LiteFold/DisProt huggingface dataset:
Protein: DP02715 (UniProt P00452)
Region: residues 737	to 761
Annotation: disorder (Structural state)
Evidence: X-ray crystallography-based structural model with missing residue coordinates used in manual assertion
Supporting statements:
The last 24 residues at the carboxyl end, which includes these two cysteines, are not visible in the electron density map.
Cross-references: PDB:1RLR
Protein: DP02715 (UniProt P00452)
Region: residues 737	to 761
Annotation: protein folding chaperone (Molecular function)
Evidence: X-ray crystallography-based structural model with missing residue coordinates used in manual assertion
Supporting statements:
The last 24 residues at the carboxyl end, which includes these two cysteines, are not visible in the electron density map.
Ribonucleotide reductase is the only enzyme that catalyses de novo formation of deoxyribonucleotides and is thus a key enzyme in DNA synthesis. The radical-based reaction involves five cysteins. Two redox-active cysteines are located at adjacent antiparallel strands in a new type of ten-stranded alpha/beta-barrel, and two others at the carboxyl end in a flexible arm.
Together with the disordered carboxyl end of the peptide this provides strong support for the theory of a  flexible tail that transfers reducing equivalents from the surface to the active site by a thiol exchange reaction.
Cross-references: PDB:1RLR
Protein: DP02716 (UniProt P0A873)
Region: residues 162	to 172
Annotation: disorder (Structural state)
Evidence: X-ray crystallography-based structural model with missing residue coordinates used in manual assertion
Supporting statements:
Each monomer consists of a C-terminal domain connected by a flexible linker to an N-terminal AdoMet-binding domain.
The monomer of TrmD consists of two discrete domains connected by an extended flexible linker region of 11 residues 
A disordered peptide linker spans the 23 Å distance between residues 161 and 173.
The disordered linker peptide that connects the two domains is expected to be in an extended conformation to span the available distance and must lie in and along one edge of the groove passing over the AdoHcy-binding site.
We have previously indicated that an unstructured peptide linker exists spanning residues 162 to 172 and running over the cofactor-binding site in the extended cleft formed by the monomer–monomer interface.
Cross-references: PDB:1P9P
Protein: DP02716 (UniProt P0A873)
Region: residues 162	to 172
Annotation: flexible linker (Disorder function)
Evidence: X-ray crystallography-based structural model with missing residue coordinates used in manual assertion
Supporting statements:
Each monomer consists of a C-terminal domain connected by a flexible linker to an N-terminal AdoMet-binding domain.
The monomer of TrmD consists of two discrete domains connected by an extended flexible linker region of 11 residues 
A disordered peptide linker spans the 23 Å distance between residues 161 and 173.
The disordered linker peptide that connects the two domains is expected to be in an extended conformation to span the available distance and must lie in and along one edge of the groove passing over the AdoHcy-binding site.
We have previously indicated that an unstructured peptide linker exists spanning residues 162 to 172 and running over the cofactor-binding site in the extended cleft formed by the monomer–monomer interface.
Cross-references: PDB:1P9P
Protein: DP02717 (UniProt O95071)
Region: residues 2738	to 2747
Annotation: disorder (Structural state)
Evidence: X-ray crystallography-based structural model with missing residue coordinates used in manual assertion
Supporting statements:
The structure also features three loops, L1 (seven residues), L2 (17 residues) and L3 (seven residues); the longest loop L2 is disordered and is absent from the density map
The final structure does not include 19 of the 113 residues, including the seven last C-­terminal residues, as these regions were disordered in the crystal.
This disordered region correspond to 12 aa of the L2 loop
Cross-references: PDB:3PT3
Protein: DP02718 (UniProt Q8ST83)
Region: residues 116	to 144
Annotation: disorder (Structural state)
Evidence: X-ray crystallography-based structural model with missing residue coordinates used in manual assertion
Supporting statements:
Pho regions flanking the spacer and connecting it to the DNA-binding domain are predicted to be disordered
In crystal form P3121, a longer Pho construct comprising 131 amino acid residues was used for cocrystallization (Supplemental Table 1), but only electron density corresponding to the Pho spacer peptide was visible.
Cross-references: PDB:4C5G
PDB:4C5H
PDB:4C5E
Protein: DP02718 (UniProt Q8ST83)
Region: residues 171	to 246
Annotation: disorder (Structural state)
Evidence: X-ray crystallography-based structural model with missing residue coordinates used in manual assertion
Supporting statements:
Pho regions flanking the spacer and connecting it to the DNA-binding domain are predicted to be disordered
In crystal form P3121, a longer Pho construct comprising 131 amino acid residues was used for cocrystallization (Supplemental Table 1), but only electron density corresponding to the Pho spacer peptide was visible.
Cross-references: PDB:4C5G
PDB:4C5H
PDB:4C5E
Protein: DP02718 (UniProt Q8ST83)
Region: residues 171	to 246
Annotation: flexible linker (Disorder function)
Evidence: X-ray crystallography-based structural model with missing residue coordinates used in manual assertion
Supporting statements:
Pho regions flanking the spacer and connecting it to the DNA-binding domain are predicted to be disordered
The spacer region of Pho, separated from the DNA-binding domain by a long flexible linker, forms a tight complex with the four malignant brain tumor (4MBT) domain of Sfmbt.
Cross-references: PDB:4C5G
PDB:4C5H
PDB:4C5E
Protein: DP02719 (UniProt Q53FT3)
Region: residues 88	to 106
Annotation: disorder (Structural state)
Evidence: X-ray crystallography-based structural model with missing residue coordinates used in manual assertion
Supporting statements:
The E-loop of Phe97Ala mutant was largely disordered
The E-loop containing the Phe97Ala mutation was largely disordered in both monomers, in contrast to the same loop of the wt (Fig. 4c), indicating that Phe97 was responsible for the decreased flexibility of the E-loop as an anchor point (see §4).
Cross-references: PDB:3WW0
Protein: DP02721 (UniProt P32357)
Region: residues 153	to 171
Annotation: disorder (Structural state)
Evidence: X-ray crystallography-based structural model with missing residue coordinates used in manual assertion
Supporting statements:
Aar2pSub is organized in two globular domains, connected via a flexible loop between residues 153 and 171, part of which was cleaved during subtilisin treatment
Cross-references: PDB:3SBT
PDB:3SBS
Protein: DP02721 (UniProt P32357)
Region: residues 153	to 171
Annotation: flexible linker (Disorder function)
Evidence: X-ray crystallography-based structural model with missing residue coordinates used in manual assertion
Supporting statements:
Aar2pSub is organized in two globular domains, connected via a flexible loop between residues 153 and 171, part of which was cleaved during subtilisin treatment
Cross-references: PDB:3SBT
PDB:3SBS
Protein: DP02722 (UniProt P33334)
Region: residues 2087	to 2147
Annotation: disorder (Structural state)
Evidence: X-ray crystallography-based structural model with missing residue coordinates used in manual assertion
Supporting statements:
Prp8pCTF* lacked 16 amino acids at the C terminus compared with Prp8pCTF. In that structure, a 60-residue linker between the domains lacked electron density, demonstrating its intrinsic flexibility
Cross-references: PDB:3SBG
PDB:3SBT
Protein: DP02722 (UniProt P33334)
Region: residues 2087	to 2147
Annotation: flexible linker (Disorder function)
Evidence: X-ray crystallography-based structural model with missing residue coordinates used in manual assertion
Supporting statements:
Prp8pCTF* lacked 16 amino acids at the C terminus compared with Prp8pCTF. In that structure, a 60-residue linker between the domains lacked electron density, demonstrating its intrinsic flexibility
Cross-references: PDB:3SBG
PDB:3SBT
Protein: DP02723 (UniProt Q8VDP3)
Region: residues 487	to 505
Annotation: disorder (Structural state)
Evidence: X-ray crystallography-based structural model with missing residue coordinates used in manual assertion
Supporting statements:
Our results suggest that the CH domain, which is loosely connected to the MO domain by a flexible linker and is far away from the catalytic site, couples F-actin to the enhancement of redox activity of MICALMO-CH by a cooperative mechanism involving a trans interaction between adjacently bound molecules.
The structures of two crystal forms, native 1 and 2 (Table 1), show electron density for residues 8–486 of the MO domain and residues 506–554 and 562–614 of the CH domain (Fig. 1).
Cross-references: PDB:4TXI
Protein: DP02723 (UniProt Q8VDP3)
Region: residues 487	to 505
Annotation: flexible linker (Disorder function)
Evidence: X-ray crystallography-based structural model with missing residue coordinates used in manual assertion
Supporting statements:
Our results suggest that the CH domain, which is loosely connected to the MO domain by a flexible linker and is far away from the catalytic site, couples F-actin to the enhancement of redox activity of MICALMO-CH by a cooperative mechanism involving a trans interaction between adjacently bound molecules.
The structures of two crystal forms, native 1 and 2 (Table 1), show electron density for residues 8–486 of the MO domain and residues 506–554 and 562–614 of the CH domain (Fig. 1).
Cross-references: PDB:4TXI
Protein: DP02724 (UniProt Q13838)
Region: residues 34	to 44
Annotation: disorder (Structural state)
Evidence: X-ray crystallography-based structural model with missing residue coordinates used in manual assertion
Supporting statements:
The corresponding residues in the N terminus of UAP56 (residues 34–44) are disordered, consistent with the limited proteolysis result.
Cross-references: PDB:1T6N
Protein: DP02724 (UniProt Q13838)
Region: residues 34	to 44
Annotation: disorder (Structural state)
Evidence: cleavage assay evidence used in manual assertion
Supporting statements:
The corresponding residues in the N terminus of UAP56 (residues 34–44) are disordered, consistent with the limited proteolysis result.
Cross-references: PDB:1T6N
Protein: DP02726 (UniProt Q42521)
Region: residues 1	to 11
Annotation: disorder (Structural state)
Evidence: X-ray crystallography-based structural model with missing residue coordinates used in manual assertion
Supporting statements:
The first 11 N-terminal residues are disordered, while residues 12–20 assume a conformation resembling that found in the low-pH structure of GadB (1PMM).
Cross-references: PDB:3HBX
Protein: DP02726 (UniProt Q42521)
Region: residues 449	to 502
Annotation: disorder (Structural state)
Evidence: X-ray crystallography-based structural model with missing residue coordinates used in manual assertion
Supporting statements:
Residues 449–502 are disordered in the Gad1 crystal structure at pH 5.5. This C-terminal domain consists of a linker of varying lengths in different plant Gads (residues 449–470 in Gad1, Fig. 3), followed by the well-characterized and conserved CaMBD (residues 471 – 502).
Cross-references: PDB:3HBX
Protein: DP02726 (UniProt Q42521)
Region: residues 449	to 470
Annotation: flexible linker (Disorder function)
Evidence: X-ray crystallography-based structural model with missing residue coordinates used in manual assertion
Supporting statements:
Residues 449–502 are disordered in the Gad1 crystal structure at pH 5.5. This C-terminal domain consists of a linker of varying lengths in different plant Gads (residues 449–470 in Gad1, Fig. 3), followed by the well-characterized and conserved CaMBD (residues 471 – 502).
Cross-references: PDB:3HBX
Protein: DP02726 (UniProt Q42521)
Region: residues 471	to 502
Annotation: protein binding (Molecular function)
Evidence: static light scattering assay evidence used in manual assertion
Supporting statements:
Residues 449–502 are disordered in the Gad1 crystal structure at pH 5.5. This C-terminal domain consists of a linker of varying lengths in different plant Gads (residues 449–470 in Gad1, Fig. 3), followed by the well-characterized and conserved CaMBD (residues 471 – 502).
The CaMBD is located at the C-terminus of the protein and is preceded by a flexible stretch of ∼20 residues. This results in the highly flexible binding mode for attached CaM molecules.
Cross-references: PDB:3HBX
Protein: DP02726 (UniProt Q42521)
Region: residues 471	to 502
Annotation: protein binding (Molecular function)
Evidence: small-angle X-ray scattering evidence used in manual assertion
Supporting statements:
Residues 449–502 are disordered in the Gad1 crystal structure at pH 5.5. This C-terminal domain consists of a linker of varying lengths in different plant Gads (residues 449–470 in Gad1, Fig. 3), followed by the well-characterized and conserved CaMBD (residues 471 – 502).
The CaMBD is located at the C-terminus of the protein and is preceded by a flexible stretch of ∼20 residues. This results in the highly flexible binding mode for attached CaM molecules.
Cross-references: PDB:3HBX
Protein: DP02726 (UniProt Q42521)
Region: residues 1	to 57
Annotation: molecular adaptor activity (Molecular function)
Evidence: X-ray crystallography-based structural model with missing residue coordinates used in manual assertion
Supporting statements:
The N-terminal domain (residues 1–57, Fig. 1 and see Fig. 6) has an important role in the formation and stabilization of the dimer and hexamer.
Cross-references: PDB:3HBX
Protein: DP02726 (UniProt Q42521)
Region: residues 471	to 502
Annotation: molecular function regulator (Molecular function)
Evidence: combinatorial experimental and author inference evidence contained in single publication used in manual assertion
Supporting statements:
CaM activates Gad1 in a unique way by relieving two C-terminal autoinhibition domains of adjacent active sites, forming a 393 kDa Gad1–CaM complex with an unusual 1:3 stoichiometry.
Many plant species like soybean, tobacco, petunia and Arabidopsis, express Gad proteins containing a 30 – 50 residue C-terminal extension compared to the bacterial enzyme sequence. The additional domain has been identified as a CaMBD15 and autoinhibits the Gad protein in the absence of Ca2+/CaM, whereas Gad activity is upregulated upon addition of Ca2+/CaM.
Cross-references: PDB:3HBX
Protein: DP02727 (UniProt Q13526)
Region: residues 39	to 50
Annotation: disorder (Structural state)
Evidence: X-ray crystallography-based structural model with missing residue coordinates used in manual assertion
Supporting statements:
Pin1 contains an N-terminal WW domain and a C-terminal peptidyl-prolyl cis-trans isomerase (PPIase) domain connected by a flexible linker.
residues 39–50 are disordered
Cross-references: PDB:1F8A
Protein: DP02727 (UniProt Q13526)
Region: residues 39	to 50
Annotation: flexible linker (Disorder function)
Evidence: X-ray crystallography-based structural model with missing residue coordinates used in manual assertion
Supporting statements:
Pin1 contains an N-terminal WW domain and a C-terminal peptidyl-prolyl cis-trans isomerase (PPIase) domain connected by a flexible linker.
residues 39–50 are disordered
Cross-references: PDB:1F8A
Protein: DP02728 (UniProt P42166)
Region: residues 51	to 110
Annotation: disorder (Structural state)
Evidence: nuclear magnetic resonance spectroscopy evidence used in manual assertion
Supporting statements:
Human LAP2(1-168) has two structurally independent, non-interacting domains located at residues 1-50 ('LAP2-N') and residues 111-152 (LEM-domain), connected by an approximately 60-residue flexible linker.
Cross-references: PDB:1GJJ
Protein: DP02728 (UniProt P42166)
Region: residues 51	to 110
Annotation: flexible linker (Disorder function)
Evidence: nuclear magnetic resonance spectroscopy evidence used in manual assertion
Supporting statements:
Human LAP2(1-168) has two structurally independent, non-interacting domains located at residues 1-50 ('LAP2-N') and residues 111-152 (LEM-domain), connected by an approximately 60-residue flexible linker.
Cross-references: PDB:1GJJ
Protein: DP02729 (UniProt Q96EP1)
Region: residues 446	to 472
Annotation: disorder (Structural state)
Evidence: X-ray crystallography-based structural model with missing residue coordinates used in manual assertion
Supporting statements:
In both structures, residues 425–445 and 473–663 are modeled, whereas no ordered electron density was observed for residues 446–472.
This incompatibility and the observation that the C terminus of CHFR and the phosphate and ribose groups of the ligand are only ordered in the CHFR-C·AMP2 structure suggest that one molecule of the AMP2 is bound to the protein, with the caveat that we were not able to model the entire ligand linker motif, presumably due to its flexibility.
Cross-references: PDB:2XOZ
PDB:2XOC
PDB:2XOY
PDB:2XP0
Protein: DP02729 (UniProt Q96EP1)
Region: residues 446	to 472
Annotation: flexible linker (Disorder function)
Evidence: X-ray crystallography-based structural model with missing residue coordinates used in manual assertion
Supporting statements:
In both structures, residues 425–445 and 473–663 are modeled, whereas no ordered electron density was observed for residues 446–472.
This incompatibility and the observation that the C terminus of CHFR and the phosphate and ribose groups of the ligand are only ordered in the CHFR-C·AMP2 structure suggest that one molecule of the AMP2 is bound to the protein, with the caveat that we were not able to model the entire ligand linker motif, presumably due to its flexibility.
Cross-references: PDB:2XOZ
PDB:2XOC
PDB:2XOY
PDB:2XP0
Protein: DP02730 (UniProt Q6P1M3)
Region: residues 471	to 484
Annotation: disorder (Structural state)
Evidence: X-ray crystallography-based structural model with missing residue coordinates used in manual assertion
Supporting statements:
The crystal form 1 Lgl2 structure includes 827 of 979 amino acids of the Lgl2 protein construct; there was no electron density for residues 13–17, 471–484, 635–707, and 853–858.
Crystal structure of the human cell polarity protein Lethal Giant Larvae 2 (Lgl2). Unphosphorylated, crystal form 1.
Cross-references: PDB:6N8P
Protein: DP02730 (UniProt Q6P1M3)
Region: residues 631	to 708
Annotation: disorder (Structural state)
Evidence: X-ray crystallography-based structural model with missing residue coordinates used in manual assertion
Supporting statements:
The crystal form 1 Lgl2 structure includes 827 of 979 amino acids of the Lgl2 protein construct; there was no electron density for residues 13–17, 471–484, 635–707, and 853–858.
Crystal structure of the human cell polarity protein Lethal Giant Larvae 2 (Lgl2). Unphosphorylated, crystal form 1.
Cross-references: PDB:6N8P
Protein: DP02730 (UniProt Q6P1M3)
Region: residues 631	to 708
Annotation: flexible linker (Disorder function)
Evidence: X-ray crystallography-based structural model with missing residue coordinates used in manual assertion
Supporting statements:
The crystal form 1 Lgl2 structure includes 827 of 979 amino acids of the Lgl2 protein construct; there was no electron density for residues 13–17, 471–484, 635–707, and 853–858.
Both the unphosphorylated and phosphorylated form 2 structures are missing residues 261–263, 472–485, and 631–708, and the loop residues 554–555 are missing in the unphosphorylated form 2 structure.
Linker separating WD40 repeats 9 and 10
Cross-references: PDB:6N8P
PDB:6N8R
PDB:6N8S
PDB:6N8Q
Protein: DP02730 (UniProt Q6P1M3)
Region: residues 471	to 484
Annotation: flexible linker (Disorder function)
Evidence: X-ray crystallography-based structural model with missing residue coordinates used in manual assertion
Supporting statements:
The crystal form 1 Lgl2 structure includes 827 of 979 amino acids of the Lgl2 protein construct; there was no electron density for residues 13–17, 471–484, 635–707, and 853–858.
Both the unphosphorylated and phosphorylated form 2 structures are missing residues 261–263, 472–485, and 631–708, and the loop residues 554–555 are missing in the unphosphorylated form 2 structure.
Linker separating WD40 repeats 8 and 9
Cross-references: PDB:6N8P
PDB:6N8R
PDB:6N8S
PDB:6N8Q
Protein: DP02730 (UniProt Q6P1M3)
Region: residues 631	to 708
Annotation: phosphorylation display site (Disorder function)
Evidence: mass spectrometry evidence used in manual assertion
Supporting statements:
We examined the phosphorylation of purified Lgl2 treated with purified aPKCι by mass spectrometry (the same sample that was used for crystallization), and found seven phosphorylated serine residues on the 10–11 loop (S641, S645, S649, S653, S660, S663, and S680), which include the previously reported sites
Cross-references: PDB:6N8R
PDB:6N8S
Protein: DP02731 (UniProt Q5U651)
Region: residues 187	to 197
Annotation: disorder (Structural state)
Evidence: X-ray crystallography-based structural model with missing residue coordinates used in manual assertion
Supporting statements:
The current RRA model excludes many residues; 141–142 (N terminus), 154–158 (loop β1-β2), 187–197 (loop α1-β3), 212–220 (loop β3-β4), and 268–285 (C terminus, not part of the RRA) as highlighted in Figures 2A and 2C, and many side chains were also poorly defined in the electron density map.
Similar to the free RA domain structure, the current Rasip1 RA domain model excludes many residues, 141–142 (N terminus), 186–195 (loop α1-β3), 212–220 (loop β3-β4), and 268–285 (C terminus), and many side chains were also poorly defined in the electron density map.
Cross-references: PDB:5KHQ
PDB:5KHO
Protein: DP02731 (UniProt Q5U651)
Region: residues 268	to 285
Annotation: disorder (Structural state)
Evidence: X-ray crystallography-based structural model with missing residue coordinates used in manual assertion
Supporting statements:
The current RRA model excludes many residues; 141–142 (N terminus), 154–158 (loop β1-β2), 187–197 (loop α1-β3), 212–220 (loop β3-β4), and 268–285 (C terminus, not part of the RRA) as highlighted in Figures 2A and 2C, and many side chains were also poorly defined in the electron density map.
Similar to the free RA domain structure, the current Rasip1 RA domain model excludes many residues, 141–142 (N terminus), 186–195 (loop α1-β3), 212–220 (loop β3-β4), and 268–285 (C terminus), and many side chains were also poorly defined in the electron density map.
Cross-references: PDB:5KHQ
PDB:5KHO
Protein: DP02731 (UniProt Q5U651)
Region: residues 268	to 285
Annotation: disorder (Structural state)
Evidence: nuclear magnetic resonance spectroscopy evidence used in manual assertion
Supporting statements:
The current RRA model excludes many residues; 141–142 (N terminus), 154–158 (loop β1-β2), 187–197 (loop α1-β3), 212–220 (loop β3-β4), and 268–285 (C terminus, not part of the RRA) as highlighted in Figures 2A and 2C, and many side chains were also poorly defined in the electron density map.
Similar to the free RA domain structure, the current Rasip1 RA domain model excludes many residues, 141–142 (N terminus), 186–195 (loop α1-β3), 212–220 (loop β3-β4), and 268–285 (C terminus), and many side chains were also poorly defined in the electron density map.
This observation was in agreement with the NMR spectrum of the complex, which showed that most of the sharp peaks remained sharp when in complex with Rap1; this suggested that the unstructured loops remained unstructured in the complex.
The Rasip1 RA domain contains many unstructured loops as demonstrated by both the presence of many sharp peaks in the NMR sfHMQC and the absence of electron density in the crystal structure.
Cross-references: PDB:5KHQ
PDB:5KHO