LiteFold/DisProt huggingface dataset:
Protein: DP00736 (UniProt Q9UKV8)
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:
The PDB evidence shows this region lacks electron density, indicating it is disordered.
Cross-references: PDB:4W5N
PDB:4W5T
PDB:4W5Q
PDB:4W5O
PDB:4W5R
Protein: DP00736 (UniProt Q9UKV8)
Region: residues 822	to 835
Annotation: disorder (Structural state)
Evidence: X-ray crystallography-based structural model with missing residue coordinates used in manual assertion
Supporting statements:
The PDB evidence shows this region lacks electron density, indicating it is disordered.
Cross-references: PDB:4W5N
PDB:4W5O
PDB:4W5R
PDB:4W5T
PDB:4W5Q
Protein: DP00741 (UniProt P03040)
Region: residues 56	to 66
Annotation: disorder (Structural state)
Evidence: nuclear magnetic resonance spectroscopy evidence used in manual assertion
Supporting statements:
Residues 2−4 at the N-terminus and 56−66 at the C-terminus of λ-WDQ showed significant NOE reductions and increases in T2, suggestive of increased mobility, in approximate agreement with the location of poorly defined regions in the ensemble.
Cross-references: PDB:2A63
BMRB:6771
Protein: DP00747 (UniProt P01160)
Region: residues 56	to 123
Annotation: disorder (Structural state)
Evidence: nuclear magnetic resonance spectroscopy evidence used in manual assertion
Supporting statements:
Moreover, it was found that the amide resonances disappeared immediately after the freshly prepared protein was dissolved in D2O solution (Fig. 2D). This indicated that the amide protons are accessible to the solvent and the protein has no well-defined hydrogen bonds.
The cross-correlation NH(i) − NH(i + 1) resonance peaks from homonuclear 2D-NOE are essentially absent (supplementary Fig. S1) indicating little overall solution structure for NT-proANP, a result also found for NT-proBNP (11).
Protein: DP00747 (UniProt P01160)
Region: residues 56	to 123
Annotation: disorder (Structural state)
Evidence: proton-based nuclear magnetic resonance evidence used in manual assertion
Supporting statements:
Figure 2B shows the 4°C proton spectra for NT-proANP in 10% D2O. The intensity in the amide region is rather low and confined to a narrow region of ~8–8.6 ppm.
Protein: DP00747 (UniProt P01160)
Region: residues 56	to 123
Annotation: disorder (Structural state)
Evidence: chromatography evidence used in manual assertion
Supporting statements:
As myoglobin is known to adopt a compact, folded three-dimensional structure (25), and as the above far-UV CD and NMR data demonstrate that NT-proANP is largely unstructured in physiologic near neutral pH non-denaturing buffer, it is evident that shape, e.g. Rs the Stoke's radius, and not molecular weight is the determining mechanistic factor in SE-HPLC. On the same column, unstructured monomeric NT-proBNP eluted at 20.6′ (data not shown).
Protein: DP00747 (UniProt P01160)
Region: residues 56	to 123
Annotation: disorder (Structural state)
Evidence: far-UV circular dichroism evidence used in manual assertion
Supporting statements:
Figure 1 displays a room temperature CD spectrum for NT-proANP in a physiologic near neutral pH buffer. A minimum is observed at ~199–200 nm giving a value of –14,800° cm2/dmol indicating that the 68-residue NT-proANP fragment is largely unstructured.
Protein: DP00748 (UniProt P46108)
Region: residues 192	to 223
Annotation: disorder (Structural state)
Evidence: nuclear magnetic resonance spectroscopy evidence used in manual assertion
Supporting statements:
The ISC makes contacts with SH2, nSH3 and cSH3. In fact, we identified 54 distance restraints from the ISC to SH2, nSH3 and cSH3, but the other region in the nSH3-cSH3 linker, aside from the ISC, is flexible.
Cross-references: PDB:2EYZ
Protein: DP00748 (UniProt P46108)
Region: residues 192	to 223
Annotation: flexible linker (Disorder function)
Evidence: nuclear magnetic resonance spectroscopy evidence used in manual assertion
Supporting statements:
The ISC makes contacts with SH2, nSH3 and cSH3. In fact, we identified 54 distance restraints from the ISC to SH2, nSH3 and cSH3, but the other region in the nSH3-cSH3 linker, aside from the ISC, is flexible.
Cross-references: PDB:2EYZ
Protein: DP00748 (UniProt P46108)
Region: residues 238	to 293
Annotation: disorder (Structural state)
Evidence: nuclear magnetic resonance spectroscopy evidence used in manual assertion
Supporting statements:
We recorded the 1H-15N HSQC spectrum of the CRKII mutant containing a W275K mutation. Most of the NMR signals from the ISC as well as from cSH3 in CRKII disappeared for this mutant, and new signals appeared in the disordered region (Supplementary Fig. 4 online). This means that the tertiary structure of cSH3 was disrupted by the W275K mutation, abrogating the interaction between the ISC and cSH3.
Protein: DP00748 (UniProt P46108)
Region: residues 219	to 223
Annotation: phosphorylation display site (Disorder function)
Evidence: nuclear magnetic resonance spectroscopy evidence used in manual assertion
Supporting statements:
The protein kinase cABL phosphorylates Tyr221 in the SH3 linker.
Protein: DP00749 (UniProt Q9TY14)
Region: residues 413	to 445
Annotation: disorder (Structural state)
Evidence: X-ray crystallography-based structural model with missing residue coordinates used in manual assertion
Supporting statements:
Although the complete recombinant PvAMA1 ectoplasmic region (residues 43–487) and domains II and III of PfAMA1 (residues 303 to 544) were complexed with Fab F8.12.19 in the protein preparations used for crystallisation, only a small but contiguous segment of domain III from these two homologues could be identified in the electron density: the 34-residue segment from Ile421 to Lys454 in PvAMA1 and the equivalent 34-residue segment from Ile479 to Arg512 in PfAMA1 (Figure 4). This part of the antigen could be identified readily in the electron density by the cystine knot formed with Cys432-Cys449 and Cys434-Cys451 in PvAMA1 and Cys490-Cys507 and Cys492-Cys509 in PfAMA1. Additional electron density, observed in the final difference maps of both PvAMA1 and PfAMA1, did not coincide with the complete, superimposed PvAMA1 structure (PDB entry 1W8K) (Figure 5). This region is connected to modelled part of the antigen via the Cys388-Cys444 bridge in PvAMA1 (443Cys-502Cys in PfAMA1) but the electron density was too disordered to propose an unambiguous interpretation. No other region of significant electron density occurred in the maps.
The region defined here is based on the missing residues in the PDB structure 2j4w. Based on the same structure, there is likely disordered regions in the N-terminal part as well, however, a close homologue from P. falciparum indicates that the N-terminal region contains a folded domain (see PDB structure 4r1a).
Cross-references: PDB:2J4W
Protein: DP00750 (UniProt Q38151)
Region: residues 68	to 126
Annotation: disorder (Structural state)
Evidence: X-ray crystallography-based structural model with missing residue coordinates used in manual assertion
Supporting statements:
Our structural analyses reveal that G39P has a completely unexpected bipartite structure comprising a folded N-terminal domain and an essentially unfolded C-terminal domain.
Our findings strongly support the idea that the disorder observed in the crystal structure for the C-terminal region was not a result of the truncation of the protein nor was it merely some form of crystal artifact but reflected an underlying flexibility that may be closely related to the function of the protein.
Our structural analysis has shown that the G39P protein has two domains: a stably folded 67-residue N-terminal domain and a highly flexible and largely unfolded 59-residue C-terminal domain.
Cross-references: PDB:1NO1
Protein: DP00750 (UniProt Q38151)
Region: residues 68	to 126
Annotation: disorder (Structural state)
Evidence: X-ray crystallography-based structural model with high relative B-factor values used in manual assertion
Supporting statements:
High relative average B-factor values (38.3 Å2 for chain A/ 38.5 Å2 for chain B/ 38.4 Å2 for chain C) supporting the presence of intrinsic disorder in the C-terminal region of the protein.
Cross-references: PDB:1NO1
Protein: DP00750 (UniProt Q38151)
Region: residues 68	to 126
Annotation: disorder (Structural state)
Evidence: nuclear magnetic resonance spectroscopy evidence used in manual assertion
Supporting statements:
For the C-terminal ~50 residues, i.e. about half the size of G39P, NMR relaxation rates are slow and are thus dominated by internal mobility far in excess of the overall rotation of the protein. Resonances from these residues show little chemical shift dispersion away from their random coil values, indicative of conformational averag- ing, and high intensity cross-peaks in TOCSY spectra, as illustrated by the correlations between the aromatic ring protons of Phe-76 and Tyr-80 in Fig. 3B.
Backbone amide proton resonances from the mobile C-terminal domain, upon heating the sample, are severely attenuated in intensity by solvent exchange, following saturation of the water resonance (Fig. 3A). This demonstrates that there is weak or no hydrogen bonding involving this part of the protein backbone other than to solvent molecules.
The NMR experiments indicate that in solution the protein behaves as a two-domain entity. One domain, corresponding to approximately the 67 N-terminal residues observed in the electron density map from the x-ray experiment, exists in the fold determined above, although at room temperature it is involved in a thermally labile, self-association process. The second domain, corresponding to the remaining 60 C-terminal residues that are not observed in the electron density map, has rapid internal motion and no well defined and stable fold involving immobilized side chains.
Protein: DP00750 (UniProt Q38151)
Region: residues 68	to 126
Annotation: disorder (Structural state)
Evidence: gel-filtration evidence used in manual assertion
Supporting statements:
The observation of a species approximating to the size of a dimer might actually arise from the rapid interchange between the monomeric and aggregated forms of the protein and is further complicated by an increase in the hydrodynamic radius arising from the flexible C-terminal domain.
Protein: DP00750 (UniProt Q38151)
Region: residues 79	to 126
Annotation: disorder (Structural state)
Evidence: cleavage assay evidence used in manual assertion
Supporting statements:
An investigation of the general susceptibility of G39P to proteolytic degradation was performed using proteinase K and both wtG39P and an N- terminal His-tagged variant. The analysis revealed a much more pronounced sensitivity to proteolytic cleavage in the C- terminal half of the protein that resulted in fragments corre- sponding to residues 1–79, 1– 87, 1–90, 1–94, and 1–106 (Fig. 6). The identity of the fragments was confirmed by the corre- spondence of the molecular weights determined by mass spec- trometry and by retention on a Ni-NTA column of equivalent fragments (as assessed by SDS-PAGE) from the N-terminal His-tagged variant.
Protein: DP00750 (UniProt Q38151)
Region: residues 79	to 126
Annotation: disorder (Structural state)
Evidence: protein mass spectrometry evidence used in manual assertion
Supporting statements:
An investigation of the general susceptibility of G39P to proteolytic degradation was performed using proteinase K and both wtG39P and an N- terminal His-tagged variant. The analysis revealed a much more pronounced sensitivity to proteolytic cleavage in the C- terminal half of the protein that resulted in fragments corre- sponding to residues 1–79, 1– 87, 1–90, 1–94, and 1–106 (Fig. 6). The identity of the fragments was confirmed by the corre- spondence of the molecular weights determined by mass spec- trometry and by retention on a Ni-NTA column of equivalent fragments (as assessed by SDS-PAGE) from the N-terminal His-tagged variant.
Protein: DP00750 (UniProt Q38151)
Region: residues 69	to 126
Annotation: protein binding (Molecular function)
Evidence: deletion mutation phenotypic evidence used in manual assertion
Supporting statements:
A series of G39P truncated variants with N termini deleted up to residue 73 still show interaction with G40P-ATP as assessed by affinity chromatography assay, but a variant consisting of the N-terminal residues 1– 68 does not (Fig. 7).
Protein: DP00750 (UniProt Q38151)
Region: residues 69	to 126
Annotation: protein binding (Molecular function)
Evidence: sodium dodecyl sulfate polyacrylamide gel electrophoresis evidence used in manual assertion
Supporting statements:
A series of G39P truncated variants with N termini deleted up to residue 73 still show interaction with G40P-ATP as assessed by affinity chromatography assay, but a variant consisting of the N-terminal residues 1– 68 does not (Fig. 7).
Protein: DP00750 (UniProt Q38151)
Region: residues 113	to 126
Annotation: molecular function inhibitor activity (Molecular function)
Evidence: affinity evidence used in manual assertion
Supporting statements:
The G39P protein is proteolytically sensitive, and our binding assays show that the C-terminal domain is essential for helicase interaction and that removal of just the 14 C-terminal residues abolishes interaction with the helicase in vitro. We propose a number of possible scenarios in which the flexibility of the C-terminal domain of G39P and its proteolytic sensitivity may have important roles for the function of G39P in vivo that are consistent with other data on SPP1 phage DNA replication.
We have observed that removal of just the C-terminal 14 residues impairs G40P binding.
The full-length wt G39P protein is able to interact with G40P-ATPγS and to inhibit all three associated activities (ssDNA binding, ATPase, and helicase activity (6)). Assays have been performed on fragments of G39P and have shown that the G39P112 variant can neither exert a negative effect on G40P activities nor compete out the wt protein from the G39P-G40P-ATP complex (data not shown).
Protein: DP00750 (UniProt Q38151)
Region: residues 113	to 126
Annotation: protein-containing complex disassembly (Biological process)
Evidence: affinity evidence used in manual assertion
Supporting statements:
The G39P protein is proteolytically sensitive, and our binding assays show that the C-terminal domain is essential for helicase interaction and that removal of just the 14 C-terminal residues abolishes interaction with the helicase in vitro. We propose a number of possible scenarios in which the flexibility of the C-terminal domain of G39P and its proteolytic sensitivity may have important roles for the function of G39P in vivo that are consistent with other data on SPP1 phage DNA replication.
We have observed that removal of just the C-terminal 14 residues impairs G40P binding.
The full-length wt G39P protein is able to interact with G40P-ATPγS and to inhibit all three associated activities (ssDNA binding, ATPase, and helicase activity (6)). Assays have been performed on fragments of G39P and have shown that the G39P112 variant can neither exert a negative effect on G40P activities nor compete out the wt protein from the G39P-G40P-ATP complex (data not shown).
Protein: DP00756 (UniProt Q04884)
Region: residues 16	to 55
Annotation: disorder (Structural state)
Evidence: nuclear magnetic resonance spectroscopy evidence used in manual assertion
Supporting statements:
The loops are unstructured based on circular dichroism (data not shown), amide proton chemical shift, and the 15N-edited NOESY spectrum (data not shown).
Using a series of 3D NMR experiments, the amide proton, nitrogen, and α-carbon were assigned for 27 of the 34 observed resonances (corresponding to residues 1–6 in the N-terminus; 109–110 in loop 2; 152–154, 160, 162–164, 166–175, and 177–178 in loop 3).
Protein: DP00756 (UniProt Q04884)
Region: residues 72	to 116
Annotation: disorder (Structural state)
Evidence: nuclear magnetic resonance spectroscopy evidence used in manual assertion
Supporting statements:
The loops are unstructured based on circular dichroism (data not shown), amide proton chemical shift, and the 15N-edited NOESY spectrum (data not shown).
Using a series of 3D NMR experiments, the amide proton, nitrogen, and α-carbon were assigned for 27 of the 34 observed resonances (corresponding to residues 1–6 in the N-terminus; 109–110 in loop 2; 152–154, 160, 162–164, 166–175, and 177–178 in loop 3).
Protein: DP00756 (UniProt Q04884)
Region: residues 142	to 190
Annotation: disorder (Structural state)
Evidence: nuclear magnetic resonance spectroscopy evidence used in manual assertion
Supporting statements:
The loops are unstructured based on circular dichroism (data not shown), amide proton chemical shift, and the 15N-edited NOESY spectrum (data not shown).
Using a series of 3D NMR experiments, the amide proton, nitrogen, and α-carbon were assigned for 27 of the 34 observed resonances (corresponding to residues 1–6 in the N-terminus; 109–110 in loop 2; 152–154, 160, 162–164, 166–175, and 177–178 in loop 3).
Protein: DP00756 (UniProt Q04884)
Region: residues 216	to 231
Annotation: disorder (Structural state)
Evidence: nuclear magnetic resonance spectroscopy evidence used in manual assertion
Supporting statements:
The loops are unstructured based on circular dichroism (data not shown), amide proton chemical shift, and the 15N-edited NOESY spectrum (data not shown).
Using a series of 3D NMR experiments, the amide proton, nitrogen, and α-carbon were assigned for 27 of the 34 observed resonances (corresponding to residues 1–6 in the N-terminus; 109–110 in loop 2; 152–154, 160, 162–164, 166–175, and 177–178 in loop 3).
Protein: DP00756 (UniProt Q04884)
Region: residues 16	to 55
Annotation: disorder (Structural state)
Evidence: nuclear magnetic resonance spectroscopy evidence used in manual assertion
Supporting statements:
The extracellular loops are intrinsically disordered yet are sampling a restricted volume such that there are interactions between the loops on the nanosecond time scale.
The β-barrel provides the scaffolding for the functional extracellular loops, which are disordered and sample a diverse ensemble of conformers.
Cross-references: PDB:2MAF
PDB:2MLH
BMRB:19343
Protein: DP00756 (UniProt Q04884)
Region: residues 72	to 116
Annotation: disorder (Structural state)
Evidence: nuclear magnetic resonance spectroscopy evidence used in manual assertion
Supporting statements:
The extracellular loops are intrinsically disordered yet are sampling a restricted volume such that there are interactions between the loops on the nanosecond time scale.
The β-barrel provides the scaffolding for the functional extracellular loops, which are disordered and sample a diverse ensemble of conformers.
Cross-references: PDB:2MAF
PDB:2MLH
BMRB:19343
Protein: DP00756 (UniProt Q04884)
Region: residues 142	to 190
Annotation: disorder (Structural state)
Evidence: nuclear magnetic resonance spectroscopy evidence used in manual assertion
Supporting statements:
The extracellular loops are intrinsically disordered yet are sampling a restricted volume such that there are interactions between the loops on the nanosecond time scale.
The β-barrel provides the scaffolding for the functional extracellular loops, which are disordered and sample a diverse ensemble of conformers.
Cross-references: PDB:2MAF
PDB:2MLH
BMRB:19343
Protein: DP00756 (UniProt Q04884)
Region: residues 216	to 231
Annotation: disorder (Structural state)
Evidence: nuclear magnetic resonance spectroscopy evidence used in manual assertion
Supporting statements:
The extracellular loops are intrinsically disordered yet are sampling a restricted volume such that there are interactions between the loops on the nanosecond time scale.
The β-barrel provides the scaffolding for the functional extracellular loops, which are disordered and sample a diverse ensemble of conformers.
Cross-references: PDB:2MAF
PDB:2MLH
BMRB:19343
Protein: DP00765 (UniProt O00585)
Region: residues 94	to 134
Annotation: disorder (Structural state)
Evidence: nuclear magnetic resonance spectroscopy evidence used in manual assertion
Supporting statements:
CCL21 also contains an unstructured C-terminus (residues 71–111, not shown for clarity) distinct from most chemokines.
The core chemokine domain of CCL21 is structured (residues 8–68) while the N-terminus and extended C-terminus are unstructured.
The authors assessed the mature protein, that lacks the first 23 residues. They describe the 94-134 region of the UniProt protein sequence. 
Cross-references: PDB:2L4N
Protein: DP00775 (UniProt P15311)
Region: residues 298	to 515
Annotation: disorder (Structural state)
Evidence: X-ray crystallography-based structural model with missing residue coordinates used in manual assertion
Supporting statements:
The final model of the ezrin FERM domain contains two molecules in the asymmetric unit (molecule A — residues 2–296 and molecule B — residues 2–137, 145–146, 150–296), with Cα root mean square deviation (RMSD) of 0.39 Å.
The structure of Ezrin-1 contains one molecule in the asymmetric unit (residues 1–297 and 516–586), whereas that of Ezrin-2 contains two molecules in the asymmetric unit (molecule A: residues 1–297, 516–586 and molecule B: residues 3–297, 515–586), with Cα RMSD of 0.73 Å over 365 residues.
Cross-references: PDB:4RMA
PDB:4RM9
PDB:4RM8
Protein: DP00775 (UniProt P15311)
Region: residues 298	to 515
Annotation: disorder (Structural state)
Evidence: far-UV circular dichroism evidence used in manual assertion
Supporting statements:
The final model of the ezrin FERM domain contains two molecules in the asymmetric unit (molecule A — residues 2–296 and molecule B — residues 2–137, 145–146, 150–296), with Cα root mean square deviation (RMSD) of 0.39 Å.
The structure of Ezrin-1 contains one molecule in the asymmetric unit (residues 1–297 and 516–586), whereas that of Ezrin-2 contains two molecules in the asymmetric unit (molecule A: residues 1–297, 516–586 and molecule B: residues 3–297, 515–586), with Cα RMSD of 0.73 Å over 365 residues.
Cross-references: PDB:4RMA
PDB:4RM9
PDB:4RM8
Protein: DP00775 (UniProt P15311)
Region: residues 298	to 515
Annotation: disorder (Structural state)
Evidence: small-angle X-ray scattering evidence used in manual assertion
Supporting statements:
The final model of the ezrin FERM domain contains two molecules in the asymmetric unit (molecule A — residues 2–296 and molecule B — residues 2–137, 145–146, 150–296), with Cα root mean square deviation (RMSD) of 0.39 Å.
The structure of Ezrin-1 contains one molecule in the asymmetric unit (residues 1–297 and 516–586), whereas that of Ezrin-2 contains two molecules in the asymmetric unit (molecule A: residues 1–297, 516–586 and molecule B: residues 3–297, 515–586), with Cα RMSD of 0.73 Å over 365 residues.
Cross-references: PDB:4RMA
PDB:4RM9
PDB:4RM8