LiteFold/DisProt huggingface dataset:
Protein: DP03125 (UniProt O14965)
Region: residues 279	to 288
Annotation: disorder (Structural state)
Evidence: X-ray crystallography-based structural model with missing residue coordinates used in manual assertion
Supporting statements:
As observed in the structures of CSK kinase (c-SRC-specific tyrosine kinase) bound to staurosporine (27) and the SRC family kinase HCK (human Cyclin-dependent kinase) bound to AMP-PNP (25), a part of the Aurora-2 activation loop (defined as residues 273–292) is disordered. Only residues 273–278 and 289–292 were clearly visible and have been included in the final model. Residue Thr-288, which is phosphorylated during activation of Aurora-2, belongs to part of the disordered region and was not visible in electron density maps
Cross-references: PDB:1MUO
Protein: DP03125 (UniProt O14965)
Region: residues 107	to 127
Annotation: disorder (Structural state)
Evidence: X-ray crystallography-based structural model with missing residue coordinates used in manual assertion
Supporting statements:
In the refined crystal structure, a number of residues located at the N and C termini of the kinase domain (residues 107–127 and 389–403, respectively) exhibited poor electron density, and these residues could not be placed in electron density
Accordingly, an expression construct comprising residues 107–403 was used for crystallographic studies. The disordered nature of residues 107–126 in the final crystal structure suggests that this spanning polypeptide linker is particularly long and flexible in Aurora-2
Cross-references: PDB:1MUO
Protein: DP03125 (UniProt O14965)
Region: residues 389	to 403
Annotation: disorder (Structural state)
Evidence: X-ray crystallography-based structural model with missing residue coordinates used in manual assertion
Supporting statements:
In the refined crystal structure, a number of residues located at the N and C termini of the kinase domain (residues 107–127 and 389–403, respectively) exhibited poor electron density, and these residues could not be placed in electron density
Cross-references: PDB:1MUO
Protein: DP03125 (UniProt O14965)
Region: residues 273	to 292
Annotation: molecular function activator activity (Molecular function)
Evidence: x-ray crystallography evidence used in manual assertion
Supporting statements:
As observed in the structures of CSK kinase (c-SRC-specific tyrosine kinase) bound to staurosporine (27) and the SRC family kinase HCK (human Cyclin-dependent kinase) bound to AMP-PNP (25), a part of the Aurora-2 activation loop (defined as residues 273–292) is disordered. Only residues 273–278 and 289–292 were clearly visible and have been included in the final model. Residue Thr-288, which is phosphorylated during activation of Aurora-2, belongs to part of the disordered region and was not visible in electron density maps
Cross-references: PDB:1MUO
Protein: DP03125 (UniProt O14965)
Region: residues 107	to 127
Annotation: flexible linker (Disorder function)
Evidence: x-ray crystallography evidence used in manual assertion
Supporting statements:
The disordered nature of residues 107–126 in the final crystal structure suggests that this spanning polypeptide linker is particularly long and flexible in Aurora-2
Cross-references: PDB:1MUO
Protein: DP03125 (UniProt O14965)
Region: residues 279	to 290
Annotation: disorder (Structural state)
Evidence: X-ray crystallography-based structural model with missing residue coordinates used in manual assertion
Supporting statements:
The activation loop, residues 279–290 containing the T287D mutation, is disordered in both structures suggesting mobility, as is the case in many other kinase structures. 
Cross-references: PDB:2C6D
PDB:2C6E
Protein: DP03126 (UniProt Q9WTL8)
Region: residues 497	to 632
Annotation: disorder (Structural state)
Evidence: analytical ultracentrifugation evidence used in manual assertion
Supporting statements:
The hydrodynamic (Stokes) radii determined by AUC analyses (Table 1) suggest that the mCRY and mBMAL1 proteins have somewhat elongated shapes and might be at least partially unstructured.
Protein: DP03126 (UniProt Q9WTL8)
Region: residues 497	to 632
Annotation: disorder (Structural state)
Evidence: far-UV circular dichroism evidence used in manual assertion
Supporting statements:
The spectra suggest, that the mBMAL1 and mCRY
proteins are partially disordered (Table 2).
Protein: DP03126 (UniProt Q9WTL8)
Region: residues 584	to 632
Annotation: disorder (Structural state)
Evidence: far-UV circular dichroism evidence used in manual assertion
Supporting statements:
The spectra suggest, that the mBMAL1 and mCRY
proteins are partially disordered (Table 2).
Protein: DP03126 (UniProt Q9WTL8)
Region: residues 584	to 632
Annotation: protein binding (Molecular function)
Evidence: experimental evidence used in manual assertion
Supporting statements:
The shorter mBMAL1-(577–625) fragment bound to both mCRYCCtail fragments with a roughly 10 μm affinity (Fig. 2A).
Region 577–625 discussed in the article corresponds to 584-632 in UniProt entry.
Protein: DP03126 (UniProt Q9WTL8)
Region: residues 497	to 632
Annotation: protein binding (Molecular function)
Evidence: experimental evidence used in manual assertion
Supporting statements:
In contrast, the longer mBMAL1-(490–625) fragment bound to mCRY1 with an ∼40 μm affinity and to mCRY2 with an ∼10 μm affinity (Fig. 2B).
Region 490–625 discussed in the article corresponds to 497-632 in UniProt entry.
Protein: DP03126 (UniProt Q9WTL8)
Region: residues 584	to 632
Annotation: protein binding (Molecular function)
Evidence: isothermal titration calorimetry evidence used in manual assertion
Supporting statements:
In good agreement with the fluorescence polarization data, mCRY1 and mCRY2 bind to the mBMAL1-(577–625) fragment with a roughly 10 μm affinity (Fig. 3A and Table 3).
Region 577–625 discussed in the article corresponds to 584-632 in UniProt entry.
Protein: DP03126 (UniProt Q9WTL8)
Region: residues 497	to 632
Annotation: protein binding (Molecular function)
Evidence: isothermal titration calorimetry evidence used in manual assertion
Supporting statements:
Whereas mCRY2 shows a similar (∼10 μm) affinity to both mBMAL1 fragments, mCRY1 binds to the longer mBMAL1-(490–625) fragment with a roughly 20 μm affinity (Fig. 3B and Table 3).
Protein: DP03126 (UniProt Q9WTL8)
Region: residues 584	to 632
Annotation: disorder (Structural state)
Evidence: analytical ultracentrifugation evidence used in manual assertion
Supporting statements:
The hydrodynamic (Stokes) radii determined by AUC analyses (Table 1) suggest that the mCRY and mBMAL1 proteins have somewhat elongated shapes and might be at least partially unstructured.
Protein: DP03127 (UniProt Q9R194)
Region: residues 489	to 592
Annotation: disorder (Structural state)
Evidence: circular dichroism evidence used in manual assertion
Supporting statements:
The spectra suggest, that the mBMAL1 and mCRY
proteins are partially disordered (Table 2).
Protein: DP03127 (UniProt Q9R194)
Region: residues 489	to 592
Annotation: disorder (Structural state)
Evidence: analytical ultracentrifugation evidence used in manual assertion
Supporting statements:
he hydrodynamic (Stokes) radii determined by AUC analyses (Table 1) suggest that the mCRY and mBMAL1 proteins have somewhat elongated shapes and might be at least partially unstructured.
Protein: DP03127 (UniProt Q9R194)
Region: residues 489	to 592
Annotation: protein binding (Molecular function)
Evidence: experimental evidence used in manual assertion
Supporting statements:
In contrast, the longer mBMAL1-(490–625) fragment bound to mCRY1 with an ∼40 μm affinity and to mCRY2 with an ∼10 μm affinity (Fig. 2B).
Protein: DP03127 (UniProt Q9R194)
Region: residues 489	to 592
Annotation: protein binding (Molecular function)
Evidence: isothermal titration calorimetry evidence used in manual assertion
Supporting statements:
In good agreement with the fluorescence polarization data, mCRY1 and mCRY2 bind to the mBMAL1-(577–625) fragment with a roughly 10 μm affinity (Fig. 3A and Table 3). Whereas mCRY2 shows a similar (∼10 μm) affinity to both mBMAL1 fragments, mCRY1 binds to the longer mBMAL1-(490–625) fragment with a roughly 20 μm affinity (Fig. 3B and Table 3).
Protein: DP03129 (UniProt O08679)
Region: residues 38	to 48
Annotation: disorder (Structural state)
Evidence: X-ray crystallography-based structural model with missing residue coordinates used in manual assertion
Supporting statements:
The 11 initial residues (G38–P48) are invisible due to disorder.
Cross-references: PDB:1ZMU
Protein: DP03129 (UniProt O08679)
Region: residues 193	to 210
Annotation: disorder (Structural state)
Evidence: X-ray crystallography-based structural model with missing residue coordinates used in manual assertion
Supporting statements:
Whereas most of the activation loop is disordered in the wild-type and K82R structures (D193–C210), the T208A/S212A mutant reveals five more residues at the end of the activation loop (L206–C210).
Cross-references: PDB:1ZMU
Protein: DP03130 (UniProt Q7KZI7)
Region: residues 197	to 209
Annotation: disorder (Structural state)
Evidence: X-ray crystallography-based structural model with missing residue coordinates used in manual assertion
Supporting statements:
The overall protein structure is very similar to what has been previously reported (S. Panneerselvam, A. Marx, E.M. Mandelkow, E. Mandelkow
Structure, 14 (2006), p. 173)
The crystallographic structure of the catalytic domain of human MARK2 is very similar to the crystallographic structure of the catalytic domain of rat MARK2 and they both present a disordered activation loop in the inactive state
Cross-references: PDB:5EAK
Protein: DP03130 (UniProt Q7KZI7)
Region: residues 196	to 211
Annotation: disorder (Structural state)
Evidence: X-ray crystallography-based structural model with missing residue coordinates used in manual assertion
Supporting statements:
The crystallographic structure of the catalytic domain of human MARK2 is very similar to the crystallographic structure of the catalytic domain of rat MARK2 and they both present a disordered activation loop in their inactive state
Cross-references: PDB:5KZ8
PDB:5KZ7
Protein: DP03130 (UniProt Q7KZI7)
Region: residues 196	to 211
Annotation: disorder to order (Structural transition)
Evidence: x-ray crystallography evidence used in manual assertion
Supporting statements:
The second major difference is in the activation loop of the kinase, which adopts an ordered and activated structure in the presence of CagA
Cross-references: PDB:3IEC
Protein: DP03130 (UniProt Q7KZI7)
Region: residues 206	to 210
Annotation: phosphorylation display site (Disorder function)
Evidence: qualitative western immunoblotting evidence used in manual assertion
Supporting statements:
The LKB1 complex phosphorylates AMPK-related kinases at the activation loop
Protein: DP03131 (UniProt Q96AE4)
Region: residues 347	to 377
Annotation: disorder (Structural state)
Evidence: nuclear magnetic resonance spectroscopy evidence used in manual assertion
Supporting statements:
The 30-residue protein linker between the KH3 and KH4 domains is highly disordered (Fig. 3a), such that in free FBP3/4 the two domains reorient essentially independently of each other (unpublished data), as in the case of other modular proteins connected by long linkers
In the paper the authors included residues 278–447 of human FBP and renumbered them as 5–174
Cross-references: PDB:1J4W
Protein: DP03131 (UniProt Q96AE4)
Region: residues 347	to 377
Annotation: flexible linker (Disorder function)
Evidence: nuclear magnetic resonance spectroscopy evidence used in manual assertion
Supporting statements:
Interdomain motion observed in the FBP3/4–M29 ssDNA complex in which the linkers, both protein and ssDNA, possess intrinsic flexibility, is likely to be an essential component of FBP function. This property can readily accommodate changes in the direction of the DNA.
Cross-references: PDB:1J4W
Protein: DP03134 (UniProt Q9NPF0)
Region: residues 90	to 128
Annotation: disorder (Structural state)
Evidence: X-ray crystallography-based structural model with missing residue coordinates used in manual assertion
Supporting statements:
Whereas clear electron density was observed for LDLR-A1 residues 53–89 and LDLR-A2 residues 129-171, no density was observed for the EGF-like domain (residues 90–128).
The EGF-like domain of CD320 is not visible in our electron density maps despite chemically being present, suggesting positional disorder in the crystal. 
Cross-references: PDB:4ZRP
Protein: DP03134 (UniProt Q9NPF0)
Region: residues 86	to 128
Annotation: disorder (Structural state)
Evidence: X-ray crystallography-based structural model with missing residue coordinates used in manual assertion
Supporting statements:
From the statement „Moreover, electron density for the Ca2+ binding residue Glu86 as well as Glu87 and disulfide forming Cys88 (equivalent to Cys89 in wild type) was missing". Besides this small region, the electron density map is missing also for the 90-128 region (as it was observed in the wild type as well (PDB: 4ZRP)).
Cross-references: PDB:4ZRQ
Protein: DP03135 (UniProt P35680)
Region: residues 188	to 230
Annotation: disorder (Structural state)
Evidence: X-ray crystallography-based structural model with missing residue coordinates used in manual assertion
Supporting statements:
The linker between the POUS and POUH domains (amino acids 186−229) of HNF1β contains the nuclear localization signal (NLS; 229KKMRRNRFK237) and is even longer than that of HNF1α (by 26 residues) (Figure 1). The majority of the linker is disordered, as also seen in the HNF1α structure.
Cross-references: PDB:2H8R
Protein: DP03136 (UniProt F4IED2)
Region: residues 254	to 274
Annotation: disorder (Structural state)
Evidence: far-UV circular dichroism evidence used in manual assertion
Supporting statements:
Experimental analysis for secondary structure content by far-UV CD indicated low α-helical contents of 12, 18, 10, and 13% in the ANAC013(254–274), DREB2A(255–272), COL10(175–208), and bZIP23(15–36) peptides, respectively (Fig. 5, B–E).
Protein: DP03136 (UniProt F4IED2)
Region: residues 254	to 274
Annotation: disorder to order (Structural transition)
Evidence: far-UV circular dichroism evidence used in manual assertion
Supporting statements:
For ANAC013(254–274) in complex with RCD1-RST, the wavelength of the absolute minimum changed slightly compared with the theoretical spectra, and the α-helical content of 32% in the complex was minimally higher than in the theoretical complex (29%) (Fig. 6C).
Together, the results suggested that complex formation involving ANAC046(319–338) and ANAC013(254–274) resulted in structure induction, although to a lower degree than that of the DREB2A(255–272)·RCD1-RST(499–572) complex.
Protein: DP03136 (UniProt F4IED2)
Region: residues 254	to 274
Annotation: disorder (Structural state)
Evidence: nuclear magnetic resonance spectroscopy evidence used in manual assertion
Supporting statements:
Similar to DREB2A(255–272), free ANAC013(254–274) and ANAC046(319–338) had poorly dispersed HSQC spectra (Fig. 7, B and C, black spectra), and ΔδCα values close to zero (Fig. 7, E and F, top figures) again confirming a lack of preformed structure.
Protein: DP03136 (UniProt F4IED2)
Region: residues 254	to 274
Annotation: protein binding (Molecular function)
Evidence: nuclear magnetic resonance spectroscopy evidence used in manual assertion
Supporting statements:
Comparison of the HSQC spectra of free and bound ANAC013(254–274) and ANAC046(319–338) confirmed their interaction with RCD1-RST(499–572) (Fig. 7, B and C), but in contrast to those of DREB2A(255–272), the dispersion in the proton dimension appeared immediately unaffected.
Protein: DP03136 (UniProt F4IED2)
Region: residues 254	to 274
Annotation: protein binding (Molecular function)
Evidence: far-UV circular dichroism evidence used in manual assertion
Supporting statements:
For ANAC013(254–274) in complex with RCD1-RST, the wavelength of the absolute minimum changed slightly compared with the theoretical spectra, and the α-helical content of 32% in the complex was minimally higher than in the theoretical complex (29%) (Fig. 6C).
Together, the results suggested that complex formation involving ANAC046(319–338) and ANAC013(254–274) resulted in structure induction, although to a lower degree than that of the DREB2A(255–272)·RCD1-RST(499–572) complex.
Protein: DP03136 (UniProt F4IED2)
Region: residues 254	to 274
Annotation: protein binding (Molecular function)
Evidence: isothermal titration calorimetry evidence used in manual assertion
Supporting statements:
The affinity increased further by additional truncation resulting in a Kd of 32 nm for ANAC013(254–299), and removal of most of the negatively charged fragment (Fig. 1) to generate ANAC013(254–274) resulted in a further decrease of Kd to 9.0 nm (Fig. 2A). This is a relatively low Kd value for an interaction involving a putative SLiM and a globular domain (10), and the results indicate that the ANAC013 context of the SLiM has negative allosteric effects on binding.
Protein: DP03136 (UniProt F4IED2)
Region: residues 161	to 498
Annotation: disorder (Structural state)
Evidence: sodium dodecyl sulfate polyacrylamide gel electrophoresis evidence used in manual assertion
Supporting statements:
Although the relative migration pattern of the recombinant proteins by SDS/PAGE was in accordance with their relative molecular mass values [NAP (162–268): 15.0 kDa; ANAC019 (163–317): 17.2 kDa; ANAC046 (172–338): 18.2 kDa; histidine–NTL8 (156–335): 20.3 kDa; histidine–SOG (210–449): 29.0 kDa; ANAC013 (161–498): 37.5 kDa], they displayed slow migration during SDS/PAGE compared with standard globular proteins, which is in accordance with their ID nature and previous analysis of two NAC TRDs [39].
Protein: DP03136 (UniProt F4IED2)
Region: residues 161	to 498
Annotation: disorder (Structural state)
Evidence: chromatography evidence used in manual assertion
Supporting statements:
The hydrodynamic radii (Stokes radii) of ANAC046 (172–338), NAP (162–268) and ANAC019 (163–317) corresponded to pre-molten globule states, whereas ANAC013 (161–498) had a more compact structure consistent with its disorder profile (Figures 1d and 3).
Protein: DP03136 (UniProt F4IED2)
Region: residues 161	to 498
Annotation: pre-molten globule (Structural state)
Evidence: far-UV circular dichroism evidence used in manual assertion
Supporting statements:
Although the spectra of the six recombinant proteins showed different characteristics, they all had a minimum around 200 nm and only slightly negative ellipticities at 222 nm (Figure 4a). Both the [θ]222 and [θ]200 values suggested that histidine–NTL8 (156–335), ANAC013 (161–498), NAP (162–268) and ANAC019 (163–317) are similar, populating pre-molten globule like ensembles, whereas the values for histidine–SOG1 (210–449) and ANAC046 (172–338) suggest more random coil-like ensembles.
Protein: DP03136 (UniProt F4IED2)
Region: residues 205	to 299
Annotation: transcription regulator activator activity (Molecular function)
Evidence: beta galactosidase functional complementation evidence used in manual assertion
Supporting statements:
Both full-length ANAC013, DBD–ANAC013(1–498) and the TRD, DBD–ANAC013 (161–498), both lacking the transmembrane region, activated transcription in yeast. 
Stepwise C-terminal truncation of both constructs revealed that removal of the region between residue 205 and 299, containing several MoRFs and α-helices (Figure 1d), abolished the ability to activate transcription (Figure 7b).
Protein: DP03136 (UniProt F4IED2)
Region: residues 205	to 299
Annotation: protein binding (Molecular function)
Evidence: yeast 2-hybrid evidence used in manual assertion
Supporting statements:
As expected, the RST domain of RCD1 interacted with both full-length ANAC013 and ANAC046 and their TRDs (Figures 7b and 7c), whereas no interaction was detected with NAP (Figure 7a) [27].
C-terminal truncations were also analysed for their ability to interact with DBD–RCD1 (498-573). This suggested that residues 205–299 of ANAC013 and that the very C-terminal MoRF region of ANAC046 were responsible for the interactions (Figures 7b–7c).
Protein: DP03136 (UniProt F4IED2)
Region: residues 161	to 498
Annotation: protein binding (Molecular function)
Evidence: far-UV circular dichroism evidence used in manual assertion
Supporting statements:
Likewise, the CD spectrum of interacting ANAC013 (161–498) and histidine–RCD1–RST (487–589) showed a shift of the minimum around 200 nm towards a lower wavelength and also a decrease in the negativity at 222 nm compared with the theoretical complex suggestive of induced unfolding (Figure 4c).
Protein: DP03136 (UniProt F4IED2)
Region: residues 161	to 498
Annotation: protein binding (Molecular function)
Evidence: isothermal titration calorimetry evidence used in manual assertion
Supporting statements:
The change in entropy for binding of ANAC013 (161–498) to RCD1–RST (499–572) is relatively small and negative, indicating that binding is enthalpically driven.
Protein: DP03136 (UniProt F4IED2)
Region: residues 184	to 274
Annotation: disorder (Structural state)
Evidence: nuclear magnetic resonance spectroscopy evidence used in manual assertion
Supporting statements:
Using NMR spectroscopy, only ∼100 of the expected 321 NMR resonances were observed in the 1H, 15N HSQC NMR spectrum, located within a narrow 1H dispersion typical of IDRs (Fig. 1C). 
Using a set of BEST-type triple-resonance NMR experiments, we assigned the backbone resonances of ANAC013161–274 to 81% completeness (Fig. 1C and E; BMRB: 51969). The secondary 13Cα and 13Cβ chemical shifts (Fig. 1E and Supplementary Fig. S2) showed few consistent patterns from transient secondary structures, inferring that ANAC013161–274 is mostly disordered, except for a transient helix between D217 and G232. This helix is populated to ∼20% as deduced from consecutive positive SCSs [52] and overlaps AD1/AI2 (Fig. 1E). 
We therefore assessed
whether supramolecular interactions could explain the lack
of NMR signals and recorded a 1H, 15N HSQC spectrum
of ANAC013161–498 in 6 M urea (Supplementary Fig. S1D).
All resonances were recovered, indicating that a relatively
large part (∼2/3) of the ANAC013 IDR contributes to these
structures.
Cross-references: BMRB:51969
Protein: DP03136 (UniProt F4IED2)
Region: residues 161	to 498
Annotation: disorder (Structural state)
Evidence: far-UV circular dichroism evidence used in manual assertion
Supporting statements:
A SEC analysis indicated higher order soluble structures (Supplementary Fig. S1B), and a far-UV CD spectrum revealed the presence of ∼15% helicity (Fig. 1D), in line with PSIPRED prediction of helicity in the regions 420–460 (Supplementary Fig. S1C).
Protein: DP03136 (UniProt F4IED2)
Region: residues 161	to 274
Annotation: disorder (Structural state)
Evidence: small-angle X-ray scattering evidence used in manual assertion
Supporting statements:
The average SAXS curve of these conformers did not reproduce the experimental data accurately (χ2 = 25) (Supplementary Fig. S6A), indicating that ANAC013161–274 does not behave as a statistical coil. The average Rg of this ensemble (31 Å) was smaller than the experimentally determined Rg (36 Å) (Supplementary Fig. S6B), showing ANAC013161–274 to be extended in solution, consistent with its net negative charge (Fig. 1A, middle panel), and correlating with the R2 values that were overall higher than expected for a random coil (Fig. 1D).