disorder (Structural state)
Evidence: X-ray crystallography-based structural model with missing residue coordinates used in manual assertion
Supporting statements:
A dashed line in the secondary structure plot indicates regions
that are not observed in the electron density.
Cross-references: PDB:4QU4
Protein: DP01867 (UniProt P47047)
Region: residues 361	to 389
Annotation: disorder (Structural state)
Evidence: X-ray crystallography-based structural model with missing residue coordinates used in manual assertion
Supporting statements:
A dashed line in the secondary structure plot indicates regions
that are not observed in the electron density.
Cross-references: PDB:4QU4
Protein: DP01867 (UniProt P47047)
Region: residues 4	to 17
Annotation: protein binding (Molecular function)
Evidence: x-ray crystallography evidence used in manual assertion
Supporting statements:
Mtr4N binds as a short α-helix (residues 6–11), with extended segments at both ends. Apolar residues of Mtr4 (Leu6, Phe7, Val9, Phe10, Val 15 and Leu17) contact hydrophobic residues of Rrp6 (Leu10, Ile14 and Val17) and Rrp47 (Tyr10, Tyr55, Phe62, Leu77, Leu80 and Met87) ​(Fig5B).
The region that contacts the protein complex formed by UniProt Q12149 and P38801 is larger that just the Helix region, as shown by the gain of electron density in the PDB structure, and so the binding region corresponds to the 4-17 residues.
Cross-references: PDB:4WFD
Protein: DP01867 (UniProt P47047)
Region: residues 1	to 20
Annotation: protein binding (Molecular function)
Evidence: gel-filtration evidence used in manual assertion
Supporting statements:
Rrp6N and Rrp47ΔC co-eluted with the N-terminal region of Mtr4 (Mtr480) (Fig1F, lane and peak 1), while no interaction was detected with the helicase domain (Mtr4Δ80) ​(Fig1E, peaks and lanes 4 and 5). In isolation, neither Rrp6N nor Rrp47ΔC interacted with Mtr4 (Fig1G, peaks and lanes 1, 2 and 3, 4, respectively), suggesting that both proteins are required for binding.
Rrp6N–Rrp47ΔC indeed formed a ternary complex with an Mtr41-20 peptide (Mtr4N) (Supplementary Fig S1B).
Protein: DP01867 (UniProt P47047)
Region: residues 6	to 11
Annotation: protein binding (Molecular function)
Evidence: loss-of-function mutant phenotype evidence used in manual assertion
Supporting statements:
Immobilized zz-Rrp6 protein retained the wild-type Mtr4-gfp protein, whereas binding of the mtr4-gfpF7A,F10A mutant was only slightly above background levels (Fig​(Fig8B,8B, right panel). These data support the conclusion that the structurally defined Rrp6N–Rrp47N–Mtr4N complex forms the principal interaction between Rrp6 and Mtr4 in yeast.
Protein: DP01867 (UniProt P47047)
Region: residues 1	to 80
Annotation: disorder (Structural state)
Evidence: cleavage assay evidence used in manual assertion
Supporting statements:
We identified by limited proteolysis the stable and conserved RNA-binding region of Saccharomyces cerevisiae Mtr4 encompassing residues 81–1073 (Mtr4-Δ80) (Figs. S1 and S2).
Protein: DP01869 (UniProt P51587)
Region: residues 48	to 284
Annotation: disorder (Structural state)
Evidence: nuclear magnetic resonance spectroscopy evidence used in manual assertion
Supporting statements:
Analysis of these chemical shifts confirmed that BRCA2 48–284 shows no stable fold: it is intrinsically disordered, with only short, transient α-helices.
The narrow range of backbone amide 1H chemical shifts (between 7.5 and 8.5 ppm) for all BRCA2 fragments reveals their disordered behavior.
The secondary structure analysis, based on 13Cα and 13Cβ chemical shifts and the neighbor corrected structural propensity method (Tamiola et al. 2010; Tamiola and Mulder 2012), confirms the absence of a stable fold for BRCA2 53–131, BRCA2 48–218(C4A) and BRCA2 190–284.
We concluded that the fragment of BRCA2 from amino acid 48 to amino acid 284 is disordered and that its shorter segments BRCA2 53–131, BRCA2 48–218(C4A) and BRCA2 190–284 have the same structural properties when isolated or within BRCA2 48–284(C4A).
Cross-references: BMRB:50077
BMRB:50078
BMRB:50079
Protein: DP01870 (UniProt P84040)
Region: residues 1	to 26
Annotation: disorder (Structural state)
Evidence: X-ray crystallography-based structural model with missing residue coordinates used in manual assertion
Supporting statements:
Missing electron density for the region.
Cross-references: PDB:6XWS
PDB:6XWT
Protein: DP01870 (UniProt P84040)
Region: residues 2	to 15
Annotation: disorder (Structural state)
Evidence: X-ray crystallography-based structural model with missing residue coordinates used in manual assertion
Supporting statements:
Unstructured residues are indicated in lower case.
Cross-references: PDB:2PYO
Protein: DP01870 (UniProt P84040)
Region: residues 2	to 15
Annotation: flexible N-terminal tail (Disorder function)
Evidence: X-ray crystallography-based structural model with missing residue coordinates used in manual assertion
Supporting statements:
Unstructured residues are indicated in lower case.
Cross-references: PDB:2PYO
Protein: DP01871 (UniProt P68246)
Region: residues 137	to 181
Annotation: disorder (Structural state)
Evidence: nuclear magnetic resonance spectroscopy evidence used in manual assertion
Supporting statements:
They have constructed a skeletal TnC-TnI chimera to study the structure and dynamics of the regulatory region of troponin, combining the skeletal N-terminal domain of TnC (sNTnC) and the C-terminal region of TnI (sTnI) in a single polypeptidic chain (chicken fast skeletal was used).
"These values are typical for a globular domain for sTnC and a disordered region for the C-terminal region of sTnI."
Protein: DP01871 (UniProt P68246)
Region: residues 145	to 183
Annotation: disorder (Structural state)
Evidence: X-ray crystallography-based structural model with missing residue coordinates used in manual assertion
Supporting statements:
There was no visible electron density for the 39 C-terminal amino acid residues (144–182) of TnI or the C-terminal residues of TnT2 (249–262).
Cross-references: PDB:1YTZ
Protein: DP01872 (UniProt O95630)
Region: residues 228	to 241
Annotation: disorder (Structural state)
Evidence: nuclear magnetic resonance spectroscopy evidence used in manual assertion
Supporting statements:
Only i,i + 1 sequential intra-NOEs could be detected from NOESY experiments, which support the previous prediction and reflect the fact that AMSH-P2 is unstructured in the free state.
As in the free state, it is important to mention that we only detected i,i + 1 sequential NOEs, supporting the fact that AMSH-P2 is also unstructured when bound to SH3.
Cross-references: PDB:5IXF
Protein: DP01872 (UniProt O95630)
Region: residues 228	to 241
Annotation: protein binding (Molecular function)
Evidence: nuclear magnetic resonance spectroscopy evidence used in manual assertion
Supporting statements:
As in the free state, it is important to mention that we only detected i,i + 1 sequential NOEs, supporting the fact that AMSH-P2 is also unstructured when bound to SH3.
Cross-references: PDB:5IXF
Protein: DP01872 (UniProt O95630)
Region: residues 219	to 245
Annotation: disorder (Structural state)
Evidence: X-ray crystallography-based structural model with missing residue coordinates used in manual assertion
Supporting statements:
 The N-terminal SH3-binding peptide segment was not visualized in the structure perhaps because of disorder in the crystal, suggesting that this peptide segment is flexible and is easily accessible for binding to the SH3 domain of STAM.
Protein: DP01873 (UniProt Q99075)
Region: residues 73	to 106
Annotation: disorder (Structural state)
Evidence: X-ray crystallography-based structural model with missing residue coordinates used in manual assertion
Supporting statements:
Residues of the heparin-binding module of HBEGF (residues 73–106). These are not visible in electron-density maps and are presumably disordered.
Cross-references: PDB:1XDT
Protein: DP01874 (UniProt O95149)
Region: residues 288	to 348
Annotation: disorder (Structural state)
Evidence: X-ray crystallography-based structural model with missing residue coordinates used in manual assertion
Supporting statements:
In the final model of SPN1, residues 31-33, 72-91, 162-165 and 288-348 of one complex in the asymmetric unit, and residues 30-32, 74-92, 162-165 and 291-348 of the other one were not defined in the electron density map and thus they were not built.
Cross-references: PDB:3GJX
Protein: DP01874 (UniProt O95149)
Region: residues 72	to 91
Annotation: disorder (Structural state)
Evidence: X-ray crystallography-based structural model with missing residue coordinates used in manual assertion
Supporting statements:
In the final model of SPN1, residues 31-33, 72-91, 162-165 and 288-348 of one complex in the asymmetric unit, and residues 30-32, 74-92, 162-165 and 291-348 of the other one were not defined in the electron density map and thus they were not built.
Cross-references: PDB:3GJX
Protein: DP01875 (UniProt Q2GI62)
Region: residues 142	to 221
Annotation: disorder (Structural state)
Evidence: nuclear magnetic resonance spectroscopy evidence used in manual assertion
Supporting statements:
We first collected 1H-15N NMR HSQC spectra of TRP120-1TR as a function of pH (5.5, 6.0, 6.5 and 7.0), and observed that the protein is essentially unstructured in solution at all pHs tested. The NMR spectrum shows around 80 (of the 102 residues) resonances between 6.7 and 8.6 ppm. Most of the chemical shifts correspond to that of a random and thus NMR data are consistent with a natively unfolded protein.
Protein: DP01875 (UniProt Q2GI62)
Region: residues 142	to 221
Annotation: nucleic acid binding (Molecular function)
Evidence: nuclear magnetic resonance spectroscopy evidence used in manual assertion
Supporting statements:
The pH of ehrlichial morulae where TRP120 is expressed is slightly acidic. Addition of DNA to TRP120-1TR at pH 5.5 resulted in several new peaks with significant differences in chemical shifts, suggesting an increase in β-strand content. Peaks corresponding to several side chain NH2 of Asn/Gln residues were resolved in the DNA-bound spectrum, indicating that they become structured upon DNA binding.
Protein: DP01875 (UniProt Q2GI62)
Region: residues 142	to 221
Annotation: disorder (Structural state)
Evidence: far-UV circular dichroism evidence used in manual assertion
Supporting statements:
The far-UV CD spectra of TRP120-1TR at pH 7.0 showed a profile with a minimum centered at 200 nm, indicating that TRP120 TR units are mostly intrinsically disordered. A shallow negative feature centered at 220 nm suggests a small percentage of β-turn/β-sheet secondary structure. CD spectra of TRP120-2TR measured as a function of pH (7.0, 6.0 and 4.5) showed similar profiles.
Protein: DP01875 (UniProt Q2GI62)
Region: residues 142	to 221
Annotation: disorder (Structural state)
Evidence: sodium dodecyl sulfate polyacrylamide gel electrophoresis evidence used in manual assertion
Supporting statements:
Although the predicted molecular weight of TRP120-1TR based on the primary sequences is 11.5 kDa, the construct migrates with apparent molecular weight of ~19 kDa. The analytical ultracentrifugation clearly shows that both TRP120-1TR and -2TR proteins are monomers with expected molecular weights. Thus, aberrant migration of the TRP120 TR unit on SDS-PAGE is intrinsic to the nature of the domain.