LiteFold/DisProt huggingface dataset:
Protein: DP03466 (UniProt E3T1W8)
Region: residues 295	to 312
Annotation: disorder (Structural state)
Evidence: X-ray crystallography-based structural model with missing residue coordinates used in manual assertion
Supporting statements:
This region is missing from the structural model (see cross reference) of this enzyme.
Cross-references: PDB:5HHZ
Protein: DP03466 (UniProt E3T1W8)
Region: residues 532	to 541
Annotation: disorder (Structural state)
Evidence: X-ray crystallography-based structural model with missing residue coordinates used in manual assertion
Supporting statements:
The C-terminal decapeptide is unmodelled in the structure (see cross reference) of this enzyme.
Cross-references: PDB:5HHZ
Protein: DP03466 (UniProt E3T1W8)
Region: residues 532	to 541
Annotation: disorder (Structural state)
Evidence: X-ray crystallography-based structural model with missing residue coordinates used in manual assertion
Supporting statements:
The C-terminal decapeptide is unmodelled in the structure (see cross reference) of this enzyme.
Cross-references: PDB:5HMR
Protein: DP03466 (UniProt E3T1W8)
Region: residues 22	to 39
Annotation: disorder (Structural state)
Evidence: X-ray crystallography-based structural model with missing residue coordinates used in manual assertion
Supporting statements:
The N-terminal segment, following the signal peptide (1-21), is unmodelled in the structure (see cross reference) of this enzyme.
Cross-references: PDB:5HMR
Protein: DP03466 (UniProt E3T1W8)
Region: residues 22	to 37
Annotation: disorder (Structural state)
Evidence: X-ray crystallography-based structural model with missing residue coordinates used in manual assertion
Supporting statements:
The N-terminal segment, following the signal peptide (1-21), is unmodelled in the structure (see cross reference) of this enzyme.
Cross-references: PDB:5HQX
Protein: DP03466 (UniProt E3T1W8)
Region: residues 293	to 318
Annotation: disorder (Structural state)
Evidence: X-ray crystallography-based structural model with missing residue coordinates used in manual assertion
Supporting statements:
This region is missing from the structural model (see cross reference) of this enzyme.
Cross-references: PDB:5HQX
Protein: DP03466 (UniProt E3T1W8)
Region: residues 292	to 318
Annotation: disorder (Structural state)
Evidence: X-ray crystallography-based structural model with missing residue coordinates used in manual assertion
Supporting statements:
This region is missing from the structural model (see cross reference) of this enzyme.
Cross-references: PDB:5HMR
Protein: DP03466 (UniProt E3T1W8)
Region: residues 294	to 318
Annotation: disorder (Structural state)
Evidence: X-ray crystallography-based structural model with missing residue coordinates used in manual assertion
Supporting statements:
A significant difference is the presence of two helices (α10 and α11) above the entrance to the substrate channel, which is similar to the structure of ZmCKX1. On the contrary, the equivalent region is highly disordered in ZmCKX4.
Cross-references: PDB:6YAO
PDB:6YAP
Protein: DP03466 (UniProt E3T1W8)
Region: residues 22	to 39
Annotation: disorder (Structural state)
Evidence: X-ray crystallography-based structural model with missing residue coordinates used in manual assertion
Supporting statements:
The N-terminal segment, following the signal peptide (1-21), is unmodelled in both structures (see cross references) of this enzyme.
Cross-references: PDB:6YAO
PDB:6YAP
Protein: DP03466 (UniProt E3T1W8)
Region: residues 532	to 541
Annotation: disorder (Structural state)
Evidence: X-ray crystallography-based structural model with missing residue coordinates used in manual assertion
Supporting statements:
The C-terminal decapeptide is unmodelled in both structures (see cross references) of this enzyme.
Cross-references: PDB:6YAO
PDB:6YAP
Protein: DP03467 (UniProt Q709Q5)
Region: residues 293	to 302
Annotation: disorder (Structural state)
Evidence: X-ray crystallography-based structural model with missing residue coordinates used in manual assertion
Supporting statements:
The major difference concerns the region of residues 294–325, which is composed of two helices and a loop and which belongs to the substrate binding domain. This region, which is well deﬁned in the ZmCKO1 structure, is disordered in the high resolution structures of ZmCKO4a and ZmCKO2 and adopts a different conformation in the low resolution structure of ZmCKO2 (Fig. 4A). The region delineating the substrate entrance comprises residues surrounding the ribose moiety of cytokinin substrate (N303 and T304 in ZmCKO1) and is most likely
responsible for the kinetic differences between the E381 variants and the ZmCKO isoforms.
Cross-references: PDB:4MLA
Protein: DP03467 (UniProt Q709Q5)
Region: residues 293	to 302
Annotation: molecular function regulator (Molecular function)
Evidence: X-ray crystallography-based structural model with missing residue coordinates used in manual assertion
Supporting statements:
The major difference concerns the region of residues 294–325, which is composed of two helices and a loop and which belongs to the substrate binding domain. This region, which is well deﬁned in the ZmCKO1 structure, is disordered in the high resolution structures of ZmCKO4a and ZmCKO2 and adopts a different conformation in the low resolution structure of ZmCKO2 (Fig. 4A). The region delineating the substrate entrance comprises residues surrounding the ribose moiety of cytokinin substrate (N303 and T304 in ZmCKO1) and is most likely
responsible for the kinetic differences between the E381 variants and the ZmCKO isoforms.
Cross-references: PDB:4MLA
Protein: DP03469 (UniProt Q8VZS8)
Region: residues 8	to 30
Annotation: disorder (Structural state)
Evidence: X-ray crystallography-based structural model with missing residue coordinates used in manual assertion
Supporting statements:
The PYL1 construct composed of 8–211 residues (PYL1(8–211)) was used for the crystallization of PYL1–(1)-ABA, and was also applied to all biochemical assays, such as the ITC, SPR, pull-down binding assay and ABI1 inhibitory assay. 
Due to the poor electron density, we could not build a structural model of the β6-β7 loops of chains A, B, and C, the β5-β6 loop of chain C, the  α1-β1 loop of chain C, or several terminal residues.
Residues 8-30 are absent from the structural model (see cross reference).
Cross-references: PDB:3JRS
Protein: DP03469 (UniProt Q8VZS8)
Region: residues 19	to 30
Annotation: disorder (Structural state)
Evidence: X-ray crystallography-based structural model with missing residue coordinates used in manual assertion
Supporting statements:
To obtain a stable ABI1–PYL1 complex, the His6-tagged core domain (residues 118–425) of ABI1 was coexpressed with PYL1 (residues 19–210) in E. coli BL21(DE3).
Residues 19-30 are absent from the structural model (see cross reference).
Cross-references: PDB:3KDJ
Protein: DP03470 (UniProt P47442)
Region: residues 124	to 148
Annotation: disorder (Structural state)
Evidence: X-ray crystallography-based structural model with missing residue coordinates used in manual assertion
Supporting statements:
A construct spanning MG200 residues 124–207, which includes the complete MG200 EAGR box, yielded highly pure and soluble protein that was crystallized as trigonal crystals.
The structure determined includes the co-ordinates of residues from Gln149 to Glu203 for the two subunits found in the crystal asymmetric unit (Fig. 1).
Cross-references: PDB:4DCZ
Protein: DP03471 (UniProt Q81GI3)
Region: residues 102	to 117
Annotation: disorder (Structural state)
Evidence: X-ray crystallography-based structural model with missing residue coordinates used in manual assertion
Supporting statements:
In addition, the residues between 102–117, 149–160, and 197–202 were disordered.
The residues between 102–117, 149–160, and 197–202 are not visible in the electron density maps.
Cross-references: PDB:3OJE
Protein: DP03471 (UniProt Q81GI3)
Region: residues 149	to 160
Annotation: disorder (Structural state)
Evidence: X-ray crystallography-based structural model with missing residue coordinates used in manual assertion
Supporting statements:
In addition, the residues between 102–117, 149–160, and 197–202 were disordered.
The residues between 102–117, 149–160, and 197–202 are not visible in the electron density maps.
Cross-references: PDB:3OJE
Protein: DP03471 (UniProt Q81GI3)
Region: residues 149	to 160
Annotation: disorder to order (Structural transition)
Evidence: X-ray crystallography-based structural model with missing residue coordinates used in manual assertion
Supporting statements:
The disordered regions in the apo structure become mostly α-helices and loops upon binding of NADP+ and INH (or presumably the substrate).
The three disordered stretches in the apo structure became ordered in the ternary complex, and the residues 149–160 and 197–202 were involved in the interaction with NADP+ as shown in the figure.
The three stretches of residues (residues 102–117, 149–160 and 197–202) that are disordered in the apo structure become well organized in the ternary complex, and the overall structure of the ternary complex is almost identical to other FabIs reported previously.
Cross-references: PDB:3OJF
Protein: DP03471 (UniProt Q81GI3)
Region: residues 102	to 117
Annotation: disorder to order (Structural transition)
Evidence: X-ray crystallography-based structural model with missing residue coordinates used in manual assertion
Supporting statements:
The disordered regions in the apo structure become mostly α-helices and loops upon binding of NADP+ and INH (or presumably the substrate).
The three disordered stretches in the apo structure became ordered in the ternary complex, and the residues 149–160 and 197–202 were involved in the interaction with NADP+ as shown in the figure.
The three stretches of residues (residues 102–117, 149–160 and 197–202) that are disordered in the apo structure become well organized in the ternary complex, and the overall structure of the ternary complex is almost identical to other FabIs reported previously.
Cross-references: PDB:3OJF
Protein: DP03471 (UniProt Q81GI3)
Region: residues 102	to 117
Annotation: small molecule binding (Molecular function)
Evidence: X-ray crystallography-based structural model with missing residue coordinates used in manual assertion
Supporting statements:
The three stretches disordered in the apo structure are important in the cofactor and the inhibitor binding as well as in tetramer formation.
The disordered regions in the apo structure become mostly α-helices and loops upon binding of NADP+ and INH (or presumably the substrate).
Cross-references: PDB:3OJF
Protein: DP03471 (UniProt Q81GI3)
Region: residues 149	to 160
Annotation: small molecule binding (Molecular function)
Evidence: X-ray crystallography-based structural model with missing residue coordinates used in manual assertion
Supporting statements:
The three stretches disordered in the apo structure are important in the cofactor and the inhibitor binding as well as in tetramer formation.
The disordered regions in the apo structure become mostly α-helices and loops upon binding of NADP+ and INH (or presumably the substrate).
The three disordered stretches in the apo structure became ordered in the ternary complex, and the residues 149–160 and 197–202 were involved in the interaction with NADP+ as shown in the figure.
Cross-references: PDB:3OJF
Protein: DP03471 (UniProt Q81GI3)
Region: residues 149	to 160
Annotation: self-assembly (Disorder function)
Evidence: X-ray crystallography-based structural model with missing residue coordinates used in manual assertion
Supporting statements:
The three stretches disordered in the apo structure are important in the cofactor and the inhibitor binding as well as in tetramer formation.
The molecules A and D (B and C) form another extensive interface in the ternary complex, and they involve the residues that are disordered in the apo structure and highlighted in cyan.
The second interface involves interactions between molecules A and D (A:D), and molecules B and C (B:C). These interactions were contributed by the residues from α3 to α7, and the loop β6 which composed of two in the three stretches, namely residues 102–117 and 149–160, disordered in the apo structure (see Fig. 2D and E), i.e., these disordered regions were crucial for tetramer formation.
The apo BcFabL exists as a homo-dimer both in crystal and solution, and the three disordered stretches affect both in the cofactor and the inhibitor binding and in tetramer formation.
Together these suggest that there is a transition from the dimer to tetramer and the three disordered stretches in the apo structure are important not only in binding of the cofactor and the inhibitor but also in the tetramer formation.
Cross-references: PDB:3OJF
Protein: DP03471 (UniProt Q81GI3)
Region: residues 102	to 117
Annotation: self-assembly (Disorder function)
Evidence: X-ray crystallography-based structural model with missing residue coordinates used in manual assertion
Supporting statements:
The three stretches disordered in the apo structure are important in the cofactor and the inhibitor binding as well as in tetramer formation.
The molecules A and D (B and C) form another extensive interface in the ternary complex, and they involve the residues that are disordered in the apo structure and highlighted in cyan.
The second interface involves interactions between molecules A and D (A:D), and molecules B and C (B:C). These interactions were contributed by the residues from α3 to α7, and the loop β6 which composed of two in the three stretches, namely residues 102–117 and 149–160, disordered in the apo structure (see Fig. 2D and E), i.e., these disordered regions were crucial for tetramer formation.
The apo BcFabL exists as a homo-dimer both in crystal and solution, and the three disordered stretches affect both in the cofactor and the inhibitor binding and in tetramer formation.
Together these suggest that there is a transition from the dimer to tetramer and the three disordered stretches in the apo structure are important not only in binding of the cofactor and the inhibitor but also in the tetramer formation.
Cross-references: PDB:3OJF
Protein: DP03471 (UniProt Q81GI3)
Region: residues 99	to 111
Annotation: disorder (Structural state)
Evidence: X-ray crystallography-based structural model with missing residue coordinates used in manual assertion
Supporting statements:
In the dimeric form, the substrate-binding loop (SBL, 197–203), the second substrate-binding loop (SBL-2, 99–111), and the active site loop (ASL, 150–160), which play a key role in catalytic activity, were disordered (Fig. 2E).
Cross-references: PDB:5YCS
PDB:5YCX
Protein: DP03471 (UniProt Q81GI3)
Region: residues 150	to 160
Annotation: disorder (Structural state)
Evidence: X-ray crystallography-based structural model with missing residue coordinates used in manual assertion
Supporting statements:
In the dimeric form, the substrate-binding loop (SBL, 197–203), the second substrate-binding loop (SBL-2, 99–111), and the active site loop (ASL, 150–160), which play a key role in catalytic activity, were disordered (Fig. 2E).
Cross-references: PDB:5YCS
PDB:5YCX
Protein: DP03471 (UniProt Q81GI3)
Region: residues 150	to 160
Annotation: disorder to order (Structural transition)
Evidence: X-ray crystallography-based structural model with missing residue coordinates used in manual assertion
Supporting statements:
ASL, which is disordered in the dimer, is rearranged by the helix-helix α7-α7′ interaction (Fig. 4B and C).
Cross-references: PDB:5YCR
PDB:5YCV
Protein: DP03471 (UniProt Q81GI3)
Region: residues 99	to 111
Annotation: disorder to order (Structural transition)
Evidence: X-ray crystallography-based structural model with missing residue coordinates used in manual assertion
Supporting statements:
During the process, SBL-2, which is disordered in the dimeric form, is becomes ordered.
Cross-references: PDB:5YCR
PDB:5YCV
Protein: DP03471 (UniProt Q81GI3)
Region: residues 150	to 160
Annotation: self-assembly (Disorder function)
Evidence: X-ray crystallography-based structural model with missing residue coordinates used in manual assertion
Supporting statements:
In the dimeric form, the substrate-binding loop (SBL, 197–203), the second substrate-binding loop (SBL-2, 99–111), and the active site loop (ASL, 150–160), which play a key role in catalytic activity, were disordered (Fig. 2E).
ASL, which is disordered in the dimer, is rearranged by the helix-helix α7-α7′ interaction (Fig. 4B and C). 
Cross-references: PDB:5YCR
PDB:5YCV
Protein: DP03472 (UniProt Q09535)
Region: residues 108	to 121
Annotation: disorder (Structural state)
Evidence: X-ray crystallography-based structural model with missing residue coordinates used in manual assertion
Supporting statements:
The final model consists of six PCH-2 monomers, with a total of 2214 residues modeled out of 2544 (6 × 424 residues);
Cross-references: PDB:4XGU
Protein: DP03472 (UniProt Q09535)
Region: residues 255	to 273
Annotation: disorder (Structural state)
Evidence: X-ray crystallography-based structural model with missing residue coordinates used in manual assertion
Supporting statements:
The final model consists of six PCH-2 monomers, with a total of 2214 residues modeled out of 2544 (6 × 424 residues);
Cross-references: PDB:4XGU
Protein: DP03473 (UniProt O94258)
Region: residues 954	to 969
Annotation: disorder to order (Structural transition)
Evidence: X-ray crystallography-based structural model with missing residue coordinates used in manual assertion
Supporting statements:
The final model contains 941 residues of Xpot and is missing a few disordered loops.
Cross-references: PDB:3IBV
Protein: DP03473 (UniProt O94258)
Region: residues 954	to 969
Annotation: disorder (Structural state)
Evidence: X-ray crystallography-based structural model with missing residue coordinates used in manual assertion
Supporting statements:
The final model contains 941 residues of Xpot and is missing a few disordered loops
Cross-references: PDB:3IBV
Protein: DP03475 (UniProt Q81EJ6)
Region: residues 1	to 67
Annotation: disorder (Structural state)
Evidence: X-ray crystallography-based structural model with missing residue coordinates used in manual assertion
Supporting statements:
 Moreover, the crystal structures revealed the structure of the region 68−273, meaning that we could not identify the electron density for the 42 N-terminus residues of the expressed construct.
Although the expressed construct contained 42 additional residues at the N-terminus, no electron density was observed for those residues, denoting the unstructured nature of the speciﬁc region 
The N-terminal region 1-67 of the full length BC_1974 (PDB:5nc6) is disordered.
Cross-references: PDB:5N1P
PDB:5NEK
PDB:5NCD
PDB:5NC9
PDB:5N1J
PDB:5NC6
PDB:5NEL
Protein: DP03476 (UniProt F1QCV2)
Region: residues 365	to 411
Annotation: disorder (Structural state)
Evidence: X-ray crystallography-based structural model with missing residue coordinates used in manual assertion
Supporting statements:
Residues omitted from the ﬁnal model due to disorder included S365-A411 (the nicked interdomain loop) and G435, D436 and H454 in the CDAC domain. 
Cross-references: PDB:5TD7
Protein: DP03477 (UniProt Q5GH54)
Region: residues 68	to 80
Annotation: disorder (Structural state)
Evidence: cryogenic electron microscopy-based structural model with missing residue coordinates used in manual assertion
Supporting statements:
Although, due to the novelty of the protein fold, model building was challenging, the high quality of the map and the distribution of sidechain density of different volume have ultimately allowed the unambiguous interpretation of residues 1–66, 81–105, 119–344, and 365–373 of rXKR9 encompassing all structured parts of the protein.
rXKR9 comprises eight membrane-spanning helices (TM1–8), which are connected by short loops on the extracellular and longer loops on the intracellular side (Figure 4A–C).
Full-length rXKR9 was built de novo into the cryo-EM density, and cleaved rXKR9 was built using the full-length structure as reference. The cryo-EM density of full-length rXKR9 was of sufficiently high resolution to unambiguously assign residues 1–66, 81–105, 119–344, and 365–373.
Cross-references: EMDB:EMD-13155
EMDB:EMD-13157
PDB:7P14
PDB:7P16
Protein: DP03477 (UniProt Q5GH54)
Region: residues 106	to 118
Annotation: disorder (Structural state)
Evidence: cryogenic electron microscopy-based structural model with missing residue coordinates used in manual assertion
Supporting statements:
Although, due to the novelty of the protein fold, model building was challenging, the high quality of the map and the distribution of sidechain density of different volume have ultimately allowed the unambiguous interpretation of residues 1–66, 81–105, 119–344, and 365–373 of rXKR9 encompassing all structured parts of the protein.
rXKR9 comprises eight membrane-spanning helices (TM1–8), which are connected by short loops on the extracellular and longer loops on the intracellular side (Figure 4A–C).
Full-length rXKR9 was built de novo into the cryo-EM density, and cleaved rXKR9 was built using the full-length structure as reference. The cryo-EM density of full-length rXKR9 was of sufficiently high resolution to unambiguously assign residues 1–66, 81–105, 119–344, and 365–373.
Cross-references: EMDB:EMD-13155
EMDB:EMD-13157
PDB:7P14
PDB:7P16
Protein: DP03477 (UniProt Q5GH54)
Region: residues 345	to 364
Annotation: disorder (Structural state)
Evidence: cryogenic electron microscopy-based structural model with missing residue coordinates used in manual assertion
Supporting statements:
Although, due to the novelty of the protein fold, model building was challenging, the high quality of the map and the distribution of sidechain density of different volume have ultimately allowed the unambiguous interpretation of residues 1–66, 81–105, 119–344, and 365–373 of rXKR9 encompassing all structured parts of the protein.
rXKR9 comprises eight membrane-spanning helices (TM1–8), which are connected by short loops on the extracellular and longer loops on the intracellular side (Figure 4A–C).
In the structure of full-length rXKR9, part of the inhibitory peptide is well-defined, whereas the connecting loop harboring the cleavage site appears unstructured (Figure 2A, Figure 2—figure supplement 4).
Cross-references: EMDB:EMD-13155
PDB:7P14
Protein: DP03477 (UniProt Q5GH54)
Region: residues 345	to 373
Annotation: disorder (Structural state)
Evidence: cryogenic electron microscopy-based structural model with missing residue coordinates used in manual assertion
Supporting statements:
In the data of the cleaved rXKR9, the density of the C-terminus is absent, exposing the hydrophobic cleft to the cytoplasm (Figure 2). Apart from smaller changes in the intracellular loop regions, the truncated protein has not changed its conformation, which is illustrated in the low RMSD of 0.72 Å between the two structures (Figure 6B).
Cross-references: PDB:7P16
EMDB:EMD-13157
Protein: DP03480 (UniProt P00392)
Region: residues 550	to 561
Annotation: disorder (Structural state)
Evidence: structure determination evidence used in manual assertion
Supporting statements:
In the PEG crystals of the Tn501 protein, the last 11 amino acids were not well ordered and only visible as disconnected patches in the electron density map. 
Cross-references: PDB:1ZK7
PDB:1ZX9
Protein: DP03481 (UniProt P10674)
Region: residues 314	to 330
Annotation: disorder (Structural state)
Evidence: x-ray crystallography evidence used in manual assertion
Supporting statements:
There is no density for the first 16 and last 5 residues of FasI 3-4, which are presumed to be disordered
Cross-references: PDB:1O70
Protein: DP03482 (UniProt P16243)
Region: residues 63	to 79
Annotation: disorder (Structural state)
Evidence: X-ray crystallography-based structural model with missing residue coordinates used in manual assertion
Supporting statements:
The aforementioned region is not visible in the crystal structure of the construct
Cross-references: PDB:5OU5