LiteFold/DisProt huggingface dataset:
Protein: DP03007 (UniProt P97784)
Region: residues 494	to 497
Annotation: selective autophagy (Biological process)
Evidence: co-immunoprecipitation evidence used in manual assertion
Supporting statements:
We then determined the role of each LIR motif in degradation of CRY1 by expressing FLAG-tagged WT-CRY1 plasmid and each CRY1 mutant LIR plasmid (mLIR1, mLIR2, mLIR3, and mLIR4 as in Figure 5B) in liver via tail vein injections using the jet-PEI in vivo transfection system (Chang et al., 2014) (Figure S5A).
Strikingly, mLIR1-CRY1 and mLIR4-CRY1 accumulated significantly more than mLIR2-CRY1 and mLIR3-CRY1 or WT-CRY1. Levels of mLIR2 and mLIR3 CRY1 were moderately higher than WT-CRY1, but differences between these groups remained statistically insignificant (Figure 5C). These results indicate that LIR1 (271DLYKKV276) and LIR4 (492SRYRGL497) are required for degradation of CRY1
by autophagy. Accumulation of mLIR1-CRY1 and mLIR4-CRY1 did not occur from reduced autophagy per se, indicated by equivalent LC3-II flux in livers injected with WT or mLIR-CRY1 plasmids (Figure 5D), or from changes in transfection
determined by qPCR showing equivalent Cry1 expression in
livers injected with WT and mLIR-CRY1 plasmids (Figure S5E).
CoIP in 293T cells confirmed that interactions of mLIR1-CRY1
and mLIR4-CRY1 with GFP-tagged LC3 were remarkably
reduced compared with WT-CRY1, mLIR2-CRY1, or mLIR3-
CRY1 (Figure S5F). These results are consistent with significant
accumulation of mLIR1-CRY1 and mLIR4-CRY1 and moderate
accumulation of mLIR2 and mLIR3 CRY1 in liver compared
with WT-CRY1 (Figure 5C). Consistent with our observation that accumulation of CRY1 in Atg7KO mice associates with
decreased BMAL1 levels (Figure 2J), accumulation of mLIR1-
CRY1 or mLIR4-CRY1 each associated with reduced BMAL1
levels (Figure 5E), indicating that expressing autophagy-resistant
forms of CRY1 is sufficient to disrupt the liver clock.
In the article, the functional LIR motif YRGL in positions 494-497 corresponds to LIR4.
The non-functional LIR motif YQQL in positions 488-491, and the functional LIR motif YRGL in positions 494-497, are both incorporated inside the disordered region fragment in positions 471-606.
mLIR4-CRY1 (492SRARGA497)
Figure 5. LIR Motifs Determine CRY1 Degradation and Regulation of Gluconeogenesis
(A) Murine CRY1 has 13 LIR motifs (green).
(B) Inactivation of selected LIR motifs (mLIR1-4) on CRY1 via mutagenesis of tyrosine (Y), valine (V), or leucine (L) residues (green) to alanine (A) (red).
(C) IB for FLAG in livers from male mice at 7 p.m. expressing FLAG-tagged WT-CRY1 plasmid or each FLAG-tagged CRY1 LIR mutant plasmid (mLIR1–4); n = 12.
(D) IB for LC3 in livers from male mice at 7 p.m. expressing FLAG-tagged WT-CRY1 or each CRY1 LIR mutant (mLIR1–4) and cultured in presence or absence of
Lys Inh for 2 hr; n = 7–10.
(E and F) IB for BMAL1 and G6P in livers from male mice at 7 p.m. expressing FLAG-tagged WT-CRY1 plasmid or each CRY1 LIR mutant plasmid (mLIR1–4);
n = 8–12.
Protein: DP03007 (UniProt P97784)
Region: residues 494	to 497
Annotation: protein binding (Molecular function)
Evidence: co-immunoprecipitation evidence used in manual assertion
Supporting statements:
We then determined the role of each LIR motif in degradation of CRY1 by expressing FLAG-tagged WT-CRY1 plasmid and each CRY1 mutant LIR plasmid (mLIR1, mLIR2, mLIR3, and mLIR4 as in Figure 5B) in liver via tail vein injections using the jet-PEI in vivo transfection system (Chang et al., 2014) (Figure S5A).
Strikingly, mLIR1-CRY1 and mLIR4-CRY1 accumulated significantly more than mLIR2-CRY1 and mLIR3-CRY1 or WT-CRY1. Levels of mLIR2 and mLIR3 CRY1 were moderately higher than WT-CRY1, but differences between these groups remained statistically insignificant (Figure 5C). These results indicate that LIR1 (271DLYKKV276) and LIR4 (492SRYRGL497) are required for degradation of CRY1
by autophagy. Accumulation of mLIR1-CRY1 and mLIR4-CRY1 did not occur from reduced autophagy per se, indicated by equivalent LC3-II flux in livers injected with WT or mLIR-CRY1 plasmids (Figure 5D), or from changes in transfection
determined by qPCR showing equivalent Cry1 expression in
livers injected with WT and mLIR-CRY1 plasmids (Figure S5E).
CoIP in 293T cells confirmed that interactions of mLIR1-CRY1
and mLIR4-CRY1 with GFP-tagged LC3 were remarkably
reduced compared with WT-CRY1, mLIR2-CRY1, or mLIR3-
CRY1 (Figure S5F). These results are consistent with significant
accumulation of mLIR1-CRY1 and mLIR4-CRY1 and moderate
accumulation of mLIR2 and mLIR3 CRY1 in liver compared
with WT-CRY1 (Figure 5C). Consistent with our observation that accumulation of CRY1 in Atg7KO mice associates with
decreased BMAL1 levels (Figure 2J), accumulation of mLIR1-
CRY1 or mLIR4-CRY1 each associated with reduced BMAL1
levels (Figure 5E), indicating that expressing autophagy-resistant
forms of CRY1 is sufficient to disrupt the liver clock.
In the article, the functional LIR motif YRGL in positions 494-497 corresponds to LIR4.
The non-functional LIR motif YQQL in positions 488-491, and the functional LIR motif YRGL in positions 494-497, are both incorporated inside the disordered region fragment in positions 471-606.
mLIR4-CRY1 (492SRARGA497)
Figure 5. LIR Motifs Determine CRY1 Degradation and Regulation of Gluconeogenesis
(A) Murine CRY1 has 13 LIR motifs (green).
(B) Inactivation of selected LIR motifs (mLIR1-4) on CRY1 via mutagenesis of tyrosine (Y), valine (V), or leucine (L) residues (green) to alanine (A) (red).
(C) IB for FLAG in livers from male mice at 7 p.m. expressing FLAG-tagged WT-CRY1 plasmid or each FLAG-tagged CRY1 LIR mutant plasmid (mLIR1–4); n = 12.
(D) IB for LC3 in livers from male mice at 7 p.m. expressing FLAG-tagged WT-CRY1 or each CRY1 LIR mutant (mLIR1–4) and cultured in presence or absence of
Lys Inh for 2 hr; n = 7–10.
(E and F) IB for BMAL1 and G6P in livers from male mice at 7 p.m. expressing FLAG-tagged WT-CRY1 plasmid or each CRY1 LIR mutant plasmid (mLIR1–4);
n = 8–12.
Protein: DP03007 (UniProt P97784)
Region: residues 494	to 497
Annotation: protein binding (Molecular function)
Evidence: mutant phenotype evidence used in manual assertion
Supporting statements:
We then determined the role of each LIR motif in degradation of CRY1 by expressing FLAG-tagged WT-CRY1 plasmid and each CRY1 mutant LIR plasmid (mLIR1, mLIR2, mLIR3, and mLIR4 as in Figure 5B) in liver via tail vein injections using the jet-PEI in vivo transfection system (Chang et al., 2014) (Figure S5A).
Strikingly, mLIR1-CRY1 and mLIR4-CRY1 accumulated significantly more than mLIR2-CRY1 and mLIR3-CRY1 or WT-CRY1. Levels of mLIR2 and mLIR3 CRY1 were moderately higher than WT-CRY1, but differences between these groups remained statistically insignificant (Figure 5C). These results indicate that LIR1 (271DLYKKV276) and LIR4 (492SRYRGL497) are required for degradation of CRY1
by autophagy. Accumulation of mLIR1-CRY1 and mLIR4-CRY1 did not occur from reduced autophagy per se, indicated by equivalent LC3-II flux in livers injected with WT or mLIR-CRY1 plasmids (Figure 5D), or from changes in transfection
determined by qPCR showing equivalent Cry1 expression in
livers injected with WT and mLIR-CRY1 plasmids (Figure S5E).
CoIP in 293T cells confirmed that interactions of mLIR1-CRY1
and mLIR4-CRY1 with GFP-tagged LC3 were remarkably
reduced compared with WT-CRY1, mLIR2-CRY1, or mLIR3-
CRY1 (Figure S5F). These results are consistent with significant
accumulation of mLIR1-CRY1 and mLIR4-CRY1 and moderate
accumulation of mLIR2 and mLIR3 CRY1 in liver compared
with WT-CRY1 (Figure 5C). Consistent with our observation that accumulation of CRY1 in Atg7KO mice associates with
decreased BMAL1 levels (Figure 2J), accumulation of mLIR1-
CRY1 or mLIR4-CRY1 each associated with reduced BMAL1
levels (Figure 5E), indicating that expressing autophagy-resistant
forms of CRY1 is sufficient to disrupt the liver clock.
In the article, the functional LIR motif YRGL in positions 494-497 corresponds to LIR4.
The non-functional LIR motif YQQL in positions 488-491, and the functional LIR motif YRGL in positions 494-497, are both incorporated inside the disordered region fragment in positions 471-606.
mLIR4-CRY1 (492SRARGA497)
Figure 5. LIR Motifs Determine CRY1 Degradation and Regulation of Gluconeogenesis
(A) Murine CRY1 has 13 LIR motifs (green).
(B) Inactivation of selected LIR motifs (mLIR1-4) on CRY1 via mutagenesis of tyrosine (Y), valine (V), or leucine (L) residues (green) to alanine (A) (red).
(C) IB for FLAG in livers from male mice at 7 p.m. expressing FLAG-tagged WT-CRY1 plasmid or each FLAG-tagged CRY1 LIR mutant plasmid (mLIR1–4); n = 12.
(D) IB for LC3 in livers from male mice at 7 p.m. expressing FLAG-tagged WT-CRY1 or each CRY1 LIR mutant (mLIR1–4) and cultured in presence or absence of
Lys Inh for 2 hr; n = 7–10.
(E and F) IB for BMAL1 and G6P in livers from male mice at 7 p.m. expressing FLAG-tagged WT-CRY1 plasmid or each CRY1 LIR mutant plasmid (mLIR1–4);
n = 8–12.
Protein: DP03007 (UniProt P97784)
Region: residues 494	to 497
Annotation: regulation of gluconeogenesis (Biological process)
Evidence: mutant phenotype evidence used in manual assertion
Supporting statements:
LIR Motifs Link CRY1 Degradation to Regulation of Gluconeogenesis
Since increases in hepatocellular CRY1 protein inhibit gluconeo￾genesis, we next tested whether accumulation of mLIR1-CRY1 or mLIR4-CRY1 was sufficient to suppress hepatic glucose production/blood glucose levels. Indeed, mice injected with mLIR1-CRY1 or mLIR4-CRY1, but not mLIR2-CRY1 and mLIR3-CRY1 constructs, displayed reduced G6P protein levels (Figure 5F) and decreased blood glucose levels at 7 p.m. (Figures 5G–5J). Furthermore, mLIR1-CRY1- or mLIR4-CRY1-injected mice, and not the mLIR2-CRY1- and mLIR3-CRY1-injected mice, exhibited less glucose production when subjected to PTTs (Figure 5K), indicating that LIR motifs 271DLYKKV276 and 492SRYRGL497 link CRY1 turnover by autophagy to regulation
of gluconeogenesis. Most surprisingly, CRY1 LIR2 (285SLYGQL290) and LIR4 (492SRYRGL497) are also required for degradation of SCF components Skp1 and FBXL3 by autophagy, since livers injected with mLIR2-CRY1, mLIR3-CRY1, and
mLIR4-CRY1 each showed accumulation of these proteins compared with WT-CRY1 or mLIR1-CRY1 (Figure S5G). These data suggest that SCF components Skp1 and Fbxl3 are likely tar￾geted for autophagic degradation via their association with CRY1 (Xing et al., 2013), which, in turn, binds to LC3 via its LIR motifs.
In the article, the functional LIR motif YRGL in positions 494-497 corresponds to LIR4.
The non-functional LIR motif YQQL in positions 488-491, and the functional LIR motif YRGL in positions 494-497, are both incorporated inside the disordered region fragment in positions 471-606.
mLIR4-CRY1 (492SRARGA497)
Figure 5. LIR Motifs Determine CRY1 Degradation and Regulation of Gluconeogenesis (A) Murine CRY1 has 13 LIR motifs (green). (B) Inactivation of selected LIR motifs (mLIR1-4) on CRY1 via mutagenesis of tyrosine (Y), valine (V), or leucine (L) residues (green) to alanine (A) (red). (C) IB for FLAG in livers from male mice at 7 p.m. expressing FLAG-tagged WT-CRY1 plasmid or each FLAG-tagged CRY1 LIR mutant plasmid (mLIR1–4); n = 12. (D) IB for LC3 in livers from male mice at 7 p.m. expressing FLAG-tagged WT-CRY1 or each CRY1 LIR mutant (mLIR1–4) and cultured in presence or absence of Lys Inh for 2 hr; n = 7–10. (E and F) IB for BMAL1 and G6P in livers from male mice at 7 p.m. expressing FLAG-tagged WT-CRY1 plasmid or each CRY1 LIR mutant plasmid (mLIR1–4); n = 8–12.
Protein: DP03007 (UniProt P97784)
Region: residues 494	to 497
Annotation: regulation of gluconeogenesis (Biological process)
Evidence: qualitative western immunoblotting evidence used in manual assertion
Supporting statements:
LIR Motifs Link CRY1 Degradation to Regulation of Gluconeogenesis
Since increases in hepatocellular CRY1 protein inhibit gluconeo￾genesis, we next tested whether accumulation of mLIR1-CRY1 or mLIR4-CRY1 was sufficient to suppress hepatic glucose production/blood glucose levels. Indeed, mice injected with mLIR1-CRY1 or mLIR4-CRY1, but not mLIR2-CRY1 and mLIR3-CRY1 constructs, displayed reduced G6P protein levels (Figure 5F) and decreased blood glucose levels at 7 p.m. (Figures 5G–5J). Furthermore, mLIR1-CRY1- or mLIR4-CRY1-injected mice, and not the mLIR2-CRY1- and mLIR3-CRY1-injected mice, exhibited less glucose production when subjected to PTTs (Figure 5K), indicating that LIR motifs 271DLYKKV276 and 492SRYRGL497 link CRY1 turnover by autophagy to regulation
of gluconeogenesis. Most surprisingly, CRY1 LIR2 (285SLYGQL290) and LIR4 (492SRYRGL497) are also required for degradation of SCF components Skp1 and FBXL3 by autophagy, since livers injected with mLIR2-CRY1, mLIR3-CRY1, and
mLIR4-CRY1 each showed accumulation of these proteins compared with WT-CRY1 or mLIR1-CRY1 (Figure S5G). These data suggest that SCF components Skp1 and Fbxl3 are likely tar￾geted for autophagic degradation via their association with CRY1 (Xing et al., 2013), which, in turn, binds to LC3 via its LIR motifs.
In the article, the functional LIR motif YRGL in positions 494-497 corresponds to LIR4.
The non-functional LIR motif YQQL in positions 488-491, and the functional LIR motif YRGL in positions 494-497, are both incorporated inside the disordered region fragment in positions 471-606.
mLIR4-CRY1 (492SRARGA497)
Figure 5. LIR Motifs Determine CRY1 Degradation and Regulation of Gluconeogenesis (A) Murine CRY1 has 13 LIR motifs (green). (B) Inactivation of selected LIR motifs (mLIR1-4) on CRY1 via mutagenesis of tyrosine (Y), valine (V), or leucine (L) residues (green) to alanine (A) (red). (C) IB for FLAG in livers from male mice at 7 p.m. expressing FLAG-tagged WT-CRY1 plasmid or each FLAG-tagged CRY1 LIR mutant plasmid (mLIR1–4); n = 12. (D) IB for LC3 in livers from male mice at 7 p.m. expressing FLAG-tagged WT-CRY1 or each CRY1 LIR mutant (mLIR1–4) and cultured in presence or absence of Lys Inh for 2 hr; n = 7–10. (E and F) IB for BMAL1 and G6P in livers from male mice at 7 p.m. expressing FLAG-tagged WT-CRY1 plasmid or each CRY1 LIR mutant plasmid (mLIR1–4); n = 8–12.
Protein: DP03007 (UniProt P97784)
Region: residues 494	to 497
Annotation: positive regulation of gluconeogenesis (Biological process)
Evidence: in vivo protein kinase assay evidence used in manual assertion
Supporting statements:
LIR motifs link CRY1 degradation to regulation of glucose homeostasis
LIR motifs on CRY1 determine their degradation and regulation of gluconeogenesis
Since increases in hepatocellular CRY1 protein inhibit gluconeogenesis, we next tested whether accumulation of mLIR1-CRY1 or mLIR4-CRY1 was sufficient to suppress hepatic glucose production/blood glucose levels. Indeed, mice injected with mLIR1-CRY1 or mLIR4-CRY1, but not mLIR2-CRY1 and mLIR3-CRY1 constructs, displayed reduced G6P protein levels (Fig. 5F) and decreased blood glucose levels at 7pm (Fig. 5G–5J). Furthermore, mLIR1-CRY1 or mLIR4-CRY1-injected mice, and not the mLIR2-CRY1 and mLIR3-CRY1-injected mice, exhibited less glucose production when subjected to PTTs (Fig. 5K) – indicating that LIR motifs 271DLYKKV276 and 492SRYRGL497 link CRY1 turnover by autophagy to regulation of gluconeogenesis.
The non-functional LIR motif YQQL in positions 488-491, and the functional LIR motif YRGL in positions 494-497, are both incorporated inside the disordered region fragment in positions 471-606.
Protein: DP03008 (UniProt P53104)
Region: residues 332	to 586
Annotation: disorder (Structural state)
Evidence: atomic force microscopy evidence used in manual assertion
Supporting statements:
The IDR of Atg1 (D211A) showed a double-Gaussian distribution of R_2D, suggesting interactions between the IDR and the dead kinase domain, in agreement with phosphorylation of the IDR by the N-terminal kinase domain of the WT protein
Protein: DP03010 (UniProt Q5D1E8)
Region: residues 297	to 334
Annotation: disorder (Structural state)
Evidence: X-ray crystallography-based structural model with missing residue coordinates used in manual assertion
Supporting statements:
The CCCH zinc-finger motif (297–334) was totally disordered in our structure of NCD-ZF, although SDS–PAGE analysis confirmed that the CCCH zinc finger was not degraded in the crystal.
Cross-references: PDB:3V33
Protein: DP03010 (UniProt Q5D1E8)
Region: residues 112	to 133
Annotation: disorder (Structural state)
Evidence: X-ray crystallography-based structural model with missing residue coordinates used in manual assertion
Supporting statements:
The N-terminal 22 residues (i.e. 112–133) and residues 216–222 are missing in the final model due to the absence of interpretable electron density.
Cross-references: PDB:3V33
PDB:3V34
PDB:3V32
Protein: DP03011 (UniProt P51787)
Region: residues 574	to 584
Annotation: disorder (Structural state)
Evidence: X-ray crystallography-based structural model with missing residue coordinates used in manual assertion
Supporting statements:
"Residues 574-584 are not observed and must be disordered"
Cross-references: PDB:3BJ4
Protein: DP03012 (UniProt P40818)
Region: residues 888	to 898
Annotation: disorder (Structural state)
Evidence: X-ray crystallography-based structural model with missing residue coordinates used in manual assertion
Supporting statements:
Residues 888– 898, which run antiparallel to helix 9, are disordered.
Cross-references: PDB:2GFO
Protein: DP03012 (UniProt P40818)
Region: residues 734	to 761
Annotation: disorder (Structural state)
Evidence: X-ray crystallography-based structural model with missing residue coordinates used in manual assertion
Supporting statements:
Based on the statement "USP8 Catalytic Domain—At the carboxyl terminus of the
molecule, a 376-residue fragment containing the catalytic
domain of USP8 was crystallized (Fig. 4)." and the missing electron density for this region this segment can considered as disordered.
Cross-references: PDB:2GFO
Protein: DP03013 (UniProt Q16821)
Region: residues 1	to 60
Annotation: disorder (Structural state)
Evidence: X-ray crystallography-based structural model with missing residue coordinates used in manual assertion
Supporting statements:
SDS/PAGE analysis of the crystal revealed no obvious degradation of GM (Fig. 1E), therefore GM residues 1–60 and 82–99 included in the crystalized complex but not observed in the electron density map are most likely disordered
Cross-references: PDB:5ZQV
Protein: DP03013 (UniProt Q16821)
Region: residues 83	to 99
Annotation: disorder (Structural state)
Evidence: X-ray crystallography-based structural model with missing residue coordinates used in manual assertion
Supporting statements:
SDS/PAGE analysis of the crystal revealed no obvious degradation of GM (Fig. 1E), therefore GM residues 1–60 and 82–99 included in the crystalized complex but not observed in the electron density map are most likely disordered
Cys82 is missing from the PDB, unclear if this affects the C-terminal disordered region
Cross-references: PDB:5ZQV
Protein: DP03014 (UniProt P62137)
Region: residues 300	to 330
Annotation: disorder (Structural state)
Evidence: X-ray crystallography-based structural model with missing residue coordinates used in manual assertion
Supporting statements:
Similarly, PP1Cα residues 300–330 that are disordered in the crystal probably do not contribute to binding GM
Cross-references: PDB:5ZQV
Protein: DP03015 (UniProt Q86XI6)
Region: residues 31	to 58
Annotation: disorder (Structural state)
Evidence: X-ray crystallography-based structural model with missing residue coordinates used in manual assertion
Supporting statements:
To test this, we reconstituted a PP1 complex containing PP1Cα (7–300) and the human GL residues 31–105 [referred to as GL (31–105) hereafter] and crystallized it.   
The final model containing PP1Cα residues 7–299 and GL residues 59–77 (Figs. 3B) was refined to a resolution of 3.32 Å, and agrees well with the diffraction data and expected geometric values (Table 2)
Statement in the paper only describes that after crystallization of the N-terminal 31-105 residues, residues 59-77 are present. To assign this IDR region I considered that the original publication 
I) also crystallized the homologous N-terminal of Q16821 (PDB: 5ZQV), where 1-60 and 78-98 residues were described as disordered (see DP03014 - Statement: SDS/PAGE analysis of the crystal revealed no obvious degradation of GM (Fig. 1E), therefore GM residues 1–60 and 82–99 included in the crystalized complex but not observed in the electron density map are most likely disordered) AND II) Missing X-ray coordinates (PDB: 5ZT0) indeed support this region is disordered
Cross-references: PDB:5ZT0
Protein: DP03015 (UniProt Q86XI6)
Region: residues 78	to 105
Annotation: disorder (Structural state)
Evidence: X-ray crystallography-based structural model with missing residue coordinates used in manual assertion
Supporting statements:
To test this, we reconstituted a PP1 complex containing PP1Cα (7–300) and the human GL residues 31–105 [referred to as GL (31–105) hereafter] and crystallized it.   
The final model containing PP1Cα residues 7–299 and GL residues 59–77 (Figs. 3B) was refined to a resolution of 3.32 Å, and agrees well with the diffraction data and expected geometric values (Table 2)

Statement in the paper only describes that after crystallization of the N-terminal 31-105 residues, residues 59-77 are present. To assign this IDR region I considered that the original publication 
I) also crystallized the homologous N-terminal of Q16821 (PDB: 5ZQV), where 1-60 and 78-98 residues were described as disordered (see DP03014 - Statement: SDS/PAGE analysis of the crystal revealed no obvious degradation of GM (Fig. 1E), therefore GM residues 1–60 and 82–99 included in the crystalized complex but not observed in the electron density map are most likely disordered) AND II) Missing X-ray coordinates (PDB: 5ZT0) indeed support this region is disordered
Cross-references: PDB:5ZT0
Protein: DP03016 (UniProt P11274)
Region: residues 622	to 638
Annotation: disorder (Structural state)
Evidence: nuclear magnetic resonance spectroscopy evidence used in manual assertion
Supporting statements:
The α4–α5 loop of the Bcr-Abl DH domain is very dynamic and does not adopt a preferred conformation (Fig. 2a).
Cross-references: PDB:5N6R
Protein: DP03016 (UniProt P11274)
Region: residues 624	to 637
Annotation: disorder (Structural state)
Evidence: X-ray crystallography-based structural model with missing residue coordinates used in manual assertion
Supporting statements:
No electron density was observed for the extended flexible α4–α5
loop region seen in the NMR structure, so this loop was not
included in the crystallographic model.
Cross-references: PDB:5N7E
Protein: DP03018 (UniProt P10565)
Region: residues 1	to 34
Annotation: disorder (Structural state)
Evidence: X-ray crystallography-based structural model with missing residue coordinates used in manual assertion
Supporting statements:
Residues 1-11 of BinA and residues 1-34 of BinB were disordered in the electron density map and therefore not included in the model (crystallization at pH 7.0)
Cross-references: PDB:5FOZ
PDB:5FOY
PDB:5G37
Protein: DP03019 (UniProt P30996)
Region: residues 205	to 214
Annotation: disorder (Structural state)
Evidence: X-ray crystallography-based structural model with missing residue coordinates used in manual assertion
Supporting statements:
The loop region Asp205-Thr214 is disordered and not modeled in both structures. Loop Glu249-Ile262 disordered and hence not modeled in form I is ordered in the form II crystal. The C-terminal residues (Val422- Lys439) are not modeled due to poor electron density in both structures. The absence of the C-terminal residues and the disordered region (Glu249-Ile262) is not due to autolysis as shown by SDS-PAGE analysis on crystals of both forms (data not shown) (24, 25).”
Cross-references: PDB:2A97