LiteFold/DisProt huggingface dataset:
Protein: DP03150 (UniProt Q99598)
Region: residues 275	to 290
Annotation: disorder (Structural state)
Evidence: X-ray crystallography-based structural model with missing residue coordinates used in manual assertion
Supporting statements:
Upon visual inspection of the crystal structure we identified this region as intrinsically disordered, as described in 21552258
Cross-references: PDB:3PJA
PDB:3QB5
Protein: DP03151 (UniProt Q13363)
Region: residues 357	to 378
Annotation: disorder (Structural state)
Evidence: X-ray crystallography-based structural model with missing residue coordinates used in manual assertion
Supporting statements:
Despite an additional 25 residues in the WT and A123V CtBP1(28–378), only four additional residues are evident in the electron density maps and modeled in our final structures (Fig. 5). These results are consistent with findings on rat CtBP that the C terminus is largely disordered (31).
Cross-references: PDB:6CDF
Protein: DP03152 (UniProt P42574)
Region: residues 57	to 66
Annotation: disorder (Structural state)
Evidence: X-ray crystallography-based structural model with missing residue coordinates used in manual assertion
Supporting statements:
The P3-1 structure contains a dimer in the asymmetric unit and resolves ∼80% of the amino acids due to a number of disordered loops.
First, loop-1 (L1), which to our knowledge is visible in every C3 and C7 structure solved to date, is disordered in the structure of P3. This includes disorder of Arg64, one of the primary residues responsible for binding the P1 aspartate in caspase substrates.
Cross-references: PDB:4JQY
PDB:4JQZ
Protein: DP03152 (UniProt P42574)
Region: residues 201	to 211
Annotation: disorder (Structural state)
Evidence: X-ray crystallography-based structural model with missing residue coordinates used in manual assertion
Supporting statements:
The P3-1 structure contains a dimer in the asymmetric unit and resolves ∼80% of the amino acids due to a number of disordered loops.
Loop-3 (L3), or the “activation loop,” which forms the primary substrate binding groove in the active enzyme, is pulled out of the active site in both P3 monomers, although one is partially disordered whereas the other is fully resolved (Fig. 1 A and B). This could be caused in part by asymmetric crystal packing contacts that appear to stabilize the single L3 resolved in our structure, although the existing structures of P7 (PDB ID codes 1K88 and 1GQF) also reveal a variety of ordered and disordered L3s, suggesting that this loop samples a large number of conformations in P3 and P7 (8, 9).
Cross-references: PDB:4JQY
PDB:4JQZ
Protein: DP03152 (UniProt P42574)
Region: residues 165	to 185
Annotation: disorder (Structural state)
Evidence: X-ray crystallography-based structural model with missing residue coordinates used in manual assertion
Supporting statements:
The P3-1 structure contains a dimer in the asymmetric unit and resolves ∼80% of the amino acids due to a number of disordered loops.
Cross-references: PDB:4JQY
PDB:4JQZ
PDB:4JR0
Protein: DP03152 (UniProt P42574)
Region: residues 174	to 184
Annotation: disorder (Structural state)
Evidence: X-ray crystallography-based structural model with missing residue coordinates used in manual assertion
Supporting statements:
Residues belonging to loop 2 are not resolved.
Cross-references: PDB:3DEI
Protein: DP03153 (UniProt Q658P3)
Region: residues 1	to 28
Annotation: disorder (Structural state)
Evidence: X-ray crystallography-based structural model with missing residue coordinates used in manual assertion
Supporting statements:
The N-terminal His-tag and Steap3 residues 1–28 are not observed in the crystal structure. However, Western blot analyses of the crystallized
material, using anti-His6 antibodies, indicate that these N-terminal residues are indeed present and are therefore disordered in the crystal.
Cross-references: PDB:2VNS
PDB:2VQ3
Protein: DP03154 (UniProt P35207)
Region: residues 542	to 606
Annotation: disorder (Structural state)
Evidence: X-ray crystallography-based structural model with missing residue coordinates used in manual assertion
Supporting statements:
The DExH helicase core of Ski2-ΔN could be built and refined almost in its entirety (with the exception of a disordered region between residues 542 and 606) and included electron density for an AMPPNP molecule.
Cross-references: PDB:4A4Z
PDB:4A4K
Protein: DP03155 (UniProt P01019)
Region: residues 428	to 439
Annotation: disorder (Structural state)
Evidence: X-ray crystallography-based structural model with missing residue coordinates used in manual assertion
Supporting statements:
 With the exception of the exposed and hence mobile reactive centre loop (residues 408-425), the overall results show the complete fold of the human molecule including the full amino-terminal extension with the renin cleavage site (Fig 1a).
The disorder region boundaries differ from the ones mentioned in the article as there is a signal peptide of 33 amino acids not accounted for.
Cross-references: PDB:2WXW
PDB:2X0B
Protein: DP03155 (UniProt P01019)
Region: residues 43	to 54
Annotation: disorder (Structural state)
Evidence: X-ray crystallography-based structural model with missing residue coordinates used in manual assertion
Supporting statements:
The mouse structures were determined at higher resolution (2.3, 2.1, 2.95Å) but the general features are preserved in the 3.15Å rat and 3.3Å human structures (as shown separately and with statistics in Figure 2 and Table 1 of the Supplementary information).
Although the disordered region in not explicitly mentioned, it is shown in the deposited PDB structure.
Cross-references: PDB:2X0B
Protein: DP03155 (UniProt P01019)
Region: residues 43	to 53
Annotation: disorder (Structural state)
Evidence: X-ray crystallography-based structural model with missing residue coordinates used in manual assertion
Supporting statements:
The segment from Glu20 to Pro29 (dashed, pale green) is disordered in the structure and modeled for illustration. 
The correct disordered region boundaries also account for angiotensinogen's signal peptide.
Cross-references: PDB:5M3Y
PDB:5M3X
PDB:6I3I
Protein: DP03155 (UniProt P01019)
Region: residues 427	to 440
Annotation: disorder (Structural state)
Evidence: X-ray crystallography-based structural model with missing residue coordinates used in manual assertion
Supporting statements:
The serpin template is in gray, and helix A (hA) is in marine with the A-sheet (sA) in light blue and the disordered RCL in red dashes. 
The disordered region boundaries for the Reactive Center Loop (RCL) are not mentioned but were deposited in PDB.
Cross-references: PDB:5M3Y
Protein: DP03155 (UniProt P01019)
Region: residues 35	to 55
Annotation: disorder (Structural state)
Evidence: X-ray crystallography-based structural model with missing residue coordinates used in manual assertion
Supporting statements:
Subsequently, we prepared spent AGT, where the N-terminal 10-residue angiotensin I peptide was removed from the AGT-N14 expression construct and loop- cleaved AGT, where AGT-N14 was cleaved between Gln412 and Leu413 by thermolysin treatment.
Removal of the N-terminal decapeptide augments the disordered region (evidence in PDB entry)
Cross-references: PDB:5M3X
Protein: DP03155 (UniProt P01019)
Region: residues 427	to 441
Annotation: disorder (Structural state)
Evidence: X-ray crystallography-based structural model with missing residue coordinates used in manual assertion
Supporting statements:
The fragments without clear electron density are shown with dashed lines for illustration.
Cross-references: PDB:6I3F
Protein: DP03155 (UniProt P01019)
Region: residues 40	to 52
Annotation: disorder (Structural state)
Evidence: X-ray crystallography-based structural model with missing residue coordinates used in manual assertion
Supporting statements:
The fragments without clear electron density are shown with dashed lines for illustration.
Cross-references: PDB:6I3F
Protein: DP03156 (UniProt P11859)
Region: residues 431	to 440
Annotation: disorder (Structural state)
Evidence: X-ray crystallography-based structural model with missing residue coordinates used in manual assertion
Supporting statements:
The mouse structures were determined at higher resolution (2.3, 2.1, 2.95Å) but the general features are preserved in the 3.15Å rat and 3.3Å human structures (as shown separately and with statistics in Figure 2 and Table 1 of the Supplementary information).
With the exception of the exposed and hence mobile reactive centre loop (residues 408-425), the overall results show the complete fold of the human molecule including the full amino-terminal extension with the renin cleavage site (Fig 1a)
Exact boundary statements in the text concern only human angiotensinogen but the exact boundaries of the disordered regions in mouse can be found at the deposited structure in PDB
Cross-references: PDB:2WY0
PDB:2WXY
Protein: DP03156 (UniProt P11859)
Region: residues 429	to 440
Annotation: disorder (Structural state)
Evidence: X-ray crystallography-based structural model with missing residue coordinates used in manual assertion
Supporting statements:
The mouse structures were determined at higher resolution (2.3, 2.1, 2.95Å) but the general features are preserved in the 3.15Å rat and 3.3Å human structures (as shown separately and with statistics in Figure 2 and Table 1 of the Supplementary information).
With the exception of the exposed and hence mobile reactive centre loop (residues 408-425), the overall results show the complete fold of the human molecule including the full amino-terminal extension with the renin cleavage site (Fig 1a)
Exact boundary statements in the text concern only human angiotensinogen but the exact boundaries of the disordered regions in mouse can be found at the deposited structure in PDB
Cross-references: PDB:2WXX
Protein: DP03156 (UniProt P11859)
Region: residues 41	to 51
Annotation: disorder (Structural state)
Evidence: X-ray crystallography-based structural model with missing residue coordinates used in manual assertion
Supporting statements:
The mouse structures were determined at higher resolution (2.3, 2.1, 2.95Å) but the general features are preserved in the 3.15Å rat and 3.3Å human structures (as shown separately and with statistics in Figure 2 and Table 1 of the Supplementary information).
Exact boundary statements in the text concern only human angiotensinogen but the exact boundaries of the disordered regions in mouse can be found at the deposited structure in PDB
Cross-references: PDB:2WXY
Protein: DP03158 (UniProt P54578)
Region: residues 484	to 494
Annotation: disorder (Structural state)
Evidence: X-ray crystallography-based structural model with missing residue coordinates used in manual assertion
Supporting statements:
There is no significant electron density for residues 94–98, 217–234, 380–397, and 484–494; these residues are
likely flexible and disordered in the crystals.
Cross-references: PDB:2AYN
PDB:2AYO
Protein: DP03159 (UniProt Q9UBR1)
Region: residues 1	to 32
Annotation: disorder (Structural state)
Evidence: X-ray crystallography-based structural model with missing residue coordinates used in manual assertion
Supporting statements:
The lack of electron density for the not modelled N-terminal 32 residues of the native sequence and two loop regions is very likely due to structural disorder.
Cross-references: PDB:6FTQ
Protein: DP03159 (UniProt Q9UBR1)
Region: residues 202	to 211
Annotation: entropic chain (Disorder function)
Evidence: mutant phenotype evidence used in manual assertion
Supporting statements:
As intended, Cys299 does indeed form a disulfide bond in the crystal structure, however, not an intermolecular bond with Cys299 from another subunit, but an intramolecular bond with Cys128 (Figure 4, S8). Both cysteines are located in active- site entrance loops that were found disordered in the “corner subunits” flanking the DmβUP octamer.
Mutation of Thr299 to cysteine, a rather conservative exchange intended to promote formation of an intersubunit disulfide bridge, renders the enzyme incapable of forming higher oligomers.
Our results show that this is synonymous with enzyme inactivation, which is in agreement with our hypothesis that ordering of flexible loops at the active site entrance, triggered by substrate binding, inserts Glu207 into the active site and induces oligomerization, which in turn stabilizes the catalytically active conformation of the interacting subunits by burying these loops between them.
Cross-references: PDB:6FTQ
Protein: DP03159 (UniProt Q9UBR1)
Region: residues 301	to 309
Annotation: entropic chain (Disorder function)
Evidence: mutant phenotype evidence used in manual assertion
Supporting statements:
As intended, Cys299 does indeed form a disulfide bond in the crystal structure, however, not an intermolecular bond with Cys299 from another subunit, but an intramolecular bond with Cys128 (Figure 4, S8). Both cysteines are located in active- site entrance loops that were found disordered in the “corner subunits” flanking the DmβUP octamer.
Mutation of Thr299 to cysteine, a rather conservative exchange intended to promote formation of an intersubunit disulfide bridge, renders the enzyme incapable of forming higher oligomers.
Our results show that this is synonymous with enzyme inactivation, which is in agreement with our hypothesis that ordering of flexible loops at the active site entrance, triggered by substrate binding, inserts Glu207 into the active site and induces oligomerization, which in turn stabilizes the catalytically active conformation of the interacting subunits by burying these loops between them.
Cross-references: PDB:6FTQ
Protein: DP03160 (UniProt S7W634)
Region: residues 1	to 32
Annotation: disorder (Structural state)
Evidence: X-ray crystallography-based structural model with missing residue coordinates used in manual assertion
Supporting statements:
The sequence-divergent
N terminus (M1–N111) comprises a disordered N-terminal extension (M1–V32) and a more domain-like region (Y33–L95).
Cross-references: PDB:6DUE
Protein: DP03161 (UniProt Q8WVQ1)
Region: residues 71	to 84
Annotation: disorder (Structural state)
Evidence: X-ray crystallography-based structural model with missing residue coordinates used in manual assertion
Supporting statements:
Iterative rounds of model building with O, refinement with Refmac (Murshudov et al., 1997), and addition of ordered solvent clarified the trace except the N-terminal region, which is not visible in the electron density maps and therefore must be disordered. 
Cross-references: PDB:1S18
PDB:1S1D
Protein: DP03162 (UniProt O00299)
Region: residues 152	to 162
Annotation: disorder (Structural state)
Evidence: X-ray crystallography-based structural model with missing residue coordinates used in manual assertion
Supporting statements:
In  the  1.4Å structure,  clear electron density was seen for all residues from Pro6to Lys241,while  in  the  second  form,  residues  Leu148–Arg165 are  disordered.
Cross-references: PDB:1K0O
Protein: DP03162 (UniProt O00299)
Region: residues 147	to 164
Annotation: flexible linker (Disorder function)
Evidence: x-ray crystallography evidence used in manual assertion
Supporting statements:
The long loop between helices h5 and h6 at the foot of CLIC1(Pro147–Gln164) is a distinctive feature of the CLICs. It is highlynegatively charged with seven acidic residues between Pro149and  Glu160in  CLIC1  giving  a  net  charge  of7(cf.a  netnegative  charge  of  6  in  CLIC4  and  p64,  5  in  CLIC2,  5  inparchorin, and 3 in CLIC3). This loop is spatially adjacent tothe loop linking the two domains, and it may be important inprotein-protein interactions.
Cross-references: PDB:1K0O
Protein: DP03162 (UniProt O00299)
Region: residues 1	to 21
Annotation: disorder (Structural state)
Evidence: X-ray crystallography-based structural model with missing residue coordinates used in manual assertion
Supporting statements:
In the dimer there is no electron density for the first 22 residues (β-strand 1 in monomer), and helix 2 is extended by an extra 2turns   to   include   residues   starting   at   Thr-44   (originally β-strand 2; Fig. 2E).

Cross-references: PDB:1RK4
Protein: DP03163 (UniProt O15247)
Region: residues 55	to 68
Annotation: disorder (Structural state)
Evidence: X-ray crystallography-based structural model with missing residue coordinates used in manual assertion
Supporting statements:
 The electron density of residues 55–69 could not be observed at the contour level of 1.0 sigma due to the flexibility of this region.
Cross-references: PDB:2PER
Protein: DP03164 (UniProt Q9Y696)
Region: residues 159	to 175
Annotation: flexible linker (Disorder function)
Evidence: x-ray crystallography evidence used in manual assertion
Supporting statements:
The observed structure consists of residues 16–163 and 173–257 with the break in density corresponding to the flexible foot loop between helix 5 and helix 6 (Fig. 1A, bottom left), which is not ordered in the CLIC4(ext) structure. 
The backbone structures overlay well except for the region around helix 2 (including connecting loops, Leu59 to His74) and the flexible foot loop (Leu159 to Thr175).
Cross-references: PDB:2AHE
Protein: DP03164 (UniProt Q9Y696)
Region: residues 160	to 173
Annotation: disorder (Structural state)
Evidence: X-ray crystallography-based structural model with missing residue coordinates used in manual assertion
Supporting statements:
The observed structure consists of residues 16–163 and 173–257 with the break in density corresponding to the flexible foot loop between helix 5 and helix 6 (Fig. 1A, bottom left), which is not ordered in the CLIC4(ext) structure. 
Cross-references: PDB:2AHE
Protein: DP03166 (UniProt P00519)
Region: residues 385	to 401
Annotation: disorder (Structural state)
Evidence: X-ray crystallography-based structural model with missing residue coordinates used in manual assertion
Supporting statements:
The main differences occur in loop regions where the temperature factors are high (e.g. the β3-αC loop and the A-loop)
There are two molecules in the asymmetric unit of the crystals and one of these shows a novel A-loop conformation, while the A-loop is not visible in the other owing to disorder.
Superposition of the various structures reported here and one recently reported structure (Levinson et al., 2006; PDB code 2g1t) shows that there are four main regions of conformational flexibility in the Abl kinase domain: the A-loop, the P-loop, the C-helix and the relative position of the N-terminal lobe with respect to the C-terminal lobe
A-loop comprises residues 381-401 but region is defined on the basis of missing residues 385-401 in 2HZ0_B.
Cross-references: PDB:2HZ0
Protein: DP03166 (UniProt P00519)
Region: residues 385	to 401
Annotation: disorder to order (Structural transition)
Evidence: x-ray crystallography evidence used in manual assertion
Supporting statements:
There are two molecules in the asymmetric unit of the crystals and one of these shows a novel A-loop conformation, while the A-loop is not visible in the other owing to disorder. The novel
A-loop conformation lies in an intermediate position between the active conformation and the imatinib-bound conformation. The path of this segment departs from the latter conformation at Leu383, superimposes again at Lys400, has Tyr393 exposed at the surface and shows some weak resemblance to the intermediate conformation observed in partially phosphorylated Igf1r kinase (Pautsch et al., 2001). However, this conformation is stabilized by crystal contacts in the Abl structure, so it is not clear if this is really a natural inactive state of the A-loop of Abl kinase.
A-loop comprises residues 381-401 but region is defined on the basis of missing residues 385-401 in 2HZ0_B
Cross-references: PDB:2HZ0
Protein: DP03168 (UniProt P00519-2)
Region: residues 1026	to 1045
Annotation: disorder (Structural state)
Evidence: nuclear magnetic resonance spectroscopy evidence used in manual assertion
Supporting statements:
We determined the three-dimensional (3D) solution structure of the FABD (corresponding to residues 1026–1149 of human c-Abl spliceform 1b) by heteronuclear NMR spectroscopy (Figures 1B and 1C and Table 1). This domain also includes the previously proposed NES (residues 1109–1118) (Taagepera et al., 1998). The ordered region of the FABD, which encompasses residues 1047–1149, is a monomer in solution
15N relaxation data shows that the αIII-αIV loop displays high internal mobility and that the 20 N-terminal residues of the expression construct are unstructured
{1H}-15N heteronuclear NOE, longitudinal and transverse 15N relaxation data of the Bcr-Abl/c-Abl FABD demonstrate significant conformational flexibility for the N-terminal region and the loop between helices αIII and αIV
Protein: DP03168 (UniProt P00519-2)
Region: residues 520	to 531
Annotation: disorder (Structural state)
Evidence: X-ray crystallography-based structural model with missing residue coordinates used in manual assertion
Supporting statements:
R-DPH binds to c-Abl in the myristoyl binding site and straightens the αI’ helix to elongate the αI helix (Figure 5A). In chain A, the αI helix extends to residue 519 and in Chain B, the αI helix extends to residue 529. The remaining C-terminal residues of the respective molecules in the asymmetric unit are disordered. In contrast, the autoinhibited c-Abl has αI helix ending at residue 515, with a loop between residues 515–521 and with αI’ helix defined by residues 521–529 (Figure 1). The elongated αI helix of Chain B with R-DPH shows significant crystal packing and is an artifact of crystallization. However, the C terminus of Chain A with R-DPH shows no crystal packing and will be the focus of subsequent discussion.
Residues 520-531 in PDB 3PYY chain A correspond to region 501-512 in the UniProt amino acid sequence of canonical isoform 1A of P00519..
Protein: DP03168 (UniProt P00519-2)
Region: residues 138	to 249
Annotation: disorder (Structural state)
Evidence: X-ray crystallography-based structural model with missing residue coordinates used in manual assertion
Supporting statements:
The crystal form has two copies of the KD in the asymmetric unit, however only one SH2 domain could be localized in the electron density map, presumably due to a high degree of disorder in the second SH2 domain. Since the conformation of both KDs is very similar, we focus our interpretation on the molecule for which the SH2 domain could be built. The structure shows the SH2 and KD in an extended conformation (Figure 4A), as was observed previously for the SH3–SH2–KD construct bound to PD166326 (PDB ID: 1OPL) [2]. The previous crystal form, however contained two different conformational states of the SH3–SH2–KD construct, (i) the compact auto-inhibited conformation, in which the SH2 domain docks on to the C-lobe of the KD and (ii) the extended conformation, for which only the SH2 and KDs could be modelled and which was characterized by very high temperature factors.
Missing electron density correspond to crystallography experiment for PDB 4XEY chain B.
Protein: DP03169 (UniProt Q9NQC7)
Region: residues 841	to 857
Annotation: disorder (Structural state)
Evidence: X-ray crystallography-based structural model with missing residue coordinates used in manual assertion
Supporting statements:
In molecule A, the surface loops 671–678, 723–723, 841–857, and 893–899 are disordered, while, in molecule B, residues 672–679, 719–727, 759–766, 894–901, 929–934, and 956 lacked electron density.
Cross-references: PDB:2VHF
Protein: DP03170 (UniProt Q8NBZ7)
Region: residues 395	to 420
Annotation: disorder (Structural state)
Evidence: X-ray crystallography-based structural model with missing residue coordinates used in manual assertion
Supporting statements:
The extreme N-terminus of both chains is disordered (residues
85–87), as is the C-terminus of chain A (395–420) and chain B (399–420).
Cross-references: PDB:4GLL