LiteFold/DisProt huggingface dataset:
Protein: DP03818 (UniProt P57104)
Region: residues 1	to 13
Annotation: lipid binding (Molecular function)
Evidence: fluorescence evidence used in manual assertion
Supporting statements:
Upon the addition of SOPC liposomes, a blue shift of the fluorescence emission maximum of Trp4 was observed (Fig. 2 A), whereas the emission intensity (F) was attenuated (Fig. 2 A). Instead, pronounced increase in F and a blue shift were evident in the presence of POPG (Fig. 2 A), the increase being progressively enhanced with increasing X POPG in the membranes (Fig.2 B).
Fluorescence of Trp4decreased in a concentration-dependent manner by the addition of acrylamide to the peptide solution both in the absence and presence of liposomes, without other effects on the spectra (data not shown). However, in the presence of liposomes, less decrement in fluorescence intensity was evident, thus revealing that Trp4 is less accessible to the quencher in the presence of LUVs.
Protein: DP03818 (UniProt P57104)
Region: residues 1	to 13
Annotation: defense response to bacterium (Biological process)
Evidence: experimental phenotypic evidence used in manual assertion
Supporting statements:
Temporin L also displayed very good activity against Gram-negative bacterial strains such as E. coli D21 and Ps. aeruginosa A.T.C.C. 15692, with LC values of 1.5 and 3.6 µM respectively.
Temporin L, like temporin B, showed increasing antibacterial potency against cell-wall-defective mutant strains of E. coli D21, i.e. D21 e7, D21 f1 and D21 f2, which have lost increasing amounts of sugar residues of their lipopolysaccharide (LPS) chain [33]
Protein: DP03818 (UniProt P57104)
Region: residues 1	to 13
Annotation: hemolysis in another organism (Biological process)
Evidence: experimental phenotypic evidence used in manual assertion
Supporting statements:
The effects of increasing temporin L concentrations on the haemolysis of human erythrocytes are reported in Figure 4. Beyond 2 µM, considerable haemolysis was observed, with 100% lysis at approx. 55 µM.
Protein: DP03818 (UniProt P57104)
Region: residues 1	to 13
Annotation: disorder (Structural state)
Evidence: far-UV circular dichroism evidence used in manual assertion
Supporting statements:
The experiments demonstrate that for both peptides an increase in TFE concentration caused a progressive change from a random coil to an α-helical structure (Figure 1).
Protein: DP03818 (UniProt P57104)
Region: residues 1	to 13
Annotation: defense response to fungus (Biological process)
Evidence: experimental phenotypic evidence used in manual assertion
Supporting statements:
Against Candida species, the potency of temporin L was of the same order as that reported for temporin B, and approx. 2–9 times lower than that indicated for amphotericin B (with the exception of C. guillier-mondii, which is totally resistant to the latter compound).
Protein: DP03818 (UniProt P57104)
Region: residues 1	to 13
Annotation: order (Structural state)
Evidence: far-UV circular dichroism evidence used in manual assertion
Supporting statements:
In SDS, both the far-UV CD and the NMR structures agree that both peptides adopt ordered α-helix conformations.
Cross-references: PDB:6GS5
Protein: DP03818 (UniProt P57104)
Region: residues 1	to 13
Annotation: disorder (Structural state)
Evidence: far-UV circular dichroism evidence used in manual assertion
Supporting statements:
After binding to lipid bilayers, in the steady-state far-UV CD again indicates similar ordered α-helix conformations are adopted by both peptides; in the absence of lipid both peptides adopt disordered conformations (Fig. S4).
Protein: DP03818 (UniProt P57104)
Region: residues 1	to 13
Annotation: lipid binding (Molecular function)
Evidence: far-UV circular dichroism evidence used in manual assertion
Supporting statements:
This shows that, while secondary amphipathic α-helix conformations are a vital element in the binding and disruption of bacterial plasma membranes, individual amino acids in the distinct structures make important structural and dynamic contributions that determine the precise mechanism of action, potency and species selectivity of AMPs.
Protein: DP03818 (UniProt P57104)
Region: residues 1	to 13
Annotation: defense response to Gram-positive bacterium (Biological process)
Evidence: cell growth assay evidence used in manual assertion
Supporting statements:
In the present study, temporin L is shown to be more potent than aurein 2.5 against all strains included in both the Gram-positive and Gram-negative bacteria panels and Candida albicans (Table 2). For the Gram-positive strains, aurein 2.5 is outperformed by temporin L with, on average a 7.6-fold greater potency for the latter. For the Gram-negative strains, the difference between the potency of aurein 2.5 and temporin L is less, notably for both Acinetobacter baumannii isolates.
Protein: DP03818 (UniProt P57104)
Region: residues 1	to 13
Annotation: defense response to Gram-negative bacterium (Biological process)
Evidence: cell growth assay evidence used in manual assertion
Supporting statements:
In the present study, temporin L is shown to be more potent than aurein 2.5 against all strains included in both the Gram-positive and Gram-negative bacteria panels and Candida albicans (Table 2). For the Gram-positive strains, aurein 2.5 is outperformed by temporin L with, on average a 7.6-fold greater potency for the latter. For the Gram-negative strains, the difference between the potency of aurein 2.5 and temporin L is less, notably for both Acinetobacter baumannii isolates.
Protein: DP03818 (UniProt P57104)
Region: residues 1	to 13
Annotation: pore formation in membrane of another organism (Biological process)
Evidence: combinatorial experimental and curator inference evidence used in manual assertion
Supporting statements:
In the present study, temporin L is shown to be more potent than aurein 2.5 against all strains included in both the Gram-positive and Gram-negative bacteria panels and Candida albicans (Table 2). For the Gram-positive strains, aurein 2.5 is outperformed by temporin L with, on average a 7.6-fold greater potency for the latter. For the Gram-negative strains, the difference between the potency of aurein 2.5 and temporin L is less, notably for both Acinetobacter baumannii isolates.
In contrast, in the present study both aurein 2.5 and temporin L were found to be capable of inducing channel like activity (Fig. 6). For aurein 2.5 this was observed in both membrane types (Fig. 6A,B) whereas for temporin L this was only found when challenging membranes formed from DPhPG (Fig. 6D).
This shows that, while secondary amphipathic α-helix conformations are a vital element in the binding and disruption of bacterial plasma membranes, individual amino acids in the distinct structures make important structural and dynamic contributions that determine the precise mechanism of action, potency and species selectivity of AMPs.
The resulting estimated pore size indicates that temporin L is capable of creating pores that are at least twice the diameter of a chloride ion.
Protein: DP03818 (UniProt P57104)
Region: residues 1	to 13
Annotation: channel activity (Molecular function)
Evidence: electrophysiology assay evidence used in manual assertion
Supporting statements:
Similar to aurein 2.5, temporin L has channel like activity when challenging DPhPG membranes.
In contrast, in the present study both aurein 2.5 and temporin L were found to be capable of inducing channel like activity (Fig. 6). For aurein 2.5 this was observed in both membrane types (Fig. 6A,B) whereas for temporin L this was only found when challenging membranes formed from DPhPG (Fig. 6D).
Protein: DP03819 (UniProt P56917)
Region: residues 1	to 13
Annotation: disorder (Structural state)
Evidence: far-UV circular dichroism evidence used in manual assertion
Supporting statements:
The experiments demonstrate that for both peptides an increase in TFE concentration caused a progressive change from a random coil to an α-helical structure (Figure 1).
Protein: DP03820 (UniProt P26196)
Region: residues 81	to 93
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 seen for residues 70-82 on either chain.
The numbering of residues on the paper conflicts with the starting amino acids from Uniprot and the paper has dismissed the first 11 amino acids for some reason. The region the authors are describing corresponds to the 81-93 residues of the Uniprot.
Cross-references: PDB:1VEC
Protein: DP03821 (UniProt Q9UL18)
Region: residues 1	to 21
Annotation: disorder (Structural state)
Evidence: X-ray crystallography-based structural model with missing residue coordinates used in manual assertion
Supporting statements:
Given that the N-terminal 1–21 aa segment is disordered in our crystal structure, we are unable to comment on the specific function of the N-terminus in target-RNA accommodation and cleavage.
Cross-references: PDB:4KXT
Protein: DP03821 (UniProt Q9UL18)
Region: residues 113	to 126
Annotation: disorder (Structural state)
Evidence: X-ray crystallography-based structural model with missing residue coordinates used in manual assertion
Supporting statements:
The majority of the hAGO1 protein chain could be traced except for amino acid (aa) segments 1–21, 113–126 and 819–834.
Cross-references: PDB:4KXT
Protein: DP03821 (UniProt Q9UL18)
Region: residues 819	to 834
Annotation: disorder (Structural state)
Evidence: X-ray crystallography-based structural model with missing residue coordinates used in manual assertion
Supporting statements:
The majority of the hAGO1 protein chain could be traced except for amino acid (aa) segments 1–21, 113–126 and 819–834.
Cross-references: PDB:4KXT
Protein: DP03822 (UniProt P78563)
Region: residues 462	to 473
Annotation: disorder (Structural state)
Evidence: X-ray crystallography-based structural model with missing residue coordinates used in manual assertion
Supporting statements:
The refined hADAR2-D model contains residues 306 to 461 and 474 to 700 (462 to 473 are disordered), one zinc ion, and one molecule of inositol hexakisphosphate (IP6).
Cross-references: PDB:1ZY7
Protein: DP03822 (UniProt P78563)
Region: residues 299	to 316
Annotation: disorder (Structural state)
Evidence: X-ray crystallography-based structural model with missing residue coordinates used in manual assertion
Supporting statements:
In each of these complexes, the first 17 residues of the deaminase domain (residues 299–316) as well as a C-terminal proline (Pro701) are disordered and were therefore not included in the model.
Cross-references: PDB:5ED2
Protein: DP03822 (UniProt P78563)
Region: residues 454	to 477
Annotation: disorder to order (Structural transition)
Evidence: X-ray crystallography-based structural model with missing residue coordinates used in manual assertion
Supporting statements:
RNA binding leads to an ordering of the 454–477 loop, which was disordered in the RNA-free hADAR2d structure (Fig. 1d, green) (Supplementary Video 2).
Cross-references: PDB:5ED1
PDB:5ED2
PDB:5HP3
PDB:5HP2
Protein: DP03822 (UniProt P78563)
Region: residues 454	to 477
Annotation: RNA binding (Molecular function)
Evidence: X-ray crystallography-based structural model with missing residue coordinates used in manual assertion
Supporting statements:
RNA binding leads to an ordering of the 454–477 loop, which was disordered in the RNA-free hADAR2d structure(Fig. 1d, green) (Supplementary Video 2).
Cross-references: PDB:5ED1
PDB:5ED2
PDB:5HP3
PDB:5HP2
Protein: DP03822 (UniProt P78563)
Region: residues 215	to 233
Annotation: disorder (Structural state)
Evidence: X-ray crystallography-based structural model with missing residue coordinates used in manual assertion
Supporting statements:
The whole of the double stranded RNA binding domain (residues 215–318) of monomer A, as well as the C-terminal residues 700 and 701 were disordered and were therefore not included in the model. The first 20 residues (215–233), 5′ binding loop residues 462–475 and C-terminal proline (701) of monomer B were disordered and were therefore not included in the model.
Cross-references: PDB:6VFF
Protein: DP03823 (UniProt P55011)
Region: residues 1	to 283
Annotation: disorder (Structural state)
Evidence: cryogenic electron microscopy-based structural model with missing residue coordinates used in manual assertion
Supporting statements:
Similar to other NKCC1 cryo-EM structures (Chew et al, 2019; Yang et al, 2020; Zhang et al, 2021), the N-terminal domain could not be identified on the map.
Cross-references: PDB:7ZGO
EMDB:14709
Protein: DP03823 (UniProt P55011)
Region: residues 1	to 285
Annotation: disorder (Structural state)
Evidence: cryogenic electron microscopy-based structural model with missing residue coordinates used in manual assertion
Supporting statements:
The final map shows well-resolved densities for the transmembrane domain, large extracellular domains, and loops connecting membrane-spanning helices; however, it lacks interpretable densities for the cytosolic domains, consistent with reference free 2D class averages that show merely a cloud of fuzz densities for the cytosolic domains (Supplementary Fig. 2).
Cross-references: PDB:6PZT
EMDB:20537
Protein: DP03823 (UniProt P55011)
Region: residues 1	to 286
Annotation: disorder (Structural state)
Evidence: cryogenic electron microscopy-based structural model with missing residue coordinates used in manual assertion
Supporting statements:
The activating phosphorylation sites of NKCC1 are in the N-terminal domain32—this region is predicted to be largely disordered and indeed the N terminus is absent from both NKCC1 structures40,41.
Cross-references: PDB:7D10
EMDB:30542
Protein: DP03823 (UniProt P55011)
Region: residues 557	to 572
Annotation: disorder (Structural state)
Evidence: cryogenic electron microscopy-based structural model with missing residue coordinates used in manual assertion
Supporting statements:
The PDB shows this region lacks electron density, indicating it is disordered.
Cross-references: PDB:7D10
EMDB:30542
Protein: DP03824 (UniProt A0A0G2KTI4)
Region: residues 1	to 205
Annotation: disorder (Structural state)
Evidence: cryogenic electron microscopy-based structural model with missing residue coordinates used in manual assertion
Supporting statements:
In the 3D reconstruction of full-length NKCC1, the NTD lacked discernible density, indicating disordered structure or conformational flexibility.
Cross-references: EMDB:0475
Protein: DP03824 (UniProt A0A0G2KTI4)
Region: residues 856	to 925
Annotation: disorder (Structural state)
Evidence: cryogenic electron microscopy-based structural model with missing residue coordinates used in manual assertion
Supporting statements:
The final CTD model contains all residues except an un-structured loop (856–925).
Cross-references: PDB:6NPJ
PDB:6NPL
EMDB:0471
EMDB:0473
Protein: DP03824 (UniProt A0A0G2KTI4)
Region: residues 856	to 925
Annotation: flexible linker (Disorder function)
Evidence: cryogenic electron microscopy-based structural model with missing residue coordinates used in manual assertion
Supporting statements:
The final CTD model contains all residues except an un-structured loop (856–925).
Cross-references: PDB:6NPJ
PDB:6NPL
EMDB:0473
EMDB:0471
Protein: DP03825 (UniProt P15056)
Region: residues 600	to 611
Annotation: disorder (Structural state)
Evidence: crystallography evidence used in manual assertion
Supporting statements:
Residues 600–611 of the activation loop are disordered (dashed lines). (Figure 4)
Cross-references: PDB:1UWH
Protein: DP03825 (UniProt P15056)
Region: residues 601	to 613
Annotation: disorder (Structural state)
Evidence: X-ray crystallography-based structural model with missing residue coordinates used in manual assertion
Supporting statements:
The PDB shows the protein lacks electron density in this region, indicating it is disordered.
Cross-references: PDB:2FB8
Protein: DP03825 (UniProt P15056)
Region: residues 597	to 613
Annotation: disorder (Structural state)
Evidence: X-ray crystallography-based structural model with missing residue coordinates used in manual assertion
Supporting statements:
The PDB shows the protein lacks electron density in this region, indicating it is disordered.
Cross-references: PDB:3C4C
Protein: DP03825 (UniProt P15056)
Region: residues 600	to 610
Annotation: disorder (Structural state)
Evidence: X-ray crystallography-based structural model with missing residue coordinates used in manual assertion
Supporting statements:
The PDB shows the protein lacks electron density in this region, indicating it is disordered.
Cross-references: PDB:3II5
Protein: DP03825 (UniProt P15056)
Region: residues 601	to 614
Annotation: disorder (Structural state)
Evidence: X-ray crystallography-based structural model with missing residue coordinates used in manual assertion
Supporting statements:
The PDB shows the protein lacks electron density in this region, indicating it is disordered.
Cross-references: PDB:3OG7
Protein: DP03825 (UniProt P15056)
Region: residues 601	to 611
Annotation: disorder (Structural state)
Evidence: X-ray crystallography-based structural model with missing residue coordinates used in manual assertion
Supporting statements:
The PDB shows the protein lacks electron density in this region, indicating it is disordered.
Cross-references: PDB:3PPK
PDB:3PRI
PDB:3PRF
PDB:3PPJ
Protein: DP03825 (UniProt P15056)
Region: residues 432	to 447
Annotation: disorder (Structural state)
Evidence: X-ray crystallography-based structural model with missing residue coordinates used in manual assertion
Supporting statements:
The PDB shows the protein lacks electron density in this region, indicating it is disordered.
Cross-references: PDB:3PPJ
PDB:3PRF
PDB:3PPK
PDB:3PRI
Protein: DP03825 (UniProt P15056)
Region: residues 432	to 447
Annotation: disorder (Structural state)
Evidence: X-ray crystallography-based structural model with missing residue coordinates used in manual assertion
Supporting statements:
The PDB shows the protein lacks electron density in this region, indicating it is disordered.
Cross-references: PDB:3II5
Protein: DP03826 (UniProt Q91V14)
Region: residues 1	to 84
Annotation: disorder (Structural state)
Evidence: cryogenic electron microscopy-based structural model with missing residue coordinates used in manual assertion
Supporting statements:
We successfully built most of the mKCC2 structure except for relatively disordered regions in the N terminus and extracellular and intracellular loops (Fig. 1d, e and Supplementary Fig. 3c).
The activating phosphorylation sites of NKCC1 are in the N-terminal domain32—this region is predicted to be largely disordered and indeed the N terminus is absent from both NKCC1 structures40,41.
Cross-references: PDB:7D14
EMDB:30543
Protein: DP03826 (UniProt Q91V14)
Region: residues 952	to 1074
Annotation: disorder (Structural state)
Evidence: cryogenic electron microscopy-based structural model with missing residue coordinates used in manual assertion
Supporting statements:
The phosphorylation sites in mKCC2 that deactivate the transport protein (T929 and T1029)50 are in a large loop of the C terminus intervening β9 and α7—the ends of this loop are highlighted in Supplementary Fig. 7, but the majority of the loop is unresolved in our mKCC2 structure. 
Cross-references: PDB:7D14
EMDB:30543
Protein: DP03826 (UniProt Q91V14)
Region: residues 1027	to 1031
Annotation: phosphorylation display site (Disorder function)
Evidence: mass spectrometry evidence used in manual assertion
Supporting statements:
In the case of mKCC2, using mass spectrometry we confirmed phosphorylation at the two sites in the C terminus (T929 and T1029) (Supplementary Fig. 6b, c) whose phosphorylation appears necessary and possibly sufficient to inactivate KCC transport function; additional evidence will be seen below from the blocked pore in the mKCC2 structure.
Cross-references: PDB:7D14
EMDB:30543
Protein: DP03828 (UniProt Q9U4H7)
Region: residues 87	to 106
Annotation: disorder (Structural state)
Evidence: cryogenic electron microscopy-based structural model with missing residue coordinates used in manual assertion
Supporting statements:
Structure of residues 87-106 is unresolved in the cryo-EM reconstructions, showing its intrinsic flexibility.
Cross-references: PDB:5T5H
Protein: DP03829 (UniProt Q00534)
Region: residues 1	to 11
Annotation: disorder (Structural state)
Evidence: X-ray crystallography-based structural model with missing residue coordinates used in manual assertion
Supporting statements:
The PDB shows the protein lacks electron density in this region, indicating it is disordered.
Cross-references: PDB:3NUP
Protein: DP03829 (UniProt Q00534)
Region: residues 46	to 55
Annotation: disorder (Structural state)
Evidence: X-ray crystallography-based structural model with missing residue coordinates used in manual assertion
Supporting statements:
The PDB shows the protein lacks electron density in this region, indicating it is disordered.
Cross-references: PDB:3NUP
Protein: DP03829 (UniProt Q00534)
Region: residues 167	to 180
Annotation: disorder (Structural state)
Evidence: X-ray crystallography-based structural model with missing residue coordinates used in manual assertion
Supporting statements:
The PDB shows the protein lacks electron density in this region, indicating it is disordered.
Cross-references: PDB:3NUP
PDB:3NUX
Protein: DP03829 (UniProt Q00534)
Region: residues 45	to 56
Annotation: disorder (Structural state)
Evidence: X-ray crystallography-based structural model with missing residue coordinates used in manual assertion
Supporting statements:
The PDB shows the protein lacks electron density in this region, indicating it is disordered.
Cross-references: PDB:4AUA
PDB:4EZ5
Protein: DP03829 (UniProt Q00534)
Region: residues 168	to 181
Annotation: disorder (Structural state)
Evidence: X-ray crystallography-based structural model with missing residue coordinates used in manual assertion
Supporting statements:
The PDB shows the protein lacks electron density in this region, indicating it is disordered.
Cross-references: PDB:4AUA
PDB:4EZ5
Protein: DP03829 (UniProt Q00534)
Region: residues 1	to 10
Annotation: disorder (Structural state)
Evidence: X-ray crystallography-based structural model with missing residue coordinates used in manual assertion
Supporting statements:
The PDB shows the protein lacks electron density in this region, indicating it is disordered.
Cross-references: PDB:4EZ5
PDB:4AUA
Protein: DP03830 (UniProt Q9Y5P4)
Region: residues 344	to 361
Annotation: disorder (Structural state)
Evidence: X-ray crystallography-based structural model with missing residue coordinates used in manual assertion
Supporting statements:
Electron density for the first 12 or 13 residues was not observed in all cases, because of disorder.
According to the PDB, residues 1 to 18 (corresponding to 344 to 361 on the protein sequence) are not mapped, hence, disordered.
Cross-references: PDB:2E3M
Protein: DP03830 (UniProt Q9Y5P4)
Region: residues 344	to 362
Annotation: disorder (Structural state)
Evidence: X-ray crystallography-based structural model with missing residue coordinates used in manual assertion
Supporting statements:
Electron density for the first 12 or 13 residues was not observed in all cases, because of disorder.
According to the PDB, residues 1 to 19 (corresponding to 344 to 362 on the protein sequence) are not mapped, hence, disordered.
Cross-references: PDB:2Z9Y
PDB:2E3P
PDB:2E3N
PDB:2E3O
PDB:2E3R
PDB:2E3S
PDB:2E3Q
PDB:2Z9Z
Protein: DP03830 (UniProt Q9Y5P4)
Region: residues 187	to 218
Annotation: disorder (Structural state)
Evidence: protein hydrogen-deuterium exchange mass spectrometry evidence used in manual assertion
Supporting statements:
The areas from aa 187 to 218 and from aa 300 to 381 were highly accessible to solvent and therefore probably contained no or a very dynamic secondary structure.
Protein: DP03830 (UniProt Q9Y5P4)
Region: residues 300	to 381
Annotation: disorder (Structural state)
Evidence: protein hydrogen-deuterium exchange mass spectrometry evidence used in manual assertion
Supporting statements:
The areas from aa 187 to 218 and from aa 300 to 381 were highly accessible to solvent and therefore probably contained no or a very dynamic secondary structure.