LiteFold/DisProt huggingface dataset:
Protein: DP03426 (UniProt P25024)
Region: residues 326	to 350
Annotation: disorder (Structural state)
Evidence: nuclear magnetic resonance spectroscopy evidence used in manual assertion
Supporting statements:
Overall, 97% of the backbone resonances for residues 20 to 325 were assigned. The missing resonances are from seven Pro (P22, P93, P170, P180, P185, P214, P257) and one Arg (R285). None of the 15N and 13C signals from the mobile N-and C-termini (residues 1-19 and 326-350) could be detected in the spectra, consistent with our observation of these signals in solid-state NMR experiments designed to detect only signals from mobile sites (Supplementary Fig. 6), as well as our previous analysis of local and global motions of CXCR124.
Supplementary Figure 6. One-dimensional refocused INEPT solid-state NMR MAS spectra of CXCR1 in proteoliposomes. Only
signals from mobile sites in the termini are detected.
Cross-references: PDB:2LNL
BMRB:18170
Protein: DP03426 (UniProt P25024)
Region: residues 1	to 29
Annotation: disorder to order (Structural transition)
Evidence: nuclear magnetic resonance spectroscopy evidence used in manual assertion
Supporting statements:
The CXCR1 N-domain is unstructured in the free state but structured with significant dynamics in the bound state.
The relaxation data for the bound state indicate that the CXCR1 N-domain is structured, with distinct differences in dynamic properties at a residue-specific level (Figure 11).
Protein: DP03426 (UniProt P25024)
Region: residues 1	to 29
Annotation: disorder (Structural state)
Evidence: nuclear magnetic resonance spectroscopy evidence used in manual assertion
Supporting statements:
In the unbound state, negative hetNOEs for all residues indicate that the CXCR1 N-domain is unstructured (Figure 10).
Chemical shifts are also characteristic of an unstructured peptide.
Protein: DP03426 (UniProt P25024)
Region: residues 1	to 29
Annotation: protein binding (Molecular function)
Evidence: nuclear magnetic resonance spectroscopy evidence used in manual assertion
Supporting statements:
The chemical shift perturbation profile of the CXCL8 (1–66) monomer upon CXCR1 N-domain 29mer binding is shown in Figure 2.
Protein: DP03426 (UniProt P25024)
Region: residues 1	to 29
Annotation: protein binding (Molecular function)
Evidence: isothermal titration calorimetry evidence used in manual assertion
Supporting statements:
Isothermal titration calorimetry (ITC) measures binding-induced heat changes from which free energy of binding (∆G), enthalpy (∆H), entropy (∆S), and stoichiometry (n) can be obtained in a straightforward manner [60]. The binding isotherm of the CXCR1 N-domain binding to the CXCL8 monomer is shown in Figure 12. The data fit best to a single-binding site model, yielding a stoichiometry of 0.93 ± 0.03, KD = 8.4 ± 0.5 μM, ΔH = −2.6 ± 0.2 kcal/mol, and T∆S = −4.3 ± 0.2 kcal/mol, indicating both enthalpic and entropic factors promote binding.
Protein: DP03427 (UniProt P31327)
Region: residues 779	to 792
Annotation: disorder (Structural state)
Evidence: X-ray crystallography-based structural model with missing residue coordinates used in manual assertion
Supporting statements:
In contrast, in the case of the L1 domain there are ~90 residues that are disordered (and thus that are not seen) in the apo form and that become ordered when the enzyme has the ligands bound to it (Fig. 1c, top panels).
Cross-references: PDB:5DOT
Protein: DP03427 (UniProt P31327)
Region: residues 562	to 623
Annotation: disorder to order (Structural transition)
Evidence: X-ray crystallography-based structural model with missing residue coordinates used in manual assertion
Supporting statements:
Region 562-623 is disordered in the crystal structure of the apo form (PDB:5dot) and becomes ordered upon ligand binding (PDB:5dou).
Cross-references: PDB:5DOU
PDB:5DOT
Protein: DP03427 (UniProt P31327)
Region: residues 779	to 784
Annotation: potassium ion binding (Molecular function)
Evidence: x-ray crystallography evidence used in manual assertion
Supporting statements:
Residues D779,F781,H782,T784 coordinate the binding of the potassium ion.
Protein: DP03427 (UniProt P31327)
Region: residues 788	to 792
Annotation: small molecule binding (Molecular function)
Evidence: x-ray crystallography evidence used in manual assertion
Supporting statements:
Residue S790 coordinates the binding of ADP.
Protein: DP03427 (UniProt P31327)
Region: residues 585	to 623
Annotation: small molecule binding (Molecular function)
Evidence: x-ray crystallography evidence used in manual assertion
Supporting statements:
Residues M585,R587,L592,G593,G594,G623 coordinate the binding of ADP.
Protein: DP03427 (UniProt P31327)
Region: residues 779	to 784
Annotation: metal ion binding (Molecular function)
Evidence: x-ray crystallography evidence used in manual assertion
Supporting statements:
Residues D779,F781,H782,T784 coordinate the binding of the potassium ion.
Protein: DP03427 (UniProt P31327)
Region: residues 779	to 792
Annotation: disorder to order (Structural transition)
Evidence: x-ray crystallography evidence used in manual assertion
Supporting statements:
In contrast, in the case of the L1 domain there are ~90 residues that are disordered (and thus that are not seen) in the apo form and that become ordered when the enzyme has the ligands bound to it (Fig. 1c, top panels).
Protein: DP03427 (UniProt P31327)
Region: residues 562	to 623
Annotation: disorder (Structural state)
Evidence: x-ray crystallography evidence used in manual assertion
Supporting statements:
Region 562-623 is disordered in the crystal structure of the apo form (PDB:5dot) and becomes ordered upon ligand binding (PDB:5dou).
Cross-references: PDB:5DOT
Protein: DP03428 (UniProt P40763)
Region: residues 690	to 722
Annotation: disorder (Structural state)
Evidence: X-ray crystallography-based structural model with missing residue coordinates used in manual assertion
Supporting statements:
Even if it is not mentioned in the paper, the 690-722 region was missing from the electron density.
Cross-references: PDB:6TLC
Protein: DP03428 (UniProt P40763)
Region: residues 689	to 702
Annotation: disorder (Structural state)
Evidence: X-ray crystallography-based structural model with missing residue coordinates used in manual assertion
Supporting statements:
Within each monomer, electron density map for most of our protein model was well defined, yet as with the crystal structure of pY705 STAT3 (PDB ID: 1BG1)[3], several residues, including loops within the SH2 domain, were poorly defined and consequently were not included in the final model; i.e., the loop connecting α-helices 1 and 2 (185–193), residues 419–427 between β-sheets e and f, a loop at the end of α-helix 7 (536–538), and several residues within the SH2 domain (626–632, 658–665, 689–702; all numbers refer to monomer A).
Cross-references: PDB:6QHD
Protein: DP03429 (UniProt P72975)
Region: residues 1	to 149
Annotation: disorder (Structural state)
Evidence: far-UV circular dichroism evidence used in manual assertion
Supporting statements:
We used far-UV CD in the analysis of the structure and conformational stability of IF17 as a spectroscopic probe that is sensitive to secondary structure.(26, 27) The CD spectrum of IF17, at 25 °C and physiological pH, showed a minimum negative ellipticity at ∼200 nm and a negative shoulder around 222 nm (Figure 1). These results suggest an unfolded protein with a small fraction of α-helix, turn-like, or PPII structures,(28) although the presence of aromatic signals, which also absorb at 222 nm, cannot be ruled out.(27)
The ellipticity of IF17 showed a linear behavior as the temperature was raised (Figure 1C), in agreement with the fluorescence thermal denaturations (see above). This behavior is commonly observed among IDPs, and it is explained as due to a redistribution of the random coil involving a loss of PPII and/or helical conformations.(35)
Protein: DP03429 (UniProt P72975)
Region: residues 1	to 149
Annotation: disorder (Structural state)
Evidence: fluorescence evidence used in manual assertion
Supporting statements:
The thermal denaturations of IF17 showed a linear decrease in the fluorescence emission as the temperature was increased (data not shown).
The ellipticity of IF17 showed a linear behavior as the temperature was raised (Figure 1C), in agreement with the fluorescence thermal denaturations (see above). This behavior is commonly observed among IDPs, and it is explained as due to a redistribution of the random coil involving a loss of PPII and/or helical conformations.(35)
Protein: DP03429 (UniProt P72975)
Region: residues 1	to 149
Annotation: disorder (Structural state)
Evidence: nuclear magnetic resonance spectroscopy evidence used in manual assertion
Supporting statements:
NMR can give information about the general fold of a polypeptide chain in solution at the residue level.(36) The 1D NMR spectrum of IF17 at 25 °C showed a poor chemical shift dispersion: the amide, the aromatic, and the methyl protons (Figure 1D) were clustered in those regions expected for random-coil proteins:(36) namely, between 8.0 and 8.7 ppm (for the amide signals), between 6.8 and 7.3 ppm (for the aromatic protons), and between 0.8 and 1.0 ppm (for the methyl groups).
We also carried out hydrogen-exchange experiments. After 10 min at 20 °C at pH 5.9, all the amide protons of IF17 in the 1D NMR spectrum were exchanged, suggesting the absence of hydrogen bonds.
Protein: DP03429 (UniProt P72975)
Region: residues 1	to 149
Annotation: pre-molten globule (Structural state)
Evidence: nuclear magnetic resonance spectroscopy evidence used in manual assertion
Supporting statements:
Therefore, we decided to determine the R, and the protein oligomerization state of the molecule, from the measurements of the translational diffusion coefficient (D), by DOSY-NMR experiments. The measured D was (7.5 ± 0.1) × 10–7 cm2 s–1, which yields an R = 26 ± 2 Å (with a dioxane D value of (9.3 ± 0.1) × 10–7 cm2 s–1).
The use of the equation for a premolten globule species(37) yields an R value of 29 ± 5 Å, which is similar, within the experimental error, to the measured one. (The R value for a molten globule according to the same equations is 22 ± 8 Å, which is also similar to the experimental value.) These findings suggest that IF17 is a monomer with a molten or premolten globule conformation.
Taken together, these results indicate that the IF17 is more compact than a fully disordered polypeptide chain but is not a fully spherical well-folded globular protein.
Protein: DP03429 (UniProt P72975)
Region: residues 1	to 149
Annotation: molecular function inhibitor activity (Molecular function)
Evidence: far-UV circular dichroism evidence used in manual assertion
Supporting statements:
The far-UV CD spectrum of GS was typical of an α-helical protein, with intense minima at 222 and 208 nm.(11) The addition spectrum obtained by the sum of the spectra of isolated GS and IF17 was different from that of the complex (Figure 3A), thus indicating that there was binding; the same was observed in IF17N/IF7 (Figure 3B).
Protein: DP03429 (UniProt P72975)
Region: residues 1	to 149
Annotation: protein binding (Molecular function)
Evidence: far-UV circular dichroism evidence used in manual assertion
Supporting statements:
The far-UV CD spectrum of GS was typical of an α-helical protein, with intense minima at 222 and 208 nm.(11) The addition spectrum obtained by the sum of the spectra of isolated GS and IF17 was different from that of the complex (Figure 3A), thus indicating that there was binding; the same was observed in IF17N/IF7 (Figure 3B).
Protein: DP03429 (UniProt P72975)
Region: residues 1	to 149
Annotation: protein binding (Molecular function)
Evidence: temperature-induced protein unfolding evidence used in manual assertion
Supporting statements:
To further confirm binding, we carried out thermal denaturations of GS in the absence and in the presence of the IFs. Binding can be detected by a change in the thermal denaturation midpoint, Tm, of the complex, when compared to that of the isolated GS:(41-43) an increase of the Tm indicates binding of the corresponding IF to the folded state of GS; a decrease of the Tm indicates binding to the unfolded state of GS and/or complex destabilization due to conformational changes. In all the GS–IFs mixtures we observed an increase in the Tm of the complex, either followed by fluorescence or CD (Table 1 and Figure 3C).
Protein: DP03429 (UniProt P72975)
Region: residues 1	to 149
Annotation: molecular function inhibitor activity (Molecular function)
Evidence: temperature-induced protein unfolding evidence used in manual assertion
Supporting statements:
To further confirm binding, we carried out thermal denaturations of GS in the absence and in the presence of the IFs. Binding can be detected by a change in the thermal denaturation midpoint, Tm, of the complex, when compared to that of the isolated GS:(41-43) an increase of the Tm indicates binding of the corresponding IF to the folded state of GS; a decrease of the Tm indicates binding to the unfolded state of GS and/or complex destabilization due to conformational changes. In all the GS–IFs mixtures we observed an increase in the Tm of the complex, either followed by fluorescence or CD (Table 1 and Figure 3C). 
The Inactivating Factor of Glutamine Synthetase IF17 Is an Intrinsically Disordered Protein, Which Folds upon Binding to Its Target
Protein: DP03430 (UniProt P0AC88)
Region: residues 35	to 55
Annotation: disorder (Structural state)
Evidence: X-ray crystallography-based structural model with missing residue coordinates used in manual assertion
Supporting statements:
Arg35 is the first residue in a disordered region of the molecule that extends through residue 56.
There were three regions of the structure for which there was no corresponding electron density. These missing regions consisted of residues 35–55, 313–318, and the last 15 residues at the C terminus of the
enzyme.
Cross-references: PDB:1DB3
Protein: DP03430 (UniProt P0AC88)
Region: residues 359	to 372
Annotation: disorder (Structural state)
Evidence: X-ray crystallography-based structural model with missing residue coordinates used in manual assertion
Supporting statements:
There were three regions of the structure for which there was no corresponding electron density. These missing regions consisted of residues 35–55, 313–318, and the last 15 residues at the C terminus of the
enzyme.
Cross-references: PDB:1DB3
Protein: DP03432 (UniProt P0DTH5)
Region: residues 1	to 45
Annotation: disorder (Structural state)
Evidence: X-ray crystallography-based structural model with missing residue coordinates used in manual assertion
Supporting statements:
Due to a lack of defined density presumably caused by high mobility, some parts of the protein could not be modeled. These comprise residues 1-45, 72-75, 148-152, 266-278, and 375-376 of subunit A and residues 1-45, 148-152, 221-223, 266-273, and 375-376 of subunit B.
Cross-references: PDB:1OF1
Protein: DP03433 (UniProt Q13153)
Region: residues 492	to 545
Annotation: disorder (Structural state)
Evidence: cleavage assay evidence used in manual assertion
Supporting statements:
 In the case of chymotrypsin, however, two proteolysis-resistant, stable fragments are obtained ​(Fig.4). By mass spectrometric analysis and N-terminal sequencing, these fragments can be identified as the N-terminal residues 57 to 200 and the C-terminal residues 201 to 491 from αPAK, which we call the RD and CD, respectively ​(Fig.1).
Protein: DP03433 (UniProt Q13153)
Region: residues 1	to 56
Annotation: disorder (Structural state)
Evidence: cleavage assay evidence used in manual assertion
Supporting statements:
 In the case of chymotrypsin, however, two proteolysis-resistant, stable fragments are obtained ​(Fig.4). By mass spectrometric analysis and N-terminal sequencing, these fragments can be identified as the N-terminal residues 57 to 200 and the C-terminal residues 201 to 491 from αPAK, which we call the RD and CD, respectively ​(Fig.1).
Protein: DP03433 (UniProt Q13153)
Region: residues 186	to 199
Annotation: protein binding (Molecular function)
Evidence: nuclear magnetic resonance spectroscopy evidence used in manual assertion
Supporting statements:
Resonances corresponding to residues 195-198 had
larger line widths than the rest of the peptide. These residues
are likely to be undergoing conformational exchange on a
millisecond to microsecond time scale
We have determined
the structure of the PIX-SH3/PAK peptide complex and shown that it differs from typical Src-like SH3/
peptide complexes
Cross-references: PDB:1ZSG
Protein: DP03433 (UniProt Q13153)
Region: residues 150	to 248
Annotation: flexible linker (Disorder function)
Evidence: chromatography evidence used in manual assertion
Supporting statements:
The hydrodynamic radius of the PAK1(70–545) dimer is significantly larger than that of the four-chain complex, probably because residues 150–248 are in an extended, flexible loop with measurable frictional drag.
Protein: DP03433 (UniProt Q13153)
Region: residues 83	to 137
Annotation: disorder (Structural state)
Evidence: far-UV circular dichroism evidence used in manual assertion
Supporting statements:
We expressed and purified residues 83–137 of PAK1 (WT_IS), which in the crystal structure of autoinhibited PAK1 interact with the C lobe of PAK1 kinase domain and form a small folded domain with three helices and a β-strand (Fig. 1). We did not include residues 138–149 of PAK1, which bind in the active site of the kinase. The circular dichroism spectrum of the purified IS domain showed that the domain does not fold in isolation (Fig. 2).
Protein: DP03433 (UniProt Q13153)
Region: residues 83	to 137
Annotation: disorder (Structural state)
Evidence: cleavage assay evidence used in manual assertion
Supporting statements:
Not surprisingly, the domain was prone to aggregation and proteolysis during expression and purification.
Protein: DP03433 (UniProt Q13153)
Region: residues 47	to 51
Annotation: localization (Biological process)
Evidence: mutant phenotype evidence used in manual assertion
Supporting statements:
We subsequently mutated the four lysines (residue numbers 48–51) in the polybasic stretch of PAK1(1–107) to alanines to investigate the importance of the polybasic motif. Whereas GFP-PAK(1–107) targets robustly to cell–cell contacts, when the lysines are mutated to alanines, targeting is abolished (Fig. 6, E, H, and I), supporting the importance of the polybasic region for targeting.
Protein: DP03433 (UniProt Q13153)
Region: residues 150	to 248
Annotation: disorder (Structural state)
Evidence: gel-filtration evidence used in manual assertion
Supporting statements:
(A) Gel filtration profiles on Superdex200 (Pharmacia) for PAK1(70–545) and for PAK1(70–149) plus PAK1(249–545). Elution positions for three calibration standards are shown. Pak70-C elutes at a position corresponding to a relative molecular mass of 160 kDa, larger than the expected dimer mass of 110 kDa, probably due to an extended loop formed by residues 150–248.
Protein: DP03433 (UniProt Q13153)
Region: residues 182	to 203
Annotation: protein binding (Molecular function)
Evidence: glutathione S-transferase pull-down assay evidence used in manual assertion
Supporting statements:
Because sequences surrounding a proline-rich motif in PAK155–207 were conserved in various PAKs (Figure 1D) and SH3 domains were present in the p78-like proteins encoded by cDNA clones (see next section), we tested a 22 residue polypeptide (αPAK182–203) containing the proline-rich core sequence for its binding ability (Figure 1C, right panel). This polypeptide bound the triplet of proteins (arrows) equally well as the larger αPAK1–250.
Protein: DP03434 (UniProt Q8I295)
Region: residues 1	to 217
Annotation: disorder (Structural state)
Evidence: X-ray crystallography-based structural model with missing residue coordinates used in manual assertion
Supporting statements:
The N-terminal region (1-217) is missing even if not mentioned in the article.
Cross-references: PDB:4N7B
Protein: DP03435 (UniProt P21109)
Region: residues 11	to 44
Annotation: disorder (Structural state)
Evidence: far-UV circular dichroism evidence used in manual assertion
Supporting statements:
On the other hand, our CD data show that the CXCR1 N-domain is unstructured in the free form, and relatively more structured in the bound form (Fig. 5). The N-domain peptide in the free form shows a minimum at 199 nm, which is characteristic of random coil structure, and on binding, the minimum is shifted to ≈ 203 nm and also shows a new peak at ≈ 220 nm.
Protein: DP03435 (UniProt P21109)
Region: residues 11	to 44
Annotation: disorder to order (Structural transition)
Evidence: far-UV circular dichroism evidence used in manual assertion
Supporting statements:
On the other hand, our CD data show that the CXCR1 N-domain is unstructured in the free form, and relatively more structured in the bound form (Fig. 5). The N-domain peptide in the free form shows a minimum at 199 nm, which is characteristic of random coil structure, and on binding, the minimum is shifted to ≈ 203 nm and also shows a new peak at ≈ 220 nm.
Protein: DP03435 (UniProt P21109)
Region: residues 11	to 44
Annotation: protein binding (Molecular function)
Evidence: far-UV circular dichroism evidence used in manual assertion
Supporting statements:
On the other hand, our CD data show that the CXCR1 N-domain is unstructured in the free form, and relatively more structured in the bound form (Fig. 5). The N-domain peptide in the free form shows a minimum at 199 nm, which is characteristic of random coil structure, and on binding, the minimum is shifted to ≈ 203 nm and also shows a new peak at ≈ 220 nm.
Protein: DP03438 (UniProt P32131)
Region: residues 445	to 457
Annotation: disorder (Structural state)
Evidence: X-ray crystallography-based structural model with missing residue coordinates used in manual assertion
Supporting statements:
 Overall, 439 of 457 residues have been located in the electron density
map. Disordered regions of the polypeptide not included in the final model include the residues 1-3, 19-21 and 446-457.
Cross-references: PDB:1OLT
Protein: DP03439 (UniProt P28327)
Region: residues 25	to 181
Annotation: disorder (Structural state)
Evidence: cryogenic electron microscopy-based structural model with missing residue coordinates used in manual assertion
Supporting statements:
 In our current model, the αN helix of GRK1 is intrinsically disordered until it binds to activated GPCRs in a form of “molecular fly-casting”44 (Fig. 5).
a) Primary structure of C-terminally truncated bovine GRK1 (residues 1–535) used in this study and its crystal structure in complex with ATP (PDB entry 3C4W45), wherein the N-terminus is disordered and the AST loop is partially ordered.
Cross-references: PDB:7MT9
EMDB:23978
Protein: DP03439 (UniProt P28327)
Region: residues 475	to 493
Annotation: disorder (Structural state)
Evidence: X-ray crystallography-based structural model with missing residue coordinates used in manual assertion
Supporting statements:
 The AST is typically disordered in structures of nucleotide-free, open PKA. Consistent with this, the AST of GRK1 is observed only in the nucleotide-bound structures (Fig. 2b), except when displaced by a crystal contact (in one chain of crystal forms I, II, and VI).
Cross-references: PDB:3C4Y
Protein: DP03439 (UniProt P28327)
Region: residues 1	to 29
Annotation: disorder (Structural state)
Evidence: X-ray crystallography-based structural model with missing residue coordinates used in manual assertion
Supporting statements:
The PDB structure shows this region lacks electron density, indicating this region is disordered. 
Cross-references: PDB:3C4Y