LiteFold/DisProt huggingface dataset:
Protein: DP01605 (UniProt P19339)
Region: residues 201	to 211
Annotation: flexible linker (Disorder function)
Evidence: x-ray crystallography evidence used in manual assertion
Supporting statements:
Characteristic of a poorly ordered region, the electron density for the 10-residue interdomain linker was weak and discontinuous in maps calculated with the multiwavelength anomalous diffraction data.
 From the C terminus of RRM1, the second-closest RRM2 N terminus is 28.8 Å away, a distance that two residues could not possibly bridge. Weak electron density and the high B-factors of the interdomain linker imply significant flexibility in this region.
In summary, SXL RRM1 and RRM2 form two discreet RNA binding surfaces that are too far apart in the crystal structure to interact simultaneously with the high-affinity, r(GU8C) RNA. These results indicate that the interdomain linker acts as flexible tether, and orientation of the RRM domains is coupled to RNA binding.
Cross-references: PDB:3SXL
Protein: DP01605 (UniProt P19339)
Region: residues 158	to 167
Annotation: disorder (Structural state)
Evidence: nuclear magnetic resonance spectroscopy evidence used in manual assertion
Supporting statements:
(a) The 20 backbone structures of RBD1FY, which were superimposed for minimal root-mean-square deviation of the backbone atoms (N, Cα, and C′) of residues 125 to 131, 137 to 157, and 167 to 201 (stereoview).
Cross-references: PDB:2SXL
Protein: DP01605 (UniProt P19339)
Region: residues 158	to 167
Annotation: flexible linker (Disorder function)
Evidence: nuclear magnetic resonance spectroscopy evidence used in manual assertion
Supporting statements:
The loop connecting the β2 and β3 strands of the Sxl RBD1 (β2/β3 loop) consists of ten amino acid residues (R158 to G167), and is as long as that of the Sxl RBD2 (R244 to G253), whereas the corresponding loop of the U1A RBD1 is composed of only six amino acid residues (R48 to G53).
Cross-references: PDB:2SXL
Protein: DP01605 (UniProt P19339)
Region: residues 244	to 253
Annotation: flexible linker (Disorder function)
Evidence: nuclear magnetic resonance spectroscopy evidence used in manual assertion
Supporting statements:
The loop connecting the β2 and β3 strands of the Sxl RBD1 (β2/β3 loop) consists of ten amino acid residues (R158 to G167), and is as long as that of the Sxl RBD2 (R244 to G253), whereas the corresponding loop of the U1A RBD1 is composed of only six amino acid residues (R48 to G53).
Protein: DP01605 (UniProt P19339)
Region: residues 111	to 123
Annotation: disorder (Structural state)
Evidence: X-ray crystallography-based structural model with missing residue coordinates used in manual assertion
Supporting statements:
Residues left out of the model for lack of interpretable electron density include 111–123, 204–205 (interdomain linker), 276–282 (α2-β4 loop of RRM2), and 290–294 (C terminus).
Cross-references: PDB:3SXL
Protein: DP01608 (UniProt Q9Y6H6)
Region: residues 31	to 56
Annotation: disorder (Structural state)
Evidence: nuclear magnetic resonance spectroscopy evidence used in manual assertion
Supporting statements:
The KCNE3 structure is composed of an extracellular N-terminal surface-associated amphipathic helix (residues 10 to 30) connected by a flexible loop to the a-helical transmembrane domain (TMD; 57 to 82), followed by a short juxtamembrane helix (90 to 95) and a disordered C terminus (96 to 103).
Protein: DP01610 (UniProt P47910)
Region: residues 69	to 101
Annotation: disorder (Structural state)
Evidence: cryogenic electron microscopy-based structural model with missing residue coordinates used in manual assertion
Supporting statements:
A loop and an extended structure were assigned for the fragment encompassing residues 69 to 91, based on poor Cryo-EM electron density.  Missing electron density did not allow the authors to model the structure for residues 92 to 101. These facts suggest the region 69 to 101 is unstructured.
Protein: DP01611 (UniProt Q06696)
Region: residues 203	to 395
Annotation: disorder (Structural state)
Evidence: cleavage assay evidence used in manual assertion
Supporting statements:
The proteolytic susceptibility of the region connecting the second NZF motif at residue 203 and the start of the C-terminal domain at 396 suggests that a flexible linker connects these two domains.
Protein: DP01611 (UniProt Q06696)
Region: residues 1	to 395
Annotation: disorder (Structural state)
Evidence: X-ray crystallography-based structural model with missing residue coordinates used in manual assertion
Supporting statements:
No density is visible for residues 1–395 of Vps36
Cross-references: PDB:1W7P
Protein: DP01611 (UniProt Q06696)
Region: residues 1	to 395
Annotation: disorder (Structural state)
Evidence: X-ray crystallography-based structural model with missing residue coordinates used in manual assertion
Supporting statements:
it was determined that the crystallized complex contained a fragment of Vps36 comprising residues 396–566
Cross-references: PDB:1U5T
Protein: DP01611 (UniProt Q06696)
Region: residues 203	to 395
Annotation: flexible linker (Disorder function)
Evidence: cleavage assay evidence used in manual assertion
Supporting statements:
The proteolytic susceptibility of the region connecting the second NZF motif at residue 203 and the start of the C-terminal domain at 396 suggests that a flexible linker connects these two domains
Cross-references: PDB:1U5T
Protein: DP01611 (UniProt Q06696)
Region: residues 177	to 205
Annotation: localization (Biological process)
Evidence: X-ray crystallography-based structural model with missing residue coordinates used in manual assertion
Supporting statements:
The N-terminal portion of Vps36 contains two copies of a NZF zinc-finger motif. The second NZF finger of Vps36 binds ubiquitin and is thought to be the main site of interaction between ESCRT-II and ubiquitinated cargo proteins
The second NZF finger, also known as Vps36-1, is also widely described in PMID:15029239 as it contains a 13TF14/Φ25 motif and binds Ub (Kd=182 μM), whereas the other NZF domain (Vps36‐2, residues 114-151) lacks this motif and does not bind Ub. Moreover, the Ub‐binding activity of the Vps36 NZF domain is required for efficient sorting of ubiquitylated substrates into the MVB.
Cross-references: PDB:1U5T
Protein: DP01611 (UniProt Q06696)
Region: residues 177	to 205
Annotation: protein binding (Molecular function)
Evidence: X-ray crystallography-based structural model with missing residue coordinates used in manual assertion
Supporting statements:
The N-terminal portion of Vps36 contains two copies of a NZF zinc-finger motif. The second NZF finger of Vps36 binds ubiquitin and is thought to be the main site of interaction between ESCRT-II and ubiquitinated cargo proteins
The second NZF finger, also known as Vps36-1, is also widely described in PMID:15029239 as it contains a 13TF14/Φ25 motif and binds Ub (Kd=182 μM), whereas the other NZF domain (Vps36‐2, residues 114-151) lacks this motif and does not bind Ub. Moreover, the Ub‐binding activity of the Vps36 NZF domain is required for efficient sorting of ubiquitylated substrates into the MVB.
Cross-references: PDB:1U5T
Protein: DP01613 (UniProt Q96AC1)
Region: residues 328	to 367
Annotation: disorder (Structural state)
Evidence: nuclear magnetic resonance spectroscopy evidence used in manual assertion
Supporting statements:
We then prepared 15N-labeled kindlin-2 residues 328–367 (termed K2F2N) (Fig. 4B). Fig. 4C shows that kindlin-2 residues 328–367 are largely unstructured but specifically bind to unlabeled ILK KLD·α-parvin CH2, with 16 kindlin-2 residues undergoing significant line-broadening and/or chemical shift perturbations including two characteristic glycine peaks.
Protein: DP01613 (UniProt Q96AC1)
Region: residues 350	to 357
Annotation: protein binding (Molecular function)
Evidence: nuclear magnetic resonance spectroscopy evidence used in manual assertion
Supporting statements:
We then prepared 15N-labeled kindlin-2 residues 328–367 (termed K2F2N) (Fig. 4B). Fig. 4C shows that kindlin-2 residues 328–367 are largely unstructured but specifically bind to unlabeled ILK KLD·α-parvin CH2, with 16 kindlin-2 residues undergoing significant line-broadening and/or chemical shift perturbations including two characteristic glycine peaks.
Using NMR, we further showed that 2H,15N-labeled HSQC spectrum of a double kindlin-2 F2 mutant (L353A and L357A; hereinafter referred to as LL/AA) exhibited a well dispersed spectrum that is similar to the wild type but has no chemical shift perturbation and line broadening upon addition of unlabeled ILK KLD·α-parvin CH2 (Fig. 5B). These data strongly suggest that the double amino acid substitution (LL/AA) completely abolished the kindlin-2 binding to ILK without perturbing the overall structure.
Protein: DP01613 (UniProt Q96AC1)
Region: residues 1	to 15
Annotation: disorder (Structural state)
Evidence: nuclear magnetic resonance spectroscopy evidence used in manual assertion
Supporting statements:
The structures are well converged except the N-terminal M1-D15 that appears to be highly flexible with few long range NOEs.
Cross-references: PDB:2LGX
BMRB:17827
Protein: DP01613 (UniProt Q96AC1)
Region: residues 95	to 105
Annotation: disorder (Structural state)
Evidence: nuclear magnetic resonance spectroscopy evidence used in manual assertion
Supporting statements:
The structure of K2-N 1-94 was calculated according to standard protocols (95-105 were disordered and therefore excluded from the calculations). 
Cross-references: PDB:2LGX
BMRB:17827
Protein: DP01613 (UniProt Q96AC1)
Region: residues 350	to 357
Annotation: protein binding (Molecular function)
Evidence: glutathione S-transferase pull-down assay evidence used in manual assertion
Supporting statements:
Using GST pulldown binding experiments, we found that the four kindlin-2 F2 point mutants (V346A, L350A, L353A, or L357A) but not others abolished ILK binding (Fig. 5A).
Protein: DP01614 (UniProt Q14653)
Region: residues 173	to 188
Annotation: disorder (Structural state)
Evidence: X-ray crystallography-based structural model with missing residue coordinates used in manual assertion
Supporting statements:
"The N-terminal residues 173–188 were disordered. "
Cross-references: PDB:1QWT
Protein: DP01615 (UniProt P03126)
Region: residues 1	to 10
Annotation: disorder (Structural state)
Evidence: nuclear magnetic resonance spectroscopy evidence used in manual assertion
Supporting statements:
The N-terminal region, corresponding to residues 1–10, adopts an extended and rather flexible structure as indicated by the low 1H-15N heteronuclear NOE values, which correlate with dynamic events in the nanosecond timescale.
Cross-references: PDB:2LJX
PDB:2LJY
BMRB:17967
BMRB:17968
Protein: DP01615 (UniProt P03126)
Region: residues 148	to 158
Annotation: disorder (Structural state)
Evidence: nuclear magnetic resonance spectroscopy evidence used in manual assertion
Supporting statements:
The C-terminal residues R141-L151, encompassing the PDZ binding motif (Thomas et al., 2002), adopt a random conformation.
The C-terminal 141-151 residues corresponds to the 148-158 region of the Uniprot entry, since residues are numbered as in the shorter transcript of HPV 16 E6. They use a E6 construct containing four Cys-Ser mutations, but they expect its structure to be identical to the wildtype because the mutated cysteins were not conserved in E6 alignments, the Cys/Ser change is relatively isosteric, the mutations did not prevent the domain from adopting a stable fold, all mutated positions turn out to be exposed on the surface of the calculated structure, and these mutations are also present in the full-length E6 6C/6S mutant displaying in vitro and in vivo p53 degradation properties indistinguishable from those of wild-type E6.
Cross-references: PDB:2FK4
BMRB:6707
Protein: DP01615 (UniProt P03126)
Region: residues 148	to 158
Annotation: flexible C-terminal tail (Disorder function)
Evidence: nuclear magnetic resonance spectroscopy evidence used in manual assertion
Supporting statements:
The C-terminal residues R141-L151, encompassing the PDZ binding motif (Thomas et al., 2002), adopt a random conformation.
 The N-terminal and C-terminal tails are highly variable in both length and sequence, but the interdomain linker has a fixed length in all HPV species and contains several highly conserved hydrophobic residues presenting the periodicity of a helix (Figure 2A).
The C-terminal 141-151 residues corresponds to the 148-158 region of the Uniprot entry, since residues are numbered as in the shorter transcript of HPV 16 E6. They use a E6 construct containing four Cys-Ser mutations, but they expect its structure to be identical to the wildtype because the mutated cysteins were not conserved in E6 alignments, the Cys/Ser change is relatively isosteric, the mutations did not prevent the domain from adopting a stable fold, all mutated positions turn out to be exposed on the surface of the calculated structure, and these mutations are also present in the full-length E6 6C/6S mutant displaying in vitro and in vivo p53 degradation properties indistinguishable from those of wild-type E6.
Cross-references: PDB:2FK4
BMRB:6707
Protein: DP01615 (UniProt P03126)
Region: residues 148	to 158
Annotation: protein binding (Molecular function)
Evidence: differential scanning calorimetry evidence used in manual assertion
Supporting statements:
For all the PBMs tested, an increase of 4 to 11 °C in the Tm was observed, showing that the PBM binding onto PTPN3-PDZ stabilizes the domain, whether the PBM is of cellular or viral origin.
The PBM region corresponds to the C-terminal 148-158 residues of the Human papillomavirus type 16 E6 protein.
Protein: DP01615 (UniProt P03126)
Region: residues 148	to 158
Annotation: protein binding (Molecular function)
Evidence: heteronuclear single quantum coherence spectroscopy evidence used in manual assertion
Supporting statements:
We obtained KD values of 29 μM, 53 μM and 37 μM for PTPN3-PDZ with HBVc PBM, HPV16E6 PBM and HPV18E6 PBM, respectively (Table 1). The KD values are all in the same tenth-of-micromolar range for the viral PBMs and are close to the one of the cellular partner p38γ. The measured affinities fall in the standard 0.1–100 μM range12 for PDZ-PBM interactions.
The PBM region corresponds to the C-terminal 148-158 residues of the Human papillomavirus type 16 E6 protein.
Protein: DP01615 (UniProt P03126)
Region: residues 148	to 158
Annotation: regulation of proteolysis (Biological process)
Evidence: x-ray crystallography evidence used in manual assertion
Supporting statements:
HPV16E6 PBM binds to the PDZ domain as an anti-parallel extension of the β2-strand domain in a conventional mode.
The PBM region corresponds to the C-terminal 148-158 residues of the Human papillomavirus type 16 E6 protein. 
Cross-references: PDB:6HKS
Protein: DP01615 (UniProt P03126)
Region: residues 148	to 158
Annotation: protein binding (Molecular function)
Evidence: x-ray crystallography evidence used in manual assertion
Supporting statements:
HPV16E6 PBM binds to the PDZ domain as an anti-parallel extension of the β2-strand domain in a conventional mode.
The PBM region corresponds to the C-terminal 148-158 residues of the Human papillomavirus type 16 E6 protein. 
Cross-references: PDB:6HKS
Protein: DP01615 (UniProt P03126)
Region: residues 148	to 158
Annotation: regulation of proteolysis (Biological process)
Evidence: heteronuclear single quantum coherence spectroscopy evidence used in manual assertion
Supporting statements:
We obtained KD values of 29 μM, 53 μM and 37 μM for PTPN3-PDZ with HBVc PBM, HPV16E6 PBM and HPV18E6 PBM, respectively (Table 1). The KD values are all in the same tenth-of-micromolar range for the viral PBMs and are close to the one of the cellular partner p38γ. The measured affinities fall in the standard 0.1–100 μM range12 for PDZ-PBM interactions.
The PBM region corresponds to the C-terminal 148-158 residues of the Human papillomavirus type 16 E6 protein.
Protein: DP01615 (UniProt P03126)
Region: residues 148	to 158
Annotation: regulation of proteolysis (Biological process)
Evidence: differential scanning calorimetry evidence used in manual assertion
Supporting statements:
For all the PBMs tested, an increase of 4 to 11 °C in the Tm was observed, showing that the PBM binding onto PTPN3-PDZ stabilizes the domain, whether the PBM is of cellular or viral origin.
The PBM region corresponds to the C-terminal 148-158 residues of the Human papillomavirus type 16 E6 protein.
Protein: DP01615 (UniProt P03126)
Region: residues 1	to 10
Annotation: flexible N-terminal tail (Disorder function)
Evidence: nuclear magnetic resonance spectroscopy evidence used in manual assertion
Supporting statements:
The N-terminal region, corresponding to residues 1–10, adopts an extended and rather flexible structure as indicated by the low 1H-15N heteronuclear NOE values, which correlate with dynamic events in the nanosecond timescale.
Cross-references: BMRB:17968
PDB:2LJY
PDB:2LJX
BMRB:17967
Protein: DP01618 (UniProt P03070)
Region: residues 17	to 26
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 of Tag can be divided in a  J-like domain and an extended loop (L4) containing the LxCxE sequence necessary for the interaction with the B box in Rb. PDB structure shows unstructured loops L1, L2 and L3 which are internal and allow proper folding of J-like domain. L2 contains the conserved HDB sequence that has been proved to be functionally important for interactions and chaperone-like activity
Protein: DP01618 (UniProt P03070)
Region: residues 39	to 48
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 of Tag can be divided in a  J-like domain and an extended loop (L4) containing the LxCxE sequence necessary for the interaction with the B box in Rb. PDB structure shows unstructured loops L1, L2 and L3 which are internal and allow proper folding of J-like domain. L2 contains the conserved HDB sequence that has been proved to be functionally important for interactions and chaperone-like activity
Protein: DP01618 (UniProt P03070)
Region: residues 39	to 48
Annotation: protein binding (Molecular function)
Evidence: X-ray crystallography-based structural model with missing residue coordinates used in manual assertion
Supporting statements:
The importance of loop L2 is indicated by the strong conservation of the HPD sequence in all J domains (Tsai and Douglas, 1996). Large T antigen mutants in this region are unable to dissociate E2F from Rb and are, as a consequence, replication defective. Also, DnaJ mutants in this region have lost their chaperone function (Srinivasan et al., 1997).
Protein: DP01618 (UniProt P03070)
Region: residues 82	to 130
Annotation: disorder (Structural state)
Evidence: nuclear magnetic resonance spectroscopy evidence used in manual assertion
Supporting statements:
Comparison between TROSY-HSQC NMR peak dispersion from protein constructs used in this work, the authors suggest that the linker between J-domain and OBD domain is flexible.
Protein: DP01618 (UniProt P03070)
Region: residues 68	to 87
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 of Tag can be divided in a  J-like domain and an extended loop (L4) containing the LxCxE sequence necessary for the interaction with the B box in Rb. PDB structure shows unstructured loops L1, L2 and L3 which are internal and allow proper folding of J-like domain. L2 contains the conserved HDB sequence that has been proved to be functionally important for interactions and chaperone-like activity
Protein: DP01618 (UniProt P03070)
Region: residues 103	to 117
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 of Tag can be divided in a  J-like domain and an extended loop (L4) containing the LxCxE sequence necessary for the interaction with the B box in Rb. PDB structure shows unstructured loops L1, L2 and L3 which are internal and allow proper folding of J-like domain. L2 contains the conserved HDB sequence that has been proved to be functionally important for interactions and chaperone-like activity
Protein: DP01618 (UniProt P03070)
Region: residues 103	to 117
Annotation: protein binding (Molecular function)
Evidence: X-ray crystallography-based structural model with missing residue coordinates used in manual assertion
Supporting statements:
The loop containing the LxCxE motifs forms an extended conformation and binds to the shallow surface groove on the B box created by five helices, three of which are from the cyclin box (in Rb).
Protein: DP01619 (UniProt Q9NR28)
Region: residues 56	to 69
Annotation: disorder (Structural state)
Evidence: X-ray crystallography-based structural model with missing residue coordinates used in manual assertion
Supporting statements:
The authors solved a structure with two molecules of Smac/DIABLO in the crystal as a dimer. In their final model, no electron density was seen for the 14 first residues in the N terminal region in Chain A and for the 12 first residues in Chain B, confirming that this protein region is highly mobile in the absence of interaction with BIR domains partners.
Protein: DP01619 (UniProt Q9NR28)
Region: residues 56	to 67
Annotation: disorder (Structural state)
Evidence: X-ray crystallography-based structural model with missing residue coordinates used in manual assertion
Supporting statements:
The authors solved a structure with two molecules of Smac/DIABLO in the crystal as a dimer. In their final model, no electron density was seen for the 14 first residues in the N terminal region in Chain A and for the 12 first residues in Chain B, confirming that this protein region is highly mobile in the absence of interaction with BIR domains partners.
Protein: DP01619 (UniProt Q9NR28)
Region: residues 56	to 70
Annotation: disorder (Structural state)
Evidence: X-ray crystallography-based structural model with missing residue coordinates used in manual assertion
Supporting statements:
The authors could only trace the N-terminal segment (residues 56 to 59) of the bound peptide in the complex SmacN-Survivin in the crystal structure. Due to missing electron density the C terminal (60-70) could not be solved. The extended interaction and the missing residues suggest this region is disordered in solution in its unbound form.
Protein: DP01619 (UniProt Q9NR28)
Region: residues 56	to 65
Annotation: disorder (Structural state)
Evidence: X-ray crystallography-based structural model with missing residue coordinates used in manual assertion
Supporting statements:
In the mature form of Smac (1-186), residue 1 corresponds to residue 56 of unprocessed Smac (1- 239). For this mature form, no electron density is seen corresponding to the N-terminal 10 residues suggesting this segment is disordered in solution.
Protein: DP01620 (UniProt P20823)
Region: residues 181	to 200
Annotation: disorder (Structural state)
Evidence: X-ray crystallography-based structural model with missing residue coordinates used in manual assertion
Supporting statements:
The linker between POUS and POUH domains (residues 182–200) is disordered. Nevertheless, connectivity between domains was established based on crystal packing and distance considerations (Figure 2A). The presence of neighboring molecules in the crystal lattice precludes the alternative configuration.
Cross-references: PDB:1IC8