LiteFold/DisProt huggingface dataset:
Protein: DP00111 (UniProt P27577)
Region: residues 244	to 301
Annotation: nucleic acid binding (Molecular function)
Evidence: nuclear magnetic resonance spectroscopy evidence used in manual assertion
Supporting statements:
ΔN2445P, a form which is homogenously phosphorylated by CaMKII, contains five specific phosphoserines in the serine-rich region (SRR, residues 244 to 300) (Fig. 1C) and appears to undergo the same structural transition upon DNA binding as do unmodified ΔN244 (fig. S1E) and other Ets-1 species (3, 7, 11).
Protein: DP00111 (UniProt P27577)
Region: residues 29	to 49
Annotation: disorder (Structural state)
Evidence: nuclear magnetic resonance spectroscopy evidence used in manual assertion
Supporting statements:
In contrast, residues 31–34, 36–37, 43–45, and 47–49 at the N terminus and 135–138 at the C terminus of Ets-1(29–138) are motionally disordered on a nano- to picosecond time scale as evident by NOEs < 0.5.
The N and C termini of the molecule (residues 29–49 and 135–138) are disordered as evidenced by both high structural rms deviations and 15N NMR relaxation data.
The region of Ets-1(29–138) that precedes helix H1 is disordered.
Cross-references: PDB:2JV3
Protein: DP00111 (UniProt P27577)
Region: residues 29	to 49
Annotation: phosphorylation display site (Disorder function)
Evidence: nuclear magnetic resonance spectroscopy evidence used in manual assertion
Supporting statements:
As shown in Fig. ​Fig.22D, the chemical shift perturbations caused by the modifications were highly localized to the amino acids immediately adjacent to Leu-36 and Thr-38. Thus, within the context of Ets-1(29–138), phosphorylation of Thr-38 does not significantly perturb the disordered character of the MAP kinase substrate site or its adjacent amino acids, nor alter the structure or oligomerization state of the PNT domain.
Protein: DP00111 (UniProt P27577)
Region: residues 29	to 49
Annotation: flexible N-terminal tail (Disorder function)
Evidence: nuclear magnetic resonance spectroscopy evidence used in manual assertion
Supporting statements:
In contrast, residues 31–34, 36–37, 43–45, and 47–49 at the N terminus and 135–138 at the C terminus of Ets-1(29–138) are motionally disordered on a nano- to picosecond time scale as evident by NOEs < 0.5.
The N and C termini of the molecule (residues 29–49 and 135–138) are disordered as evidenced by both high structural rms deviations and 15N NMR relaxation data.
The region of Ets-1(29–138) that precedes helix H1 is disordered.
Cross-references: PDB:2JV3
Protein: DP00112 (UniProt P22239)
Region: residues 1	to 155
Annotation: disorder (Structural state)
Evidence: far-UV circular dichroism evidence used in manual assertion
Supporting statements:
The CD (circular dichroism) spectra in the far-UV show a strong minimum at 198 nm in the native state which indicates a largely random conformation.
Protein: DP00112 (UniProt P22239)
Region: residues 1	to 155
Annotation: disorder (Structural state)
Evidence: proton-based nuclear magnetic resonance evidence used in manual assertion
Supporting statements:
1H-NMR(nuclear magnetic resonance) spectra in aqueous solution are characterized by a small chemical shift dispersion typical for an unfolded protein; however, the observed line-widths are not typical  for a highly mobile random coil structure.
In order to get some deeper insight into the structure, one-dimensional 1H-NMR spectra were recorded under different conditions (pH 2.3, 4.4 and 6.6, 0 and 100 mM KCI, 10 °C and 35 °C. They were typical for a predominantly non-folded protein.
Assuming that essentially all amide Hα cross peaks are visible in the spectrum, the frequency distribution suggests the protein to be essentially unstructured.
Protein: DP00112 (UniProt P22239)
Region: residues 1	to 155
Annotation: disorder (Structural state)
Evidence: cleavage assay evidence used in manual assertion
Supporting statements:
As a consequence of its loose structure, Dsp16 is extremely sensitive towards proteolysis unless its structure is stabilized by structure-making additives such as trifluoroethanol.
At 20 °C, the protein undergoes slow proteolytic degradation in the course of the equilibration.
Protein: DP00112 (UniProt P22239)
Region: residues 1	to 155
Annotation: disorder (Structural state)
Evidence: chromatography evidence used in manual assertion
Supporting statements:
The protein exhibits anomalous elution behavior, showing a
homogeneous band at = 20 kDa; using an anti-Dspl 6 antiserum (Schneider ef a/., 1993), the authenticity of the protein was clearly confirmed in a Western blot (Figure 4).
Protein: DP00113 (UniProt P31109)
Region: residues 1	to 93
Annotation: disorder (Structural state)
Evidence: far-UV circular dichroism evidence used in manual assertion
Supporting statements:
The evolutionarily conserved SNARE (SNAP receptor) proteins and their complexes are key players in the docking and fusion of secretory vesicles with their target membrane. Biophysical techniques were used to characterize structural and energetic properties of the cytoplasmic domains of the yeast SNAREs Snc1 and Sso1, of the SNAP-25-like domain of Sec9, and of the Sso1:Sec9 and Sso1:Sec9:Snc1 complexes. Individually, all three SNAREs are monomeric; Sso1 shows significant secondary structure while Snc1 and Sec9 are largely unstructured. Ternary SNARE complex formation (KD <50 nM) is accompanied by a more than two-fold increase in secondary structure. This binding induced structure, the large increase in thermal stability, and the self-association of the ternary complex represent conserved properties of SNAREs that are probably important in vesicle docking and fusion.
Protein: DP00113 (UniProt P31109)
Region: residues 1	to 93
Annotation: disorder (Structural state)
Evidence: temperature-induced protein unfolding evidence used in manual assertion
Supporting statements:
The evolutionarily conserved SNARE (SNAP receptor) proteins and their complexes are key players in the docking and fusion of secretory vesicles with their target membrane. Biophysical techniques were used to characterize structural and energetic properties of the cytoplasmic domains of the yeast SNAREs Snc1 and Sso1, of the SNAP-25-like domain of Sec9, and of the Sso1:Sec9 and Sso1:Sec9:Snc1 complexes. Individually, all three SNAREs are monomeric; Sso1 shows significant secondary structure while Snc1 and Sec9 are largely unstructured. Ternary SNARE complex formation (KD <50 nM) is accompanied by a more than two-fold increase in secondary structure. This binding induced structure, the large increase in thermal stability, and the self-association of the ternary complex represent conserved properties of SNAREs that are probably important in vesicle docking and fusion.
Protein: DP00113 (UniProt P31109)
Region: residues 1	to 93
Annotation: disorder to order (Structural transition)
Evidence: far-UV circular dichroism evidence used in manual assertion
Supporting statements:
Individual SNAREs and the Sso1:Sec9c complex are monomeric; the Sso1:Sec9c:Snc1 complex self‐associates.
The individual SNAREs, the Sso1:Sec9c complex, and the Sso1:Sec9c:Snc1 complex are all well‐defined entities (Figs. 1 and 2) that can be isolated chromatographically. CD spectroscopy can therefore be used to investigate possible structural changes that may accompany binding events.
The spectra for Sec9c and Snc1 are very similar to each other and are suggestive of largely random coil conformation. The unstructured state of Sec9c and Snc1 was recently confirmed by ongoing NMR studies (Fiebig et al., unpublished).
Fig. 4 (right panel) shows the CD spectrum recorded from the purified ternary complex. It too shows a significant α‐helical signal, in large excess of that expected from computing the theoretical non‐interacting CD spectrum from spectra of the three individual proteins, or from the observed Sso1:Sec9c complex spectrum and that of Snc1. Again, this increase in mean residue ellipticity could result from increases in any of the individual protein's secondary structure content although most of the changes are likely to occur in Sec9c and in Snc1. The high mean residue ellipticity observed for the ternary complex suggests a large α‐helical content.
Protein: DP00113 (UniProt P31109)
Region: residues 1	to 93
Annotation: protein binding (Molecular function)
Evidence: far-UV circular dichroism evidence used in manual assertion
Supporting statements:
Individual SNAREs and the Sso1:Sec9c complex are monomeric; the Sso1:Sec9c:Snc1 complex self‐associates.
The individual SNAREs, the Sso1:Sec9c complex, and the Sso1:Sec9c:Snc1 complex are all well‐defined entities (Figs. 1 and 2) that can be isolated chromatographically. CD spectroscopy can therefore be used to investigate possible structural changes that may accompany binding events.
Fig. 4 (right panel) shows the CD spectrum recorded from the purified ternary complex. It too shows a significant α‐helical signal, in large excess of that expected from computing the theoretical non‐interacting CD spectrum from spectra of the three individual proteins, or from the observed Sso1:Sec9c complex spectrum and that of Snc1. Again, this increase in mean residue ellipticity could result from increases in any of the individual protein's secondary structure content although most of the changes are likely to occur in Sec9c and in Snc1. The high mean residue ellipticity observed for the ternary complex suggests a large α‐helical content.
Protein: DP00113 (UniProt P31109)
Region: residues 1	to 93
Annotation: molecular adaptor activity (Molecular function)
Evidence: far-UV circular dichroism evidence used in manual assertion
Supporting statements:
Individual SNAREs and the Sso1:Sec9c complex are monomeric; the Sso1:Sec9c:Snc1 complex self‐associates.
The individual SNAREs, the Sso1:Sec9c complex, and the Sso1:Sec9c:Snc1 complex are all well‐defined entities (Figs. 1 and 2) that can be isolated chromatographically. CD spectroscopy can therefore be used to investigate possible structural changes that may accompany binding events.
Fig. 4 (right panel) shows the CD spectrum recorded from the purified ternary complex. It too shows a significant α‐helical signal, in large excess of that expected from computing the theoretical non‐interacting CD spectrum from spectra of the three individual proteins, or from the observed Sso1:Sec9c complex spectrum and that of Snc1. Again, this increase in mean residue ellipticity could result from increases in any of the individual protein's secondary structure content although most of the changes are likely to occur in Sec9c and in Snc1. The high mean residue ellipticity observed for the ternary complex suggests a large α‐helical content.
Protein: DP00113 (UniProt P31109)
Region: residues 1	to 93
Annotation: molecular adaptor activity (Molecular function)
Evidence: experimental evidence used in manual assertion
Supporting statements:
Increase in tryptophan fluorescence upon formation of the Sso1:Sec9c:Snc1 complex.
There is a single tryptophan in the Sso1:Sec9c:Snc1 complex, at position 86 in Snc1 which is close to (within ten residues) its putative transmembrane domain. Fig. 6 shows the result of titrating Snc1 with increasing amounts of binary complex. Formation of the ternary complex causes a significant increase in fluorescence intensity. The increase in fluorescence is saturable and up to saturation is linear with concentration. This behavior could be explained by tight binding and by structural re‐arrangements in the vicinity of the tryptophan residue.
Changes in tryptophan fluorescence resulting from formation of the Sso1:Sec9c:Snc1 complex. The fluorescence intensity ratio is the measured fluorescence intensity divided by the fluorescence intensity of 2.5 μM Snc1 at 350 nm. The increase in fluoresence intensity is saturable, and up to saturation increases linearly with Sso1:Sec9c complex concentration, suggesting very tight binding. All measurements were performed at 25°C.
Increase in fluorescence intensity ratio as a function of Sso1:Sec9c complex concentration.
Protein: DP00113 (UniProt P31109)
Region: residues 1	to 93
Annotation: disorder to order (Structural transition)
Evidence: experimental evidence used in manual assertion
Supporting statements:
Increase in tryptophan fluorescence upon formation of the Sso1:Sec9c:Snc1 complex.
There is a single tryptophan in the Sso1:Sec9c:Snc1 complex, at position 86 in Snc1 which is close to (within ten residues) its putative transmembrane domain. Fig. 6 shows the result of titrating Snc1 with increasing amounts of binary complex. Formation of the ternary complex causes a significant increase in fluorescence intensity. The increase in fluorescence is saturable and up to saturation is linear with concentration. This behavior could be explained by tight binding and by structural re‐arrangements in the vicinity of the tryptophan residue.
Changes in tryptophan fluorescence resulting from formation of the Sso1:Sec9c:Snc1 complex. The fluorescence intensity ratio is the measured fluorescence intensity divided by the fluorescence intensity of 2.5 μM Snc1 at 350 nm. The increase in fluoresence intensity is saturable, and up to saturation increases linearly with Sso1:Sec9c complex concentration, suggesting very tight binding. All measurements were performed at 25°C.
Increase in fluorescence intensity ratio as a function of Sso1:Sec9c complex concentration.
Protein: DP00113 (UniProt P31109)
Region: residues 1	to 93
Annotation: protein binding (Molecular function)
Evidence: experimental evidence used in manual assertion
Supporting statements:
Increase in tryptophan fluorescence upon formation of the Sso1:Sec9c:Snc1 complex.
There is a single tryptophan in the Sso1:Sec9c:Snc1 complex, at position 86 in Snc1 which is close to (within ten residues) its putative transmembrane domain. Fig. 6 shows the result of titrating Snc1 with increasing amounts of binary complex. Formation of the ternary complex causes a significant increase in fluorescence intensity. The increase in fluorescence is saturable and up to saturation is linear with concentration. This behavior could be explained by tight binding and by structural re‐arrangements in the vicinity of the tryptophan residue.
Changes in tryptophan fluorescence resulting from formation of the Sso1:Sec9c:Snc1 complex. The fluorescence intensity ratio is the measured fluorescence intensity divided by the fluorescence intensity of 2.5 μM Snc1 at 350 nm. The increase in fluoresence intensity is saturable, and up to saturation increases linearly with Sso1:Sec9c complex concentration, suggesting very tight binding. All measurements were performed at 25°C.
Increase in fluorescence intensity ratio as a function of Sso1:Sec9c complex concentration.
Protein: DP00113 (UniProt P31109)
Region: residues 1	to 93
Annotation: protein binding (Molecular function)
Evidence: temperature-induced protein unfolding evidence used in manual assertion
Supporting statements:
As a first step towards characterizing the energetics of SNARE assembly, we have measured thermal denaturation profiles of Sso1, the Sso1:Sec9c complex, and the Sso1:Sec9c:Snc1 complex. Fig. 5 (left panel) shows the thermal denaturation profiles for Sso1 and the binary Sso1:Sec9c complex, and Fig. 5 (right panel) shows the thermal denaturation profiles for Sso1 and the ternary Sso1:Sec9c:Snc1 complex. Sso1 melts with a single transition with a T m of about 48°C. The Sso1:Sec9c complex also unfolds in a single transition with a T m of about 50°C. The melting profile of the ternary complex is more complicated, but it shows a cooperative transition at about 71°C.
Thermal stability of Sso1 and of the Sso1:Sec9c and Sso1:Sec9c:Snc1 complexes. Change in mean residue ellipticity at 222 nm (Θ222) was measured as a function of temperature. Buffer conditions were as in Figs. 3 and 4. Measurements were made at 1° temperature increments after 1 min of equilibration, and averaged for 30 s. The dashed line shows the denaturation profile for Sso1 in both panels. Left panel: thermal denaturation profiles for Sso1 and the Sso1:Sec9c complex (solid line), right panel: thermal denaturation profiles for Sso1 and the Sso1:Sec9c:Snc1 complex (solid line).
Protein: DP00113 (UniProt P31109)
Region: residues 1	to 93
Annotation: disorder to order (Structural transition)
Evidence: temperature-induced protein unfolding evidence used in manual assertion
Supporting statements:
As a first step towards characterizing the energetics of SNARE assembly, we have measured thermal denaturation profiles of Sso1, the Sso1:Sec9c complex, and the Sso1:Sec9c:Snc1 complex. Fig. 5 (left panel) shows the thermal denaturation profiles for Sso1 and the binary Sso1:Sec9c complex, and Fig. 5 (right panel) shows the thermal denaturation profiles for Sso1 and the ternary Sso1:Sec9c:Snc1 complex. Sso1 melts with a single transition with a T m of about 48°C. The Sso1:Sec9c complex also unfolds in a single transition with a T m of about 50°C. The melting profile of the ternary complex is more complicated, but it shows a cooperative transition at about 71°C.
Thermal stability of Sso1 and of the Sso1:Sec9c and Sso1:Sec9c:Snc1 complexes. Change in mean residue ellipticity at 222 nm (Θ222) was measured as a function of temperature. Buffer conditions were as in Figs. 3 and 4. Measurements were made at 1° temperature increments after 1 min of equilibration, and averaged for 30 s. The dashed line shows the denaturation profile for Sso1 in both panels. Left panel: thermal denaturation profiles for Sso1 and the Sso1:Sec9c complex (solid line), right panel: thermal denaturation profiles for Sso1 and the Sso1:Sec9c:Snc1 complex (solid line).
Protein: DP00113 (UniProt P31109)
Region: residues 1	to 93
Annotation: molecular adaptor activity (Molecular function)
Evidence: temperature-induced protein unfolding evidence used in manual assertion
Supporting statements:
As a first step towards characterizing the energetics of SNARE assembly, we have measured thermal denaturation profiles of Sso1, the Sso1:Sec9c complex, and the Sso1:Sec9c:Snc1 complex. Fig. 5 (left panel) shows the thermal denaturation profiles for Sso1 and the binary Sso1:Sec9c complex, and Fig. 5 (right panel) shows the thermal denaturation profiles for Sso1 and the ternary Sso1:Sec9c:Snc1 complex. Sso1 melts with a single transition with a T m of about 48°C. The Sso1:Sec9c complex also unfolds in a single transition with a T m of about 50°C. The melting profile of the ternary complex is more complicated, but it shows a cooperative transition at about 71°C.
Thermal stability of Sso1 and of the Sso1:Sec9c and Sso1:Sec9c:Snc1 complexes. Change in mean residue ellipticity at 222 nm (Θ222) was measured as a function of temperature. Buffer conditions were as in Figs. 3 and 4. Measurements were made at 1° temperature increments after 1 min of equilibration, and averaged for 30 s. The dashed line shows the denaturation profile for Sso1 in both panels. Left panel: thermal denaturation profiles for Sso1 and the Sso1:Sec9c complex (solid line), right panel: thermal denaturation profiles for Sso1 and the Sso1:Sec9c:Snc1 complex (solid line).
Protein: DP00113 (UniProt P31109)
Region: residues 1	to 93
Annotation: disorder (Structural state)
Evidence: experimental evidence used in manual assertion
Supporting statements:
There is a single tryptophan in the Sso1:Sec9c:Snc1 complex, at position 86 in Snc1 which is close to (within ten residues) its putative transmembrane domain. Fig. 6 shows the result of titrating Snc1 with increasing amounts of binary complex. Formation of the ternary complex causes a significant increase in fluorescence intensity. The increase in fluorescence is saturable and up to saturation is linear with concentration. This behavior could be explained by tight binding and by structural re‐arrangements in the vicinity of the tryptophan residue.
Changes in tryptophan fluorescence resulting from formation of the Sso1:Sec9c:Snc1 complex. The fluorescence intensity ratio is the measured fluorescence intensity divided by the fluorescence intensity of 2.5 μM Snc1 at 350 nm. The increase in fluoresence intensity is saturable, and up to saturation increases linearly with Sso1:Sec9c complex concentration, suggesting very tight binding. All measurements were performed at 25°C. (a) Emission spectra of Snc1 (2.5 μM) (lower line) and of Snc1 (2.5 μM) combined with purified Sso1:Sec9c complex (3.2 μM) (upper line). (b) Increase in fluorescence intensity ratio as a function of Sso1:Sec9c complex concentration.
Protein: DP00116 (UniProt P81455)
Region: residues 1	to 49
Annotation: disorder (Structural state)
Evidence: nuclear magnetic resonance spectroscopy evidence used in manual assertion
Supporting statements:
Neither the 3,5 (6.70-6.90 ppm) nor the 2.6 (7.00-7.24 ppm) resonances of the four Tyr residues in apo BGP were equivalent, indicating that the apoprotein had some tertiary structure (Figure 1A).
Protein: DP00116 (UniProt P81455)
Region: residues 1	to 49
Annotation: disorder to order (Structural transition)
Evidence: nuclear magnetic resonance spectroscopy evidence used in manual assertion
Supporting statements:
These results showed that dog osteocalcin undergoes a major conformational change when it associates with calcium and that its calcium affinity is relatively strong (Kd < 10-4 M).
Protein: DP00116 (UniProt P81455)
Region: residues 1	to 49
Annotation: calcium ion binding (Molecular function)
Evidence: nuclear magnetic resonance spectroscopy evidence used in manual assertion
Supporting statements:
These results showed that dog osteocalcin undergoes a major conformational change when it associates with calcium and that its calcium affinity is relatively strong (Kd < 10-4 M).
Protein: DP00118 (UniProt P05059)
Region: residues 1	to 449
Annotation: disorder (Structural state)
Evidence: nuclear magnetic resonance spectroscopy evidence used in manual assertion
Supporting statements:
The NMR spectrum of purified chromogranin A in D2O at pH 6.05 shown in Fig. 7(a) is in general closely similar to that computed for an extended random coil by the method of MACDONALD & PHILLIPS (1969) shown in Fig. 7(c).
Protein: DP00118 (UniProt P05059)
Region: residues 407	to 431
Annotation: disorder (Structural state)
Evidence: far-UV circular dichroism evidence used in manual assertion
Supporting statements:
The CD spectra showed that the magnitude of molar ellipticity at 222 nm increased as the pH was changed from 7.5 to 5.5. The increase in the magnitude of the molar ellipticity in the region from -207 to -225 nm indicates an increase of a-helicity at pH 5.5, while the decrease in the magnitude of molar ellipticity at -200 nm indicates a  decrease of coil structure as the pH changed from 7.5 to 5.5 [13-15].
Protein: DP00118 (UniProt P05059)
Region: residues 407	to 431
Annotation: disorder to order (Structural transition)
Evidence: far-UV circular dichroism evidence used in manual assertion
Supporting statements:
The CD spectra showed that the magnitude of molar ellipticity at 222 nm increased as the pH was changed from 7.5 to 5.5. The increase in the magnitude of the molar ellipticity in the region from -207 to -225 nm indicates an increase of a-helicity at pH 5.5, while the decrease in the magnitude of molar ellipticity at -200 nm indicates a  decrease of coil structure as the pH changed from 7.5 to 5.5 [13-15].
Protein: DP00118 (UniProt P05059)
Region: residues 1	to 449
Annotation: disorder to order (Structural transition)
Evidence: fluorescence evidence used in manual assertion
Supporting statements:
Therefore, the increased binding of bis-ANS is probably due to a Ca2+-induced conformational change in CGA rather than a mere charge neutralization of bis-ANS by Ca2+.
Protein: DP00118 (UniProt P05059)
Region: residues 1	to 449
Annotation: calcium ion binding (Molecular function)
Evidence: fluorescence evidence used in manual assertion
Supporting statements:
Therefore, the increased binding of bis-ANS is probably due to a Ca2+-induced conformational change in CGA rather than a mere charge neutralization of bis-ANS by Ca2+.