LiteFold/DisProt huggingface dataset:
Protein: DP01150 (UniProt P03255)
Region: residues 53	to 91
Annotation: disorder to order (Structural transition)
Evidence: nuclear magnetic resonance spectroscopy evidence used in manual assertion
Supporting statements:
Binding of the NCBD to 15N‐labeled AdV5 E1A(53–91) leads to large, fast exchange shifts of E1A cross peaks (Supporting Information Fig. S11); the chemical shift changes are considerably larger than for the corresponding AdV12 E1A(52–81) construct [Fig.3(C)]. This may reflect local sequence differences or, more likely, the presence of additional hydrophobic residues beyond the C‐terminus of the AdV5 CR1 motif that are absent from AdV12[Fig.1(A)].
Protein: DP01150 (UniProt P03255)
Region: residues 1	to 91
Annotation: disorder (Structural state)
Evidence: nuclear magnetic resonance spectroscopy evidence used in manual assertion
Supporting statements:
The AdV5 E1A constructs are intrinsically disordered, with chemical shifts that deviate little from random coil values except for residues E13‐D21, which have a small propensity to form helical structure (∼30% population)
Protein: DP01150 (UniProt P03255)
Region: residues 1	to 91
Annotation: protein binding (Molecular function)
Evidence: nuclear magnetic resonance spectroscopy evidence used in manual assertion
Supporting statements:
Titrations were performed in which aliquots of the unlabeled NCBD were added to 15N‐labeled AdV5 E1A(1‐91) and AdV12 E1A(1‐81) in order to map the NCBD binding sites (Supporting Information Figs. S13 and S17).
The chemical shift perturbations reveal three NCBD binding sites in homologous regions of AdV5 and AdV12 E1A; for AdV12, the NCBD binding sites are located between residues L10‐V30, S40‐L47, and V61‐F78 ​[Fig.3(B)].
Thus the interaction between E1A and TAZ2 can be characterized as a partly “fuzzy” complex, with one portion of the E1A sequence participating in a strong interaction with TAZ2, while the other portion, corresponding to the N‐terminal region, participating in an interaction characterized by multiple states in intermediate exchange on the NMR time scale.
For AdV5 E1A, the precise boundaries of the NCBD binding sites were more difficult to identify due to cross peak overlap and because of differences in the exchange regime, with many AdV5 E1A residues exchange broadened or in slow exchange on the chemical shift time scale.
Protein: DP01150 (UniProt P03255)
Region: residues 1	to 139
Annotation: disorder (Structural state)
Evidence: nuclear magnetic resonance spectroscopy evidence used in manual assertion
Supporting statements:
More dramatic differences are observed between
the HSQC spectra of free and bound E1A (Fig. 2B). E1A is
largely unstructured in the free state as seen by the limited
chemical shift dispersion in the 1H dimension; backbone resonances
of both E1A(53–91) and E1A(1–139) show little deviation
of chemical shifts from random coil values (Fig. S2 A and
B)
Protein: DP01150 (UniProt P03255)
Region: residues 53	to 91
Annotation: disorder (Structural state)
Evidence: nuclear magnetic resonance spectroscopy evidence used in manual assertion
Supporting statements:
More dramatic differences are observed between
the HSQC spectra of free and bound E1A (Fig. 2B). E1A is
largely unstructured in the free state as seen by the limited
chemical shift dispersion in the 1H dimension; backbone resonances
of both E1A(53–91) and E1A(1–139) show little deviation
of chemical shifts from random coil values (Fig. S2 A and
B)
Protein: DP01150 (UniProt P03255)
Region: residues 27	to 91
Annotation: protein binding (Molecular function)
Evidence: nuclear magnetic resonance spectroscopy evidence used in manual assertion
Supporting statements:
HSQC cross peaks associated with these residues are broadened and/or shifted upon binding of pRb to E1A(27–91) or E1A(53–91) (Fig. S4C).
Protein: DP01150 (UniProt P03255)
Region: residues 106	to 139
Annotation: disorder (Structural state)
Evidence: nuclear magnetic resonance spectroscopy evidence used in manual assertion
Supporting statements:
As expected (16), the LXCXE motif
in CR2 binds with high affinity to pRb; there is a large increase
in dispersion of the HSQC spectrum of E1A(106–139) in the
presence of pRb and exchange is slow on the chemical shift
timescale (Fig. S4A).
Protein: DP01150 (UniProt P03255)
Region: residues 106	to 139
Annotation: protein binding (Molecular function)
Evidence: nuclear magnetic resonance spectroscopy evidence used in manual assertion
Supporting statements:
Interactions between the pRb pocket domain and 15N-labeled E1A peptides were examined using HSQC titrations (Fig. S4). As expected (16), the LXCXE motif in CR2 binds with high affinity to pRb; there is a large increase in dispersion of the HSQC spectrum of E1A(106–139) in the presence of pRb and exchange is slow on the chemical shift timescale (Fig. S4A).
Protein: DP01150 (UniProt P03255)
Region: residues 1	to 91
Annotation: molecular sequestering activity (Molecular function)
Evidence: nuclear magnetic resonance spectroscopy evidence used in manual assertion
Supporting statements:
Efficient displacement of p53 likely requires E1A to compete with both the AD1 and AD2 motifs for binding to NCBD, which would be favored in E1A constructs containing two or three NCBD binding sites. By competing for binding of p53, E1A may interfere with p53‐activated transcriptional programs that are mediated through interactions with the NCBD (also called IBiD) domain of CBP/p300,25 providing a plausible structural insight into the means whereby E1A might repress p53‐mediated apoptosis by inhibiting binding of p53 to both the NCBD and TAZ2 domains of CBP/p300.
Increased competition efficiency was observed for the longer CR1 constructs (AdV5 E1A(36–91) and AdV12 E1A(35–81)), which contain two NCBD binding sites, and the highest efficiency was observed for AdV5 E1A(1–91) and AdV12 E1A(1–81), an indication that both the N‐terminal and CR1 regions are required for efficient competition with p53 for the NCBD.
Protein: DP01150 (UniProt P03255)
Region: residues 53	to 91
Annotation: molecular sequestering activity (Molecular function)
Evidence: nuclear magnetic resonance spectroscopy evidence used in manual assertion
Supporting statements:
To test the hypothesis that E1A and p53 compete directly for TAZ2, p53(13–61) and E1A(53–91) were titrated into 15N-labeled TAZ2 and HSQC spectra were recorded.
Addition of equimolar E1A to the TAZ:p53 complex causes all TAZ2 cross peaks to shift to their characteristic positions in the HSQC spectrum of the binary TAZ2:E1A complex (Fig. 4A, Fig. S3C), indicating that E1A displaces the p53 TAD from TAZ2.
Cross-references: PDB:2KJE
Protein: DP01150 (UniProt P03255)
Region: residues 59	to 82
Annotation: disorder to order (Structural transition)
Evidence: nuclear magnetic resonance spectroscopy evidence used in manual assertion
Supporting statements:
A well-defined α-helix is formed by residues E59–I65, with shorter helical turns between L72–V74 and L80–T82, and a compact loop between F66–A73.
Upon interaction with TAZ2, there are large changes in the E1A chemical shifts (Fig. S2C) indicative of coupled folding and binding.
Cross-references: PDB:2KJE
BMRB:16318
Protein: DP01150 (UniProt P03255)
Region: residues 53	to 91
Annotation: protein binding (Molecular function)
Evidence: nuclear magnetic resonance spectroscopy evidence used in manual assertion
Supporting statements:
E1A binds in a deep hydrophobic groove in the surface of TAZ2, formed at the interfaces between helices α1/α2 and α1/α3, and buries ≈1400 Å2 of the TAZ2 surface (Fig. 3 B and C).
Cross-references: PDB:2KJE
BMRB:16318
Protein: DP01150 (UniProt P03255)
Region: residues 27	to 91
Annotation: molecular adaptor activity (Molecular function)
Evidence: nuclear magnetic resonance spectroscopy evidence used in manual assertion
Supporting statements:
Upon titration with pRb, the A53 cross peak shifts in slow exchange from its position in the spectrum of the TAZ2 binary complex to its position in the binary E1A(27–91):pRb complex (Fig. 5B) while the cross peaks of many residues in the region 39–51 are broadened (Fig. S5), confirming binding of pRb to its cognate site. Thus, despite the close proximity of the pRb and CBP/p300 binding sites in the E1A CR1 region, the NMR data provide unequivocal evidence that both TAZ2 and the pRb pocket domain can bind simultaneously to form a ternary TAZ2-E1A-pRb complex.
Protein: DP01150 (UniProt P03255)
Region: residues 113	to 117
Annotation: protein binding (Molecular function)
Evidence: loss-of-function mutant phenotype evidence used in manual assertion
Supporting statements:
To determine whether this motif is involved in binding to BS69, the central invariable leucine residue was mutated into an alanine in E1A. As shown in Fig. 3A, the resulting 12S and 13S E1A (E1A,L115A) mutant proteins failed to interact with BS69.
We found that BS69-type Mynd domains interact through conserved PXLXP peptide motifs with the oncoviral proteins E1A and EBNA2 and with the cellular MGA protein.
Cross-references: ELM:ELME000145
Protein: DP01151 (UniProt P03259)
Region: residues 1	to 266
Annotation: disorder (Structural state)
Evidence: nuclear magnetic resonance spectroscopy evidence used in manual assertion
Supporting statements:
The 1H‐15N heteronuclear single‐quantum coherence (HSQC) spectra of the unbound 15N‐labeled NCBD and 15N‐labeled E1A constructs are poorly dispersed​(Fig.2,2, black), especially in the 1H dimension, since both proteins are intrinsically disordered.
Protein: DP01151 (UniProt P03259)
Region: residues 1	to 81
Annotation: protein binding (Molecular function)
Evidence: nuclear magnetic resonance spectroscopy evidence used in manual assertion
Supporting statements:
Titrations were performed in which aliquots of the unlabeled NCBD were added to 15N‐labeled AdV5 E1A(1‐91) and AdV12 E1A(1‐81) in order to map the NCBD binding sites (Supporting Information Figs. S13 and S17).
The chemical shift perturbations reveal three NCBD binding sites in homologous regions of AdV5 and AdV12 E1A; for AdV12, the NCBD binding sites are located between residues L10‐V30, S40‐L47, and V61‐F78 [Fig.3(B)].
Thus the interaction between E1A and TAZ2 can be characterized as a partly “fuzzy” complex, with one portion of the E1A sequence participating in a strong interaction with TAZ2, while the other portion, corresponding to the N‐terminal region, participating in an interaction characterized by multiple states in intermediate exchange on the NMR time scale.
Protein: DP01151 (UniProt P03259)
Region: residues 13	to 27
Annotation: disorder to order (Structural transition)
Evidence: nuclear magnetic resonance spectroscopy evidence used in manual assertion
Supporting statements:
The large shifts of E1A HSQC cross peaks upon binding to the NCBD reflect formation of structure in the bound state. The secondary structure of AdV12 E1A in complex with the NCBD was predicted from the bound E1A 1H, 13Cα and 15N chemical shifts using the program TALOS+.33 The results ​[Fig.3(D)] show that, upon binding to the NCBD, AdV12 E1A folds to form local helical structure between residues Q13 and F27 in the N‐terminal region and between residues E67 and A73 in the C‐terminal part of the CR1 region.
Protein: DP01151 (UniProt P03259)
Region: residues 1	to 81
Annotation: molecular sequestering activity (Molecular function)
Evidence: nuclear magnetic resonance spectroscopy evidence used in manual assertion
Supporting statements:
Efficient displacement of p53 likely requires E1A to compete with both the AD1 and AD2 motifs for binding to NCBD, which would be favored in E1A constructs containing two or three NCBD binding sites. By competing for binding of p53, E1A may interfere with p53‐activated transcriptional programs that are mediated through interactions with the NCBD (also called IBiD) domain of CBP/p300,25 providing a plausible structural insight into the means whereby E1A might repress p53‐mediated apoptosis by inhibiting binding of p53 to both the NCBD and TAZ2 domains of CBP/p300.
Increased competition efficiency was observed for the longer CR1 constructs (AdV5 E1A(36–91) and AdV12 E1A(35–81)), which contain two NCBD binding sites, and the highest efficiency was observed for AdV5 E1A(1–91) and AdV12 E1A(1–81), an indication that both the N‐terminal and CR1 regions are required for efficient competition with p53 for the NCBD.
Protein: DP01152 (UniProt Q9JK11)
Region: residues 544	to 725
Annotation: disorder (Structural state)
Evidence: nuclear magnetic resonance spectroscopy evidence used in manual assertion
Supporting statements:
A 2D-NMR [15N,1H]-HSQC spectrum confirmed the intrinsically disordered character of Nogo-A-Δ20, as deduced from the low chemical shift dispersion in the 1H dimension. Using triple resonance experiments, 94% of the non-proline backbone residues were assigned. While secondary structure analysis and relaxation measurements highlighted the intrinsically disordered character of Nogo-A-Δ20, three stretches comprising residues 561-EAIQESL-567, 639-EAMNVALKALGT-650, and 693-SNYSEIAK-700 form transient α-helical structures.
Protein: DP01152 (UniProt Q9JK11)
Region: residues 544	to 725
Annotation: protein binding (Molecular function)
Evidence: nuclear magnetic resonance spectroscopy evidence used in manual assertion
Supporting statements:
Nogo-A-Δ20 interacts with sphingosine 1-phosphate receptor 2 (S1PR2) and tetraspanin-3. Extracellular loops 2 and 3 of S1PR2 were concluded to be the primary binding sites for Nogo-A-Δ20, binding occurred with affinities in the nanomolar range.
Protein: DP01152 (UniProt Q9JK11)
Region: residues 544	to 725
Annotation: disorder (Structural state)
Evidence: far-UV circular dichroism evidence used in manual assertion
Supporting statements:
The CD spectrum of Nogo-A-Δ20 with its minimum at around 200 nm suggests a high proportion of unstructured regions, with some residual secondary structure.
Protein: DP01152 (UniProt Q9JK11)
Region: residues 31	to 54
Annotation: disorder (Structural state)
Evidence: curator inference from database used in manual assertion
Supporting statements:
This poly-E region is inferred by the curator to be disordered, based on MobiDB-Lite and according to experimental evidence demonstrating that poly-E repeats display random-coil-like conformation (PMID:16949547)
Protein: DP01153 (UniProt P9WI73)
Region: residues 1	to 75
Annotation: disorder (Structural state)
Evidence: nuclear magnetic resonance spectroscopy evidence used in manual assertion
Supporting statements:
The low signal dispersion of the NORS region indicates already that it is indeed a natively disordered protein (IDP) region. 
The NORS region (approximately residues 1–75) shows strongly negative 13Cα secondary shifts for residues preceding a proline.
Overall, the NORS region appears, as predicted, natively disordered.
The presented NMR structural and dynamic data for the NORS region (His-PknG1–75; Fig. 1, C and D, and supplemental Figs. S2 and S3A) demonstrate that the NORS region is indeed rather unstructured and dynamic.
Protein: DP01153 (UniProt P9WI73)
Region: residues 61	to 65
Annotation: phosphorylation display site (Disorder function)
Evidence: nuclear magnetic resonance spectroscopy evidence used in manual assertion
Supporting statements:
Based on the available assignments, this includes residues near the known in vivo phosphorylation site Thr63 (11) as well as residues near other threonine residues know to be phosphorylated in vitro (Thr23, Thr32, and Thr64) (10).
Protein: DP01153 (UniProt P9WI73)
Region: residues 1	to 75
Annotation: flexible N-terminal tail (Disorder function)
Evidence: nuclear magnetic resonance spectroscopy evidence used in manual assertion
Supporting statements:
The presented NMR structural and dynamic data for the NORS region (His-PknG1–75; Fig. 1, C and D, and supplemental Figs. S2 and S3A) demonstrate that the NORS region is indeed rather unstructured and dynamic.
Protein: DP01153 (UniProt P9WI73)
Region: residues 1	to 73
Annotation: protein autophosphorylation (Biological process)
Evidence: loss-of-function mutant phenotype evidence used in manual assertion
Supporting statements:
Compared with the wild type (Fig. 2A, blue columns), deletion of the N-terminal NORS region reduces PknG catalytic activity significantly (Fig. 2A, green columns), and additional removal of the C-terminal TPRD results in a further reduction (Fig. 2A, red columns). This is consistent with published results (10, 11, 14).
Compared with the wild type (Fig. 2A, blue columns), deletion of the N-terminal NORS region reduces PknG catalytic activity significantly (Fig. 2A, green columns), and additional removal of the C-terminal TPRD results in a further reduction (Fig. 2A, red columns). This is consistent with published results (10, 11, 14).
Protein: DP01153 (UniProt P9WI73)
Region: residues 21	to 25
Annotation: phosphorylation display site (Disorder function)
Evidence: loss-of-function mutant phenotype evidence used in manual assertion
Supporting statements:
As shown in Fig. ​3C, PknG autophosphorylation was reduced when a threonine residue at either position 32 or position 63/64 is mutated into alanine. Autophosphorylation was further reduced when a second threonine residue was mutated into an alanine as demonstrated for construct T32/63/64. 
These results demonstrate that the major autophosphorylation sites of PknG are T23, T32, and T63/64, which are located close to the N terminus (Fig. 3D).
Protein: DP01153 (UniProt P9WI73)
Region: residues 30	to 34
Annotation: phosphorylation display site (Disorder function)
Evidence: loss-of-function mutant phenotype evidence used in manual assertion
Supporting statements:
As shown in Fig. ​3C, PknG autophosphorylation was reduced when a threonine residue at either position 32 or position 63/64 is mutated into alanine. Autophosphorylation was further reduced when a second threonine residue was mutated into an alanine as demonstrated for construct T32/63/64. 
These results demonstrate that the major autophosphorylation sites of PknG are T23, T32, and T63/64, which are located close to the N terminus (Fig. 3D).
Protein: DP01153 (UniProt P9WI73)
Region: residues 61	to 65
Annotation: phosphorylation display site (Disorder function)
Evidence: loss-of-function mutant phenotype evidence used in manual assertion
Supporting statements:
As shown in Fig. ​3C, PknG autophosphorylation was reduced when a threonine residue at either position 32 or position 63/64 is mutated into alanine. Autophosphorylation was further reduced when a second threonine residue was mutated into an alanine as demonstrated for construct T32/63/64. 
These results demonstrate that the major autophosphorylation sites of PknG are T23, T32, and T63/64, which are located close to the N terminus (Fig. 3D).
Protein: DP01153 (UniProt P9WI73)
Region: residues 75	to 147
Annotation: order (Structural state)
Evidence: nuclear magnetic resonance spectroscopy evidence used in manual assertion
Supporting statements:
Thus, it appears to be present in a folded metal-bound state.
Altogether, the data indicate that the RD can switch between a reduced, metal-bound folded state and an oxidized, metal-free unfolded state (Fig. 3B).
Protein: DP01153 (UniProt P9WI73)
Region: residues 75	to 147
Annotation: disorder (Structural state)
Evidence: nuclear magnetic resonance spectroscopy evidence used in manual assertion
Supporting statements:
Indicated by the low signal dispersion, the RD in the oxidized, metal-free form is, as the NORS, largely unfolded.
Altogether, the data indicate that the RD can switch between a reduced, metal-bound folded state and an oxidized, metal-free unfolded state (Fig. 3B).
Protein: DP01153 (UniProt P9WI73)
Region: residues 75	to 147
Annotation: order to disorder (Structural transition)
Evidence: nuclear magnetic resonance spectroscopy evidence used in manual assertion
Supporting statements:
Indicated by the low signal dispersion, the RD in the oxidized, metal-free form is, as the NORS, largely unfolded.
Altogether, the data indicate that the RD can switch between a reduced, metal-bound folded state and an oxidized, metal-free unfolded state (Fig. 3B). Thus, a change of the redox conditions may regulate the catalytic kinase domain by controlled un- and refolding of the RD, which is expected to influence the substrate access.
Protein: DP01153 (UniProt P9WI73)
Region: residues 21	to 64
Annotation: modulation by symbiont of host cellular process (Biological process)
Evidence: loss-of-function mutant phenotype evidence used in manual assertion
Supporting statements:
The results, shown in Fig. ​Fig.5B,5B, show that for mycobacteria expressing PknG-Pmut as well as PknG-ΔN, lysosomal delivery was significantly increased compared to wild-type mycobacteria, suggesting that autophosphorylation is essential for the prevention of mycobacterial trafficking to lysosomes.
Protein: DP01153 (UniProt P9WI73)
Region: residues 21	to 64
Annotation: antiphagocytosis (Biological process)
Evidence: loss-of-function mutant phenotype evidence used in manual assertion
Supporting statements:
The lysosomal transfer of the mycobacterial strains expressing PknG lacking the autophosphorylation sites suggests that autophosphorylation is required for intracellular survival.
While as expected wild-type mycobacteria were able to survive as indicated by the incorporation of [3H]uracil, none of the PknG mutant strains proliferated, as evidenced by the lack of tritium incorporation (Fig. ​5D). We conclude, based upon uracil incorporation, that autophosphorylation of PknG is essential for the intracellular survival of mycobacteria within macrophages.
The virulence of pathogenic mycobacteria is dependent on their capacity to survive within macrophages by preventing phagosome-lysosome fusion (21, 22).
Protein: DP01154 (UniProt P19594)
Region: residues 22	to 64
Annotation: disorder (Structural state)
Evidence: nuclear magnetic resonance spectroscopy evidence used in manual assertion
Supporting statements:
The obtained 13Cα,β chemical shifts were then compared with random-coil values in order to estimate secondary structure propensities. The reduced lunasin form shows some residual secondary structure. The calculated Δδi values are small, as compared to the characteristic values for structured regions in proteins (|Δδi| > 1 ppm), indicating that there is a reduced population of the secondary structures in solution because of an equilibrium with unstructured conformations.
Protein: DP01154 (UniProt P19594)
Region: residues 22	to 64
Annotation: protein binding (Molecular function)
Evidence: nuclear magnetic resonance spectroscopy evidence used in manual assertion
Supporting statements:
Both, the helical region (Glu23-Ile30) as well as the 22 residues of the N-terminus were found to facilitate the binding to deacetylated N-terminal tail of histone H4.
Protein: DP01155 (UniProt O66858)
Region: residues 1	to 60
Annotation: disorder (Structural state)
Evidence: nuclear magnetic resonance spectroscopy evidence used in manual assertion
Supporting statements:
Nearly all of the amide peaks in the previously assigned σ54(60-135) spectrum perfectly match the peaks in the σ54(1-135) spectrum. Almost all of the additional peaks in the σ54(1-135) spectrum have low dispersion of chemical shifts in the 1H dimension. These peaks correspond to the first 60 residues of σ54 and the low shift dispersion is characteristic of an unfolded protein segment.
Protein: DP01155 (UniProt O66858)
Region: residues 1	to 60
Annotation: protein binding (Molecular function)
Evidence: nuclear magnetic resonance spectroscopy evidence used in manual assertion
Supporting statements:
The N-terminal activator interacting domain (AID) of σ54/rpoN binds the transcriptional activator NtrC1. σ54 only binds the transcriptional activators with significant affinity when the activator subunits are primarily in the ATP state.
Protein: DP01155 (UniProt O66858)
Region: residues 1	to 60
Annotation: disorder to order (Structural transition)
Evidence: nuclear magnetic resonance spectroscopy evidence used in manual assertion
Supporting statements:
The σ54 AID becomes structured after associating with the core loops of the transcriptional activator NtrC1C in its ATP state and the primary site of the interaction is the first predicted helix (residues 6-12).