LiteFold/DisProt huggingface dataset:
Protein: DP02704 (UniProt P41214)
Region: residues 348	to 373
Annotation: flexible linker (Disorder function)
Evidence: cryogenic electron microscopy evidence used in manual assertion
Supporting statements:
The structures, supported by biochemical experiments, reveal how eIF2D emulates the function of several canonical translation initiation factors by using three independent, flexibly connected RNA binding domains to simultaneously monitor codon-anticodon interactions in the ribosomal P-site and position the initiator tRNA.
Cross-references: PDB:5OA3
Protein: DP02704 (UniProt P41214)
Region: residues 184	to 259
Annotation: flexible linker (Disorder function)
Evidence: cryogenic electron microscopy evidence used in manual assertion
Supporting statements:
The structures, supported by biochemical experiments, reveal how eIF2D emulates the function of several canonical translation initiation factors by using three independent, flexibly connected RNA binding domains to simultaneously monitor codon-anticodon interactions in the ribosomal P-site and position the initiator tRNA.
Cross-references: PDB:5OA3
Protein: DP02705 (UniProt P45379)
Region: residues 193	to 212
Annotation: disorder (Structural state)
Evidence: X-ray crystallography-based structural model with missing residue coordinates used in manual assertion
Supporting statements:
Further upstream of H1(T2), residues 183–202 of TnT were not defined in the electron density map.
IDR corresponding to region 193-212 on the amino acid sequence.
Cross-references: PDB:1J1E
PDB:1J1D
Protein: DP02705 (UniProt P45379)
Region: residues 272	to 288
Annotation: disorder (Structural state)
Evidence: X-ray crystallography-based structural model with missing residue coordinates used in manual assertion
Supporting statements:
The C terminus of TnT (denoted as C-TnT, residues 272–288), which has been shown to bind to tropomyosin is not always defined in the crystal (the residues down to 276 are defined in Tn52KB)
As described above, most of the electron densities associated with the potential actin–tropomyosin interfaces are ambiguous. These include the inhibitory region (residues 137–148) and the C-terminus of TnI (residues 163–210 in Tn52KA and 192–210 in Tn52KB), and the C-TnT (residues 272–288).
Cross-references: PDB:1J1E
PDB:1J1D
Protein: DP02705 (UniProt P45379)
Region: residues 1	to 66
Annotation: disorder (Structural state)
Evidence: curator inference from database used in manual assertion
Supporting statements:
This poly-E region is inferred by the curator to be disordered, based on MobiDB-Lite and according to experimental evidence demonstrating that poly-E repeats display random-coil-like conformation (PMID:16949547)
Protein: DP02706 (UniProt Q9NXV2)
Region: residues 212	to 234
Annotation: disorder (Structural state)
Evidence: X-ray crystallography-based structural model with missing residue coordinates used in manual assertion
Supporting statements:
C-terminal residues 212–234 were not visible in electron density maps. Residues 34–43 adopt different conformations in high- and low-salt crystals. Other flexible regions include residues 77–82 near the α2-helix and residues 188–200 near theβ5-β6 loops.
Cross-references: PDB:3DRZ
PDB:3DRX
PDB:3DRY
Protein: DP02706 (UniProt Q9NXV2)
Region: residues 188	to 200
Annotation: disorder (Structural state)
Evidence: X-ray crystallography-based structural model with missing residue coordinates used in manual assertion
Supporting statements:
C-terminal residues 212–234 were not visible in electron density maps. Residues 34–43 adopt different conformations in high- and low-salt crystals. Other flexible regions include residues 77–82 near the α2-helix and residues 188–200 near theβ5-β6 loops.
Cross-references: PDB:3DRZ
PDB:3DRX
PDB:3DRY
Protein: DP02707 (UniProt P25891)
Region: residues 163	to 179
Annotation: disorder (Structural state)
Evidence: X-ray crystallography-based structural model with missing residue coordinates used in manual assertion
Supporting statements:
In Pro-RIP, the internal inactivating region Ala163–Asp189 is very rich in acidic residues. Our structure shows that the internal inactivating region consists of a flexible loop (Ala163–Ala179) and a long α-helix (Ala180–Ala188)
In the precursor, the inactivation region is found on the protein surface and consists of a flexible loop followed by a long alpha-helix. This region diminished both the interaction with ribosome and cytotoxicity, but not cellular uptake.
Cross-references: PDB:2PQG
Protein: DP02707 (UniProt P25891)
Region: residues 163	to 179
Annotation: molecular function regulator (Molecular function)
Evidence: X-ray crystallography-based structural model with missing residue coordinates used in manual assertion
Supporting statements:
In Pro-RIP, the internal inactivating region Ala163–Asp189 is very rich in acidic residues. Our structure shows that the internal inactivating region consists of a flexible loop (Ala163–Ala179) and a long α-helix (Ala180–Ala188)
In the precursor, the inactivation region is found on the protein surface and consists of a flexible loop followed by a long alpha-helix. This region diminished both the interaction with ribosome and cytotoxicity, but not cellular uptake.
Among the sequences to be removed during the activation of maize RIP, the 25 aa internal region (known as internal inactivation region) is the most crucial, as removal of this region increases the activity by at least 600-fold, whereas removal of the N- or C-terminal region only increases the activity by 6- or 5-fold, respectively
These indicated that the internal inactivation region of Pro-RIP might obstruct the protein to dock onto the ribosome.
Therefore, the internal inactivation region may serve the purpose of preventing the maize RIP from attacking its cognate ribosomes in vivo.
The internal inactivation region is removed in the active form
Cross-references: PDB:2PQG
Protein: DP02709 (UniProt P04035)
Region: residues 861	to 888
Annotation: disorder (Structural state)
Evidence: X-ray crystallography-based structural model with missing residue coordinates used in manual assertion
Supporting statements:
Near the carboxyl terminus of HMGR, several catalytically relevant residues are disordered in the enzyme-statin complexes. If these residues were not flexible, they would sterically hinder statin binding.
In the electron-density maps of the statin-complex structures, residues COOH-terminal to Gly860 are missing.
In the statin-bound structures, these residues are disordered, revealing a shallow hydrophobic groove that accommodates the hydrophobic moieties of the statins.
The structurally diverse, rigid hydrophobic groups of the statins are accommodated in a shallow non-polar groove that is present only when COOH-terminal residues of HMGR are disordered.
Statins are HMGR inhibitors. Here HMGR is complexed with six different statins: rosuvastatin (PDB:1hwl), cerivastatin (PDB:1hwj), fluvastatin (PDB:1hwi), mevastatin (PDB:1hw8), atorvastatin (PDB:1hwk), simvastatin (PDB:1hw9).
Cross-references: PDB:1HWL
PDB:1HWJ
PDB:1HWI
PDB:1HW8
PDB:1HWK
PDB:1HW9
Protein: DP02709 (UniProt P04035)
Region: residues 861	to 888
Annotation: flexible C-terminal tail (Disorder function)
Evidence: X-ray crystallography-based structural model with missing residue coordinates used in manual assertion
Supporting statements:
Near the carboxyl terminus of HMGR, several catalytically relevant residues are disordered in the enzyme-statin complexes. If these residues were not flexible, they would sterically hinder statin binding.
In the electron-density maps of the statin-complex structures, residues COOH-terminal to Gly860 are missing.
In the statin-bound structures, these residues are disordered, revealing a shallow hydrophobic groove that accommodates the hydrophobic moieties of the statins.
The structurally diverse, rigid hydrophobic groups of the statins are accommodated in a shallow non-polar groove that is present only when COOH-terminal residues of HMGR are disordered.
It appears that the innate flexibility of the COOH-terminal region of HMGR is fortuitously exploited by statins to create a binding site for the inhibitor molecules.
Statins exploit the conformational flexibility of HMGR to create a hydrophobic binding pocket near the active site.
Statins are HMGR inhibitors. Here HMGR is complexed with six different statins: rosuvastatin (PDB:1hwl), cerivastatin (PDB:1hwj), fluvastatin (PDB:1hwi), mevastatin (PDB:1hw8), atorvastatin (PDB:1hwk), simvastatin (PDB:1hw9).
Cross-references: PDB:1HWL
PDB:1HWJ
PDB:1HWI
PDB:1HW8
PDB:1HWK
PDB:1HW9
Protein: DP02709 (UniProt P04035)
Region: residues 861	to 888
Annotation: molecular function regulator (Molecular function)
Evidence: X-ray crystallography-based structural model with missing residue coordinates used in manual assertion
Supporting statements:
Near the carboxyl terminus of HMGR, several catalytically relevant residues are disordered in the enzyme-statin complexes. If these residues were not flexible, they would sterically hinder statin binding.
In the electron-density maps of the statin-complex structures, residues COOH-terminal to Gly860 are missing.
In the statin-bound structures, these residues are disordered, revealing a shallow hydrophobic groove that accommodates the hydrophobic moieties of the statins.
The structurally diverse, rigid hydrophobic groups of the statins are accommodated in a shallow non-polar groove that is present only when COOH-terminal residues of HMGR are disordered.
It appears that the innate flexibility of the COOH-terminal region of HMGR is fortuitously exploited by statins to create a binding site for the inhibitor molecules.
Statins exploit the conformational flexibility of HMGR to create a hydrophobic binding pocket near the active site.
Statins are HMGR inhibitors. Here HMGR is complexed with six different statins: rosuvastatin (PDB:1hwl), cerivastatin (PDB:1hwj), fluvastatin (PDB:1hwi), mevastatin (PDB:1hw8), atorvastatin (PDB:1hwk), simvastatin (PDB:1hw9).
Cross-references: PDB:1HWL
PDB:1HWJ
PDB:1HWI
PDB:1HW8
PDB:1HWK
PDB:1HW9
Protein: DP02710 (UniProt Q9BQ50)
Region: residues 159	to 168
Annotation: disorder (Structural state)
Evidence: X-ray crystallography-based structural model with missing residue coordinates used in manual assertion
Supporting statements:
Three segments spanning residues 159–168, 185–187, and 229–236 were disordered in both monomers and omitted from the crystallographic model.
Adjacent to each active site is a flexible region containing three arginines positioned appropriately to bind DNA and to control its entry into the active site.
This loop is largely disordered, indicating that it is somewhat mobile, and it contains the positively charged arginines at positions 163, 165, and 167. 
Cross-references: PDB:1Y97
Protein: DP02710 (UniProt Q9BQ50)
Region: residues 159	to 168
Annotation: DNA binding (Molecular function)
Evidence: X-ray crystallography-based structural model with missing residue coordinates used in manual assertion
Supporting statements:
Three segments spanning residues 159–168, 185–187, and 229–236 were disordered in both monomers and omitted from the crystallographic model.
Adjacent to each active site is a flexible region containing three arginines positioned appropriately to bind DNA and to control its entry into the active site.
This loop is largely disordered, indicating that it is somewhat mobile, and it contains the positively charged arginines at positions 163, 165, and 167. 
Arginines 163, 165, and 167 within the loop are unique to TREX2 and strongly contribute to its high affinity for DNA
The position of the active sites in the TREX2 dimer and the adjacent flexible region provides an explanation for the tight DNA binding and robust catalytic activity of the TREX2 enzyme.
Involvement of all three of the arginines positioned at 163, 165, and 167 on the flexible loop is supported by additional mutagenesis studies that demonstrate contributions to DNA binding by each of the individual arginines in TREX2.
These data suggest a model for TREX2 catalysis in which the negatively charged phosphodiester backbone of DNA is first bound by the positively charged arginine residues present on this flexible loop, and the DNA is subsequently moved into the active site for catalysis.
Together, the efficient excision of 3′-terminal nucleotides facilitated by a presumed two-metal ion mechanism of phosphodiester bond cleavage similar to that proposed for the exonuclease of E. coli DNA polymerase I and the efficient binding and movement of the DNA substrate into the active site by the α6–α7 flexible loop can account for the robust nature of the TREX2 enzyme.
Cross-references: PDB:1Y97
Protein: DP02710 (UniProt Q9BQ50)
Region: residues 159	to 168
Annotation: molecular adaptor activity (Molecular function)
Evidence: X-ray crystallography-based structural model with missing residue coordinates used in manual assertion
Supporting statements:
Adjacent to each active site is a flexible region containing three arginines positioned appropriately to bind DNA and to control its entry into the active site.
These data suggest a model for TREX2 catalysis in which the negatively charged phosphodiester backbone of DNA is first bound by the positively charged arginine residues present on this flexible loop, and the DNA is subsequently moved into the active site for catalysis.
Together, the efficient excision of 3′-terminal nucleotides facilitated by a presumed two-metal ion mechanism of phosphodiester bond cleavage similar to that proposed for the exonuclease of E. coli DNA polymerase I and the efficient binding and movement of the DNA substrate into the active site by the α6–α7 flexible loop can account for the robust nature of the TREX2 enzyme.
Cross-references: PDB:1Y97
Protein: DP02710 (UniProt Q9BQ50)
Region: residues 159	to 168
Annotation: molecular function regulator (Molecular function)
Evidence: X-ray crystallography-based structural model with missing residue coordinates used in manual assertion
Supporting statements:
Adjacent to each active site is a flexible region containing three arginines positioned appropriately to bind DNA and to control its entry into the active site.
These data suggest a model for TREX2 catalysis in which the negatively charged phosphodiester backbone of DNA is first bound by the positively charged arginine residues present on this flexible loop, and the DNA is subsequently moved into the active site for catalysis.
Together, the efficient excision of 3′-terminal nucleotides facilitated by a presumed two-metal ion mechanism of phosphodiester bond cleavage similar to that proposed for the exonuclease of E. coli DNA polymerase I and the efficient binding and movement of the DNA substrate into the active site by the α6–α7 flexible loop can account for the robust nature of the TREX2 enzyme.
Cross-references: PDB:1Y97
Protein: DP02711 (UniProt Q9V6K1)
Region: residues 408	to 417
Annotation: disorder (Structural state)
Evidence: X-ray crystallography-based structural model with missing residue coordinates used in manual assertion
Supporting statements:
Furthermore, the structure suggests a model for activation of TPP II involving the relocation of a flexible loop and a repositioning of the active–site serine, coupling it to holocomplex assembly and active site sequestration.
Density for most of the structure was observed; the disordered regions were limited to a few predicted loop regions, which were not modelled due to lack of density or weak density (Fig. 1a, c). These loops include residues Asn90–Pro112, loop “L1” (Glu408–Gly417), which is highly conserved and unique to the TPP II family, residues Gly442–Gln456 of loop “L2” (Gly441–Gly460), which is likewise highly conserved and contains active–site residue Ser462 at its C–terminal side, and loop “L3” (Lys1027–Lys1098) which is substantially shorter in human TPP II and is prone to nicking in both purified Drosophila and human TPP II with no observable effect on activity.
Cross-references: PDB:3LXU
Protein: DP02711 (UniProt Q9V6K1)
Region: residues 442	to 456
Annotation: disorder (Structural state)
Evidence: X-ray crystallography-based structural model with missing residue coordinates used in manual assertion
Supporting statements:
Furthermore, the structure suggests a model for activation of TPP II involving the relocation of a flexible loop and a repositioning of the active–site serine, coupling it to holocomplex assembly and active site sequestration.
Density for most of the structure was observed; the disordered regions were limited to a few predicted loop regions, which were not modelled due to lack of density or weak density (Fig. 1a, c). These loops include residues Asn90–Pro112, loop “L1” (Glu408–Gly417), which is highly conserved and unique to the TPP II family, residues Gly442–Gln456 of loop “L2” (Gly441–Gly460), which is likewise highly conserved and contains active–site residue Ser462 at its C–terminal side, and loop “L3” (Lys1027–Lys1098) which is substantially shorter in human TPP II and is prone to nicking in both purified Drosophila and human TPP II with no observable effect on activity.
Cross-references: PDB:3LXU
Protein: DP02711 (UniProt Q9V6K1)
Region: residues 1027	to 1098
Annotation: disorder (Structural state)
Evidence: X-ray crystallography-based structural model with missing residue coordinates used in manual assertion
Supporting statements:
Furthermore, the structure suggests a model for activation of TPP II involving the relocation of a flexible loop and a repositioning of the active–site serine, coupling it to holocomplex assembly and active site sequestration.
Density for most of the structure was observed; the disordered regions were limited to a few predicted loop regions, which were not modelled due to lack of density or weak density (Fig. 1a, c). These loops include residues Asn90–Pro112, loop “L1” (Glu408–Gly417), which is highly conserved and unique to the TPP II family, residues Gly442–Gln456 of loop “L2” (Gly441–Gly460), which is likewise highly conserved and contains active–site residue Ser462 at its C–terminal side, and loop “L3” (Lys1027–Lys1098) which is substantially shorter in human TPP II and is prone to nicking in both purified Drosophila and human TPP II with no observable effect on activity.
Cross-references: PDB:3LXU
Protein: DP02712 (UniProt Q9H3P2)
Region: residues 189	to 528
Annotation: disorder (Structural state)
Evidence: cryogenic electron microscopy-based structural model with missing residue coordinates used in manual assertion
Supporting statements:
Additionally, NELF possesses two flexible 'tentacles' that can contact DSIF and exiting RNA.
It also unveiled that NELF comprises three structured lobes and two flexible tentacles that approach DSIF and exiting RNA.
Residues 189-528 of NELF-A form a flexible tentacle that binds Pol II and DSIF.
Negative elongation factor (NELF), is composed of the four subunits NELF-A, -B, -C (or isoform NELF-D that lacks the first nine NELF-C residues), and -E. One of the two flexible "tentacles" is in NELF-A, the other flexible "tentacle" is in NELF-E. They contact DSIF, composed of SPT5 and SPT4
Cross-references: PDB:6GML
Protein: DP02712 (UniProt Q9H3P2)
Region: residues 189	to 528
Annotation: protein binding (Molecular function)
Evidence: cryogenic electron microscopy evidence used in manual assertion
Supporting statements:
Additionally, NELF possesses two flexible 'tentacles' that can contact DSIF and exiting RNA.
It also unveiled that NELF comprises three structured lobes and two flexible tentacles that approach DSIF and exiting RNA.
Residues 189-528 of NELF-A form a flexible tentacle that binds Pol II and DSIF.
Negative elongation factor (NELF), is composed of the four subunits NELF-A, -B, -C (or isoform NELF-D that lacks the first nine NELF-C residues), and -E. One of the two flexible "tentacles" is in NELF-A, the other flexible "tentacle" is in NELF-E. They contact DSIF, composed of SPT5 and SPT4
Cross-references: PDB:6GML
Protein: DP02712 (UniProt Q9H3P2)
Region: residues 189	to 528
Annotation: molecular adaptor activity (Molecular function)
Evidence: cryogenic electron microscopy evidence used in manual assertion
Supporting statements:
Additionally, NELF possesses two flexible 'tentacles' that can contact DSIF and exiting RNA.
It also unveiled that NELF comprises three structured lobes and two flexible tentacles that approach DSIF and exiting RNA.
Residues 189-528 of NELF-A form a flexible tentacle that binds Pol II and DSIF.
Negative elongation factor (NELF), is composed of the four subunits NELF-A, -B, -C (or isoform NELF-D that lacks the first nine NELF-C residues), and -E. One of the two flexible "tentacles" is in NELF-A, the other flexible "tentacle" is in NELF-E. They contact DSIF, composed of SPT5 and SPT4
Cross-references: PDB:6GML
Protein: DP02712 (UniProt Q9H3P2)
Region: residues 189	to 528
Annotation: molecular adaptor activity (Molecular function)
Evidence: cross-linking evidence used in manual assertion
Supporting statements:
Additionally, NELF possesses two flexible 'tentacles' that can contact DSIF and exiting RNA.
It also unveiled that NELF comprises three structured lobes and two flexible tentacles that approach DSIF and exiting RNA.
Residues 189-528 of NELF-A form a flexible tentacle that binds Pol II and DSIF.
Crosslinking data indicate that the NELF-A flexible "tentacle" reach the DSIF DNA clamp, in particular SPT4 and the SPT5 NGN domain, and is involved in the binding of Pol II subunits RBP1, RBP2, RBP9 
Negative elongation factor (NELF), is composed of the four subunits NELF-A, -B, -C (or isoform NELF-D that lacks the first nine NELF-C residues), and -E. One of the two flexible "tentacles" is in NELF-A, the other flexible "tentacle" is in NELF-E. They contact DSIF, composed of SPT5 and SPT4
Cross-references: PDB:6GML
Protein: DP02712 (UniProt Q9H3P2)
Region: residues 189	to 528
Annotation: molecular adaptor activity (Molecular function)
Evidence: cryogenic electron microscopy evidence used in manual assertion
Supporting statements:
Additionally, NELF possesses two flexible 'tentacles' that can contact DSIF and exiting RNA.
It also unveiled that NELF comprises three structured lobes and two flexible tentacles that approach DSIF and exiting RNA.
Residues 189-528 of NELF-A form a flexible tentacle that binds Pol II and DSIF.
Crosslinking data indicate that the NELF-A flexible "tentacle" reach the DSIF DNA clamp, in particular SPT4 and the SPT5 NGN domain, and is involved in the binding of Pol II subunits RBP1, RBP2, RBP9 
Negative elongation factor (NELF), is composed of the four subunits NELF-A, -B, -C (or isoform NELF-D that lacks the first nine NELF-C residues), and -E. One of the two flexible "tentacles" is in NELF-A, the other flexible "tentacle" is in NELF-E. They contact DSIF, composed of SPT5 and SPT4
Cross-references: PDB:6GML
Protein: DP02713 (UniProt P18615)
Region: residues 139	to 363
Annotation: disorder (Structural state)
Evidence: cryogenic electron microscopy-based structural model with missing residue coordinates used in manual assertion
Supporting statements:
Residues 139-363 of NELF-E form a flexible tentacle that extends over DSIF near exiting RNA.
Density for NELF-E was largely lacking except for the N-terminal helix α1.
Cross-references: PDB:6GML
Protein: DP02714 (UniProt O60880)
Region: residues 103	to 128
Annotation: disorder (Structural state)
Evidence: nuclear magnetic resonance spectroscopy evidence used in manual assertion
Supporting statements:
The C-terminal 25 residues of SAP/SH2D1A were unstructured in both complexes. The 1H–15N HSQC cross-peaks corresponding to this region of the protein were very narrow and intense, indicative of rapid and unhindered tumbling in solution (Li et al., 1999). Moreover, no intermediate- or long-range nuclear Overhauser effects (NOEs) could be observed beyond residue 105. Consequently, only residues 1–107, corresponding essentially to the SH2 domain region of the protein (residues 6–102)
Cross-references: PDB:1KA6
PDB:1KA7