LiteFold/DisProt huggingface dataset:
Protein: DP02768 (UniProt P09950)
Region: residues 538	to 548
Annotation: disorder to order (Structural transition)
Evidence: X-ray crystallography-based structural model with missing residue coordinates used in manual assertion
Supporting statements:
CT is comprised of residues 538–548, the last 11 residues of the eukaryote-specific C-terminal extension in ALASSc. The ordered CTA element from the PLP-free subunit also contributed to the assembled active site of the opposite B subunit.
PLP binding is coupled to disorder-order transitions in three distinct regions of ALAS
Cross-references: PDB:5TXT
PDB:5TXR
Protein: DP02769 (UniProt P06782)
Region: residues 200	to 214
Annotation: disorder (Structural state)
Evidence: X-ray crystallography-based structural model with missing residue coordinates used in manual assertion
Supporting statements:
The activation loop of the kinase (residues 200-215) enclosed between the highly conserved DFG and APE motifs (Fig. 1B) is disordered in the current structure"..."The current structure of Snf1-KD is in the unphosphorylated form. It has been reported that mutating the Thr residue in the activation loop to an Asp residue can confer partial activity to AMPK [18,19]. We have therefore produced crystals of the T210D mutant of yeast Snf1-KD and determined its structure at 2.7 A˚ resolution. This structure showed that the activation loop is still disordered in the T210D mutant

This structure corresponds to an unphosphorylated state and also the T210D phspophomimetic mutant
Cross-references: PDB:3HYH
Protein: DP02769 (UniProt P06782)
Region: residues 197	to 212
Annotation: disorder (Structural state)
Evidence: X-ray crystallography-based structural model with missing residue coordinates used in manual assertion
Supporting statements:
Snf1-pKD displays a ‘closed’ conformation, although the phosphorylated Thr 210 is invisible,

This structure corresponds to an active form that is phosphorylated on the activation loop residue T210 (this is part of the disordered region)
Cross-references: PDB:3DAE
Protein: DP02769 (UniProt P06782)
Region: residues 197	to 212
Annotation: molecular function activator activity (Molecular function)
Evidence: x-ray crystallography evidence used in manual assertion
Supporting statements:
A new inhibited conformation of the KD is observed in a DFG-out conformation and with the glycine-rich loop adopting a structure that blocks ATP binding to the active site.
A large part of the activation segment of the KD, including Thr210 that is phosphorylated for activation, is ordered in the new structure. These residues are positioned far from the rest of the KD (Fig. 1  c). 
This region corresponds to the activation loop that contains T210. This structure reports an unphosphorylated and inactive form of the enzyme. Phosphorylation at T210 leads to disorder in a larger region of the activation loop (197-212) and when the domain is in the unphosphorylated inhibited conformation, structuring is observed and only residues 199-205 remain disordered. 
Cross-references: PDB:3MN3
Protein: DP02770 (UniProt P01127)
Region: residues 106	to 119
Annotation: disorder (Structural state)
Evidence: X-ray crystallography-based structural model with missing residue coordinates used in manual assertion
Supporting statements:
The strand connections, denoted as loops I, II and III, range from residues Ile25-Leu38, Cys53-Val58 and Val78 -Lys81, respectively, are exposed to solvent and show partial disorder in all three independent monomers
Because processing removes residues 1-81 from the mature protein form, the L1 loop residue numbering and boundaries are as follows: residue Ile25 named by the authors corresponds to Ile 106 in the UNIPROT entry, and Leu 38 named by the authors corresponds to Leu 119.
Cross-references: PDB:1PDG
Protein: DP02770 (UniProt P01127)
Region: residues 106	to 119
Annotation: disorder to order (Structural transition)
Evidence: x-ray crystallography evidence used in manual assertion
Supporting statements:
A large-scale structural organization and rearrangement is observed for PDGF-B upon receptor binding, in which the PDGF-B L1 loop, disordered in the structure of the free form, adopts a highly specific conformation to form hydrophobic interactions with the third Ig domain of PDGFRbeta
The loop itself is exquisitely configured in the complex, with the aromatic ring of Phe37 at the center of the hydrophobic core, and numerous intraloop hydrogen bonds to maintain main chain peptide conformation (Fig. 3C). Therefore, this loop has an intrinsic propensity to fold into the observed conformation. In support of this notion, the L1 loop of the propeptide-bound PDGF-A, which is only marginally stabilized at its base by the interaction with the propeptide, is ordered and adopts a similar conformation to PDGF-B (Fig. S3D). Hence, the free PDGF-B L1 loop, which was disordered in that structure, may exist in equilibrium between folded and unfolded states, the former only selected by receptor binding.
Figure 4 Legend: Comparison between the free PDGF-B (PDB code 1PDG) dimer (red) and the PDGFRβ-bound PDGF-B dimer (cyan for the protruding protomer and green for the receding protomer) shows that PDGFRβ-binding induces the structural organization of the previously disordered large L1 loop
Because processing removes residues 1-81 from the mature protein form, the L1 loop residue numbering and boundaries are as follows: residue Ile25 named by the authors corresponds to Ile 106 in the UNIPROT entry, and Leu 38 named by the authors corresponds to Leu 119. The Phe 37 residue named by the authors corresponds to Phe 118 in the UNIPROT entry
Cross-references: PDB:3MJG
Protein: DP02770 (UniProt P01127)
Region: residues 106	to 119
Annotation: platelet-derived growth factor receptor binding (Molecular function)
Evidence: x-ray crystallography evidence used in manual assertion
Supporting statements:
A large-scale structural organization and rearrangement is observed for PDGF-B upon receptor binding, in which the PDGF-B L1 loop, disordered in the structure of the free form, adopts a highly specific conformation to form hydrophobic interactions with the third Ig domain of PDGFRbeta
Because processing removes residues 1-81 from the mature protein form, the L1 loop residue numbering and boundaries are as follows: residue Ile25 named by the authors corresponds to Ile 106 in the UNIPROT entry, and Leu 38 named by the authors corresponds to Leu 119. The Phe 37 residue named by the authors corresponds to Phe 118 in the UNIPROT entry
Figure 4 Legend: Comparison between the free PDGF-B (PDB code 1PDG) dimer (red) and the PDGFRβ-bound PDGF-B dimer (cyan for the protruding protomer and green for the receding protomer) shows that PDGFRβ-binding induces the structural organization of the previously disordered large L1 loop
The L1 loop becomes ordered as a part of the recognition of the receptor PDGFRbeta
Cross-references: PDB:3MJG
Protein: DP02772 (UniProt P0DTC2)
Region: residues 70	to 79
Annotation: disorder (Structural state)
Evidence: cryogenic electron microscopy-based structural model with missing residue coordinates used in manual assertion
Supporting statements:
The atomic model comprises residues 27-1147, with internal breaks corresponding to flexible regions (including part of the RBM), and lacks the C-terminal most segment (including the heptad repeat 2) that is not visible in the map, as is the case for all S structures determined to date.
Cross-references: PDB:6VYB
PDB:6VXX
Protein: DP02772 (UniProt P0DTC2)
Region: residues 144	to 164
Annotation: disorder (Structural state)
Evidence: cryogenic electron microscopy-based structural model with missing residue coordinates used in manual assertion
Supporting statements:
The atomic model comprises residues 27-1147, with internal breaks corresponding to flexible regions (including part of the RBM), and lacks the C-terminal most segment (including the heptad repeat 2) that is not visible in the map, as is the case for all S structures determined to date.
Cross-references: PDB:6VYB
PDB:6VXX
Protein: DP02772 (UniProt P0DTC2)
Region: residues 173	to 185
Annotation: disorder (Structural state)
Evidence: cryogenic electron microscopy-based structural model with missing residue coordinates used in manual assertion
Supporting statements:
The atomic model comprises residues 27-1147, with internal breaks corresponding to flexible regions (including part of the RBM), and lacks the C-terminal most segment (including the heptad repeat 2) that is not visible in the map, as is the case for all S structures determined to date.
Cross-references: PDB:6VYB
PDB:6VXX
Protein: DP02772 (UniProt P0DTC2)
Region: residues 246	to 262
Annotation: disorder (Structural state)
Evidence: cryogenic electron microscopy-based structural model with missing residue coordinates used in manual assertion
Supporting statements:
The atomic model comprises residues 27-1147, with internal breaks corresponding to flexible regions (including part of the RBM), and lacks the C-terminal most segment (including the heptad repeat 2) that is not visible in the map, as is the case for all S structures determined to date.
Cross-references: PDB:6VYB
PDB:6VXX
Protein: DP02772 (UniProt P0DTC2)
Region: residues 469	to 488
Annotation: disorder (Structural state)
Evidence: cryogenic electron microscopy-based structural model with missing residue coordinates used in manual assertion
Supporting statements:
The atomic model comprises residues 27-1147, with internal breaks corresponding to flexible regions (including part of the RBM), and lacks the C-terminal most segment (including the heptad repeat 2) that is not visible in the map, as is the case for all S structures determined to date.
Cross-references: PDB:6VYB
PDB:6VXX
Protein: DP02772 (UniProt P0DTC2)
Region: residues 621	to 640
Annotation: disorder (Structural state)
Evidence: cryogenic electron microscopy-based structural model with missing residue coordinates used in manual assertion
Supporting statements:
The atomic model comprises residues 27-1147, with internal breaks corresponding to flexible regions (including part of the RBM), and lacks the C-terminal most segment (including the heptad repeat 2) that is not visible in the map, as is the case for all S structures determined to date.
Cross-references: PDB:6VYB
PDB:6VXX
Protein: DP02772 (UniProt P0DTC2)
Region: residues 677	to 687
Annotation: disorder (Structural state)
Evidence: cryogenic electron microscopy-based structural model with missing residue coordinates used in manual assertion
Supporting statements:
The atomic model comprises residues 27-1147, with internal breaks corresponding to flexible regions (including part of the RBM), and lacks the C-terminal most segment (including the heptad repeat 2) that is not visible in the map, as is the case for all S structures determined to date.
Cross-references: PDB:6VYB
PDB:6VXX
Protein: DP02772 (UniProt P0DTC2)
Region: residues 828	to 853
Annotation: disorder (Structural state)
Evidence: cryogenic electron microscopy-based structural model with missing residue coordinates used in manual assertion
Supporting statements:
The atomic model comprises residues 27-1147, with internal breaks corresponding to flexible regions (including part of the RBM), and lacks the C-terminal most segment (including the heptad repeat 2) that is not visible in the map, as is the case for all S structures determined to date.
Cross-references: PDB:6VYB
PDB:6VXX
Protein: DP02772 (UniProt P0DTC2)
Region: residues 1148	to 1273
Annotation: disorder (Structural state)
Evidence: cryogenic electron microscopy-based structural model with missing residue coordinates used in manual assertion
Supporting statements:
The atomic model comprises residues 27-1147, with internal breaks corresponding to flexible regions (including part of the RBM), and lacks the C-terminal most segment (including the heptad repeat 2) that is not visible in the map, as is the case for all S structures determined to date.
Cross-references: PDB:6VYB
PDB:6VXX
Protein: DP02772 (UniProt P0DTC2)
Region: residues 1	to 26
Annotation: disorder (Structural state)
Evidence: cryogenic electron microscopy-based structural model with missing residue coordinates used in manual assertion
Supporting statements:
Our final model spans S residues 27 to 1146, with several flexible loops omitted. Like all previously reported coronavirus S ectodomain structures, the density for 2019-nCoV S begins to fade after the connector domain, reflecting the flexibility of the heptad repeat 2 domain in the prefusion conformation.
Cross-references: PDB:6VSB
Protein: DP02772 (UniProt P0DTC2)
Region: residues 67	to 80
Annotation: disorder (Structural state)
Evidence: cryogenic electron microscopy-based structural model with missing residue coordinates used in manual assertion
Supporting statements:
Our final model spans S residues 27 to 1146, with several flexible loops omitted. Like all previously reported coronavirus S ectodomain structures, the density for 2019-nCoV S begins to fade after the connector domain, reflecting the flexibility of the heptad repeat 2 domain in the prefusion conformation.
Cross-references: PDB:6VSB
Protein: DP02772 (UniProt P0DTC2)
Region: residues 142	to 154
Annotation: disorder (Structural state)
Evidence: cryogenic electron microscopy-based structural model with missing residue coordinates used in manual assertion
Supporting statements:
Our final model spans S residues 27 to 1146, with several flexible loops omitted. Like all previously reported coronavirus S ectodomain structures, the density for 2019-nCoV S begins to fade after the connector domain, reflecting the flexibility of the heptad repeat 2 domain in the prefusion conformation.
Cross-references: PDB:6VSB
Protein: DP02772 (UniProt P0DTC2)
Region: residues 246	to 262
Annotation: disorder (Structural state)
Evidence: cryogenic electron microscopy-based structural model with missing residue coordinates used in manual assertion
Supporting statements:
Our final model spans S residues 27 to 1146, with several flexible loops omitted. Like all previously reported coronavirus S ectodomain structures, the density for 2019-nCoV S begins to fade after the connector domain, reflecting the flexibility of the heptad repeat 2 domain in the prefusion conformation.
Cross-references: PDB:6VSB
Protein: DP02772 (UniProt P0DTC2)
Region: residues 455	to 490
Annotation: disorder (Structural state)
Evidence: cryogenic electron microscopy-based structural model with missing residue coordinates used in manual assertion
Supporting statements:
Our final model spans S residues 27 to 1146, with several flexible loops omitted. Like all previously reported coronavirus S ectodomain structures, the density for 2019-nCoV S begins to fade after the connector domain, reflecting the flexibility of the heptad repeat 2 domain in the prefusion conformation.
This disordered region corresponds to the so called RBM or Receptor Binding Motif, a long flexible loop that is disordered and flexible in the unbound conformation, but becomes ordered in the ACE2-bound form
Cross-references: PDB:6VSB
Protein: DP02772 (UniProt P0DTC2)
Region: residues 621	to 637
Annotation: disorder (Structural state)
Evidence: cryogenic electron microscopy-based structural model with missing residue coordinates used in manual assertion
Supporting statements:
Our final model spans S residues 27 to 1146, with several flexible loops omitted. Like all previously reported coronavirus S ectodomain structures, the density for 2019-nCoV S begins to fade after the connector domain, reflecting the flexibility of the heptad repeat 2 domain in the prefusion conformation.
Cross-references: PDB:6VSB
Protein: DP02772 (UniProt P0DTC2)
Region: residues 673	to 686
Annotation: disorder (Structural state)
Evidence: cryogenic electron microscopy-based structural model with missing residue coordinates used in manual assertion
Supporting statements:
Our final model spans S residues 27 to 1146, with several flexible loops omitted. Like all previously reported coronavirus S ectodomain structures, the density for 2019-nCoV S begins to fade after the connector domain, reflecting the flexibility of the heptad repeat 2 domain in the prefusion conformation.
Cross-references: PDB:6VSB
Protein: DP02772 (UniProt P0DTC2)
Region: residues 829	to 852
Annotation: disorder (Structural state)
Evidence: cryogenic electron microscopy-based structural model with missing residue coordinates used in manual assertion
Supporting statements:
Our final model spans S residues 27 to 1146, with several flexible loops omitted. Like all previously reported coronavirus S ectodomain structures, the density for 2019-nCoV S begins to fade after the connector domain, reflecting the flexibility of the heptad repeat 2 domain in the prefusion conformation.
Cross-references: PDB:6VSB
Protein: DP02772 (UniProt P0DTC2)
Region: residues 1147	to 1208
Annotation: disorder (Structural state)
Evidence: cryogenic electron microscopy-based structural model with missing residue coordinates used in manual assertion
Supporting statements:
Our final model spans S residues 27 to 1146, with several flexible loops omitted. Like all previously reported coronavirus S ectodomain structures, the density for 2019-nCoV S begins to fade after the connector domain, reflecting the flexibility of the heptad repeat 2 domain in the prefusion conformation.
Cross-references: PDB:6VSB
Protein: DP02772 (UniProt P0DTC2)
Region: residues 319	to 332
Annotation: disorder (Structural state)
Evidence: X-ray crystallography-based structural model with missing residue coordinates used in manual assertion
Supporting statements:
The final model contains residues Thr333 to Gly526 of the SARS-CoV-2 RBD, residues Ser19 to Asp615 of the ACE2 N-terminal peptidase domain, one zinc ion, four NAG glycans linked to ACE2 Asn90, Asn322 and Asn546 and to RBD Asn343, as well as 80 water molecules.
Receptor-binding domain (RBD, 319-542) of the Spike glycoprotein
Cross-references: PDB:6M0J
Protein: DP02772 (UniProt P0DTC2)
Region: residues 527	to 541
Annotation: disorder (Structural state)
Evidence: X-ray crystallography-based structural model with missing residue coordinates used in manual assertion
Supporting statements:
The final model contains residues Thr333 to Gly526 of the SARS-CoV-2 RBD, residues Ser19 to Asp615 of the ACE2 N-terminal peptidase domain, one zinc ion, four NAG glycans linked to ACE2 Asn90, Asn322 and Asn546 and to RBD Asn343, as well as 80 water molecules.
Receptor-binding domain (RBD, 319-542) of the Spike glycoprotein
Cross-references: PDB:6M0J
Protein: DP02772 (UniProt P0DTC2)
Region: residues 319	to 332
Annotation: disorder (Structural state)
Evidence: cryogenic electron microscopy-based structural model with missing residue coordinates used in manual assertion
Supporting statements:
Missing electron density region identified upon visual inspection of the structure inside the receptor-binding domain (RBD, 319-542) of the Spike glycoprotein
Cross-references: PDB:6W41
Protein: DP02772 (UniProt P0DTC2)
Region: residues 527	to 541
Annotation: disorder (Structural state)
Evidence: cryogenic electron microscopy-based structural model with missing residue coordinates used in manual assertion
Supporting statements:
Missing electron density region identified upon visual inspection of the structure inside the receptor-binding domain (RBD, 319-542) of the Spike glycoprotein
Cross-references: PDB:6W41
Protein: DP02772 (UniProt P0DTC2)
Region: residues 319	to 541
Annotation: protein binding (Molecular function)
Evidence: cryogenic electron microscopy evidence used in manual assertion
Supporting statements:
Here, we present cryo-electron microscopy structures of full-length human ACE2 in the presence of the neutral amino acid transporter B0AT1 with or without the receptor binding domain (RBD) of the surface spike glycoprotein (S protein) of SARS-CoV-2, both at an overall resolution of 2.9 angstroms, with a local resolution of 3.5 angstroms at the ACE2-RBD interface.
Cross-references: PDB:6M17
EMDB:30039
EMDB:30046
Protein: DP02772 (UniProt P0DTC2)
Region: residues 319	to 335
Annotation: disorder (Structural state)
Evidence: cryogenic electron microscopy-based structural model with missing residue coordinates used in manual assertion
Supporting statements:
Here, we present cryo-electron microscopy structures of full-length human ACE2 in the presence of the neutral amino acid transporter B0AT1 with or without the receptor binding domain (RBD) of the surface spike glycoprotein (S protein) of SARS-CoV-2, both at an overall resolution of 2.9 angstroms, with a local resolution of 3.5 angstroms at the ACE2-RBD interface.
Missing electron density region identified upon visual inspection of the structure.
Cross-references: PDB:6M17
EMDB:30039
EMDB:30046
Protein: DP02772 (UniProt P0DTC2)
Region: residues 519	to 541
Annotation: disorder (Structural state)
Evidence: cryogenic electron microscopy-based structural model with missing residue coordinates used in manual assertion
Supporting statements:
Here, we present cryo-electron microscopy structures of full-length human ACE2 in the presence of the neutral amino acid transporter B0AT1 with or without the receptor binding domain (RBD) of the surface spike glycoprotein (S protein) of SARS-CoV-2, both at an overall resolution of 2.9 angstroms, with a local resolution of 3.5 angstroms at the ACE2-RBD interface.
Missing electron density region identified upon visual inspection of the structure.
Cross-references: PDB:6M17
EMDB:30039
EMDB:30046
Protein: DP02772 (UniProt P0DTC2)
Region: residues 680	to 685
Annotation: limited proteolysis display site (Disorder function)
Evidence: combinatorial experimental and author inference evidence contained in single publication used in manual assertion
Supporting statements:
Despite a high similarity with the genome sequence of SARS-CoV and SARS-like CoVs, we identified a peculiar furin-like cleavage site in the Spike protein of the 2019-nCoV, lacking in the other SARS-like CoVs.
In this article, we focus on a specific furin-like protease recognition pattern present in the vicinity of one of the maturation sites of the S protein (Fig. 1B) that may have significant functional implications for virus entry.
For instance, the pathogenesis of some CoV has been previously related to the presence of a furin-like cleavage site in the S-protein sequence. For example, the insertion of a similar cleavage site in the infectious bronchitis virus (IBV) S-protein results in higher pathogenicity, pronounced neural symptoms and neurotropism in infected chickens (Cheng et al., 2019).
Similarly, in the case of influenza virus, low-pathogenicity forms of influenza virus contain a single basic residue at the cleavage site, which is cleaved by trypsin-like proteases and the tissue distribution of the activating protease(s) typically restricts infections to the respiratory and/or intestinal organs (Sun et al., 2010). Conversely, the highly pathogenic forms of influenza have a furin-like cleavage site cleaved by different cellular proteases, including furin, which are expressed in a wide variety of cell types allowing a widening of the cell tropism of the virus (Kido et al., 2012).
This furin-like cleavage site, is supposed to be cleaved during virus egress (Mille and Whittaker, 2014) for S-protein “priming” and may provide a gain-of-function to the 2019-nCoV for efficient spreading in the human population compared to other lineage b betacoronaviruses.