LiteFold/DisProt huggingface dataset:
Protein: DP03281 (UniProt Q2MKA7)
Region: residues 131	to 146
Annotation: disorder to order (Structural transition)
Evidence: x-ray crystallography evidence used in manual assertion
Supporting statements:
Structure of (unbound) Rspo1-Fu1Fu2 (residues 31–145) at 2 Å resolution. Indicated are disulphide bonds (ball and stick) and disordered residues (dashed line).
Overlay of bound and unbound Rspo1. The arrow indicates a hinge around which the orientation between the Fu1 and Fu2 domains differs by ∼90° between the LGR5-bound and unbound structure of Rspo1.
Cross-references: PDB:4BSO
PDB:4BSU
PDB:4BSR
PDB:4BSS
PDB:4BST
Protein: DP03281 (UniProt Q2MKA7)
Region: residues 131	to 146
Annotation: disorder to order (Structural transition)
Evidence: x-ray crystallography evidence used in manual assertion
Supporting statements:
Overlay of four representative RSPO1 structures in two orientations with free RSPO1 (grey; PDB code 4BSO), RSPO1 in LGR5-RSPO1-RNF43 complex (blue, PDB code 4KNG) and RSPO1 in complex with ZNRF3 (orange and red).
Cross-references: PDB:4BSO
PDB:4CDK
Protein: DP03282 (UniProt Q8L3W1)
Region: residues 208	to 220
Annotation: disorder (Structural state)
Evidence: X-ray crystallography-based structural model with missing residue coordinates used in manual assertion
Supporting statements:
Of the 133 residues in the designed construct, 117 residues were modeled in each of the two molecules in the asymmetric unit. In both molecules, residues 208–220 and 339–341 of VRN1(208–341) were not modeled due to poor electron density at the N and C termini, indicating disorder.
Cross-references: PDB:4I1K
Protein: DP03283 (UniProt O80452)
Region: residues 140	to 211
Annotation: disorder (Structural state)
Evidence: X-ray crystallography-based structural model with missing residue coordinates used in manual assertion
Supporting statements:
The final crystallographic model of the I139M FAC1 enzyme comprises only 616 of the 701 amino acids in this polypeptide (residues
212–273 and 286–839). Whereas 13 of the 85 unstructured amino acids
are part of a loop that forms the Walker A motif, the remainder are
located in the N terminus of this truncated enzyme. Regarding these
latter residues, several computer-based prediction servers (ROBETTA,
GLOBPLOT, FoldIndex, and DRIPPRED) indicate that the entire
stretch of sequence (residues 32–211) between the N-terminal helical
transmembrane domain and the globular catalytic domain is largely
unstructured. 
The proposed configuration between FAC1 and a lipid bilayer is reminiscent
of a “paddleball,” with the globular catalytic domain representing the
“ball” and the transmembrane domains (residues 6–31) and disordered
linker regions (residues 32–211) comprising the anchors and flexible
connectors, respectively. 
The authors state that region from positions 32 to 211 is disordered from computer based predictions. However only the region from 140 to 211 is disordered in the PDB structure (N-terminal region). 
Cross-references: PDB:2A3L
Protein: DP03283 (UniProt O80452)
Region: residues 274	to 285
Annotation: disorder (Structural state)
Evidence: X-ray crystallography-based structural model with missing residue coordinates used in manual assertion
Supporting statements:
The final crystallographic model of the I139M FAC1 enzyme comprises only 616 of the 701 amino acids in this polypeptide (residues
212–273 and 286–839). Whereas 13 of the 85 unstructured amino acids
are part of a loop that forms the Walker A motif, the remainder are
located in the N terminus of this truncated enzyme. Regarding these
latter residues, several computer-based prediction servers (ROBETTA,
GLOBPLOT, FoldIndex, and DRIPPRED) indicate that the entire
stretch of sequence (residues 32–211) between the N-terminal helical
transmembrane domain and the globular catalytic domain is largely
unstructured. 
The region of 13 disordered aminoacids correspond to positions 274 to 285 according to the PDB structure (2A3L).
Cross-references: PDB:2A3L
Protein: DP03283 (UniProt O80452)
Region: residues 274	to 285
Annotation: flexible linker (Disorder function)
Evidence: x-ray crystallography evidence used in manual assertion
Supporting statements:
The final crystallographic model of the I139M FAC1 enzyme comprises only 616 of the 701 amino acids in this polypeptide (residues
212–273 and 286–839). Whereas 13 of the 85 unstructured amino acids
are part of a loop that forms the Walker A motif, the remainder are
located in the N terminus of this truncated enzyme. Regarding these
latter residues, several computer-based prediction servers (ROBETTA,
GLOBPLOT, FoldIndex, and DRIPPRED) indicate that the entire
stretch of sequence (residues 32–211) between the N-terminal helical
transmembrane domain and the globular catalytic domain is largely
unstructured. 
The proposed configuration between FAC1 and a lipid bilayer is reminiscent of a “paddleball,” with the globular catalytic domain representing the “ball” and the transmembrane domains (residues 6–31) and disordered linker regions (residues 32–211) comprising the anchors and flexible connectors, respectively
Cross-references: PDB:2A3L
Protein: DP03284 (UniProt Q8GUI6)
Region: residues 125	to 168
Annotation: disorder (Structural state)
Evidence: X-ray crystallography-based structural model with missing residue coordinates used in manual assertion
Supporting statements:
In our JMJ14CD structure, the region corresponding to human KDM5
ARID-PHD cassette (residues 125–168) has no annotated domain
and is disordered in the structure.
Cross-references: PDB:5YKN
PDB:5YKO
Protein: DP03284 (UniProt Q8GUI6)
Region: residues 196	to 211
Annotation: disorder (Structural state)
Evidence: X-ray crystallography-based structural model with missing residue coordinates used in manual assertion
Supporting statements:
PDB structures of both, free and ligand bound, forms have a range of missing residues from positions 196 to 212.
Cross-references: PDB:5YKN
PDB:5YKO
Protein: DP03285 (UniProt Q8H1D4)
Region: residues 154	to 293
Annotation: disorder (Structural state)
Evidence: nuclear magnetic resonance spectroscopy evidence used in manual assertion
Supporting statements:
The 1H–15N HSQC confirmed that most of the DRB4C is disordered in solution as we observed narrow spectral dispersion in the proton dimension (Supplementary Figure S1E). The random
coil nature of DRB4C was also evident from the chemical
shifts of C-alpha and C-beta. Moreover, the majority of DRB4C resonances assume a negative value in 15N–{1H} hetronuclear NOE corroborating its unstructured nature (Figure 1B). Interestingly, resonances belonging to residues 294–355 (i.e.
DRB4Cc) were absent in the 1H–15N HSQC of DRB4C.
Protein disorder algorithms predicted that DRB4Cc may assume an ordered conformation. Subsequently, a welldispersed 1H–15N HSQC for DRB4Cc implied the presence of a tertiary structure.
The truncated fragments of DRB4; DRB4 (1-153) (hereafter DRB4D1D2), DRB4 (1-75) (hereafter: DRB4D1), DRB4 (80-153) (hereafter: DRB4D2), DRB4 (154-355) (hereafter: DRB4C), DRB4 (294-355) (hereafter: DRB4Cc), DRB4 (72-81 connected to 4-71) (hereafter: DRB4LD1) and DRB4 (72-153) (hereafter: DRB4LD2) were also cloned into pET-30a in a similar way.
The unstructured region of DRB4 is a flexible linker connecting DRB4D1D2 (1-153) and DRB4Cc (294-355).
Protein: DP03285 (UniProt Q8H1D4)
Region: residues 154	to 293
Annotation: flexible linker (Disorder function)
Evidence: nuclear magnetic resonance spectroscopy evidence used in manual assertion
Supporting statements:
The 1H–15N HSQC confirmed that most of the DRB4C is disordered in solution as we observed narrow spectral dispersion in the proton dimension (Supplementary Figure S1E). The random coil nature of DRB4C was also evident from the chemical shifts of C-alpha and C-beta. Moreover, the majority of DRB4C resonances assume a negative value in 15N–{1H} hetronuclear NOE corroborating its unstructured nature (Figure 1B). Interestingly, resonances belonging to residues 294–355 (i.e. DRB4Cc) were absent in the 1H–15N HSQC of DRB4C. Protein disorder algorithms predicted that DRB4Cc may assume an ordered conformation. Subsequently, a welldispersed 1H–15N HSQC for DRB4Cc implied the presence of a tertiary structure.
The truncated fragments of DRB4; DRB4 (1-153) (hereafter DRB4D1D2), DRB4 (1-75) (hereafter: DRB4D1), DRB4 (80-153) (hereafter: DRB4D2), DRB4 (154-355) (hereafter: DRB4C), DRB4 (294-355) (hereafter: DRB4Cc), DRB4 (72-81 connected to 4-71) (hereafter: DRB4LD1) and DRB4 (72-153) (hereafter: DRB4LD2) were also cloned into pET-30a in a similar way.
The unstructured region of DRB4 is a flexible linker connecting DRB4D1D2 (1-153) and DRB4Cc (294-355).
Protein: DP03286 (UniProt Q03479)
Region: residues 549	to 559
Annotation: disorder (Structural state)
Evidence: X-ray crystallography-based structural model with missing residue coordinates used in manual assertion
Supporting statements:
PDB - unmodeled residues 549-559
Cross-references: PDB:1LKX
Protein: DP03287 (UniProt P13022)
Region: residues 271	to 281
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 2–272 (and 2–270 for the second molecule within the asymmetric unit, respectively) of the 281 residues of the α-subunit.
PDB - unmodeled residues 271-281 (Chain A)
Cross-references: PDB:4AKR
Protein: DP03288 (UniProt P13021)
Region: residues 253	to 272
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 2–272 (and 2–270 for the second molecule within the asymmetric unit, respectively) of the 281 residues of the α-subunit and all residues of the β-subunit except for residues 1, 140–145 and 251–272 (253–272 for the second molecule within the asymmetric unit).
PDB - unmodeled residues 253-272 (chain D)
In contrast to the α-tentacle, neither Cap32/34 nor CapZ crystals grown at physiological pH provided an interpretable electron density for the C-terminal segment of the β-subunit (β-tentacle), indicating that this part of the CP molecule is highly mobile.
Cross-references: PDB:4AKR
Protein: DP03288 (UniProt P13021)
Region: residues 253	to 272
Annotation: protein binding (Molecular function)
Evidence: loss-of-function mutant phenotype evidence used in manual assertion
Supporting statements:
Although the β-tentacle sequence is not conserved in general, the three hydrophobic positions (residues L258, L262, and L266 in GgCapZ) at intervals of four residues are conserved (Figure  5) and exchanging them by polar residues abolishes actin-binding 
Mutational analysis done with His-tagged mouse CP alpha1/beta2 (PMID 20969875) 
Cross-references: PDB:4AKR
Protein: DP03288 (UniProt P13021)
Region: residues 251	to 272
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 2–272 (and 2–270 for the second molecule within the asymmetric unit, respectively) of the 281 residues of the α-subunit and all residues of the β-subunit except for residues 1, 140–145 and 251–272 (253–272 for the second molecule within the asymmetric unit)
PDB - unmodeled residues 253-272 (Chain B)
Cross-references: PDB:4AKR
Protein: DP03288 (UniProt P13021)
Region: residues 251	to 272
Annotation: lipid binding (Molecular function)
Evidence: loss-of-function mutant phenotype evidence used in manual assertion
Supporting statements:
the region around the “basic triad” that harbours many solvent exposed lysines and arginines has been proposed to be the PIP2 binding site of CP. A triple mutation of two of the basic residues of the “basic triad” (K256 and R260) together with a closely located arginine of the β-subunit (R225) has been most effective in abolishing PIP2-binding 
Mutational analysis done with chicken CP α1/β1 (PMID 17182619)
Protein: DP03288 (UniProt P13021)
Region: residues 253	to 272
Annotation: lipid binding (Molecular function)
Evidence: loss-of-function mutant phenotype evidence used in manual assertion
Supporting statements:
the region around the “basic triad” that harbours many solvent exposed lysines and arginines has been proposed to be the PIP2 binding site of CP. A triple mutation of two of the basic residues of the “basic triad” (K256 and R260) together with a closely located arginine of the β-subunit (R225) has been most effective in abolishing PIP2-binding 
Mutational analysis done with chicken CP α1/β1 (PMID 17182619)
Protein: DP03289 (UniProt P0ACG8)
Region: residues 111	to 133
Annotation: disorder (Structural state)
Evidence: X-ray crystallography-based structural model with missing residue coordinates used in manual assertion
Supporting statements:
The electron density ends at approximately residue 110, leaving 23 residues unaccounted for in the electron density. Mass spectrometry of the crystals reveals completely intact protein of ~133 amino acids, suggesting that the unobserved residues are present in the crystal lattice but not visible in the electron density.
The C-terminal 23 residues were never visible in electron density maps despite map improvement and refinement, and are presumably disordered, which may contribute to the observed R-factors.
Cross-references: PDB:1DM9
Protein: DP03290 (UniProt Q8RNT4)
Region: residues 19	to 49
Annotation: disorder (Structural state)
Evidence: X-ray crystallography-based structural model with missing residue coordinates used in manual assertion
Supporting statements:
PDB - unmodeled residues 19-49
Cross-references: PDB:4G32
Protein: DP03290 (UniProt Q8RNT4)
Region: residues 19	to 49
Annotation: disorder to order (Structural transition)
Evidence: x-ray crystallography evidence used in manual assertion
Supporting statements:
the 2 Pa_LOX structures available differ mainly in the N-terminal region, with models starting at residues Ile50 (Fig. 1A) and Ala19 (Fig. 1B).
Cross-references: PDB:4G33
Protein: DP03290 (UniProt Q8RNT4)
Region: residues 19	to 49
Annotation: protein binding (Molecular function)
Evidence: x-ray crystallography evidence used in manual assertion
Supporting statements:
The longer N-terminal tail of the structure starting at Ala19 protrudes toward a neighboring molecule, where it is stabilized by a large number of interactions, in particular with the polar head of the phospholipid
Cross-references: PDB:4G33
Protein: DP03291 (UniProt Q9UK55)
Region: residues 22	to 59
Annotation: disorder (Structural state)
Evidence: X-ray crystallography-based structural model with missing residue coordinates used in manual assertion
Supporting statements:
The first 38 residues of ZPI, which include many acidic amino acids, are disordered and were not built in the structure
According to PDB available sequence, the 38 firsts residues correspond to the annotated region (22-59) as the protein structure is built from A60, considered in the structure as residue 39. Residues 1-21 correspond to the signal peptide
Cross-references: PDB:3F1S
Protein: DP03291 (UniProt Q9UK55)
Region: residues 22	to 60
Annotation: disorder (Structural state)
Evidence: X-ray crystallography-based structural model with missing residue coordinates used in manual assertion
Supporting statements:
For the ZPI moiety, the whole of the backbone is visible (Fig.1A), with the exception of the first 39 residues, all of which are part of the N-terminal tail, which is an extension that is not present in other serpins. 
According to PDB available sequence, the 39 firsts residues correspond to the annotated region (22-60). Residues 1-21 correspond to the signal peptide
Cross-references: PDB:3H5C
Protein: DP03292 (UniProt P00742)
Region: residues 90	to 120
Annotation: disorder (Structural state)
Evidence: X-ray crystallography-based structural model with missing residue coordinates used in manual assertion
Supporting statements:
All atoms of the inhibitors and of FXa lie in well-defined electron density except the EGF1 domain which was not visible
EGF1 domain is comprised on residues 90-120
Cross-references: PDB:1EZQ
PDB:1F0S
PDB:1F0R
Protein: DP03292 (UniProt P00742)
Region: residues 90	to 120
Annotation: disorder (Structural state)
Evidence: X-ray crystallography-based structural model with missing residue coordinates used in manual assertion
Supporting statements:
The EGF1 domain, disordered in the tetragonal, arginine-bound crystal form, was suggested to become ordered in the presence of calcium (24). However, the orthorhombic crystals of fXazDX-9065a grown at 10 mM calcium also show apparent disorder of the EGF1 domain. Furthermore, the crystal packing of the two crystal forms is not compatible with a unique EGF1 orientation (relative to EGF2)
EGF1 domain is comprised on residues 90-120
Cross-references: PDB:1FAX
Protein: DP03292 (UniProt P00742)
Region: residues 90	to 126
Annotation: disorder (Structural state)
Evidence: X-ray crystallography-based structural model with missing residue coordinates used in manual assertion
Supporting statements:
The electron density for the factor Xa/ZK-807834 complex indicates that the first residue in the light chain is Lys-L87 and no electron density was observed for the EGF1 domain. 
EGF1 domain is comprised on residues 90-120
Lys-L87 corresponds to Lys 127 in protein original sequence
However, the protein used by Kamata et al. (9) included the first EGF domain of factor Xa, which was apparently missing from our own construct
Cross-references: PDB:1FJS
Protein: DP03292 (UniProt P00742)
Region: residues 90	to 120
Annotation: disorder (Structural state)
Evidence: X-ray crystallography-based structural model with missing residue coordinates used in manual assertion
Supporting statements:
The EGF-1 domain is not visible in the electron density maps probably because of disorder, and the rather high free R factors might relate to this disordered EGF-1 domain. 
EGF1 domain is comprised on residues 90-120
Cross-references: PDB:1LPG
PDB:1LPK
PDB:1LPZ
PDB:1LQD
Protein: DP03292 (UniProt P00742)
Region: residues 90	to 120
Annotation: disorder (Structural state)
Evidence: X-ray crystallography-based structural model with missing residue coordinates used in manual assertion
Supporting statements:
All atoms of the inhibitors and of fXa lie in well-defined electron density except the EGF1 domain that was not visible.
EGF1 domain is comprised on residues 90-120
Cross-references: PDB:1NFU
PDB:1NFY
PDB:1NFW
PDB:1NFX
Protein: DP03292 (UniProt P00742)
Region: residues 90	to 120
Annotation: disorder (Structural state)
Evidence: X-ray crystallography-based structural model with missing residue coordinates used in manual assertion
Supporting statements:
X-ray structure analysis confirmed the biochemical characterisation and also revealed that the N-terminal epidermal growth factor (EGF)-like domain is flexibly disordered in crystals
We report here the molecular consituents of these chemically characterized FXa crystals and the refined strcuture of the truncated FXa molecule (Fig. 1), which consists of the second EGF module, the catalytic domain of activated factor X and a flexibly disordered N-terminal EGF. 
EGF1 domain is comprised on residues 90-120
This led us to conclude that the first EGF domain might be flexibly disordered so that subsequent refinement was based upon this premise
However, there was no indication of a Gla domain and the N-terminal EGF module still remained disordered
The final electron and difference density maps showed no evidence of a Gla domain or the N-terminal EGF module
Due to the disorder of the first EGF module, however, the FXa structure described here begins with Cys389 (Fig. 1)
In contrast to the foregoing, the final electron density did not show any region assignable to the N-terminal EGF domain of FXa. Since biochemical analysis indicated presence of the module, it must be concluded that it is flexibly disordered in the crystal about its heptapeptide interdomain bridge (Fig. 1).
Cross-references: PDB:1HCG
Protein: DP03292 (UniProt P00742)
Region: residues 90	to 120
Annotation: disorder (Structural state)
Evidence: X-ray crystallography-based structural model with missing residue coordinates used in manual assertion
Supporting statements:
The EGF-1 domain is not visible in the electron density maps probably because of disorder, and the rather high free R factors might relate to this disordered EGF-1 domain.
EGF1 domain is comprised on residues 90-120
Cross-references: PDB:2BMG
Protein: DP03292 (UniProt P00742)
Region: residues 90	to 120
Annotation: disorder (Structural state)
Evidence: X-ray crystallography-based structural model with missing residue coordinates used in manual assertion
Supporting statements:
The EGF-1 domain is not visible in the electron density maps probably because of disorder, and the rather high free R-factors might relate to this disordered EGF-1 domain.
EGF1 domain is comprised on residues 90-120
Cross-references: PDB:2BQ7
PDB:2BOH
PDB:2BQW
PDB:2BQ6
Protein: DP03292 (UniProt P00742)
Region: residues 90	to 120
Annotation: disorder (Structural state)
Evidence: X-ray crystallography-based structural model with missing residue coordinates used in manual assertion
Supporting statements:
 Surprisingly, the N-terminal EGF domain (EGF1) was found to be disordered. Numerous sparse density peaks in this region were observed in electron density maps, but efforts to trace a backbone through these
peaks did not improve refinement statistics or result in improved density. The EGF1 domain was therefore omitted from the model
EGF1 domain is comprised on residues 90-120
The EGF1 domain (transparent white) was disordered and modeled using the EGF1 domain from PDB 1XKA.
Cross-references: PDB:1P0S
Protein: DP03292 (UniProt P00742)
Region: residues 90	to 120
Annotation: disorder (Structural state)
Evidence: X-ray crystallography-based structural model with missing residue coordinates used in manual assertion
Supporting statements:
The entire N-terminal EGF1 domain, and its leading pentapeptide, which is flexibly disordered in other des-fXastructures was not located in the electron density maps. 
EGF1 domain is comprised on residues 90-120
Cross-references: PDB:2H9E
Protein: DP03292 (UniProt P00742)
Region: residues 90	to 120
Annotation: disorder (Structural state)
Evidence: X-ray crystallography-based structural model with missing residue coordinates used in manual assertion
Supporting statements:
The majority of the rest of the protein is in well-determined electron density, except for the EGF1 domain, which was not visible.
EGF1 domain is comprised on residues 90-120
Cross-references: PDB:4Y76
PDB:4Y79
PDB:2J94
PDB:2J95
Protein: DP03292 (UniProt P00742)
Region: residues 90	to 120
Annotation: disorder (Structural state)
Evidence: X-ray crystallography-based structural model with missing residue coordinates used in manual assertion
Supporting statements:
In addition, the whole N-terminal EGF1 module, and its leading pentapeptide, is flexibly disordered as in other des-fXa structures
EGF1 domain is comprised on residues 90-120
Cross-references: PDB:2P3F
Protein: DP03292 (UniProt P00742)
Region: residues 90	to 120
Annotation: disorder (Structural state)
Evidence: X-ray crystallography-based structural model with missing residue coordinates used in manual assertion
Supporting statements:
There is no electron density observed for the first EGF domain, thus models for the EGF1 domain were not included in subsequent refinement steps.
EGF1 domain is comprised on residues 90-120
Cross-references: PDB:2Q1J