#####################################################
# Mutual Folding Induced by Binding (MFIB) database #
#                Version: 26-06-2017                #
#       Source: http://mfib.enzim.ttk.mta.hu/       #
#####################################################

[Entry]
[Accession]=MF2120001
[Name]=Bacterial antidote ParD
[Source organism]=Escherichia coli
[Assembly]=Homodimer
[Total number of proteins]=2
[Number of unique proteins]=1
[Class]=Other
[Subclass]=Ribbon-helix-helix (RHH)
[PDB ID]=2an7
[PDB chain IDs]=AB
[PDB note]=No modifications of the original PDB file. Chain identifiers are identical with the PDB's identifiers.
[PDB experimental technique]=NMR
[Evidence global]=The interacting chains form a ribbon-helix-helix (RHH) structure (PMID:17656583). These structures in general have been described with the two monomers adopting a stable conformation upon the interaction (PMID:17676053). The hydrophobic core stabilizing the complex is formed by both interactors and is thus absent prior to the interaction (PMID:25713077).
[Chain A name]=Antitoxin ParD
[Chain A source organism]=Escherichia coli
[Chain A UniProt accession]=P22995
[Chain A UniProt boundaries]=1-83
[Chain A UniProt coverage]=100%
[Chain A UniRef90 accession]=UniRef90_P22995
[Chain A UniRef90 boundaries]=1-83
[Chain B name]=Antitoxin ParD
[Chain B source organism]=Escherichia coli
[Chain B UniProt accession]=P22995
[Chain B UniProt boundaries]=1-83
[Chain B UniProt coverage]=100%
[Chain B UniRef90 accession]=UniRef90_P22995
[Chain B UniRef90 boundaries]=1-83

[Entry]
[Accession]=MF2120002
[Name]=Helicobacter pylori HP0222
[Source organism]=Helicobacter pylori
[Assembly]=Homodimer
[Total number of proteins]=2
[Number of unique proteins]=1
[Class]=Other
[Subclass]=Ribbon-helix-helix (RHH)
[PDB ID]=1x93
[PDB chain IDs]=AB
[PDB note]=No modifications of the original PDB file. Chain identifiers are identical with the PDB's identifiers.
[PDB experimental technique]=NMR
[Evidence global]=The interacting chains form a ribbon-helix-helix (RHH) structure (PMID:15723352). These structures in general have been described with the two monomers adopting a stable conformation upon the interaction (PMID:17676053). The hydrophobic core stabilizing the complex is formed by both interactors and is thus absent prior to the interaction (PMID:25713077).
[Chain A name]=Uncharacterized protein
[Chain A source organism]=Helicobacter pylori
[Chain A UniProt accession]=O25010
[Chain A UniProt boundaries]=31-73
[Chain A UniProt coverage]=58.9%
[Chain A UniRef90 accession]=UniRef90_A0A060Q0Z2
[Chain A UniRef90 boundaries]=31-77
[Chain B name]=Uncharacterized protein
[Chain B source organism]=Helicobacter pylori
[Chain B UniProt accession]=O25010
[Chain B UniProt boundaries]=31-73
[Chain B UniProt coverage]=58.9%
[Chain B UniRef90 accession]=UniRef90_A0A060Q0Z2
[Chain B UniRef90 boundaries]=31-77

[Entry]
[Accession]=MF2120003
[Name]=Helicobacter pylori JHP0511 (HP0564)
[Source organism]=Helicobacter pylori
[Assembly]=Homodimer
[Total number of proteins]=2
[Number of unique proteins]=1
[Class]=Other
[Subclass]=Ribbon-helix-helix (RHH)
[PDB ID]=2k1o
[PDB chain IDs]=AB
[PDB note]=No modifications of the original PDB file. Chain identifiers are identical with the PDB's identifiers.
[PDB experimental technique]=NMR
[Evidence global]=The interacting chains form a ribbon-helix-helix (RHH) structure (PMID:18623065). These structures in general have been described with the two monomers adopting a stable conformation upon the interaction (PMID:17676053). The hydrophobic core stabilizing the complex is formed by both interactors and is thus absent prior to the interaction (PMID:25713077).
[Chain A name]=Putative
[Chain A source organism]=Helicobacter pylori
[Chain A UniProt accession]=Q9ZLR7
[Chain A UniProt boundaries]=21-74
[Chain A UniProt coverage]=66.7%
[Chain A UniRef90 accession]=UniRef90_B5Z6T5
[Chain A UniRef90 boundaries]=21-74
[Chain B name]=Putative
[Chain B source organism]=Helicobacter pylori
[Chain B UniProt accession]=Q9ZLR7
[Chain B UniProt boundaries]=21-74
[Chain B UniProt coverage]=66.7%
[Chain B UniRef90 accession]=UniRef90_B5Z6T5
[Chain B UniRef90 boundaries]=21-74

[Entry]
[Accession]=MF2120004
[Name]=ParG
[Source organism]=Salmonella newport
[Assembly]=Homodimer
[Total number of proteins]=2
[Number of unique proteins]=1
[Class]=Other
[Subclass]=Ribbon-helix-helix (RHH)
[PDB ID]=1p94
[PDB chain IDs]=AB
[PDB note]=No modifications of the original PDB file. Chain identifiers are identical with the PDB's identifiers.
[PDB experimental technique]=NMR
[Evidence global]=The interacting chains form a ribbon-helix-helix (RHH) structure (PMID:14622405). These structures in general have been described with the two monomers adopting a stable conformation upon the interaction (PMID:17676053). The hydrophobic core stabilizing the complex is formed by both interactors and is thus absent prior to the interaction (PMID:25713077).
[Chain A name]=Plasmid partition protein ParG
[Chain A source organism]=Salmonella newport
[Chain A UniProt accession]=Q9KJ82
[Chain A UniProt boundaries]=1-76
[Chain A UniProt coverage]=100%
[Chain A UniRef90 accession]=UniRef90_K3K332
[Chain A UniRef90 boundaries]=1-76
[Chain B name]=Plasmid partition protein ParG
[Chain B source organism]=Salmonella newport
[Chain B UniProt accession]=Q9KJ82
[Chain B UniProt boundaries]=1-76
[Chain B UniProt coverage]=100%
[Chain B UniRef90 accession]=UniRef90_K3K332
[Chain B UniRef90 boundaries]=1-76

[Entry]
[Accession]=MF2100001
[Name]=Human parathyroid hormone
[Source organism]=Homo sapiens
[Assembly]=Homodimer
[Total number of proteins]=2
[Number of unique proteins]=1
[Class]=Other
[Subclass]=Other
[PDB ID]=1et1
[PDB chain IDs]=AB
[PDB note]=No modifications of the original PDB file. Chain identifiers are identical with the PDB's identifiers.
[PDB experimental technique]=X-ray
[PDB resolution]=0.90
[Evidence chain A]=The 32-65 region described in DisProt entry DP00637 covers 100% of the sequence present in the structure.
[Evidence chain B]=The 32-65 region described in DisProt entry DP00637 covers 100% of the sequence present in the structure.
[Chain A name]=Parathyroid hormone
[Chain A source organism]=Homo sapiens
[Chain A UniProt accession]=P01270
[Chain A UniProt boundaries]=32-65
[Chain A UniProt coverage]=29.6%
[Chain A UniRef90 accession]=UniRef90_P01270
[Chain A UniRef90 boundaries]=32-65
[Chain B name]=Parathyroid hormone
[Chain B source organism]=Homo sapiens
[Chain B UniProt accession]=P01270
[Chain B UniProt boundaries]=32-65
[Chain B UniProt coverage]=29.6%
[Chain B UniRef90 accession]=UniRef90_P01270
[Chain B UniRef90 boundaries]=32-65

[Entry]
[Accession]=MF2200001
[Name]=Human ribosomal protein P1-P2 heterodimer
[Source organism]=Homo sapiens
[Assembly]=Heterodimer
[Total number of proteins]=2
[Number of unique proteins]=2
[Class]=Other
[Subclass]=Other
[PDB ID]=4beh
[PDB chain IDs]=AB
[PDB note]=No modifications of the original PDB file. Chain identifiers are identical with the PDB's identifiers.
[PDB experimental technique]=NMR
[Evidence chain A]=A close homologue sharing the same Pfam domain (PF00428.16) has been experimentally characterized as disordered in DisProt entry DP00001.
[Evidence chain B]=A close homologue sharing the same Pfam domain (PF00428.16) has been experimentally characterized as disordered in DisProt entry DP00002.
[Chain A name]=60S acidic ribosomal protein P1
[Chain A source organism]=Homo sapiens
[Chain A UniProt accession]=P05386
[Chain A UniProt boundaries]=1-114
[Chain A UniProt coverage]=100%
[Chain A UniRef90 accession]=UniRef90_P05386
[Chain A UniRef90 boundaries]=1-114
[Chain B name]=60S acidic ribosomal protein P2
[Chain B source organism]=Homo sapiens
[Chain B UniProt accession]=P05387
[Chain B UniProt boundaries]=1-115
[Chain B UniProt coverage]=100%
[Chain B UniRef90 accession]=UniRef90_P05387
[Chain B UniRef90 boundaries]=1-115
[Related structures]=2lbf

[Entry]
[Accession]=MF2100002
[Name]=Dimerization domain of ribosomal protein P2
[Source organism]=Homo sapiens
[Assembly]=Homodimer
[Total number of proteins]=2
[Number of unique proteins]=1
[Class]=Other
[Subclass]=Other
[PDB ID]=2w1o
[PDB chain IDs]=AB
[PDB note]=No modifications of the original PDB file. Chain identifiers are identical with the PDB's identifiers.
[PDB experimental technique]=NMR
[Evidence chain A]=A close homologue sharing the same Pfam domain (PF00428.16) has been experimentally characterized as disordered in DisProt entry DP00002.
[Evidence chain B]=A close homologue sharing the same Pfam domain (PF00428.16) has been experimentally characterized as disordered in DisProt entry DP00002.
[Chain A name]=60S acidic ribosomal protein P2
[Chain A source organism]=Homo sapiens
[Chain A UniProt accession]=P05387
[Chain A UniProt boundaries]=1-69
[Chain A UniProt coverage]=60%
[Chain A UniRef90 accession]=UniRef90_P05387
[Chain A UniRef90 boundaries]=1-66
[Chain B name]=60S acidic ribosomal protein P2
[Chain B source organism]=Homo sapiens
[Chain B UniProt accession]=P05387
[Chain B UniProt boundaries]=1-69
[Chain B UniProt coverage]=60%
[Chain B UniRef90 accession]=UniRef90_P05387
[Chain B UniRef90 boundaries]=1-66

[Entry]
[Accession]=MF2201001
[Name]=Nuclear receptor coactivators CBP and ACTR
[Source organism]=Homo sapiens / Mus musculus
[Assembly]=Heterodimer
[Total number of proteins]=2
[Number of unique proteins]=2
[Class]=Other
[Subclass]=Other
[PDB ID]=1kbh
[PDB chain IDs]=AB
[PDB note]=No modifications of the original PDB file. Chain identifiers are identical with the PDB's identifiers.
[PDB experimental technique]=NMR
[Evidence global]=The interacting monomers have been described to undergo mutual synergistic folding upon binding (PMID:11823864).
[Evidence chain A]=The 1018-1088 region described in DisProt entry DP00343 and the 1018-1088 region described in IDEAL entry IID00110 cover 100% of the sequence present in the structure.
[Evidence chain B]=The 2059-2152 region described in DisProt entry DP00348 and the 2057-2117 region described in IDEAL entry IID50008 cover 100% of the sequence present in the structure.
[Chain A name]=Nuclear receptor coactivator 3
[Chain A source organism]=Homo sapiens
[Chain A UniProt accession]=Q9Y6Q9
[Chain A UniProt boundaries]=1045-1091
[Chain A UniProt coverage]=3.3%
[Chain A UniRef90 accession]=UniRef90_Q9Y6Q9
[Chain A UniRef90 boundaries]=1045-1091
[Chain B name]=CREB-binding protein
[Chain B source organism]=Mus musculus
[Chain B UniProt accession]=P45481
[Chain B UniProt boundaries]=2059-2117
[Chain B UniProt coverage]=2.4%
[Chain B UniRef90 accession]=UniRef90_Q92793
[Chain B UniRef90 boundaries]=2058-2116

[Entry]
[Accession]=MF4210001
[Name]=L27 (Lin-2, Lin-7) domain complex (rat)
[Source organism]=Rattus norvegicus
[Assembly]=Heterotetramer
[Total number of proteins]=4
[Number of unique proteins]=2
[Class]=L27 domains
[Subclass]=L27_1 type
[PDB ID]=1rso
[PDB chain IDs]=ABCD
[PDB note]=No modifications of the original PDB file. Chain identifiers are identical with the PDB's identifiers.
[PDB experimental technique]=NMR
[Evidence global]=The interacting chains form a heterotetrameric L27 complex (PMID:15048107). L27 complexes formed by Lin-2 and Lin-7 proteins were shown to function as obligate heterodimers/tetramers undergoing a cooperative unfolding transition. Circular dichroism studies reveal that the individual monomers are largely unfolded outside the complex form (PMID:12110687).
[Chain A name]=Disks large homolog 1
[Chain A source organism]=Rattus norvegicus
[Chain A UniProt accession]=Q62696
[Chain A UniProt boundaries]=4-63
[Chain A UniProt coverage]=6.6%
[Chain A UniRef90 accession]=UniRef90_Q12959
[Chain A UniRef90 boundaries]=4-63
[Chain B name]=Peripheral plasma membrane protein CASK
[Chain B source organism]=Rattus norvegicus
[Chain B UniProt accession]=Q62915
[Chain B UniProt boundaries]=339-394
[Chain B UniProt coverage]=6.2%
[Chain B UniRef90 accession]=UniRef90_O14936
[Chain B UniRef90 boundaries]=339-394
[Chain C name]=Disks large homolog 1
[Chain C source organism]=Rattus norvegicus
[Chain C UniProt accession]=Q62696
[Chain C UniProt boundaries]=4-63
[Chain C UniProt coverage]=6.6%
[Chain C UniRef90 accession]=UniRef90_Q12959
[Chain C UniRef90 boundaries]=4-63
[Chain D name]=Peripheral plasma membrane protein CASK
[Chain D source organism]=Rattus norvegicus
[Chain D UniProt accession]=Q62915
[Chain D UniProt boundaries]=339-394
[Chain D UniProt coverage]=6.2%
[Chain D UniRef90 accession]=UniRef90_O14936
[Chain D UniRef90 boundaries]=339-394

[Entry]
[Accession]=MF2201002
[Name]=CBP nuclear coactivator binding domain in complex with p53 TAD
[Source organism]=Mus musculus / Homo sapiens
[Assembly]=Heterodimer
[Total number of proteins]=2
[Number of unique proteins]=2
[Class]=Other
[Subclass]=Other
[PDB ID]=2l14
[PDB chain IDs]=AB
[PDB note]=No modifications of the original PDB file. Chain identifiers are identical with the PDB's identifiers.
[PDB experimental technique]=NMR
[Evidence chain A]=The 2059-2152 region described in DisProt entry DP00348 and the 2057-2117 region described in IDEAL entry IID50008 cover 100% of the sequence present in the structure.
[Evidence chain B]=The 1-73 region described in DisProt entry DP00086 and the 1-96 region described in IDEAL entry IID00015 cover 100% of the sequence present in the structure.
[Chain A name]=CREB-binding protein
[Chain A source organism]=Mus musculus
[Chain A UniProt accession]=P45481
[Chain A UniProt boundaries]=2059-2117
[Chain A UniProt coverage]=2.4%
[Chain A UniRef90 accession]=UniRef90_Q92793
[Chain A UniRef90 boundaries]=2058-2116
[Chain B name]=Cellular tumor antigen p53
[Chain B source organism]=Homo sapiens
[Chain B UniProt accession]=P04637
[Chain B UniProt boundaries]=13-61
[Chain B UniProt coverage]=12.5%
[Chain B UniRef90 accession]=UniRef90_P04637
[Chain B UniRef90 boundaries]=13-61

[Entry]
[Accession]=MF2201003
[Name]=P160/CREB-binding protein coactivator complex
[Source organism]=Mus musculus / Homo sapiens
[Assembly]=Heterodimer
[Total number of proteins]=2
[Number of unique proteins]=2
[Class]=Other
[Subclass]=Other
[PDB ID]=2c52
[PDB chain IDs]=AB
[PDB note]=No modifications of the original PDB file. Chain identifiers are identical with the PDB's identifiers.
[PDB experimental technique]=NMR
[Evidence chain A]=The 2059-2152 region described in DisProt entry DP00348 and the 2057-2117 region described in IDEAL entry IID50008 cover 100% of the sequence present in the structure.
[Evidence chain B]=A close homologue sharing the same Pfam domain (PF08815.7) has been experimentally characterized as disordered in DisProt entry DP00343 and IDEAL entry IID00110.
[Chain A name]=CREB-binding protein
[Chain A source organism]=Mus musculus
[Chain A UniProt accession]=P45481
[Chain A UniProt boundaries]=2059-2117
[Chain A UniProt coverage]=2.4%
[Chain A UniRef90 accession]=UniRef90_Q92793
[Chain A UniRef90 boundaries]=2058-2116
[Chain B name]=Nuclear receptor coactivator 1
[Chain B source organism]=Homo sapiens
[Chain B UniProt accession]=Q15788
[Chain B UniProt boundaries]=920-974
[Chain B UniProt coverage]=3.8%
[Chain B UniRef90 accession]=UniRef90_Q15788
[Chain B UniRef90 boundaries]=920-974

[Entry]
[Accession]=MF4120001
[Name]=YefM antitoxin (Mycobacterium tuberculosis)
[Source organism]=Mycobacterium tuberculosis
[Assembly]=Homotetramer
[Total number of proteins]=4
[Number of unique proteins]=1
[Class]=Other
[Subclass]=Phd antitoxin
[PDB ID]=3cto
[PDB chain IDs]=ABCD
[PDB note]=Chain E has been removed, as it is possibly a fragment of one of the chains forming the tetramer and is not involved in molecular interactions stabilizing the complex
[PDB experimental technique]=X-ray
[PDB resolution]=2.50
[Evidence global]=The dimerization of the prevents host death (phd) antitoxin from Escherichia virus P1 has been shown with differential scanning calorimetry to fit well to a two-state model consisting of a dimer unfolding into monomer species (PMID:20603017).
[Evidence chain A]=A close homologue sharing the same Pfam domain (PF02604.16) has been experimentally characterized as disordered in DisProt entry DP00288.
[Evidence chain B]=A close homologue sharing the same Pfam domain (PF02604.16) has been experimentally characterized as disordered in DisProt entry DP00288.
[Evidence chain C]=A close homologue sharing the same Pfam domain (PF02604.16) has been experimentally characterized as disordered in DisProt entry DP00288.
[Evidence chain D]=A close homologue sharing the same Pfam domain (PF02604.16) has been experimentally characterized as disordered in DisProt entry DP00288.
[Chain A name]=Antitoxin RelJ
[Chain A source organism]=Mycobacterium tuberculosis
[Chain A UniProt accession]=P9WF24
[Chain A UniProt boundaries]=1-91
[Chain A UniProt coverage]=100%
[Chain A UniRef90 accession]=UniRef90_P9WF24
[Chain A UniRef90 boundaries]=1-91
[Chain B name]=Antitoxin RelJ
[Chain B source organism]=Mycobacterium tuberculosis
[Chain B UniProt accession]=P9WF24
[Chain B UniProt boundaries]=1-91
[Chain B UniProt coverage]=100%
[Chain B UniRef90 accession]=UniRef90_P9WF24
[Chain B UniRef90 boundaries]=1-91
[Chain C name]=Antitoxin RelJ
[Chain C source organism]=Mycobacterium tuberculosis
[Chain C UniProt accession]=P9WF24
[Chain C UniProt boundaries]=1-91
[Chain C UniProt coverage]=100%
[Chain C UniRef90 accession]=UniRef90_P9WF24
[Chain C UniRef90 boundaries]=1-91
[Chain D name]=Antitoxin RelJ
[Chain D source organism]=Mycobacterium tuberculosis
[Chain D UniProt accession]=P9WF24
[Chain D UniProt boundaries]=1-91
[Chain D UniProt coverage]=100%
[Chain D UniRef90 accession]=UniRef90_P9WF24
[Chain D UniRef90 boundaries]=1-91
[Related structures]=3d55,3oei

[Entry]
[Accession]=MF2140001
[Name]=Arc repressor
[Source organism]=Enterobacteria phage P22
[Assembly]=Homodimer
[Total number of proteins]=2
[Number of unique proteins]=1
[Class]=Other
[Subclass]=Ribbon-helix-helix (RHH)
[PDB ID]=1arq
[PDB chain IDs]=AB
[PDB note]=No modifications of the original PDB file. Chain identifiers are identical with the PDB's identifiers.
[PDB experimental technique]=NMR
[Evidence global]=The Arc repressor protein has been experimentally shown to be a molten globule in monomeric form (PMID:8446590,PMID:7696567). Adopting the proper three dimensional structure is linked to dimerization (PMID:8110744,PMID:10889040).
[Chain A name]=Transcriptional repressor arc
[Chain A source organism]=Enterobacteria phage P22
[Chain A UniProt accession]=P03050
[Chain A UniProt boundaries]=1-53
[Chain A UniProt coverage]=100%
[Chain A UniRef90 accession]=UniRef90_P03050
[Chain A UniRef90 boundaries]=1-53
[Chain B name]=Transcriptional repressor arc
[Chain B source organism]=Enterobacteria phage P22
[Chain B UniProt accession]=P03050
[Chain B UniProt boundaries]=1-53
[Chain B UniProt coverage]=100%
[Chain B UniRef90 accession]=UniRef90_P03050
[Chain B UniRef90 boundaries]=1-53
[Related structures]=1arr,1b28,1baz,1bdt,1bdv,1myk,1myl,1nla,1par,1qtg

[Entry]
[Accession]=MF2120005
[Name]=Trp repressor protein (Ruminococcus obeum)
[Source organism]=Blautia obeum ATCC 29174
[Assembly]=Homodimer
[Total number of proteins]=2
[Number of unique proteins]=1
[Class]=Other
[Subclass]=Trp repressor-like
[PDB ID]=3frw
[PDB chain IDs]=AB
[PDB note]=Chains C,D,E,F,G and H were removed as chains A and B represent the biologically active dimer.
[PDB experimental technique]=X-ray
[PDB resolution]=2.05
[Evidence global]=The folding and dimerization of the Trp repressor were shown to be linked by both experimental (PMID:10329154,PMID:2223756,PMID:7578063) and computational studies (PMID:10465773).
[Chain A name]=TrpR family protein YerC/YecD
[Chain A source organism]=Blautia obeum ATCC 29174
[Chain A UniProt accession]=A5ZMD8
[Chain A UniProt boundaries]=1-104
[Chain A UniProt coverage]=100%
[Chain A UniRef90 accession]=UniRef90_D4LQW8
[Chain A UniRef90 boundaries]=1-104
[Chain B name]=TrpR family protein YerC/YecD
[Chain B source organism]=Blautia obeum ATCC 29174
[Chain B UniProt accession]=A5ZMD8
[Chain B UniProt boundaries]=1-104
[Chain B UniProt coverage]=100%
[Chain B UniRef90 accession]=UniRef90_D4LQW8
[Chain B UniRef90 boundaries]=1-104

[Entry]
[Accession]=MF2120006
[Name]=Transcriptional repressor CopG
[Source organism]=Streptococcus agalactiae
[Assembly]=Homodimer
[Total number of proteins]=2
[Number of unique proteins]=1
[Class]=Other
[Subclass]=Ribbon-helix-helix (RHH)
[PDB ID]=2cpg
[PDB chain IDs]=AB
[PDB note]=Chain C has been removed as chains A and B represent the biologically active dimer.
[PDB experimental technique]=X-ray
[PDB resolution]=1.60
[Evidence global]=The interacting chains form a ribbon-helix-helix (RHH) structure (PMID:17656583). These structures in general have been described with the two monomers adopting a stable conformation upon the interaction (PMID:9857196). The hydrophobic core stabilizing the complex is formed by both interactors and is thus absent prior to the interaction (PMID:25713077). Furthermore, CopG was directly shown to associate and fold cooperatively via a two state folding and binding process (PMID:9857196,PMID:15169951).
[Chain A name]=Protein CopG
[Chain A source organism]=Streptococcus agalactiae
[Chain A UniProt accession]=P13920
[Chain A UniProt boundaries]=1-45
[Chain A UniProt coverage]=100%
[Chain A UniRef90 accession]=UniRef90_P13920
[Chain A UniRef90 boundaries]=1-45
[Chain B name]=Protein CopG
[Chain B source organism]=Streptococcus agalactiae
[Chain B UniProt accession]=P13920
[Chain B UniProt boundaries]=1-45
[Chain B UniProt coverage]=100%
[Chain B UniRef90 accession]=UniRef90_P13920
[Chain B UniRef90 boundaries]=1-45
[Related structures]=1b01,1ea4

[Entry]
[Accession]=MF2120007
[Name]=UmuD' protein filament
[Source organism]=Escherichia coli O157:H7
[Assembly]=Homodimer
[Total number of proteins]=2
[Number of unique proteins]=1
[Class]=Other
[Subclass]=Other
[PDB ID]=1ay9
[PDB chain IDs]=AB
[PDB note]=No modifications of the original PDB file. Chain identifiers are identical with the PDB's identifiers.
[PDB experimental technique]=X-ray
[PDB resolution]=3.00
[Evidence chain A]=The 1-139 region described in DisProt entry DP00626 covers 100% of the sequence present in the structure.
[Evidence chain B]=The 1-139 region described in DisProt entry DP00626 covers 100% of the sequence present in the structure.
[Chain A name]=Protein UmuD
[Chain A source organism]=Escherichia coli O157:H7
[Chain A UniProt accession]=P0AG12
[Chain A UniProt boundaries]=32-139
[Chain A UniProt coverage]=77.7%
[Chain A UniRef90 accession]=UniRef90_P0AG12
[Chain A UniRef90 boundaries]=32-139
[Chain B name]=Protein UmuD
[Chain B source organism]=Escherichia coli O157:H7
[Chain B UniProt accession]=P0AG12
[Chain B UniProt boundaries]=32-139
[Chain B UniProt coverage]=77.7%
[Chain B UniRef90 accession]=UniRef90_P0AG12
[Chain B UniRef90 boundaries]=32-139
[Related structures]=1i4v,1umu

[Entry]
[Accession]=MF4100001
[Name]=Transthyretin (human)
[Source organism]=Homo sapiens
[Assembly]=Homotetramer
[Total number of proteins]=4
[Number of unique proteins]=1
[Class]=Transthyretin-like folds
[Subclass]=Transthyretin
[PDB ID]=3a4d
[PDB chain IDs]=ABCD
[PDB note]=Chains C and D were generated from chains A and B respectively, using the biomatrices described in the original PDB file.
[PDB experimental technique]=X-ray
[PDB resolution]=2.00
[Evidence global]=Transthyretin was shown in calorimetrics experiments to follow two-state folding/binding kinetics with the emergence of structure being linked to oligomerization (PMID:11152276).
[Chain A name]=Transthyretin
[Chain A source organism]=Homo sapiens
[Chain A UniProt accession]=P02766
[Chain A UniProt boundaries]=21-147
[Chain A UniProt coverage]=86.4%
[Chain A UniRef90 accession]=UniRef90_P02766
[Chain A UniRef90 boundaries]=21-147
[Chain B name]=Transthyretin
[Chain B source organism]=Homo sapiens
[Chain B UniProt accession]=P02766
[Chain B UniProt boundaries]=21-147
[Chain B UniProt coverage]=86.4%
[Chain B UniRef90 accession]=UniRef90_P02766
[Chain B UniRef90 boundaries]=21-147
[Chain C name]=Transthyretin
[Chain C source organism]=Homo sapiens
[Chain C UniProt accession]=P02766
[Chain C UniProt boundaries]=21-147
[Chain C UniProt coverage]=86.4%
[Chain C UniRef90 accession]=UniRef90_P02766
[Chain C UniRef90 boundaries]=21-147
[Chain D name]=Transthyretin
[Chain D source organism]=Homo sapiens
[Chain D UniProt accession]=P02766
[Chain D UniProt boundaries]=21-147
[Chain D UniProt coverage]=86.4%
[Chain D UniRef90 accession]=UniRef90_P02766
[Chain D UniRef90 boundaries]=21-147
[Related structures]=1bm7,1bmz,1bz8,1bzd,1bze,1dvq,1dvs,1dvt,1dvu,1dvx,1dvy,1dvz,1e3f,1e4h,1e5a,1eta,1etb,1f41,1f86,1fh2,1fhn,1g1o,1gko,1ict,1iii,1iik,1ijn,1qab,1qwh,1rlb,1sok,1soq,1tha,1thc,1tlm,1tsh,1tt6,1tta,1ttb,1ttc,1ttr,1tyr,1tz8,1u21,1x7s,1x7t,1y1d,1z7j,1zcr,1zd6,2b14,2b15,2b16,2b77,2b9a,2f7i,2f8i,2fbr,2flm,2g3x,2g3z,2g4e,2g4g,2g5u,2g9k,2gab,2h4e,2nbo,2nbp,2noy,2pab,2qel,2qgb,2qgc,2qgd,2qge,2rox,2roy,2trh,2try,2wqa,3a4e,3a4f,3b56,3bsz,3bt0,3cbr,3cfm,3cfn,3cfq,3cft,3cn0,3cn1,3cn2,3cn3,3cn4,3cxf,3d2t,3d7p,3dgd,3did,3djr,3djs,3djt,3djz,3dk0,3dk2,3do4,3esn,3eso,3esp,3fc8,3fcb,3glz,3gps,3grb,3grg,3gs0,3gs4,3gs7,3hj0,3i9a,3i9i,3i9p,3imr,3ims,3imt,3imu,3imv,3imw,3ipb,3ipe,3kgs,3kgt,3kgu,3m1o,3nee,3neo,3nes,3nex,3ng5,3ozk,3ozl,3p3r,3p3s,3p3t,3p3u,3ssg,3tct,3tfb,3u2i,3u2j,3w3b,4abq,4abu,4abv,4abw,4ac2,4ac4,4act,4ank,4d7b,4der,4des,4det,4deu,4dew,4fi6,4fi7,4fi8,4hiq,4his,4hjs,4hjt,4hju,4i85,4i87,4i89,4iiz,4ik6,4ik7,4iki,4ikj,4ikk,4ikl,4ky2,4l1s,4l1t,4mas,4mrb,4mrc,4n85,4n86,4n87,4pm1,4pme,4pmf,4pvl,4pvm,4pvn,4pwe,4pwf,4pwg,4pwh,4pwi,4pwj,4pwk,4qrf,4qxv,4qya,4tkw,4tl4,4tl5,4tlk,4tls,4tlt,4tlu,4tm9,4tne,4tnf,4tng,4tq8,4tqh,4tqi,4tqp,4wnj,4wns,4wo0,4y9b,4y9c,4y9e,4y9f,4y9g,4ydm,4ydn,5a6i,5aks,5akt,5akv,5al0,5al8,5ayt,5boj,5clx,5cly,5clz,5cm1,5cn3,5cnh,5cr1,5dej,5dwp,5e23,5e4a,5e4o,5en3,5ezp,5fo2,5fw6,5fw7,5fw8,5hjg,5ihh,5jid,5jim,5jiq,5k1j,5k1n,5l4f,5l4i,5l4j,5l4m,5ttr

[Entry]
[Accession]=MF4110001
[Name]=Transthyretin (rat)
[Source organism]=Rattus norvegicus
[Assembly]=Homotetramer
[Total number of proteins]=4
[Number of unique proteins]=1
[Class]=Transthyretin-like folds
[Subclass]=Transthyretin
[PDB ID]=1gke
[PDB chain IDs]=ABCD
[PDB note]=No modifications of the original PDB file. Chain identifiers are identical with the PDB's identifiers.
[PDB experimental technique]=X-ray
[PDB resolution]=2.50
[Evidence global]=Transthyretin was shown in calorimetrics experiments to follow two-state folding/binding kinetics with the emergence of structure being linked to oligomerization (PMID:11152276).
[Chain A name]=Transthyretin
[Chain A source organism]=Rattus norvegicus
[Chain A UniProt accession]=P02767
[Chain A UniProt boundaries]=28-147
[Chain A UniProt coverage]=81.6%
[Chain A UniRef90 accession]=UniRef90_P02767
[Chain A UniRef90 boundaries]=28-147
[Chain B name]=Transthyretin
[Chain B source organism]=Rattus norvegicus
[Chain B UniProt accession]=P02767
[Chain B UniProt boundaries]=28-147
[Chain B UniProt coverage]=81.6%
[Chain B UniRef90 accession]=UniRef90_P02767
[Chain B UniRef90 boundaries]=28-147
[Chain C name]=Transthyretin
[Chain C source organism]=Rattus norvegicus
[Chain C UniProt accession]=P02767
[Chain C UniProt boundaries]=28-147
[Chain C UniProt coverage]=81.6%
[Chain C UniRef90 accession]=UniRef90_P02767
[Chain C UniRef90 boundaries]=28-147
[Chain D name]=Transthyretin
[Chain D source organism]=Rattus norvegicus
[Chain D UniProt accession]=P02767
[Chain D UniProt boundaries]=28-147
[Chain D UniProt coverage]=81.6%
[Chain D UniRef90 accession]=UniRef90_P02767
[Chain D UniRef90 boundaries]=28-147
[Related structures]=1ie4,1kgi,1kgj,2qpf

[Entry]
[Accession]=MF4110002
[Name]=Transthyretin (Sparus aurata)
[Source organism]=Sparus aurata
[Assembly]=Homotetramer
[Total number of proteins]=4
[Number of unique proteins]=1
[Class]=Transthyretin-like folds
[Subclass]=Transthyretin
[PDB ID]=1oo2
[PDB chain IDs]=ABCD
[PDB note]=No modifications of the original PDB file. Chain identifiers are identical with the PDB's identifiers.
[PDB experimental technique]=X-ray
[PDB resolution]=1.56
[Evidence global]=Transthyretin was shown in calorimetrics experiments to follow two-state folding/binding kinetics with the emergence of structure being linked to oligomerization (PMID:11152276).
[Chain A name]=Transthyretin (Precursor)
[Chain A source organism]=Sparus aurata
[Chain A UniProt accession]=Q9PTT3
[Chain A UniProt boundaries]=33-148
[Chain A UniProt coverage]=76.8%
[Chain A UniRef90 accession]=UniRef90_O93330
[Chain A UniRef90 boundaries]=32-149
[Chain B name]=Transthyretin (Precursor)
[Chain B source organism]=Sparus aurata
[Chain B UniProt accession]=Q9PTT3
[Chain B UniProt boundaries]=33-148
[Chain B UniProt coverage]=76.8%
[Chain B UniRef90 accession]=UniRef90_O93330
[Chain B UniRef90 boundaries]=32-149
[Chain C name]=Transthyretin (Precursor)
[Chain C source organism]=Sparus aurata
[Chain C UniProt accession]=Q9PTT3
[Chain C UniProt boundaries]=33-148
[Chain C UniProt coverage]=76.8%
[Chain C UniRef90 accession]=UniRef90_O93330
[Chain C UniRef90 boundaries]=32-149
[Chain D name]=Transthyretin (Precursor)
[Chain D source organism]=Sparus aurata
[Chain D UniProt accession]=Q9PTT3
[Chain D UniProt boundaries]=33-148
[Chain D UniProt coverage]=76.8%
[Chain D UniRef90 accession]=UniRef90_O93330
[Chain D UniRef90 boundaries]=32-149
[Related structures]=1sn0,1sn2,1sn5

[Entry]
[Accession]=MF4201001
[Name]=Patj/Pals1 L27 domain complex (human/rat)
[Source organism]=Mus musculus / Homo sapiens
[Assembly]=Heterotetramer
[Total number of proteins]=4
[Number of unique proteins]=2
[Class]=L27 domains
[Subclass]=L27_2/N type
[PDB ID]=1y76
[PDB chain IDs]=ABCD
[PDB note]=No modifications of the original PDB file. Chain identifiers are identical with the PDB's identifiers.
[PDB experimental technique]=NMR
[Evidence global]=The interacting chains form a heterotetrameric L27 complex (PMID:15863617). L27 complexes formed by Lin-2 and Lin-7 proteins were shown to function as obligate heterodimers/tetramers undergoing a cooperative unfolding transition. Circular dichroism studies reveal that the individual monomers are largely unfolded outside the complex form (PMID:12110687).
[Chain A name]=InaD-like protein
[Chain A source organism]=Mus musculus
[Chain A UniProt accession]=Q63ZW7
[Chain A UniProt boundaries]=4-65
[Chain A UniProt coverage]=3.4%
[Chain A UniRef90 accession]=UniRef90_Q63ZW7
[Chain A UniRef90 boundaries]=4-65
[Chain B name]=MAGUK p55 subfamily member 5
[Chain B source organism]=Homo sapiens
[Chain B UniProt accession]=Q8N3R9
[Chain B UniProt boundaries]=118-177
[Chain B UniProt coverage]=8.9%
[Chain B UniRef90 accession]=UniRef90_Q9JLB2
[Chain B UniRef90 boundaries]=118-177
[Chain C name]=InaD-like protein
[Chain C source organism]=Mus musculus
[Chain C UniProt accession]=Q63ZW7
[Chain C UniProt boundaries]=4-65
[Chain C UniProt coverage]=3.4%
[Chain C UniRef90 accession]=UniRef90_Q63ZW7
[Chain C UniRef90 boundaries]=4-65
[Chain D name]=MAGUK p55 subfamily member 5
[Chain D source organism]=Homo sapiens
[Chain D UniProt accession]=Q8N3R9
[Chain D UniProt boundaries]=118-177
[Chain D UniProt coverage]=8.9%
[Chain D UniRef90 accession]=UniRef90_Q9JLB2
[Chain D UniRef90 boundaries]=118-177

[Entry]
[Accession]=MF4201002
[Name]=Patj/Pals1 L27 domain complex (human/mouse)
[Source organism]=Homo sapiens / Mus musculus
[Assembly]=Heterotetramer
[Total number of proteins]=4
[Number of unique proteins]=2
[Class]=L27 domains
[Subclass]=L27_2/N type
[PDB ID]=1vf6
[PDB chain IDs]=ABCD
[PDB note]=No modifications of the original PDB file. Chain identifiers are identical with the PDB's identifiers.
[PDB experimental technique]=X-ray
[PDB resolution]=2.10
[Evidence global]=The interacting chains form a heterotetrameric L27 complex (PMID:15241471). L27 complexes formed by Lin-2 and Lin-7 proteins were shown to function as obligate heterodimers/tetramers undergoing a cooperative unfolding transition. Circular dichroism studies reveal that the individual monomers are largely unfolded outside the complex form (PMID:12110687).
[Chain A name]=InaD-like protein
[Chain A source organism]=Homo sapiens
[Chain A UniProt accession]=Q8NI35
[Chain A UniProt boundaries]=9-67
[Chain A UniProt coverage]=3.3%
[Chain A UniRef90 accession]=UniRef90_UPI0006B1AC65
[Chain A UniRef90 boundaries]=9-82
[Chain B name]=InaD-like protein
[Chain B source organism]=Homo sapiens
[Chain B UniProt accession]=Q8NI35
[Chain B UniProt boundaries]=9-67
[Chain B UniProt coverage]=3.3%
[Chain B UniRef90 accession]=UniRef90_UPI0006B1AC65
[Chain B UniRef90 boundaries]=9-82
[Chain C name]=MAGUK p55 subfamily member 5
[Chain C source organism]=Mus musculus
[Chain C UniProt accession]=Q9JLB2
[Chain C UniProt boundaries]=123-180
[Chain C UniProt coverage]=8.6%
[Chain C UniRef90 accession]=UniRef90_Q9JLB2
[Chain C UniRef90 boundaries]=123-180
[Chain D name]=MAGUK p55 subfamily member 5
[Chain D source organism]=Mus musculus
[Chain D UniProt accession]=Q9JLB2
[Chain D UniProt boundaries]=123-180
[Chain D UniProt coverage]=8.6%
[Chain D UniRef90 accession]=UniRef90_Q9JLB2
[Chain D UniRef90 boundaries]=123-180

[Entry]
[Accession]=MF4210002
[Name]=L27 (Lin-2, Lin-7) domain complex (mouse)
[Source organism]=Mus musculus
[Assembly]=Heterotetramer
[Total number of proteins]=4
[Number of unique proteins]=2
[Class]=L27 domains
[Subclass]=L27_1 type
[PDB ID]=1y74
[PDB chain IDs]=ABCD
[PDB note]=No modifications of the original PDB file. Chain identifiers are identical with the PDB's identifiers.
[PDB experimental technique]=NMR
[Evidence global]=The interacting chains form a heterotetrameric L27 complex (PMID:15863617). L27 complexes formed by Lin-2 and Lin-7 proteins were shown to function as obligate heterodimers/tetramers undergoing a cooperative unfolding transition. Circular dichroism studies reveal that the individual monomers are largely unfolded outside the complex form (PMID:12110687).
[Chain A name]=Protein lin-7 homolog B
[Chain A source organism]=Mus musculus
[Chain A UniProt accession]=O88951
[Chain A UniProt boundaries]=8-64
[Chain A UniProt coverage]=27.5%
[Chain A UniRef90 accession]=UniRef90_Q9Z252
[Chain A UniRef90 boundaries]=8-64
[Chain B name]=Peripheral plasma membrane protein CASK
[Chain B source organism]=Mus musculus
[Chain B UniProt accession]=O70589
[Chain B UniProt boundaries]=405-454
[Chain B UniProt coverage]=5.4%
[Chain B UniRef90 accession]=UniRef90_O14936
[Chain B UniRef90 boundaries]=405-454
[Chain C name]=Protein lin-7 homolog B
[Chain C source organism]=Mus musculus
[Chain C UniProt accession]=O88951
[Chain C UniProt boundaries]=8-64
[Chain C UniProt coverage]=27.5%
[Chain C UniRef90 accession]=UniRef90_Q9Z252
[Chain C UniRef90 boundaries]=8-64
[Chain D name]=Peripheral plasma membrane protein CASK
[Chain D source organism]=Mus musculus
[Chain D UniProt accession]=O70589
[Chain D UniProt boundaries]=405-454
[Chain D UniProt coverage]=5.4%
[Chain D UniRef90 accession]=UniRef90_O14936
[Chain D UniRef90 boundaries]=405-454

[Entry]
[Accession]=MF2201004
[Name]=L27 (Lin-2, Lin-7) domain complex (human/C. elegans)
[Source organism]=Caenorhabditis elegans / Homo sapiens
[Assembly]=Heterodimer
[Total number of proteins]=2
[Number of unique proteins]=2
[Class]=L27 domains
[Subclass]=L27_1 type
[PDB ID]=1zl8
[PDB chain IDs]=AB
[PDB note]=No modifications of the original PDB file. Chain identifiers are identical with the PDB's identifiers.
[PDB experimental technique]=NMR
[Evidence global]=The interacting chains form half of a heterotetrameric L27 complex (a dimer of dimers) (PMID:16147993). L27 complexes formed by Lin-2 and Lin-7 proteins were shown to function as obligate heterodimers/tetramers undergoing a cooperative unfolding transition. Circular dichroism studies reveal that the individual monomers are largely unfolded outside the complex form (PMID:12110687).
[Chain A name]=LIN-7 (Fragment)
[Chain A source organism]=Caenorhabditis elegans
[Chain A UniProt accession]=P90976
[Chain A UniProt boundaries]=116-165
[Chain A UniProt coverage]=16.8%
[Chain A UniRef90 accession]=UniRef90_Q9U245
[Chain A UniRef90 boundaries]=8-57
[Chain B name]=Peripheral plasma membrane protein CASK
[Chain B source organism]=Homo sapiens
[Chain B UniProt accession]=O14936
[Chain B UniProt boundaries]=403-456
[Chain B UniProt coverage]=5.8%
[Chain B UniRef90 accession]=UniRef90_O14936
[Chain B UniRef90 boundaries]=403-456

[Entry]
[Accession]=MF2140002
[Name]=HPV E7 oncoprotein CR3 domain
[Source organism]=Human papillomavirus type 1a
[Assembly]=Homodimer
[Total number of proteins]=2
[Number of unique proteins]=1
[Class]=Other
[Subclass]=Other
[PDB ID]=2b9d
[PDB chain IDs]=AC
[PDB note]=Chain B was deleted. Chain C was generated from chain A using the biomatrix described in the original PDB file.
[PDB experimental technique]=X-ray
[PDB resolution]=1.60
[Evidence global]=Evidence suggests that the E7-CR3 domain would not be able to maintain this tertiary structure in monomeric form or in the absence of zinc coordination and is, therefore, likely to be an obligate and zinc-dependent dimer (PMID:16249186). This is consistent with solution studies showing that HPV-E7 undergoes a monomer-dimer equilibrium with a dissociation constant of about 1 μm (PMID:11123931).
[Evidence chain A]=A close homologue sharing the same Pfam domain (PF00527.15) has been experimentally characterized as disordered in DisProt entry DP00024.
[Evidence chain C]=A close homologue sharing the same Pfam domain (PF00527.15) has been experimentally characterized as disordered in DisProt entry DP00024.
[Chain A name]=Protein E7
[Chain A source organism]=Human papillomavirus type 1a
[Chain A UniProt accession]=P06465
[Chain A UniProt boundaries]=42-93
[Chain A UniProt coverage]=55.9%
[Chain A UniRef90 accession]=UniRef90_P06465
[Chain A UniRef90 boundaries]=43-93
[Chain C name]=Protein E7
[Chain C source organism]=Human papillomavirus type 1a
[Chain C UniProt accession]=P06465
[Chain C UniProt boundaries]=42-93
[Chain C UniProt coverage]=55.9%
[Chain C UniRef90 accession]=UniRef90_P06465
[Chain C UniRef90 boundaries]=43-93

[Entry]
[Accession]=MF2110001
[Name]=RhoA-binding domain in Rho-kinase
[Source organism]=Bos taurus
[Assembly]=Homodimer
[Total number of proteins]=2
[Number of unique proteins]=1
[Class]=Coils and zippers
[Subclass]=Coiled coil (dimeric)
[PDB ID]=1uix
[PDB chain IDs]=AB
[PDB note]=No modifications of the original PDB file. Chain identifiers are identical with the PDB's identifiers.
[PDB experimental technique]=X-ray
[PDB resolution]=1.80
[Evidence global]=The subunits in the structure are bound via coiled coil interactions (PMID:12954645). Coiled coils are highly versatile folding units (PMID:11166216), where the formation of the structure and the interaction between subunits is almost ubiquitously linked. This cooperative nature of binding and folding that results in a two-step process has been demonstrated for coiled coils with varying oligomeric state from dimers (PMID:9811815) and trimers (PMID:10933510) up to heptamers (PMID:17030805). While the interaction and folding are linked, in certain cases there can be significant residual structure before association (PMID:8401212). However, these residual structural elements usually encompass 1-2 turns of helices that serve as a 'nucleation site' driving interaction and helix formation (zipping up) (PMID:17438295), thus even in these cases monomeric coiled coil subunits cannot be considered to have a stable structure.
[Chain A name]=Rho-associated protein kinase 2
[Chain A source organism]=Bos taurus
[Chain A UniProt accession]=Q28021
[Chain A UniProt boundaries]=977-1047
[Chain A UniProt coverage]=5.1%
[Chain A UniRef90 accession]=UniRef90_O75116
[Chain A UniRef90 boundaries]=979-1047
[Chain B name]=Rho-associated protein kinase 2
[Chain B source organism]=Bos taurus
[Chain B UniProt accession]=Q28021
[Chain B UniProt boundaries]=977-1047
[Chain B UniProt coverage]=5.1%
[Chain B UniRef90 accession]=UniRef90_O75116
[Chain B UniRef90 boundaries]=979-1047

[Entry]
[Accession]=MF2120008
[Name]=Trp repressor protein (Escherichia coli)
[Source organism]=Escherichia coli
[Assembly]=Homodimer
[Total number of proteins]=2
[Number of unique proteins]=1
[Class]=Other
[Subclass]=Trp repressor-like
[PDB ID]=3wrp
[PDB chain IDs]=AB
[PDB note]=Chain B was generated from chain A using the biomatrix described in the original PDB file.
[PDB experimental technique]=X-ray
[PDB resolution]=1.80
[Evidence global]=The folding and dimerization of the Trp repressor were shown to be linked by both experimental (PMID:10329154,PMID:2223756,PMID:7578063) and computational studies (PMID:10465773).
[Chain A name]=Trp operon repressor
[Chain A source organism]=Escherichia coli
[Chain A UniProt accession]=P0A881
[Chain A UniProt boundaries]=1-108
[Chain A UniProt coverage]=100%
[Chain A UniRef90 accession]=UniRef90_A9MR96
[Chain A UniRef90 boundaries]=1-106
[Chain B name]=Trp operon repressor
[Chain B source organism]=Escherichia coli
[Chain B UniProt accession]=P0A881
[Chain B UniProt boundaries]=1-108
[Chain B UniProt coverage]=100%
[Chain B UniRef90 accession]=UniRef90_A9MR96
[Chain B UniRef90 boundaries]=1-106
[Related structures]=1co0,1jhg,1rcs,1tro,1trr,1wrp,1wrs,1wrt,1zt9,2oz9,3ssw,3ssx,2xdi

[Entry]
[Accession]=MF2100003
[Name]=Dimerization motif of Geminin
[Source organism]=Homo sapiens
[Assembly]=Homodimer
[Total number of proteins]=2
[Number of unique proteins]=1
[Class]=Coils and zippers
[Subclass]=Coiled coil (dimeric)
[PDB ID]=1uii
[PDB chain IDs]=AB
[PDB note]=No modifications of the original PDB file. Chain identifiers are identical with the PDB's identifiers.
[PDB experimental technique]=X-ray
[PDB resolution]=2.00
[Evidence global]=The subunits in the structure are bound via coiled coil interactions (PMID:15260975). Coiled coils are highly versatile folding units (PMID:11166216), where the formation of the structure and the interaction between subunits is almost ubiquitously linked. This cooperative nature of binding and folding that results in a two-step process has been demonstrated for coiled coils with varying oligomeric state from dimers (PMID:9811815) and trimers (PMID:10933510) up to heptamers (PMID:17030805). While the interaction and folding are linked, in certain cases there can be significant residual structure before association (PMID:8401212). However, these residual structural elements usually encompass 1-2 turns of helices that serve as a 'nucleation site' driving interaction and helix formation (zipping up) (PMID:17438295), thus even in these cases monomeric coiled coil subunits cannot be considered to have a stable structure.
[Chain A name]=Geminin
[Chain A source organism]=Homo sapiens
[Chain A UniProt accession]=O75496
[Chain A UniProt boundaries]=70-152
[Chain A UniProt coverage]=39.7%
[Chain A UniRef90 accession]=UniRef90_O75496
[Chain A UniRef90 boundaries]=70-152
[Chain B name]=Geminin
[Chain B source organism]=Homo sapiens
[Chain B UniProt accession]=O75496
[Chain B UniProt boundaries]=70-152
[Chain B UniProt coverage]=39.7%
[Chain B UniRef90 accession]=UniRef90_O75496
[Chain B UniRef90 boundaries]=70-152
[Related structures]=1t6f,2wvr

[Entry]
[Accession]=MF2110002
[Name]=GAL4 dimerization domain
[Source organism]=Saccharomyces cerevisiae
[Assembly]=Homodimer
[Total number of proteins]=2
[Number of unique proteins]=1
[Class]=Coils and zippers
[Subclass]=Coiled coil (dimeric)
[PDB ID]=1hbw
[PDB chain IDs]=AB
[PDB note]=No modifications of the original PDB file. Chain identifiers are identical with the PDB's identifiers.
[PDB experimental technique]=NMR
[Evidence global]=The subunits in the structure are bound via coiled coil interactions (PMID:11316794). Coiled coils are highly versatile folding units (PMID:11166216), where the formation of the structure and the interaction between subunits is almost ubiquitously linked. This cooperative nature of binding and folding that results in a two-step process has been demonstrated for coiled coils with varying oligomeric state from dimers (PMID:9811815) and trimers (PMID:10933510) up to heptamers (PMID:17030805). While the interaction and folding are linked, in certain cases there can be significant residual structure before association (PMID:8401212). However, these residual structural elements usually encompass 1-2 turns of helices that serve as a 'nucleation site' driving interaction and helix formation (zipping up) (PMID:17438295), thus even in these cases monomeric coiled coil subunits cannot be considered to have a stable structure.
[Chain A name]=Regulatory protein GAL4
[Chain A source organism]=Saccharomyces cerevisiae
[Chain A UniProt accession]=P04386
[Chain A UniProt boundaries]=50-106
[Chain A UniProt coverage]=6.5%
[Chain A UniRef90 accession]=UniRef90_P04386
[Chain A UniRef90 boundaries]=50-106
[Chain B name]=Regulatory protein GAL4
[Chain B source organism]=Saccharomyces cerevisiae
[Chain B UniProt accession]=P04386
[Chain B UniProt boundaries]=50-106
[Chain B UniProt coverage]=6.5%
[Chain B UniRef90 accession]=UniRef90_P04386
[Chain B UniRef90 boundaries]=50-106
[Related structures]=3coq

[Entry]
[Accession]=MF2110003
[Name]=Spindle pole body component SPC42
[Source organism]=Saccharomyces cerevisiae
[Assembly]=Homodimer
[Total number of proteins]=2
[Number of unique proteins]=1
[Class]=Coils and zippers
[Subclass]=Coiled coil (dimeric)
[PDB ID]=2q6q
[PDB chain IDs]=AB
[PDB note]=No modifications of the original PDB file. Chain identifiers are identical with the PDB's identifiers.
[PDB experimental technique]=X-ray
[PDB resolution]=1.97
[Evidence global]=The subunits in the structure are bound via coiled coil interactions (PMID:18850724). Coiled coils are highly versatile folding units (PMID:11166216), where the formation of the structure and the interaction between subunits is almost ubiquitously linked. This cooperative nature of binding and folding that results in a two-step process has been demonstrated for coiled coils with varying oligomeric state from dimers (PMID:9811815) and trimers (PMID:10933510) up to heptamers (PMID:17030805). While the interaction and folding are linked, in certain cases there can be significant residual structure before association (PMID:8401212). However, these residual structural elements usually encompass 1-2 turns of helices that serve as a 'nucleation site' driving interaction and helix formation (zipping up) (PMID:17438295), thus even in these cases monomeric coiled coil subunits cannot be considered to have a stable structure.
[Chain A name]=Spindle pole body component SPC42
[Chain A source organism]=Saccharomyces cerevisiae
[Chain A UniProt accession]=P36094
[Chain A UniProt boundaries]=65-138
[Chain A UniProt coverage]=20.4%
[Chain A UniRef90 accession]=UniRef90_P36094
[Chain A UniRef90 boundaries]=65-138
[Chain B name]=Spindle pole body component SPC42
[Chain B source organism]=Saccharomyces cerevisiae
[Chain B UniProt accession]=P36094
[Chain B UniProt boundaries]=65-138
[Chain B UniProt coverage]=20.4%
[Chain B UniRef90 accession]=UniRef90_P36094
[Chain B UniRef90 boundaries]=65-138

[Entry]
[Accession]=MF2120009
[Name]=Basic coiled-coil protein of unknown function (Eubacterium eligens ATCC 27750)
[Source organism]=Eubacterium eligens
[Assembly]=Homodimer
[Total number of proteins]=2
[Number of unique proteins]=1
[Class]=Coils and zippers
[Subclass]=Leucine zipper (dimeric)
[PDB ID]=3hnw
[PDB chain IDs]=AB
[PDB note]=No modifications of the original PDB file. Chain identifiers are identical with the PDB's identifiers.
[PDB experimental technique]=X-ray
[PDB resolution]=2.20
[Evidence global]=The subunits in the structure are bound via coiled coil interactions. Coiled coils are highly versatile folding units (PMID:11166216), where the formation of the structure and the interaction between subunits is almost ubiquitously linked. This cooperative nature of binding and folding that results in a two-step process has been demonstrated for coiled coils with varying oligomeric state from dimers (PMID:9811815) and trimers (PMID:10933510) up to heptamers (PMID:17030805). While the interaction and folding are linked, in certain cases there can be significant residual structure before association (PMID:8401212). However, these residual structural elements usually encompass 1-2 turns of helices that serve as a 'nucleation site' driving interaction and helix formation (zipping up) (PMID:17438295), thus even in these cases monomeric coiled coil subunits cannot be considered to have a stable structure. Leucine zippers, phenylalanine zippers and alanine zippers are subclasses of coiled coils where the hydrophobic interactions between subunits are predominantly formed by leucine, phenylalanine or alanine residues, respectively.
[Chain A name]=Uncharacterized protein
[Chain A source organism]=Eubacterium eligens
[Chain A UniProt accession]=D0VWZ2
[Chain A UniProt boundaries]=1-138
[Chain A UniProt coverage]=100%
[Chain A UniRef90 accession]=UniRef90_D0VWZ2
[Chain A UniRef90 boundaries]=1-138
[Chain B name]=Uncharacterized protein
[Chain B source organism]=Eubacterium eligens
[Chain B UniProt accession]=D0VWZ2
[Chain B UniProt boundaries]=1-138
[Chain B UniProt coverage]=100%
[Chain B UniRef90 accession]=UniRef90_D0VWZ2
[Chain B UniRef90 boundaries]=1-138

[Entry]
[Accession]=MF2200002
[Name]=Geminin:Idas coiled coil dimer
[Source organism]=Homo sapiens
[Assembly]=Heterodimer
[Total number of proteins]=2
[Number of unique proteins]=2
[Class]=Coils and zippers
[Subclass]=Coiled coil (dimeric)
[PDB ID]=4bry
[PDB chain IDs]=AB
[PDB note]=No modifications of the original PDB file. Chain identifiers are identical with the PDB's identifiers.
[PDB experimental technique]=X-ray
[PDB resolution]=2.89
[Evidence global]=The subunits in the structure are bound via coiled coil interactions (PMID:24064211). Coiled coils are highly versatile folding units (PMID:11166216), where the formation of the structure and the interaction between subunits is almost ubiquitously linked. This cooperative nature of binding and folding that results in a two-step process has been demonstrated for coiled coils with varying oligomeric state from dimers (PMID:9811815) and trimers (PMID:10933510) up to heptamers (PMID:17030805). While the interaction and folding are linked, in certain cases there can be significant residual structure before association (PMID:8401212). However, these residual structural elements usually encompass 1-2 turns of helices that serve as a 'nucleation site' driving interaction and helix formation (zipping up) (PMID:17438295), thus even in these cases monomeric coiled coil subunits cannot be considered to have a stable structure.
[Chain A name]=Geminin
[Chain A source organism]=Homo sapiens
[Chain A UniProt accession]=O75496
[Chain A UniProt boundaries]=83-160
[Chain A UniProt coverage]=37.3%
[Chain A UniRef90 accession]=UniRef90_O75496
[Chain A UniRef90 boundaries]=83-160
[Chain B name]=Multicilin
[Chain B source organism]=Homo sapiens
[Chain B UniProt accession]=D6RGH6
[Chain B UniProt boundaries]=173-245
[Chain B UniProt coverage]=19%
[Chain B UniRef90 accession]=UniRef90_D6RGH6
[Chain B UniRef90 boundaries]=179-245

[Entry]
[Accession]=MF2110004
[Name]=Coiled-coil trigger site of the rod domain of cortexillin I
[Source organism]=Dictyostelium discoideum
[Assembly]=Homodimer
[Total number of proteins]=2
[Number of unique proteins]=1
[Class]=Coils and zippers
[Subclass]=Coiled coil (dimeric)
[PDB ID]=1d7m
[PDB chain IDs]=AB
[PDB note]=No modifications of the original PDB file. Chain identifiers are identical with the PDB's identifiers.
[PDB experimental technique]=X-ray
[PDB resolution]=2.70
[Evidence global]=The subunits in the structure are bound via coiled coil interactions (PMID:10745004). Coiled coils are highly versatile folding units (PMID:11166216), where the formation of the structure and the interaction between subunits is almost ubiquitously linked. This cooperative nature of binding and folding that results in a two-step process has been demonstrated for coiled coils with varying oligomeric state from dimers (PMID:9811815) and trimers (PMID:10933510) up to heptamers (PMID:17030805). While the interaction and folding are linked, in certain cases there can be significant residual structure before association (PMID:8401212). However, these residual structural elements usually encompass 1-2 turns of helices that serve as a 'nucleation site' driving interaction and helix formation (zipping up) (PMID:17438295), thus even in these cases monomeric coiled coil subunits cannot be considered to have a stable structure.
[Chain A name]=Cortexillin-1
[Chain A source organism]=Dictyostelium discoideum
[Chain A UniProt accession]=Q54HG2
[Chain A UniProt boundaries]=243-343
[Chain A UniProt coverage]=22.7%
[Chain A UniRef90 accession]=UniRef90_Q54HG2
[Chain A UniRef90 boundaries]=243-343
[Chain B name]=Cortexillin-1
[Chain B source organism]=Dictyostelium discoideum
[Chain B UniProt accession]=Q54HG2
[Chain B UniProt boundaries]=243-343
[Chain B UniProt coverage]=22.7%
[Chain B UniRef90 accession]=UniRef90_Q54HG2
[Chain B UniRef90 boundaries]=243-343

[Entry]
[Accession]=MF2120010
[Name]=Cell division factor ZapA
[Source organism]=Shigella sonnei
[Assembly]=Homodimer
[Total number of proteins]=2
[Number of unique proteins]=1
[Class]=Coils and zippers
[Subclass]=Coiled coil (dimeric)
[PDB ID]=4p1m
[PDB chain IDs]=AB
[PDB note]=No modifications of the original PDB file. Chain identifiers are identical with the PDB's identifiers.
[PDB experimental technique]=X-ray
[PDB resolution]=1.95
[Evidence global]=The subunits in the structure are bound via coiled coil interactions (PMID:25002581). Coiled coils are highly versatile folding units (PMID:11166216), where the formation of the structure and the interaction between subunits is almost ubiquitously linked. This cooperative nature of binding and folding that results in a two-step process has been demonstrated for coiled coils with varying oligomeric state from dimers (PMID:9811815) and trimers (PMID:10933510) up to heptamers (PMID:17030805). While the interaction and folding are linked, in certain cases there can be significant residual structure before association (PMID:8401212). However, these residual structural elements usually encompass 1-2 turns of helices that serve as a 'nucleation site' driving interaction and helix formation (zipping up) (PMID:17438295), thus even in these cases monomeric coiled coil subunits cannot be considered to have a stable structure.
[Chain A name]=Cell division protein ZapA
[Chain A source organism]=Shigella sonnei
[Chain A UniProt accession]=Q3YXW0
[Chain A UniProt boundaries]=1-109
[Chain A UniProt coverage]=100%
[Chain A UniRef90 accession]=UniRef90_A9MRG5
[Chain A UniRef90 boundaries]=1-109
[Chain B name]=Cell division protein ZapA
[Chain B source organism]=Shigella sonnei
[Chain B UniProt accession]=Q3YXW0
[Chain B UniProt boundaries]=1-109
[Chain B UniProt coverage]=100%
[Chain B UniRef90 accession]=UniRef90_A9MRG5
[Chain B UniRef90 boundaries]=1-109

[Entry]
[Accession]=MF2120011
[Name]=Cell division factor ZapB
[Source organism]=Escherichia coli
[Assembly]=Homodimer
[Total number of proteins]=2
[Number of unique proteins]=1
[Class]=Coils and zippers
[Subclass]=Coiled coil (dimeric)
[PDB ID]=2jee
[PDB chain IDs]=AB
[PDB note]=Chains C and D were removed as chains A and B represent the biologically relevant dimer.
[PDB experimental technique]=X-ray
[PDB resolution]=2.8
[Evidence global]=The subunits in the structure are bound via coiled coil interactions (PMID:18394147). Coiled coils are highly versatile folding units (PMID:11166216), where the formation of the structure and the interaction between subunits is almost ubiquitously linked. This cooperative nature of binding and folding that results in a two-step process has been demonstrated for coiled coils with varying oligomeric state from dimers (PMID:9811815) and trimers (PMID:10933510) up to heptamers (PMID:17030805). While the interaction and folding are linked, in certain cases there can be significant residual structure before association (PMID:8401212). However, these residual structural elements usually encompass 1-2 turns of helices that serve as a 'nucleation site' driving interaction and helix formation (zipping up) (PMID:17438295), thus even in these cases monomeric coiled coil subunits cannot be considered to have a stable structure.
[Chain A name]=Cell division protein ZapB
[Chain A source organism]=Escherichia coli
[Chain A UniProt accession]=P0AF36
[Chain A UniProt boundaries]=1-81
[Chain A UniProt coverage]=100%
[Chain A UniRef90 accession]=UniRef90_A7ZUE3
[Chain A UniRef90 boundaries]=1-81
[Chain B name]=Cell division protein ZapB
[Chain B source organism]=Escherichia coli
[Chain B UniProt accession]=P0AF36
[Chain B UniProt boundaries]=1-81
[Chain B UniProt coverage]=100%
[Chain B UniRef90 accession]=UniRef90_A7ZUE3
[Chain B UniRef90 boundaries]=1-81

[Entry]
[Accession]=MF2110005
[Name]=Autophagy protein 16
[Source organism]=Saccharomyces cerevisiae
[Assembly]=Homodimer
[Total number of proteins]=2
[Number of unique proteins]=1
[Class]=Coils and zippers
[Subclass]=Coiled coil (dimeric)
[PDB ID]=3a7o
[PDB chain IDs]=AB
[PDB note]=Chains C, D, E and F were removed as chains A and B represent the biologically relevant dimer.
[PDB experimental technique]=X-ray
[PDB resolution]=2.50
[Evidence global]=The subunits in the structure are bound via coiled coil interactions. Coiled coils are highly versatile folding units (PMID:11166216), where the formation of the structure and the interaction between subunits is almost ubiquitously linked. This cooperative nature of binding and folding that results in a two-step process has been demonstrated for coiled coils with varying oligomeric state from dimers (PMID:9811815) and trimers (PMID:10933510) up to heptamers (PMID:17030805). While the interaction and folding are linked, in certain cases there can be significant residual structure before association (PMID:8401212). However, these residual structural elements usually encompass 1-2 turns of helices that serve as a 'nucleation site' driving interaction and helix formation (zipping up) (PMID:17438295), thus even in these cases monomeric coiled coil subunits cannot be considered to have a stable structure.
[Chain A name]=Autophagy protein 16
[Chain A source organism]=Saccharomyces cerevisiae
[Chain A UniProt accession]=Q03818
[Chain A UniProt boundaries]=49-123
[Chain A UniProt coverage]=50%
[Chain A UniRef90 accession]=UniRef90_A6ZML8
[Chain A UniRef90 boundaries]=50-123
[Chain B name]=Autophagy protein 16
[Chain B source organism]=Saccharomyces cerevisiae
[Chain B UniProt accession]=Q03818
[Chain B UniProt boundaries]=49-123
[Chain B UniProt coverage]=50%
[Chain B UniRef90 accession]=UniRef90_A6ZML8
[Chain B UniRef90 boundaries]=50-123
[Related structures]=3a7p

[Entry]
[Accession]=MF3110001
[Name]=Assembly domain of cartilage oligomeric matrix protein (chicken)
[Source organism]=Gallus gallus
[Assembly]=Homotrimer
[Total number of proteins]=3
[Number of unique proteins]=1
[Class]=Coils and zippers
[Subclass]=Coiled coil (trimeric)
[PDB ID]=1aq5
[PDB chain IDs]=ABC
[PDB note]=No modifications of the original PDB file. Chain identifiers are identical with the PDB's identifiers.
[PDB experimental technique]=NMR
[Evidence global]=The subunits in the structure are bound via coiled coil interactions (PMID:9699631). Coiled coils are highly versatile folding units (PMID:11166216), where the formation of the structure and the interaction between subunits is almost ubiquitously linked. This cooperative nature of binding and folding that results in a two-step process has been demonstrated for coiled coils with varying oligomeric state from dimers (PMID:9811815) and trimers (PMID:10933510) up to heptamers (PMID:17030805). While the interaction and folding are linked, in certain cases there can be significant residual structure before association (PMID:8401212). However, these residual structural elements usually encompass 1-2 turns of helices that serve as a 'nucleation site' driving interaction and helix formation (zipping up) (PMID:17438295), thus even in these cases monomeric coiled coil subunits cannot be considered to have a stable structure.
[Chain A name]=Cartilage matrix protein
[Chain A source organism]=Gallus gallus
[Chain A UniProt accession]=P05099
[Chain A UniProt boundaries]=447-493
[Chain A UniProt coverage]=9.5%
[Chain A UniRef90 accession]=UniRef90_P05099
[Chain A UniRef90 boundaries]=450-493
[Chain B name]=Cartilage matrix protein
[Chain B source organism]=Gallus gallus
[Chain B UniProt accession]=P05099
[Chain B UniProt boundaries]=447-493
[Chain B UniProt coverage]=9.5%
[Chain B UniRef90 accession]=UniRef90_P05099
[Chain B UniRef90 boundaries]=450-493
[Chain C name]=Cartilage matrix protein
[Chain C source organism]=Gallus gallus
[Chain C UniProt accession]=P05099
[Chain C UniProt boundaries]=447-493
[Chain C UniProt coverage]=9.5%
[Chain C UniRef90 accession]=UniRef90_P05099
[Chain C UniRef90 boundaries]=450-493

[Entry]
[Accession]=MF3140001
[Name]=Bacteriophage T4 fibritin
[Source organism]=Enterobacteria phage T4
[Assembly]=Homotrimer
[Total number of proteins]=3
[Number of unique proteins]=1
[Class]=Other
[Subclass]=Coiled coil/foldon domain
[PDB ID]=1aa0
[PDB chain IDs]=ABC
[PDB note]=Chains B and C were generated from chain A using the biomatrices described in the original PDB file.
[PDB experimental technique]=X-ray
[PDB resolution]=2.20
[Evidence global]=The foldon domain folds into a trimeric beta-propeller structure and undergoes a two-state unfolding transition from folded trimer to unfolded monomers (PMID:15033360). The other subunits in the structure are bound via coiled coil interactions (PMID:9261070). Coiled coils are highly versatile folding units (PMID:11166216), where the formation of the structure and the interaction between subunits is almost ubiquitously linked. This cooperative nature of binding and folding that results in a two-step process has been demonstrated for coiled coils with varying oligomeric state from dimers (PMID:9811815) and trimers (PMID:10933510) up to heptamers (PMID:17030805). While the interaction and folding are linked, in certain cases there can be significant residual structure before association (PMID:8401212). However, these residual structural elements usually encompass 1-2 turns of helices that serve as a 'nucleation site' driving interaction and helix formation (zipping up) (PMID:17438295), thus even in these cases monomeric coiled coil subunits cannot be considered to have a stable structure.
[Chain A name]=Fibritin
[Chain A source organism]=Enterobacteria phage T4
[Chain A UniProt accession]=P10104
[Chain A UniProt boundaries]=372-484
[Chain A UniProt coverage]=23.2%
[Chain A UniRef90 accession]=UniRef90_P10104
[Chain A UniRef90 boundaries]=372-484
[Chain B name]=Fibritin
[Chain B source organism]=Enterobacteria phage T4
[Chain B UniProt accession]=P10104
[Chain B UniProt boundaries]=372-484
[Chain B UniProt coverage]=23.2%
[Chain B UniRef90 accession]=UniRef90_P10104
[Chain B UniRef90 boundaries]=372-484
[Chain C name]=Fibritin
[Chain C source organism]=Enterobacteria phage T4
[Chain C UniProt accession]=P10104
[Chain C UniProt boundaries]=372-484
[Chain C UniProt coverage]=23.2%
[Chain C UniRef90 accession]=UniRef90_P10104
[Chain C UniRef90 boundaries]=372-484
[Related structures]=1avy,2bsg,3j2o,2ww6,2ww7,4ncu,4ncv,4ncw,1v1h,1v1i,2kbl,3a1m,1u0p

[Entry]
[Accession]=MF3100001
[Name]=Trimerization domain from lung surfactant protein D
[Source organism]=Homo sapiens
[Assembly]=Homotrimer
[Total number of proteins]=3
[Number of unique proteins]=1
[Class]=Coils and zippers
[Subclass]=Coiled coil (trimeric)
[PDB ID]=1m7l
[PDB chain IDs]=ABC
[PDB note]=No modifications of the original PDB file. Chain identifiers are identical with the PDB's identifiers.
[PDB experimental technique]=NMR
[Evidence global]=The subunits in the structure are bound via coiled coil interactions (PMID:12495025). Coiled coils are highly versatile folding units (PMID:11166216), where the formation of the structure and the interaction between subunits is almost ubiquitously linked. This cooperative nature of binding and folding that results in a two-step process has been demonstrated for coiled coils with varying oligomeric state from dimers (PMID:9811815) and trimers (PMID:10933510) up to heptamers (PMID:17030805). While the interaction and folding are linked, in certain cases there can be significant residual structure before association (PMID:8401212). However, these residual structural elements usually encompass 1-2 turns of helices that serve as a 'nucleation site' driving interaction and helix formation (zipping up) (PMID:17438295), thus even in these cases monomeric coiled coil subunits cannot be considered to have a stable structure.
[Chain A name]=Pulmonary surfactant-associated protein D
[Chain A source organism]=Homo sapiens
[Chain A UniProt accession]=P35247
[Chain A UniProt boundaries]=220-259
[Chain A UniProt coverage]=10.7%
[Chain A UniRef90 accession]=UniRef90_P35247
[Chain A UniRef90 boundaries]=220-257
[Chain B name]=Pulmonary surfactant-associated protein D
[Chain B source organism]=Homo sapiens
[Chain B UniProt accession]=P35247
[Chain B UniProt boundaries]=220-259
[Chain B UniProt coverage]=10.7%
[Chain B UniRef90 accession]=UniRef90_P35247
[Chain B UniRef90 boundaries]=220-257
[Chain C name]=Pulmonary surfactant-associated protein D
[Chain C source organism]=Homo sapiens
[Chain C UniProt accession]=P35247
[Chain C UniProt boundaries]=220-259
[Chain C UniProt coverage]=10.7%
[Chain C UniRef90 accession]=UniRef90_P35247
[Chain C UniRef90 boundaries]=220-257
[Related structures]=1b08,1pw9,1pwb,2ggu,2ggx,2orj,2ork,2os9,2ria,2rib,2ric,2rid,2rie,3dbz,3g81,3g83,3g84,3ikn,3ikp,3ikq,3ikr,4e52,4m17,4m18

[Entry]
[Accession]=MF3120001
[Name]=Major outer membrane lipoprotein
[Source organism]=Shigella flexneri
[Assembly]=Homotrimer
[Total number of proteins]=3
[Number of unique proteins]=1
[Class]=Coils and zippers
[Subclass]=Alanine zipper (trimeric)
[PDB ID]=1jcc
[PDB chain IDs]=ABC
[PDB note]=No modifications of the original PDB file. Chain identifiers are identical with the PDB's identifiers.
[PDB experimental technique]=X-ray
[PDB resolution]=1.70
[Evidence global]=The subunits in the structure are bound via coiled coil interactions (PMID:12741822). Coiled coils are highly versatile folding units (PMID:11166216), where the formation of the structure and the interaction between subunits is almost ubiquitously linked. This cooperative nature of binding and folding that results in a two-step process has been demonstrated for coiled coils with varying oligomeric state from dimers (PMID:9811815) and trimers (PMID:10933510) up to heptamers (PMID:17030805). While the interaction and folding are linked, in certain cases there can be significant residual structure before association (PMID:8401212). However, these residual structural elements usually encompass 1-2 turns of helices that serve as a 'nucleation site' driving interaction and helix formation (zipping up) (PMID:17438295), thus even in these cases monomeric coiled coil subunits cannot be considered to have a stable structure. Leucine zippers, phenylalanine zippers and alanine zippers are subclasses of coiled coils where the hydrophobic interactions between subunits are predominantly formed by leucine, phenylalanine or alanine residues, respectively.
[Chain A name]=Major outer membrane lipoprotein
[Chain A source organism]=Shigella flexneri
[Chain A UniProt accession]=P69780
[Chain A UniProt boundaries]=22-77
[Chain A UniProt coverage]=71.8%
[Chain A UniRef90 accession]=UniRef90_P69778
[Chain A UniRef90 boundaries]=22-77
[Chain B name]=Major outer membrane lipoprotein
[Chain B source organism]=Shigella flexneri
[Chain B UniProt accession]=P69780
[Chain B UniProt boundaries]=22-77
[Chain B UniProt coverage]=71.8%
[Chain B UniRef90 accession]=UniRef90_P69778
[Chain B UniRef90 boundaries]=22-77
[Chain C name]=Major outer membrane lipoprotein
[Chain C source organism]=Shigella flexneri
[Chain C UniProt accession]=P69780
[Chain C UniProt boundaries]=22-77
[Chain C UniProt coverage]=71.8%
[Chain C UniRef90 accession]=UniRef90_P69778
[Chain C UniRef90 boundaries]=22-77
[Related structures]=1eq7,1kfm,1kfn,1jcd,1t8z,2gus,2guv

[Entry]
[Accession]=MF3120002
[Name]=DUF16 domain of MPN010 (Mycoplasma pneumoniae)
[Source organism]=Mycoplasma pneumoniae
[Assembly]=Homotrimer
[Total number of proteins]=3
[Number of unique proteins]=1
[Class]=Coils and zippers
[Subclass]=Coiled coil (trimeric)
[PDB ID]=2ba2
[PDB chain IDs]=ABC
[PDB note]=No modifications of the original PDB file. Chain identifiers are identical with the PDB's identifiers.
[PDB experimental technique]=X-ray
[PDB resolution]=1.80
[Evidence global]=The subunits in the structure are bound via coiled coil interactions (PMID:16522803). Coiled coils are highly versatile folding units (PMID:11166216), where the formation of the structure and the interaction between subunits is almost ubiquitously linked. This cooperative nature of binding and folding that results in a two-step process has been demonstrated for coiled coils with varying oligomeric state from dimers (PMID:9811815) and trimers (PMID:10933510) up to heptamers (PMID:17030805). While the interaction and folding are linked, in certain cases there can be significant residual structure before association (PMID:8401212). However, these residual structural elements usually encompass 1-2 turns of helices that serve as a 'nucleation site' driving interaction and helix formation (zipping up) (PMID:17438295), thus even in these cases monomeric coiled coil subunits cannot be considered to have a stable structure.
[Chain A name]=UPF0134 protein MPN_010
[Chain A source organism]=Mycoplasma pneumoniae
[Chain A UniProt accession]=P75103
[Chain A UniProt boundaries]=46-130
[Chain A UniProt coverage]=64.9%
[Chain A UniRef90 accession]=UniRef90_P75103
[Chain A UniRef90 boundaries]=46-130
[Chain B name]=UPF0134 protein MPN_010
[Chain B source organism]=Mycoplasma pneumoniae
[Chain B UniProt accession]=P75103
[Chain B UniProt boundaries]=46-130
[Chain B UniProt coverage]=64.9%
[Chain B UniRef90 accession]=UniRef90_P75103
[Chain B UniRef90 boundaries]=46-130
[Chain C name]=UPF0134 protein MPN_010
[Chain C source organism]=Mycoplasma pneumoniae
[Chain C UniProt accession]=P75103
[Chain C UniProt boundaries]=46-130
[Chain C UniProt coverage]=64.9%
[Chain C UniRef90 accession]=UniRef90_P75103
[Chain C UniRef90 boundaries]=46-130

[Entry]
[Accession]=MF3100002
[Name]=Dystrophia myotonin-protein kinase coiled-coil domain
[Source organism]=Homo sapiens
[Assembly]=Homotrimer
[Total number of proteins]=3
[Number of unique proteins]=1
[Class]=Coils and zippers
[Subclass]=Coiled coil (trimeric)
[PDB ID]=1wt6
[PDB chain IDs]=ABD
[PDB note]=No modifications of the original PDB file. Chain identifiers are identical with the PDB's identifiers.
[PDB experimental technique]=X-ray
[PDB resolution]=1.60
[Evidence global]=The subunits in the structure are bound via coiled coil interactions (PMID:16770013). Coiled coils are highly versatile folding units (PMID:11166216), where the formation of the structure and the interaction between subunits is almost ubiquitously linked. This cooperative nature of binding and folding that results in a two-step process has been demonstrated for coiled coils with varying oligomeric state from dimers (PMID:9811815) and trimers (PMID:10933510) up to heptamers (PMID:17030805). While the interaction and folding are linked, in certain cases there can be significant residual structure before association (PMID:8401212). However, these residual structural elements usually encompass 1-2 turns of helices that serve as a 'nucleation site' driving interaction and helix formation (zipping up) (PMID:17438295), thus even in these cases monomeric coiled coil subunits cannot be considered to have a stable structure.
[Chain A name]=Myotonin-protein kinase
[Chain A source organism]=Homo sapiens
[Chain A UniProt accession]=Q09013
[Chain A UniProt boundaries]=457-537
[Chain A UniProt coverage]=12.9%
[Chain A UniRef90 accession]=UniRef90_Q09013
[Chain A UniRef90 boundaries]=467-537
[Chain B name]=Myotonin-protein kinase
[Chain B source organism]=Homo sapiens
[Chain B UniProt accession]=Q09013
[Chain B UniProt boundaries]=457-537
[Chain B UniProt coverage]=12.9%
[Chain B UniRef90 accession]=UniRef90_Q09013
[Chain B UniRef90 boundaries]=467-537
[Chain D name]=Myotonin-protein kinase
[Chain D source organism]=Homo sapiens
[Chain D UniProt accession]=Q09013
[Chain D UniProt boundaries]=457-537
[Chain D UniProt coverage]=12.9%
[Chain D UniRef90 accession]=UniRef90_Q09013
[Chain D UniRef90 boundaries]=467-537

[Entry]
[Accession]=MF2140003
[Name]=Gene V protein
[Source organism]=Enterobacteria phage f1
[Assembly]=Homodimer
[Total number of proteins]=2
[Number of unique proteins]=1
[Class]=Other
[Subclass]=Other
[PDB ID]=1gvp
[PDB chain IDs]=AB
[PDB note]=Chain B was generated from chain A using the biomatrices described in the original PDB file.
[PDB experimental technique]=X-ray
[PDB resolution]=1.60
[Evidence global]=Reversible denaturation experiments have shown that the dimeric gene V protein unfolds in a single cooperative transition from a folded dimer into two unfolded monomers (PMID:2007116).
[Chain A name]=DNA-Binding protein G5P
[Chain A source organism]=Enterobacteria phage f1
[Chain A UniProt accession]=P69543
[Chain A UniProt boundaries]=1-87
[Chain A UniProt coverage]=100%
[Chain A UniRef90 accession]=UniRef90_P69543
[Chain A UniRef90 boundaries]=1-87
[Chain B name]=DNA-Binding protein G5P
[Chain B source organism]=Enterobacteria phage f1
[Chain B UniProt accession]=P69543
[Chain B UniProt boundaries]=1-87
[Chain B UniProt coverage]=100%
[Chain B UniRef90 accession]=UniRef90_P69543
[Chain B UniRef90 boundaries]=1-87
[Related structures]=1ae2,1ae3,1gkh,2gn5,2gva,2gvb,1vqa,1vqb,1vqc,1vqd,1vqe,1vqf,1vqg,1vqh,1vqi,1vqj,1yha,1yhb

[Entry]
[Accession]=MF2140004
[Name]=Bacteriophage f29 scaffolding protein gp7
[Source organism]=Bacillus phage phi29
[Assembly]=Homodimer
[Total number of proteins]=2
[Number of unique proteins]=1
[Class]=Coils and zippers
[Subclass]=Coiled coil (dimeric)
[PDB ID]=1no4
[PDB chain IDs]=AB
[PDB note]=Chains C and D were removed as chains A and B represent the biologically relevant dimer.
[PDB experimental technique]=X-ray
[PDB resolution]=2.20
[Evidence global]=The subunits in the structure are bound via coiled coil interactions (PMID:12778115). Coiled coils are highly versatile folding units (PMID:11166216), where the formation of the structure and the interaction between subunits is almost ubiquitously linked. This cooperative nature of binding and folding that results in a two-step process has been demonstrated for coiled coils with varying oligomeric state from dimers (PMID:9811815) and trimers (PMID:10933510) up to heptamers (PMID:17030805). While the interaction and folding are linked, in certain cases there can be significant residual structure before association (PMID:8401212). However, these residual structural elements usually encompass 1-2 turns of helices that serve as a 'nucleation site' driving interaction and helix formation (zipping up) (PMID:17438295), thus even in these cases monomeric coiled coil subunits cannot be considered to have a stable structure.
[Chain A name]=Head morphogenesis protein
[Chain A source organism]=Bacillus phage phi29
[Chain A UniProt accession]=P13848
[Chain A UniProt boundaries]=2-98
[Chain A UniProt coverage]=99%
[Chain A UniRef90 accession]=UniRef90_P13848
[Chain A UniRef90 boundaries]=2-98
[Chain B name]=Head morphogenesis protein
[Chain B source organism]=Bacillus phage phi29
[Chain B UniProt accession]=P13848
[Chain B UniProt boundaries]=2-98
[Chain B UniProt coverage]=99%
[Chain B UniRef90 accession]=UniRef90_P13848
[Chain B UniRef90 boundaries]=2-98
[Related structures]=1noh,4iff,4xa1

[Entry]
[Accession]=MF4130001
[Name]=Tetrabrachion tetramerization region
[Source organism]=Staphylothermus marinus
[Assembly]=Homotetramer
[Total number of proteins]=4
[Number of unique proteins]=1
[Class]=Coils and zippers
[Subclass]=Coiled coil (tetrameric)
[PDB ID]=1fe6
[PDB chain IDs]=ABCD
[PDB note]=No modifications of the original PDB file. Chain identifiers are identical with the PDB's identifiers.
[PDB experimental technique]=X-ray
[PDB resolution]=1.80
[Evidence global]=The subunits in the structure are bound via coiled coil interactions (PMID:10966648). Coiled coils are highly versatile folding units (PMID:11166216), where the formation of the structure and the interaction between subunits is almost ubiquitously linked. This cooperative nature of binding and folding that results in a two-step process has been demonstrated for coiled coils with varying oligomeric state from dimers (PMID:9811815) and trimers (PMID:10933510) up to heptamers (PMID:17030805). While the interaction and folding are linked, in certain cases there can be significant residual structure before association (PMID:8401212). However, these residual structural elements usually encompass 1-2 turns of helices that serve as a 'nucleation site' driving interaction and helix formation (zipping up) (PMID:17438295), thus even in these cases monomeric coiled coil subunits cannot be considered to have a stable structure.
[Chain A name]=Tetrabrachion (Precursor)
[Chain A source organism]=Staphylothermus marinus
[Chain A UniProt accession]=Q54436
[Chain A UniProt boundaries]=1236-1287
[Chain A UniProt coverage]=3.4%
[Chain A UniRef90 accession]=UniRef90_Q54436
[Chain A UniRef90 boundaries]=1237-1286
[Chain B name]=Tetrabrachion (Precursor)
[Chain B source organism]=Staphylothermus marinus
[Chain B UniProt accession]=Q54436
[Chain B UniProt boundaries]=1236-1287
[Chain B UniProt coverage]=3.4%
[Chain B UniRef90 accession]=UniRef90_Q54436
[Chain B UniRef90 boundaries]=1237-1286
[Chain C name]=Tetrabrachion (Precursor)
[Chain C source organism]=Staphylothermus marinus
[Chain C UniProt accession]=Q54436
[Chain C UniProt boundaries]=1236-1287
[Chain C UniProt coverage]=3.4%
[Chain C UniRef90 accession]=UniRef90_Q54436
[Chain C UniRef90 boundaries]=1237-1286
[Chain D name]=Tetrabrachion (Precursor)
[Chain D source organism]=Staphylothermus marinus
[Chain D UniProt accession]=Q54436
[Chain D UniProt boundaries]=1236-1287
[Chain D UniProt coverage]=3.4%
[Chain D UniRef90 accession]=UniRef90_Q54436
[Chain D UniRef90 boundaries]=1237-1286
[Related structures]=1ybk,5jr5

[Entry]
[Accession]=MF4140001
[Name]=Virion-associated protein P3
[Source organism]=Cauliflower mosaic virus
[Assembly]=Homotetramer
[Total number of proteins]=4
[Number of unique proteins]=1
[Class]=Coils and zippers
[Subclass]=Coiled coil (tetrameric)
[PDB ID]=3f6n
[PDB chain IDs]=ABCD
[PDB note]=No modifications of the original PDB file. Chain identifiers are identical with the PDB's identifiers.
[PDB experimental technique]=X-ray
[PDB resolution]=3.10
[Evidence global]=The subunits in the structure are bound via coiled coil interactions (PMID:20181714). Coiled coils are highly versatile folding units (PMID:11166216), where the formation of the structure and the interaction between subunits is almost ubiquitously linked. This cooperative nature of binding and folding that results in a two-step process has been demonstrated for coiled coils with varying oligomeric state from dimers (PMID:9811815) and trimers (PMID:10933510) up to heptamers (PMID:17030805). While the interaction and folding are linked, in certain cases there can be significant residual structure before association (PMID:8401212). However, these residual structural elements usually encompass 1-2 turns of helices that serve as a 'nucleation site' driving interaction and helix formation (zipping up) (PMID:17438295), thus even in these cases monomeric coiled coil subunits cannot be considered to have a stable structure.
[Chain A name]=Virion-associated protein
[Chain A source organism]=Cauliflower mosaic virus
[Chain A UniProt accession]=P03551
[Chain A UniProt boundaries]=1-129
[Chain A UniProt coverage]=100%
[Chain A UniRef90 accession]=UniRef90_P03551
[Chain A UniRef90 boundaries]=1-129
[Chain B name]=Virion-associated protein
[Chain B source organism]=Cauliflower mosaic virus
[Chain B UniProt accession]=P03551
[Chain B UniProt boundaries]=1-129
[Chain B UniProt coverage]=100%
[Chain B UniRef90 accession]=UniRef90_P03551
[Chain B UniRef90 boundaries]=1-129
[Chain C name]=Virion-associated protein
[Chain C source organism]=Cauliflower mosaic virus
[Chain C UniProt accession]=P03551
[Chain C UniProt boundaries]=1-129
[Chain C UniProt coverage]=100%
[Chain C UniRef90 accession]=UniRef90_P03551
[Chain C UniRef90 boundaries]=1-129
[Chain D name]=Virion-associated protein
[Chain D source organism]=Cauliflower mosaic virus
[Chain D UniProt accession]=P03551
[Chain D UniProt boundaries]=1-129
[Chain D UniProt coverage]=100%
[Chain D UniRef90 accession]=UniRef90_P03551
[Chain D UniRef90 boundaries]=1-129
[Related structures]=3k4t

[Entry]
[Accession]=MF5110001
[Name]=Assembly domain of cartilage oligomeric matrix protein (rat)
[Source organism]=Rattus norvegicus
[Assembly]=Homopentamer
[Total number of proteins]=5
[Number of unique proteins]=1
[Class]=Coils and zippers
[Subclass]=Coiled coil (pentameric)
[PDB ID]=1fbm
[PDB chain IDs]=ABCDE
[PDB note]=No modifications of the original PDB file. Chain identifiers are identical with the PDB's identifiers.
[PDB experimental technique]=X-ray
[PDB resolution]=2.70
[Evidence global]=The subunits in the structure are bound via coiled coil interactions (PMID:9736606). Coiled coils are highly versatile folding units (PMID:11166216), where the formation of the structure and the interaction between subunits is almost ubiquitously linked. This cooperative nature of binding and folding that results in a two-step process has been demonstrated for coiled coils with varying oligomeric state from dimers (PMID:9811815) and trimers (PMID:10933510) up to heptamers (PMID:17030805). While the interaction and folding are linked, in certain cases there can be significant residual structure before association (PMID:8401212). However, these residual structural elements usually encompass 1-2 turns of helices that serve as a 'nucleation site' driving interaction and helix formation (zipping up) (PMID:17438295), thus even in these cases monomeric coiled coil subunits cannot be considered to have a stable structure.
[Chain A name]=Cartilage oligomeric matrix protein
[Chain A source organism]=Rattus norvegicus
[Chain A UniProt accession]=P35444
[Chain A UniProt boundaries]=27-72
[Chain A UniProt coverage]=6.1%
[Chain A UniRef90 accession]=UniRef90_P49747
[Chain A UniRef90 boundaries]=29-73
[Chain B name]=Cartilage oligomeric matrix protein
[Chain B source organism]=Rattus norvegicus
[Chain B UniProt accession]=P35444
[Chain B UniProt boundaries]=27-72
[Chain B UniProt coverage]=6.1%
[Chain B UniRef90 accession]=UniRef90_P49747
[Chain B UniRef90 boundaries]=29-73
[Chain C name]=Cartilage oligomeric matrix protein
[Chain C source organism]=Rattus norvegicus
[Chain C UniProt accession]=P35444
[Chain C UniProt boundaries]=27-72
[Chain C UniProt coverage]=6.1%
[Chain C UniRef90 accession]=UniRef90_P49747
[Chain C UniRef90 boundaries]=29-73
[Chain D name]=Cartilage oligomeric matrix protein
[Chain D source organism]=Rattus norvegicus
[Chain D UniProt accession]=P35444
[Chain D UniProt boundaries]=27-72
[Chain D UniProt coverage]=6.1%
[Chain D UniRef90 accession]=UniRef90_P49747
[Chain D UniRef90 boundaries]=29-73
[Chain E name]=Cartilage oligomeric matrix protein
[Chain E source organism]=Rattus norvegicus
[Chain E UniProt accession]=P35444
[Chain E UniProt boundaries]=27-72
[Chain E UniProt coverage]=6.1%
[Chain E UniRef90 accession]=UniRef90_P49747
[Chain E UniRef90 boundaries]=29-73
[Related structures]=1vdf

[Entry]
[Accession]=MF5110002
[Name]=Assembly domain of cartilage oligomeric matrix protein (mouse)
[Source organism]=Mus musculus
[Assembly]=Homopentamer
[Total number of proteins]=5
[Number of unique proteins]=1
[Class]=Coils and zippers
[Subclass]=Coiled coil (pentameric)
[PDB ID]=1mz9
[PDB chain IDs]=ABCDE
[PDB note]=No modifications of the original PDB file. Chain identifiers are identical with the PDB's identifiers.
[PDB experimental technique]=X-ray
[PDB resolution]=1.70
[Evidence global]=The subunits in the structure are bound via coiled coil interactions (PMID:12426368). Coiled coils are highly versatile folding units (PMID:11166216), where the formation of the structure and the interaction between subunits is almost ubiquitously linked. This cooperative nature of binding and folding that results in a two-step process has been demonstrated for coiled coils with varying oligomeric state from dimers (PMID:9811815) and trimers (PMID:10933510) up to heptamers (PMID:17030805). While the interaction and folding are linked, in certain cases there can be significant residual structure before association (PMID:8401212). However, these residual structural elements usually encompass 1-2 turns of helices that serve as a 'nucleation site' driving interaction and helix formation (zipping up) (PMID:17438295), thus even in these cases monomeric coiled coil subunits cannot be considered to have a stable structure.
[Chain A name]=Cartilage oligomeric matrix protein
[Chain A source organism]=Mus musculus
[Chain A UniProt accession]=Q9R0G6
[Chain A UniProt boundaries]=27-71
[Chain A UniProt coverage]=6%
[Chain A UniRef90 accession]=UniRef90_Q9R0G6
[Chain A UniRef90 boundaries]=28-71
[Chain B name]=Cartilage oligomeric matrix protein
[Chain B source organism]=Mus musculus
[Chain B UniProt accession]=Q9R0G6
[Chain B UniProt boundaries]=27-71
[Chain B UniProt coverage]=6%
[Chain B UniRef90 accession]=UniRef90_Q9R0G6
[Chain B UniRef90 boundaries]=28-71
[Chain C name]=Cartilage oligomeric matrix protein
[Chain C source organism]=Mus musculus
[Chain C UniProt accession]=Q9R0G6
[Chain C UniProt boundaries]=27-71
[Chain C UniProt coverage]=6%
[Chain C UniRef90 accession]=UniRef90_Q9R0G6
[Chain C UniRef90 boundaries]=28-71
[Chain D name]=Cartilage oligomeric matrix protein
[Chain D source organism]=Mus musculus
[Chain D UniProt accession]=Q9R0G6
[Chain D UniProt boundaries]=27-71
[Chain D UniProt coverage]=6%
[Chain D UniRef90 accession]=UniRef90_Q9R0G6
[Chain D UniRef90 boundaries]=28-71
[Chain E name]=Cartilage oligomeric matrix protein
[Chain E source organism]=Mus musculus
[Chain E UniProt accession]=Q9R0G6
[Chain E UniProt boundaries]=27-71
[Chain E UniProt coverage]=6%
[Chain E UniRef90 accession]=UniRef90_Q9R0G6
[Chain E UniRef90 boundaries]=28-71
[Related structures]=3v2n,3v2p,3v2q,3v2r

[Entry]
[Accession]=MF2110006
[Name]=Leucine zipper domain of the c-Jun homodimer
[Source organism]=Serinus canaria
[Assembly]=Homodimer
[Total number of proteins]=2
[Number of unique proteins]=1
[Class]=Coils and zippers
[Subclass]=Leucine zipper (dimeric)
[PDB ID]=1jun
[PDB chain IDs]=AB
[PDB note]=No modifications of the original PDB file. Chain identifiers are identical with the PDB's identifiers.
[PDB experimental technique]=NMR
[Evidence global]=The subunits in the structure are bound via coiled coil interactions (PMID:8662824). Coiled coils are highly versatile folding units (PMID:11166216), where the formation of the structure and the interaction between subunits is almost ubiquitously linked. This cooperative nature of binding and folding that results in a two-step process has been demonstrated for coiled coils with varying oligomeric state from dimers (PMID:9811815) and trimers (PMID:10933510) up to heptamers (PMID:17030805). While the interaction and folding are linked, in certain cases there can be significant residual structure before association (PMID:8401212). However, these residual structural elements usually encompass 1-2 turns of helices that serve as a 'nucleation site' driving interaction and helix formation (zipping up) (PMID:17438295), thus even in these cases monomeric coiled coil subunits cannot be considered to have a stable structure. Leucine zippers, phenylalanine zippers and alanine zippers are subclasses of coiled coils where the hydrophobic interactions between subunits are predominantly formed by leucine, phenylalanine or alanine residues, respectively.
[Chain A name]=Transcription factor AP-1
[Chain A source organism]=Serinus canaria
[Chain A UniProt accession]=P54864
[Chain A UniProt boundaries]=259-298
[Chain A UniProt coverage]=12.7%
[Chain A UniRef90 accession]=UniRef90_P18870
[Chain A UniRef90 boundaries]=259-298
[Chain B name]=Transcription factor AP-1
[Chain B source organism]=Serinus canaria
[Chain B UniProt accession]=P54864
[Chain B UniProt boundaries]=259-298
[Chain B UniProt coverage]=12.7%
[Chain B UniRef90 accession]=UniRef90_P18870
[Chain B UniRef90 boundaries]=259-298
[Related structures]=1fos,1jnm,1s9k,1t2k,5t01

[Entry]
[Accession]=MF2110007
[Name]=Delta sleep-inducing peptide immunoreactive peptide A homolog
[Source organism]=Sus scrofa
[Assembly]=Homodimer
[Total number of proteins]=2
[Number of unique proteins]=1
[Class]=Coils and zippers
[Subclass]=Leucine zipper (dimeric)
[PDB ID]=1dip
[PDB chain IDs]=AB
[PDB note]=No modifications of the original PDB file. Chain identifiers are identical with the PDB's identifiers.
[PDB experimental technique]=NMR
[Evidence global]=The subunits in the structure are bound via coiled coil interactions (PMID:9388238). Coiled coils are highly versatile folding units (PMID:11166216), where the formation of the structure and the interaction between subunits is almost ubiquitously linked. This cooperative nature of binding and folding that results in a two-step process has been demonstrated for coiled coils with varying oligomeric state from dimers (PMID:9811815) and trimers (PMID:10933510) up to heptamers (PMID:17030805). While the interaction and folding are linked, in certain cases there can be significant residual structure before association (PMID:8401212). However, these residual structural elements usually encompass 1-2 turns of helices that serve as a 'nucleation site' driving interaction and helix formation (zipping up) (PMID:17438295), thus even in these cases monomeric coiled coil subunits cannot be considered to have a stable structure. Leucine zippers, phenylalanine zippers and alanine zippers are subclasses of coiled coils where the hydrophobic interactions between subunits are predominantly formed by leucine, phenylalanine or alanine residues, respectively.
[Chain A name]=TSC22 domain family protein 3
[Chain A source organism]=Sus scrofa
[Chain A UniProt accession]=P80220
[Chain A UniProt boundaries]=1-77
[Chain A UniProt coverage]=100%
[Chain A UniRef90 accession]=UniRef90_P80220
[Chain A UniRef90 boundaries]=1-77
[Chain B name]=TSC22 domain family protein 3
[Chain B source organism]=Sus scrofa
[Chain B UniProt accession]=P80220
[Chain B UniProt boundaries]=1-77
[Chain B UniProt coverage]=100%
[Chain B UniRef90 accession]=UniRef90_P80220
[Chain B UniRef90 boundaries]=1-77

[Entry]
[Accession]=MF2110008
[Name]=VBP leucine zipper
[Source organism]=Gallus gallus
[Assembly]=Homodimer
[Total number of proteins]=2
[Number of unique proteins]=1
[Class]=Coils and zippers
[Subclass]=Leucine zipper (dimeric)
[PDB ID]=4u5t
[PDB chain IDs]=AB
[PDB note]=No modifications of the original PDB file. Chain identifiers are identical with the PDB's identifiers.
[PDB experimental technique]=X-ray
[PDB resolution]=3.30
[Evidence global]=The subunits in the structure are bound via coiled coil interactions (PMID:22851716). Coiled coils are highly versatile folding units (PMID:11166216), where the formation of the structure and the interaction between subunits is almost ubiquitously linked. This cooperative nature of binding and folding that results in a two-step process has been demonstrated for coiled coils with varying oligomeric state from dimers (PMID:9811815) and trimers (PMID:10933510) up to heptamers (PMID:17030805). While the interaction and folding are linked, in certain cases there can be significant residual structure before association (PMID:8401212). However, these residual structural elements usually encompass 1-2 turns of helices that serve as a 'nucleation site' driving interaction and helix formation (zipping up) (PMID:17438295), thus even in these cases monomeric coiled coil subunits cannot be considered to have a stable structure. Leucine zippers, phenylalanine zippers and alanine zippers are subclasses of coiled coils where the hydrophobic interactions between subunits are predominantly formed by leucine, phenylalanine or alanine residues, respectively.
[Evidence chain A]=A close homologue sharing the same Pfam domain (PF07716.12) has been experimentally characterized as disordered in DisProt entry DP00083.
[Evidence chain B]=A close homologue sharing the same Pfam domain (PF07716.12) has been experimentally characterized as disordered in DisProt entry DP00083.
[Chain A name]=Transcription factor VBP
[Chain A source organism]=Gallus gallus
[Chain A UniProt accession]=Q92172
[Chain A UniProt boundaries]=271-305
[Chain A UniProt coverage]=11%
[Chain A UniRef90 accession]=UniRef90_Q92172
[Chain A UniRef90 boundaries]=271-305
[Chain B name]=Transcription factor VBP
[Chain B source organism]=Gallus gallus
[Chain B UniProt accession]=Q92172
[Chain B UniProt boundaries]=271-305
[Chain B UniProt coverage]=11%
[Chain B UniRef90 accession]=UniRef90_Q92172
[Chain B UniRef90 boundaries]=271-305

[Entry]
[Accession]=MF2100004
[Name]=SH2B adapter protein 2 dimerization domain
[Source organism]=Homo sapiens
[Assembly]=Homodimer
[Total number of proteins]=2
[Number of unique proteins]=1
[Class]=Coils and zippers
[Subclass]=Phenylalanine zipper (dimeric, forming a 4-helix bundle)
[PDB ID]=1q2h
[PDB chain IDs]=AB
[PDB note]=Chain C was removed as chains A and B represent the biologically relevant dimer.
[PDB experimental technique]=X-ray
[PDB resolution]=1.70
[Evidence global]=The subunits in the structure are bound via coiled coil interactions (PMID:15378031). Coiled coils are highly versatile folding units (PMID:11166216), where the formation of the structure and the interaction between subunits is almost ubiquitously linked. This cooperative nature of binding and folding that results in a two-step process has been demonstrated for coiled coils with varying oligomeric state from dimers (PMID:9811815) and trimers (PMID:10933510) up to heptamers (PMID:17030805). While the interaction and folding are linked, in certain cases there can be significant residual structure before association (PMID:8401212). However, these residual structural elements usually encompass 1-2 turns of helices that serve as a 'nucleation site' driving interaction and helix formation (zipping up) (PMID:17438295), thus even in these cases monomeric coiled coil subunits cannot be considered to have a stable structure. Leucine zippers, phenylalanine zippers and alanine zippers are subclasses of coiled coils where the hydrophobic interactions between subunits are predominantly formed by leucine, phenylalanine or alanine residues, respectively.
[Chain A name]=SH2B adapter protein 2
[Chain A source organism]=Homo sapiens
[Chain A UniProt accession]=O14492
[Chain A UniProt boundaries]=17-85
[Chain A UniProt coverage]=10.9%
[Chain A UniRef90 accession]=UniRef90_O14492
[Chain A UniRef90 boundaries]=20-85
[Chain B name]=SH2B adapter protein 2
[Chain B source organism]=Homo sapiens
[Chain B UniProt accession]=O14492
[Chain B UniProt boundaries]=17-85
[Chain B UniProt coverage]=10.9%
[Chain B UniRef90 accession]=UniRef90_O14492
[Chain B UniRef90 boundaries]=20-85

[Entry]
[Accession]=MF2202001
[Name]=GTPase binding domain of neural Wiskott-Aldrich syndrome protein in complex with E. coli EspF(U)
[Source organism]=Homo sapiens / Escherichia coli O157:H7
[Assembly]=Heterodimer
[Total number of proteins]=2
[Number of unique proteins]=2
[Class]=Other
[Subclass]=Other
[PDB ID]=2lnh
[PDB chain IDs]=AC
[PDB note]=Chain B was removed as it is ordered and does not directly contribute to the interaction between chains A and C. Chain C was truncated to exclude the region in contact with chain B.
[PDB experimental technique]=NMR
[Evidence chain A]=A close homologue sharing the same Pfam domain (PF00786.25) has been experimentally characterized as disordered in DisProt entry DP00215 and IDEAL entry IID00269.
[Evidence chain C]=The 221-314 region described in IDEAL entry IID90008 covers 97.9% of the sequence present in the structure. The interacting region has also been shown to be disordered in the structure's source publication (PMID:22921828).
[Chain A name]=Neural Wiskott-Aldrich syndrome protein
[Chain A source organism]=Homo sapiens
[Chain A UniProt accession]=O00401
[Chain A UniProt boundaries]=206-270
[Chain A UniProt coverage]=12.9%
[Chain A UniRef90 accession]=UniRef90_O00401
[Chain A UniRef90 boundaries]=207-270
[Chain C name]=Secreted effector protein EspF(U)
[Chain C source organism]=Escherichia coli O157:H7
[Chain C UniProt accession]=P0DJ89
[Chain C UniProt boundaries]=220-267
[Chain C UniProt coverage]=14.2%
[Chain C UniRef90 accession]=UniRef90_P0DJ88
[Chain C UniRef90 boundaries]=221-267

[Entry]
[Accession]=MF2220001
[Name]=CesA-EspA complex
[Source organism]=Escherichia coli
[Assembly]=Heterodimer
[Total number of proteins]=2
[Number of unique proteins]=2
[Class]=Coils and zippers
[Subclass]=Coiled coil (dimeric, forming a 4-helix bundle)
[PDB ID]=1xou
[PDB chain IDs]=AB
[PDB note]=No modifications of the original PDB file. Chain identifiers are identical with the PDB's identifiers.
[PDB experimental technique]=X-ray
[PDB resolution]=2.80
[Evidence global]=The subunits in the structure are bound via coiled coil interactions (PMID:15619638). Coiled coils are highly versatile folding units (PMID:11166216), where the formation of the structure and the interaction between subunits is almost ubiquitously linked. This cooperative nature of binding and folding that results in a two-step process has been demonstrated for coiled coils with varying oligomeric state from dimers (PMID:9811815) and trimers (PMID:10933510) up to heptamers (PMID:17030805). While the interaction and folding are linked, in certain cases there can be significant residual structure before association (PMID:8401212). However, these residual structural elements usually encompass 1-2 turns of helices that serve as a 'nucleation site' driving interaction and helix formation (zipping up) (PMID:17438295), thus even in these cases monomeric coiled coil subunits cannot be considered to have a stable structure.
[Chain A name]=EspA
[Chain A source organism]=Escherichia coli
[Chain A UniProt accession]=Q47184
[Chain A UniProt boundaries]=1-192
[Chain A UniProt coverage]=100%
[Chain A UniRef90 accession]=UniRef90_Q47184
[Chain A UniRef90 boundaries]=1-192
[Chain B name]=L0052
[Chain B source organism]=Escherichia coli
[Chain B UniProt accession]=O52124
[Chain B UniProt boundaries]=1-95
[Chain B UniProt coverage]=88.8%
[Chain B UniRef90 accession]=UniRef90_O52124
[Chain B UniRef90 boundaries]=1-95

[Entry]
[Accession]=MF2120012
[Name]=Cell division factor ZapA (mutant)
[Source organism]=Geobacillus kaustophilus
[Assembly]=Homodimer
[Total number of proteins]=2
[Number of unique proteins]=1
[Class]=Coils and zippers
[Subclass]=Coiled coil (dimeric)
[PDB ID]=2mmv
[PDB chain IDs]=AB
[PDB note]=No modifications of the original PDB file. Chain identifiers are identical with the PDB's identifiers.
[PDB experimental technique]=NMR
[Evidence global]=The subunits in the structure are bound via coiled coil interactions. Coiled coils are highly versatile folding units (PMID:11166216), where the formation of the structure and the interaction between subunits is almost ubiquitously linked. This cooperative nature of binding and folding that results in a two-step process has been demonstrated for coiled coils with varying oligomeric state from dimers (PMID:9811815) and trimers (PMID:10933510) up to heptamers (PMID:17030805). While the interaction and folding are linked, in certain cases there can be significant residual structure before association (PMID:8401212). However, these residual structural elements usually encompass 1-2 turns of helices that serve as a 'nucleation site' driving interaction and helix formation (zipping up) (PMID:17438295), thus even in these cases monomeric coiled coil subunits cannot be considered to have a stable structure.
[Chain A name]=Cell division protein ZapA
[Chain A source organism]=Geobacillus kaustophilus
[Chain A UniProt accession]=Q5KWF5
[Chain A UniProt boundaries]=1-83
[Chain A UniProt coverage]=91.2%
[Chain A UniRef90 accession]=UniRef90_Q5KWF5
[Chain A UniRef90 boundaries]=1-83
[Chain B name]=Cell division protein ZapA
[Chain B source organism]=Geobacillus kaustophilus
[Chain B UniProt accession]=Q5KWF5
[Chain B UniProt boundaries]=1-83
[Chain B UniProt coverage]=91.2%
[Chain B UniRef90 accession]=UniRef90_Q5KWF5
[Chain B UniRef90 boundaries]=1-83

[Entry]
[Accession]=MF2120013
[Name]=5-hydroxyisourate hydrolase (Brucella melitensis)
[Source organism]=Brucella melitensis biotype 1
[Assembly]=Homodimer
[Total number of proteins]=2
[Number of unique proteins]=1
[Class]=Transthyretin-like folds
[Subclass]=HIUase
[PDB ID]=4q14
[PDB chain IDs]=AB
[PDB note]=No modifications of the original PDB file. Chain identifiers are identical with the PDB's identifiers.
[PDB experimental technique]=X-ray
[PDB resolution]=1.70
[Evidence global]=The protein belongs to the 5-hydroxyisourate hydrolase (HIUase)/transthyretin protein family. Accordingly, the complex adopts a transthyterin-like fold (based on Pfam entry PF00576.18). Transthyretin was shown in calorimetrics experiments to follow two-state folding/binding kinetics with the emergence of structure being linked to oligomerization (PMID:11152276).
[Chain A name]=5-hydroxyisourate hydrolase
[Chain A source organism]=Brucella melitensis biotype 1
[Chain A UniProt accession]=Q8YFU1
[Chain A UniProt boundaries]=1-118
[Chain A UniProt coverage]=100%
[Chain A UniRef90 accession]=UniRef90_Q8YFU1
[Chain A UniRef90 boundaries]=1-118
[Chain B name]=5-hydroxyisourate hydrolase
[Chain B source organism]=Brucella melitensis biotype 1
[Chain B UniProt accession]=Q8YFU1
[Chain B UniProt boundaries]=1-118
[Chain B UniProt coverage]=100%
[Chain B UniRef90 accession]=UniRef90_Q8YFU1
[Chain B UniRef90 boundaries]=1-118

[Entry]
[Accession]=MF4120002
[Name]=5-hydroxyisourate hydrolase (Salmonella dublin)
[Source organism]=Salmonella typhi
[Assembly]=Homotetramer
[Total number of proteins]=4
[Number of unique proteins]=1
[Class]=Transthyretin-like folds
[Subclass]=HIUase
[PDB ID]=2gpz
[PDB chain IDs]=ABCD
[PDB note]=Chains C and D were generated from chains A and B respectively, using the biomatrices described in the original PDB file.
[PDB experimental technique]=X-ray
[PDB resolution]=2.50
[Evidence global]=The protein belongs to the 5-hydroxyisourate hydrolase (HIUase)/transthyretin protein family. Accordingly, the complex adopts a transthyterin-like fold (based on Pfam entry PF00576.18 and the publication PMID:16787778). Transthyretin was shown in calorimetrics experiments to follow two-state folding/binding kinetics with the emergence of structure being linked to oligomerization (PMID:11152276).
[Chain A name]=5-hydroxyisourate hydrolase
[Chain A source organism]=Salmonella typhi
[Chain A UniProt accession]=Q8Z7Q6
[Chain A UniProt boundaries]=27-136
[Chain A UniProt coverage]=80.9%
[Chain A UniRef90 accession]=UniRef90_Q4VYA5
[Chain A UniRef90 boundaries]=27-136
[Chain B name]=5-hydroxyisourate hydrolase
[Chain B source organism]=Salmonella typhi
[Chain B UniProt accession]=Q8Z7Q6
[Chain B UniProt boundaries]=27-136
[Chain B UniProt coverage]=80.9%
[Chain B UniRef90 accession]=UniRef90_Q4VYA5
[Chain B UniRef90 boundaries]=27-136
[Chain C name]=5-hydroxyisourate hydrolase
[Chain C source organism]=Salmonella typhi
[Chain C UniProt accession]=Q8Z7Q6
[Chain C UniProt boundaries]=27-136
[Chain C UniProt coverage]=80.9%
[Chain C UniRef90 accession]=UniRef90_Q4VYA5
[Chain C UniRef90 boundaries]=27-136
[Chain D name]=5-hydroxyisourate hydrolase
[Chain D source organism]=Salmonella typhi
[Chain D UniProt accession]=Q8Z7Q6
[Chain D UniProt boundaries]=27-136
[Chain D UniProt coverage]=80.9%
[Chain D UniRef90 accession]=UniRef90_Q4VYA5
[Chain D UniRef90 boundaries]=27-136

[Entry]
[Accession]=MF4120003
[Name]=5-hydroxyisourate hydrolase (Bacillus subtilis)
[Source organism]=Bacillus subtilis
[Assembly]=Homotetramer
[Total number of proteins]=4
[Number of unique proteins]=1
[Class]=Transthyretin-like folds
[Subclass]=HIUase
[PDB ID]=2h0e
[PDB chain IDs]=ACDE
[PDB note]=Chains C, D and E were generated from chain A using the biomatrices described in the original PDB file. Chain B was removed as chains A, C, D and E represent the biologically relevant tetramer.
[PDB experimental technique]=X-ray
[PDB resolution]=2.20
[Evidence global]=The protein belongs to the 5-hydroxyisourate hydrolase (HIUase)/transthyretin protein family. Accordingly, the complex adopts a transthyterin-like fold (based on Pfam entry PF00576.18 and the publication PMID:16782815). Transthyretin was shown in calorimetrics experiments to follow two-state folding/binding kinetics with the emergence of structure being linked to oligomerization (PMID:11152276).
[Chain A name]=5-hydroxyisourate hydrolase
[Chain A source organism]=Bacillus subtilis
[Chain A UniProt accession]=O32142
[Chain A UniProt boundaries]=1-114
[Chain A UniProt coverage]=100%
[Chain A UniRef90 accession]=UniRef90_O32142
[Chain A UniRef90 boundaries]=1-114
[Chain C name]=5-hydroxyisourate hydrolase
[Chain C source organism]=Bacillus subtilis
[Chain C UniProt accession]=O32142
[Chain C UniProt boundaries]=1-114
[Chain C UniProt coverage]=100%
[Chain C UniRef90 accession]=UniRef90_O32142
[Chain C UniRef90 boundaries]=1-114
[Chain D name]=5-hydroxyisourate hydrolase
[Chain D source organism]=Bacillus subtilis
[Chain D UniProt accession]=O32142
[Chain D UniProt boundaries]=1-114
[Chain D UniProt coverage]=100%
[Chain D UniRef90 accession]=UniRef90_O32142
[Chain D UniRef90 boundaries]=1-114
[Chain E name]=5-hydroxyisourate hydrolase
[Chain E source organism]=Bacillus subtilis
[Chain E UniProt accession]=O32142
[Chain E UniProt boundaries]=1-114
[Chain E UniProt coverage]=100%
[Chain E UniRef90 accession]=UniRef90_O32142
[Chain E UniRef90 boundaries]=1-114
[Related structures]=2h0f,2h0j

[Entry]
[Accession]=MF4120004
[Name]=5-hydroxyisourate hydrolase (Klebsiella pneumoniae)
[Source organism]=Klebsiella pneumoniae subsp. pneumoniae
[Assembly]=Homotetramer
[Total number of proteins]=4
[Number of unique proteins]=1
[Class]=Transthyretin-like folds
[Subclass]=HIUase
[PDB ID]=3qva
[PDB chain IDs]=ABCD
[PDB note]=No modifications of the original PDB file. Chain identifiers are identical with the PDB's identifiers.
[PDB experimental technique]=X-ray
[PDB resolution]=1.75
[Evidence global]=The protein belongs to the 5-hydroxyisourate hydrolase (HIUase)/transthyretin protein family. Accordingly, the complex adopts a transthyterin-like fold (based on Pfam entry PF00576.18 and the publication PMID:21795808). Transthyretin was shown in calorimetrics experiments to follow two-state folding/binding kinetics with the emergence of structure being linked to oligomerization (PMID:11152276).
[Chain A name]=Transthyretin-like protein
[Chain A source organism]=Klebsiella pneumoniae subsp. pneumoniae
[Chain A UniProt accession]=A6T926
[Chain A UniProt boundaries]=1-108
[Chain A UniProt coverage]=100%
[Chain A UniRef90 accession]=UniRef90_R4YDW2
[Chain A UniRef90 boundaries]=1-108
[Chain B name]=Transthyretin-like protein
[Chain B source organism]=Klebsiella pneumoniae subsp. pneumoniae
[Chain B UniProt accession]=A6T926
[Chain B UniProt boundaries]=1-108
[Chain B UniProt coverage]=100%
[Chain B UniRef90 accession]=UniRef90_R4YDW2
[Chain B UniRef90 boundaries]=1-108
[Chain C name]=Transthyretin-like protein
[Chain C source organism]=Klebsiella pneumoniae subsp. pneumoniae
[Chain C UniProt accession]=A6T926
[Chain C UniProt boundaries]=1-108
[Chain C UniProt coverage]=100%
[Chain C UniRef90 accession]=UniRef90_R4YDW2
[Chain C UniRef90 boundaries]=1-108
[Chain D name]=Transthyretin-like protein
[Chain D source organism]=Klebsiella pneumoniae subsp. pneumoniae
[Chain D UniProt accession]=A6T926
[Chain D UniProt boundaries]=1-108
[Chain D UniProt coverage]=100%
[Chain D UniRef90 accession]=UniRef90_R4YDW2
[Chain D UniRef90 boundaries]=1-108

[Entry]
[Accession]=MF4120005
[Name]=5-hydroxyisourate hydrolase (Escherichia coli)
[Source organism]=Escherichia coli
[Assembly]=Homotetramer
[Total number of proteins]=4
[Number of unique proteins]=1
[Class]=Transthyretin-like folds
[Subclass]=HIUase
[PDB ID]=2g2n
[PDB chain IDs]=ABCD
[PDB note]=No modifications of the original PDB file. Chain identifiers are identical with the PDB's identifiers.
[PDB experimental technique]=X-ray
[PDB resolution]=1.65
[Evidence global]=The protein belongs to the 5-hydroxyisourate hydrolase (HIUase)/transthyretin protein family. Accordingly, the complex adopts a transthyterin-like fold (based on Pfam entry PF00576.18 and the publication PMID:16723258). Transthyretin was shown in calorimetrics experiments to follow two-state folding/binding kinetics with the emergence of structure being linked to oligomerization (PMID:11152276).
[Chain A name]=5-hydroxyisourate hydrolase
[Chain A source organism]=Escherichia coli
[Chain A UniProt accession]=P76341
[Chain A UniProt boundaries]=24-137
[Chain A UniProt coverage]=83.2%
[Chain A UniRef90 accession]=UniRef90_P76341
[Chain A UniRef90 boundaries]=24-137
[Chain B name]=5-hydroxyisourate hydrolase
[Chain B source organism]=Escherichia coli
[Chain B UniProt accession]=P76341
[Chain B UniProt boundaries]=24-137
[Chain B UniProt coverage]=83.2%
[Chain B UniRef90 accession]=UniRef90_P76341
[Chain B UniRef90 boundaries]=24-137
[Chain C name]=5-hydroxyisourate hydrolase
[Chain C source organism]=Escherichia coli
[Chain C UniProt accession]=P76341
[Chain C UniProt boundaries]=24-137
[Chain C UniProt coverage]=83.2%
[Chain C UniRef90 accession]=UniRef90_P76341
[Chain C UniRef90 boundaries]=24-137
[Chain D name]=5-hydroxyisourate hydrolase
[Chain D source organism]=Escherichia coli
[Chain D UniProt accession]=P76341
[Chain D UniProt boundaries]=24-137
[Chain D UniProt coverage]=83.2%
[Chain D UniRef90 accession]=UniRef90_P76341
[Chain D UniRef90 boundaries]=24-137
[Related structures]=2g2p,2igl

[Entry]
[Accession]=MF4110003
[Name]=5-hydroxyisourate hydrolase (Danio rerio)
[Source organism]=Danio rerio
[Assembly]=Homotetramer
[Total number of proteins]=4
[Number of unique proteins]=1
[Class]=Transthyretin-like folds
[Subclass]=HIUase
[PDB ID]=2h1x
[PDB chain IDs]=ABCD
[PDB note]=No modifications of the original PDB file. Chain identifiers are identical with the PDB's identifiers.
[PDB experimental technique]=X-ray
[PDB resolution]=1.98
[Evidence global]=The protein belongs to the 5-hydroxyisourate hydrolase (HIUase)/transthyretin protein family. Accordingly, the complex adopts a transthyterin-like fold (based on Pfam entry PF00576.18 and the publication PMID:16952372). Transthyretin was shown in calorimetrics experiments to follow two-state folding/binding kinetics with the emergence of structure being linked to oligomerization (PMID:11152276).
[Chain A name]=5-hydroxyisourate hydrolase
[Chain A source organism]=Danio rerio
[Chain A UniProt accession]=Q06S87
[Chain A UniProt boundaries]=20-138
[Chain A UniProt coverage]=86.2%
[Chain A UniRef90 accession]=UniRef90_Q06S87
[Chain A UniRef90 boundaries]=20-138
[Chain B name]=5-hydroxyisourate hydrolase
[Chain B source organism]=Danio rerio
[Chain B UniProt accession]=Q06S87
[Chain B UniProt boundaries]=20-138
[Chain B UniProt coverage]=86.2%
[Chain B UniRef90 accession]=UniRef90_Q06S87
[Chain B UniRef90 boundaries]=20-138
[Chain C name]=5-hydroxyisourate hydrolase
[Chain C source organism]=Danio rerio
[Chain C UniProt accession]=Q06S87
[Chain C UniProt boundaries]=20-138
[Chain C UniProt coverage]=86.2%
[Chain C UniRef90 accession]=UniRef90_Q06S87
[Chain C UniRef90 boundaries]=20-138
[Chain D name]=5-hydroxyisourate hydrolase
[Chain D source organism]=Danio rerio
[Chain D UniProt accession]=Q06S87
[Chain D UniProt boundaries]=20-138
[Chain D UniProt coverage]=86.2%
[Chain D UniRef90 accession]=UniRef90_Q06S87
[Chain D UniRef90 boundaries]=20-138
[Related structures]=2h6u,3iwu,3iwv,3q1e

[Entry]
[Accession]=MF4110004
[Name]=Oligomerization region of the general control protein GCN4 
[Source organism]=Saccharomyces cerevisiae
[Assembly]=Homotetramer
[Total number of proteins]=4
[Number of unique proteins]=1
[Class]=Coils and zippers
[Subclass]=Leucine zipper (tetrameric)
[PDB ID]=2b1f
[PDB chain IDs]=ABCD
[PDB note]=No modifications of the original PDB file. Chain identifiers are identical with the PDB's identifiers.
[PDB experimental technique]=X-ray
[PDB resolution]=1.50
[Evidence global]=The subunits in the structure are bound via coiled coil interactions. Coiled coils are highly versatile folding units (PMID:11166216), where the formation of the structure and the interaction between subunits is almost ubiquitously linked. This cooperative nature of binding and folding that results in a two-step process has been demonstrated for coiled coils with varying oligomeric state from dimers (PMID:9811815) and trimers (PMID:10933510) up to heptamers (PMID:17030805). While the interaction and folding are linked, in certain cases there can be significant residual structure before association (PMID:8401212). However, these residual structural elements usually encompass 1-2 turns of helices that serve as a 'nucleation site' driving interaction and helix formation (zipping up) (PMID:17438295), thus even in these cases monomeric coiled coil subunits cannot be considered to have a stable structure. Leucine zippers, phenylalanine zippers and alanine zippers are subclasses of coiled coils where the hydrophobic interactions between subunits are predominantly formed by leucine, phenylalanine or alanine residues, respectively. In the specific case of GCN4 refolding studies have explicitly shown that structure formation and dimerization happens at the same time (PMID:7548036)
[Evidence chain A]=The 225-281 region described in DisProt entry DP00083 covers 100% of the sequence present in the structure.
[Evidence chain B]=The 225-281 region described in DisProt entry DP00083 covers 100% of the sequence present in the structure.
[Evidence chain C]=The 225-281 region described in DisProt entry DP00083 covers 100% of the sequence present in the structure.
[Evidence chain D]=The 225-281 region described in DisProt entry DP00083 covers 100% of the sequence present in the structure.
[Chain A name]=General control protein GCN4
[Chain A source organism]=Saccharomyces cerevisiae
[Chain A UniProt accession]=P03069
[Chain A UniProt boundaries]=249-281
[Chain A UniProt coverage]=11.7%
[Chain A UniRef90 accession]=UniRef90_P03069
[Chain A UniRef90 boundaries]=249-281
[Chain B name]=General control protein GCN4
[Chain B source organism]=Saccharomyces cerevisiae
[Chain B UniProt accession]=P03069
[Chain B UniProt boundaries]=249-281
[Chain B UniProt coverage]=11.7%
[Chain B UniRef90 accession]=UniRef90_P03069
[Chain B UniRef90 boundaries]=249-281
[Chain C name]=General control protein GCN4
[Chain C source organism]=Saccharomyces cerevisiae
[Chain C UniProt accession]=P03069
[Chain C UniProt boundaries]=249-281
[Chain C UniProt coverage]=11.7%
[Chain C UniRef90 accession]=UniRef90_P03069
[Chain C UniRef90 boundaries]=249-281
[Chain D name]=General control protein GCN4
[Chain D source organism]=Saccharomyces cerevisiae
[Chain D UniProt accession]=P03069
[Chain D UniProt boundaries]=249-281
[Chain D UniProt coverage]=11.7%
[Chain D UniRef90 accession]=UniRef90_P03069
[Chain D UniRef90 boundaries]=249-281
[Related structures]=1ce9,1dgc,1env,1fav,1fmh,1gcl,1gcm,1gk6,1gzl,1ihq,1ij0,1ij1,1ij2,1ij3,1kql,1ld4,1llm,1piq,1rb4,1rb5,1rb6,1swi,1tmz,1unt,1unu,1unv,1unw,1unx,1uny,1unz,1uo0,1uo1,1uo2,1uo3,1uo4,1uo5,1w5g,1w5h,1w5i,1w5j,1w5k,1w5l,1ysa,1zii,1zij,1zik,1zil,1zim,1zta,2ahp,2b22,2bni,2cce,2ccf,2ccn,2dgc,2g9j,2hy6,2ipz,2k8x,2n9b,2nrn,2o7h,2ovn,2vky,2vnl,2wg5,2wg6,2wpy,2wpz,2wq0,2wq1,2wq2,2wq3,2yny,2ynz,2yo0,2yo1,2yo2,2yo3,2zta,3azd,3ck4,3crp,3g9r,3gjp,3i1g,3i5c,3k7z,3p8m,3zmf,4c46,4dmd,4g2k,4hu5,4hu6,4niz,4nj0,4nj1,4nj2,4owi,4tl1,5apq,5aps,5apt,5apu,5apv,5apw,5apx,5apy,5iew,5iir,5iiv

[Entry]
[Accession]=MF2120014
[Name]=Regulatory protein Rop
[Source organism]=Escherichia coli
[Assembly]=Homodimer
[Total number of proteins]=2
[Number of unique proteins]=1
[Class]=Coils and zippers
[Subclass]=Coiled coil (dimeric, forming a 4-helix bundle)
[PDB ID]=2ijk
[PDB chain IDs]=AB
[PDB note]=No modifications of the original PDB file. Chain identifiers are identical with the PDB's identifiers.
[PDB experimental technique]=X-ray
[PDB resolution]=1.55
[Evidence global]=Detailed thermodynamic and spectroscopic studies were carried out on the ColE1-ROP protein in order to establish a quantitative basis for the contribution of noncovalent interactions to the stability of four-helix-bundle proteins. The energetics of both heat- and GdnHCl-induced denaturation were measured by differential scanning microcalorimetry (DSC) and/or by following the change in circular dichroism in the far-UV range. No intermediate species could be detected during thermal unfolding of the dimer in the absence of GdnHCl. Under these conditions ROP unfolding exhibits a strict two-state behavior (PMID:8471599).
[Chain A name]=Regulatory protein rop
[Chain A source organism]=Escherichia coli
[Chain A UniProt accession]=P03051
[Chain A UniProt boundaries]=1-63
[Chain A UniProt coverage]=100%
[Chain A UniRef90 accession]=UniRef90_P03051
[Chain A UniRef90 boundaries]=2-63
[Chain B name]=Regulatory protein rop
[Chain B source organism]=Escherichia coli
[Chain B UniProt accession]=P03051
[Chain B UniProt boundaries]=1-63
[Chain B UniProt coverage]=100%
[Chain B UniRef90 accession]=UniRef90_P03051
[Chain B UniRef90 boundaries]=2-63
[Related structures]=1b6q,4do2,1f4m,1f4n,2ghy,1gto,2ijh,2iji,2ijj,1qx8,1rpr,1gmg,3k79,1nkd,1rop,1rpo,1yo7

[Entry]
[Accession]=MF4100002
[Name]=Bcr-Abl oncoprotein oligomerization domain
[Source organism]=Homo sapiens
[Assembly]=Homotetramer
[Total number of proteins]=4
[Number of unique proteins]=1
[Class]=Coils and zippers
[Subclass]=Coiled coil (tetrameric)
[PDB ID]=1k1f
[PDB chain IDs]=ABCD
[PDB note]=Chains E, F, G and H were removed as chains A, B, C and D represent the biologically relevant tetramer.
[PDB experimental technique]=X-ray
[PDB resolution]=2.20
[Evidence global]=The subunits in the structure are bound via coiled coil interactions (PMID:11780146). Coiled coils are highly versatile folding units (PMID:11166216), where the formation of the structure and the interaction between subunits is almost ubiquitously linked. This cooperative nature of binding and folding that results in a two-step process has been demonstrated for coiled coils with varying oligomeric state from dimers (PMID:9811815) and trimers (PMID:10933510) up to heptamers (PMID:17030805). While the interaction and folding are linked, in certain cases there can be significant residual structure before association (PMID:8401212). However, these residual structural elements usually encompass 1-2 turns of helices that serve as a 'nucleation site' driving interaction and helix formation (zipping up) (PMID:17438295), thus even in these cases monomeric coiled coil subunits cannot be considered to have a stable structure.
[Chain A name]=Breakpoint cluster region protein
[Chain A source organism]=Homo sapiens
[Chain A UniProt accession]=P11274
[Chain A UniProt boundaries]=1-72
[Chain A UniProt coverage]=5.7%
[Chain A UniRef90 accession]=UniRef90_P11274
[Chain A UniRef90 boundaries]=1-72
[Chain B name]=Breakpoint cluster region protein
[Chain B source organism]=Homo sapiens
[Chain B UniProt accession]=P11274
[Chain B UniProt boundaries]=1-72
[Chain B UniProt coverage]=5.7%
[Chain B UniRef90 accession]=UniRef90_P11274
[Chain B UniRef90 boundaries]=1-72
[Chain C name]=Breakpoint cluster region protein
[Chain C source organism]=Homo sapiens
[Chain C UniProt accession]=P11274
[Chain C UniProt boundaries]=1-72
[Chain C UniProt coverage]=5.7%
[Chain C UniRef90 accession]=UniRef90_P11274
[Chain C UniRef90 boundaries]=1-72
[Chain D name]=Breakpoint cluster region protein
[Chain D source organism]=Homo sapiens
[Chain D UniProt accession]=P11274
[Chain D UniProt boundaries]=1-72
[Chain D UniProt coverage]=5.7%
[Chain D UniRef90 accession]=UniRef90_P11274
[Chain D UniRef90 boundaries]=1-72

[Entry]
[Accession]=MF2120015
[Name]=Antitoxin phd dimer (Escherichia coli)
[Source organism]=Escherichia coli
[Assembly]=Homodimer
[Total number of proteins]=2
[Number of unique proteins]=1
[Class]=Other
[Subclass]=Phd antitoxin
[PDB ID]=3hry
[PDB chain IDs]=AB
[PDB note]=Chain C was removed as chains A and B represent the biologically relevant dimer.
[PDB experimental technique]=X-ray
[PDB resolution]=2.25
[Evidence global]=The dimerization of the prevents host death (phd) antitoxin from Escherichia virus P1 has been shown with differential scanning calorimetry to fit well to a two-state model consisting of a dimer unfolding into monomer species (PMID:20603017).
[Evidence chain A]=The 1-73 region described in DisProt entry DP00288 covers 100% of the sequence present in the structure.
[Evidence chain B]=The 1-73 region described in DisProt entry DP00288 covers 100% of the sequence present in the structure.
[Chain A name]=Phd protein
[Chain A source organism]=Escherichia coli
[Chain A UniProt accession]=Q79A04
[Chain A UniProt boundaries]=1-73
[Chain A UniProt coverage]=100%
[Chain A UniRef90 accession]=UniRef90_Q06253
[Chain A UniRef90 boundaries]=1-73
[Chain B name]=Phd protein
[Chain B source organism]=Escherichia coli
[Chain B UniProt accession]=Q79A04
[Chain B UniProt boundaries]=1-73
[Chain B UniProt coverage]=100%
[Chain B UniRef90 accession]=UniRef90_Q06253
[Chain B UniRef90 boundaries]=1-73

[Entry]
[Accession]=MF4120006
[Name]=Cell division factor ZapA (Pseudomonas aeruginosa)
[Source organism]=Pseudomonas aeruginosa
[Assembly]=Homotetramer
[Total number of proteins]=4
[Number of unique proteins]=1
[Class]=Coils and zippers
[Subclass]=Coiled coil (tetrameric)
[PDB ID]=1t3u
[PDB chain IDs]=ABCD
[PDB note]=No modifications of the original PDB file. Chain identifiers are identical with the PDB's identifiers.
[PDB experimental technique]=X-ray
[PDB resolution]=2.50
[Evidence global]=The subunits in the structure are bound via coiled coil interactions as evidenced by the presence of a ZapA domain (Pfam PF05164.10, PMID:25002581). Coiled coils are highly versatile folding units (PMID:11166216), where the formation of the structure and the interaction between subunits is almost ubiquitously linked. This cooperative nature of binding and folding that results in a two-step process has been demonstrated for coiled coils with varying oligomeric state from dimers (PMID:9811815) and trimers (PMID:10933510) up to heptamers (PMID:17030805). While the interaction and folding are linked, in certain cases there can be significant residual structure before association (PMID:8401212). However, these residual structural elements usually encompass 1-2 turns of helices that serve as a 'nucleation site' driving interaction and helix formation (zipping up) (PMID:17438295), thus even in these cases monomeric coiled coil subunits cannot be considered to have a stable structure.
[Chain A name]=Cell division protein ZapA
[Chain A source organism]=Pseudomonas aeruginosa
[Chain A UniProt accession]=Q9HTW3
[Chain A UniProt boundaries]=1-104
[Chain A UniProt coverage]=100%
[Chain A UniRef90 accession]=UniRef90_Q9HTW3
[Chain A UniRef90 boundaries]=1-104
[Chain B name]=Cell division protein ZapA
[Chain B source organism]=Pseudomonas aeruginosa
[Chain B UniProt accession]=Q9HTW3
[Chain B UniProt boundaries]=1-104
[Chain B UniProt coverage]=100%
[Chain B UniRef90 accession]=UniRef90_Q9HTW3
[Chain B UniRef90 boundaries]=1-104
[Chain C name]=Cell division protein ZapA
[Chain C source organism]=Pseudomonas aeruginosa
[Chain C UniProt accession]=Q9HTW3
[Chain C UniProt boundaries]=1-104
[Chain C UniProt coverage]=100%
[Chain C UniRef90 accession]=UniRef90_Q9HTW3
[Chain C UniRef90 boundaries]=1-104
[Chain D name]=Cell division protein ZapA
[Chain D source organism]=Pseudomonas aeruginosa
[Chain D UniProt accession]=Q9HTW3
[Chain D UniProt boundaries]=1-104
[Chain D UniProt coverage]=100%
[Chain D UniRef90 accession]=UniRef90_Q9HTW3
[Chain D UniRef90 boundaries]=1-104
[Related structures]=1w2e

[Entry]
[Accession]=MF2120016
[Name]=Putative antitoxin phd dimer (Nitrosomonas europaea)
[Source organism]=Nitrosomonas europaea
[Assembly]=Homodimer
[Total number of proteins]=2
[Number of unique proteins]=1
[Class]=Other
[Subclass]=Phd antitoxin
[PDB ID]=2odk
[PDB chain IDs]=AB
[PDB note]=Chains C and D were removed as chains A and B represent the biologically relevant dimer.
[PDB experimental technique]=X-ray
[PDB resolution]=1.40
[Evidence global]=The dimerization of the prevents host death (phd) antitoxin from Escherichia virus P1 has been shown with differential scanning calorimetry to fit well to a two-state model consisting of a dimer unfolding into monomer species (PMID:20603017).
[Evidence chain A]=A homologue sharing the same Pfam domain (PF02604.16) has been experimentally characterized as disordered in DisProt entry DP00288.
[Evidence chain B]=A homologue sharing the same Pfam domain (PF02604.16) has been experimentally characterized as disordered in DisProt entry DP00288.
[Chain A name]=Uncharacterized protein
[Chain A source organism]=Nitrosomonas europaea
[Chain A UniProt accession]=Q82T22
[Chain A UniProt boundaries]=1-85
[Chain A UniProt coverage]=100%
[Chain A UniRef90 accession]=UniRef90_Q82T22
[Chain A UniRef90 boundaries]=1-85
[Chain B name]=Uncharacterized protein
[Chain B source organism]=Nitrosomonas europaea
[Chain B UniProt accession]=Q82T22
[Chain B UniProt boundaries]=1-85
[Chain B UniProt coverage]=100%
[Chain B UniRef90 accession]=UniRef90_Q82T22
[Chain B UniRef90 boundaries]=1-85

[Entry]
[Accession]=MF4140002
[Name]=Tetramerization domain of the Mnt repressor
[Source organism]=Enterobacteria phage P22
[Assembly]=Homotetramer
[Total number of proteins]=4
[Number of unique proteins]=1
[Class]=Coils and zippers
[Subclass]=Coiled coil (tetrameric)
[PDB ID]=1qey
[PDB chain IDs]=ABCD
[PDB note]=No modifications of the original PDB file. Chain identifiers are identical with the PDB's identifiers.
[PDB experimental technique]=NMR
[Evidence global]=The subunits in the structure are bound via coiled coil interactions (PMID:10426954). Coiled coils are highly versatile folding units (PMID:11166216), where the formation of the structure and the interaction between subunits is almost ubiquitously linked. This cooperative nature of binding and folding that results in a two-step process has been demonstrated for coiled coils with varying oligomeric state from dimers (PMID:9811815) and trimers (PMID:10933510) up to heptamers (PMID:17030805). While the interaction and folding are linked, in certain cases there can be significant residual structure before association (PMID:8401212). However, these residual structural elements usually encompass 1-2 turns of helices that serve as a 'nucleation site' driving interaction and helix formation (zipping up) (PMID:17438295), thus even in these cases monomeric coiled coil subunits cannot be considered to have a stable structure.
[Chain A name]=Regulatory protein mnt
[Chain A source organism]=Enterobacteria phage P22
[Chain A UniProt accession]=P03049
[Chain A UniProt boundaries]=53-83
[Chain A UniProt coverage]=37.3%
[Chain A UniRef90 accession]=UniRef90_P03049
[Chain A UniRef90 boundaries]=53-83
[Chain B name]=Regulatory protein mnt
[Chain B source organism]=Enterobacteria phage P22
[Chain B UniProt accession]=P03049
[Chain B UniProt boundaries]=53-83
[Chain B UniProt coverage]=37.3%
[Chain B UniRef90 accession]=UniRef90_P03049
[Chain B UniRef90 boundaries]=53-83
[Chain C name]=Regulatory protein mnt
[Chain C source organism]=Enterobacteria phage P22
[Chain C UniProt accession]=P03049
[Chain C UniProt boundaries]=53-83
[Chain C UniProt coverage]=37.3%
[Chain C UniRef90 accession]=UniRef90_P03049
[Chain C UniRef90 boundaries]=53-83
[Chain D name]=Regulatory protein mnt
[Chain D source organism]=Enterobacteria phage P22
[Chain D UniProt accession]=P03049
[Chain D UniProt boundaries]=53-83
[Chain D UniProt coverage]=37.3%
[Chain D UniRef90 accession]=UniRef90_P03049
[Chain D UniRef90 boundaries]=53-83

[Entry]
[Accession]=MF2100005
[Name]=ING4 dimerization domain
[Source organism]=Homo sapiens
[Assembly]=Homodimer
[Total number of proteins]=2
[Number of unique proteins]=1
[Class]=Coils and zippers
[Subclass]=Coiled coil (dimeric, forming a 4-helix bundle)
[PDB ID]=4afl
[PDB chain IDs]=AC
[PDB note]=Chains B, D, E and F were removed as chains A and C represent the biologically relevant dimer.
[PDB experimental technique]=X-ray
[PDB resolution]=2.28
[Evidence global]=The subunits in the structure are bound via coiled coil interactions (PMID:22334692). Coiled coils are highly versatile folding units (PMID:11166216), where the formation of the structure and the interaction between subunits is almost ubiquitously linked. This cooperative nature of binding and folding that results in a two-step process has been demonstrated for coiled coils with varying oligomeric state from dimers (PMID:9811815) and trimers (PMID:10933510) up to heptamers (PMID:17030805). While the interaction and folding are linked, in certain cases there can be significant residual structure before association (PMID:8401212). However, these residual structural elements usually encompass 1-2 turns of helices that serve as a 'nucleation site' driving interaction and helix formation (zipping up) (PMID:17438295), thus even in these cases monomeric coiled coil subunits cannot be considered to have a stable structure.
[Chain A name]=Inhibitor of growth protein 4
[Chain A source organism]=Homo sapiens
[Chain A UniProt accession]=Q9UNL4
[Chain A UniProt boundaries]=2-105
[Chain A UniProt coverage]=41.8%
[Chain A UniRef90 accession]=UniRef90_Q9UNL4
[Chain A UniRef90 boundaries]=2-105
[Chain C name]=Inhibitor of growth protein 4
[Chain C source organism]=Homo sapiens
[Chain C UniProt accession]=Q9UNL4
[Chain C UniProt boundaries]=2-105
[Chain C UniProt coverage]=41.8%
[Chain C UniRef90 accession]=UniRef90_Q9UNL4
[Chain C UniRef90 boundaries]=2-105

[Entry]
[Accession]=MF2201005
[Name]=H2A-H2B histone dimer (human/mouse), containing histone variants macro-H2A.1 and H2B type 3-A
[Source organism]=Homo sapiens / Mus musculus
[Assembly]=Heterodimer
[Total number of proteins]=2
[Number of unique proteins]=2
[Class]=Histone-like interactions
[Subclass]=Histones
[PDB ID]=1u35
[PDB chain IDs]=CD
[PDB note]=Chains A, B, E, F, G, H, I and J have been removed to highlight the basic interaction that forms the histone dimer composed of chains C and D.
[PDB experimental technique]=X-ray
[PDB resolution]=3.00
[Evidence global]=Histones form parts of the nucleosome particle by dimerization and subsequent multimerization (PMID:1946434). The dimer contains both histone subunits in a highly intertwined conformation reflecting the possible domain-swapped origins of the structure (PMID:17391511). Accordingly, this dimerization has been experimentally characterized to be coupled to the structure formation of both interacting partners (PMID:12779337); this synergistic folding has been shown separately for H2A-H2B dimers (PMID:15588829) and H3-H4 dimers as well (PMID:15096635). Histones containing various types of monomeric subunits can exhibit varying stability and folding kinetics. E.g. in the case of H3-H4 histones, the dimerization is a complex process with the two monomers first adopting an intermediate state upon encounter and then reaching the classical histone fold through restructurization (PMID:12779337). However, independent of composition and folding kinetics, all histones appear to fold in a cooperative fashion that is coupled to binding (PMID:11669650).
[Chain C name]=Core histone macro-H2A.1
[Chain C source organism]=Homo sapiens
[Chain C UniProt accession]=O75367
[Chain C UniProt boundaries]=1-120
[Chain C UniProt coverage]=32.3%
[Chain C UniRef90 accession]=UniRef90_O75367
[Chain C UniRef90 boundaries]=1-120
[Chain D name]=Histone H2B type 3-A
[Chain D source organism]=Mus musculus
[Chain D UniProt accession]=Q9D2U9
[Chain D UniProt boundaries]=1-126
[Chain D UniProt coverage]=100%
[Chain D UniRef90 accession]=UniRef90_Q9D2U9
[Chain D UniRef90 boundaries]=1-126

[Entry]
[Accession]=MF2201006
[Name]=H2A-H2B histone dimer (human/Xenopus laevis), containing histone variants macro-H2A.1 and H2B 1.1
[Source organism]=Homo sapiens / Xenopus laevis
[Assembly]=Heterodimer
[Total number of proteins]=2
[Number of unique proteins]=2
[Class]=Histone-like interactions
[Subclass]=Histones
[PDB ID]=2f8n
[PDB chain IDs]=GH
[PDB note]=Chains A, B, D, E, F, I, J and K have been removed to highlight the basic interaction that forms the histone dimer composed of chains G and H.
[PDB experimental technique]=X-ray
[PDB resolution]=2.90
[Evidence global]=Histones form parts of the nucleosome particle by dimerization and subsequent multimerization (PMID:1946434). The dimer contains both histone subunits in a highly intertwined conformation reflecting the possible domain-swapped origins of the structure (PMID:17391511). Accordingly, this dimerization has been experimentally characterized to be coupled to the structure formation of both interacting partners (PMID:12779337); this synergistic folding has been shown separately for H2A-H2B dimers (PMID:15588829) and H3-H4 dimers as well (PMID:15096635). Histones containing various types of monomeric subunits can exhibit varying stability and folding kinetics. E.g. in the case of H3-H4 histones, the dimerization is a complex process with the two monomers first adopting an intermediate state upon encounter and then reaching the classical histone fold through restructurization (PMID:12779337). However, independent of composition and folding kinetics, all histones appear to fold in a cooperative fashion that is coupled to binding (PMID:11669650).
[Chain G name]=Core histone macro-H2A.1
[Chain G source organism]=Homo sapiens
[Chain G UniProt accession]=O75367
[Chain G UniProt boundaries]=1-120
[Chain G UniProt coverage]=32.3%
[Chain G UniRef90 accession]=UniRef90_O75367
[Chain G UniRef90 boundaries]=1-120
[Chain H name]=Histone H2B 1.1
[Chain H source organism]=Xenopus laevis
[Chain H UniProt accession]=P02281
[Chain H UniProt boundaries]=4-126
[Chain H UniProt coverage]=97.6%
[Chain H UniRef90 accession]=UniRef90_P57053
[Chain H UniRef90 boundaries]=5-126

[Entry]
[Accession]=MF2211001
[Name]=H2A-H2B histone dimer (human/Xenopus laevis), containing histone variants H2A.Z and H2B 1.1
[Source organism]=Mus musculus / Xenopus laevis
[Assembly]=Heterodimer
[Total number of proteins]=2
[Number of unique proteins]=2
[Class]=Histone-like interactions
[Subclass]=Histones
[PDB ID]=1f66
[PDB chain IDs]=CD
[PDB note]=Chains A, B, E, F, G, H, I and J have been removed to highlight the basic interaction that forms the histone dimer composed of chains C and D.
[PDB experimental technique]=X-ray
[PDB resolution]=2.60
[Evidence global]=Histones form parts of the nucleosome particle by dimerization and subsequent multimerization (PMID:1946434). The dimer contains both histone subunits in a highly intertwined conformation reflecting the possible domain-swapped origins of the structure (PMID:17391511). Accordingly, this dimerization has been experimentally characterized to be coupled to the structure formation of both interacting partners (PMID:12779337); this synergistic folding has been shown separately for H2A-H2B dimers (PMID:15588829) and H3-H4 dimers as well (PMID:15096635). Histones containing various types of monomeric subunits can exhibit varying stability and folding kinetics. E.g. in the case of H3-H4 histones, the dimerization is a complex process with the two monomers first adopting an intermediate state upon encounter and then reaching the classical histone fold through restructurization (PMID:12779337). However, independent of composition and folding kinetics, all histones appear to fold in a cooperative fashion that is coupled to binding (PMID:11669650).
[Chain C name]=Histone H2A.Z
[Chain C source organism]=Mus musculus
[Chain C UniProt accession]=P0C0S6
[Chain C UniProt boundaries]=1-128
[Chain C UniProt coverage]=100%
[Chain C UniRef90 accession]=UniRef90_P0C0S5
[Chain C UniRef90 boundaries]=1-128
[Chain D name]=Histone H2B 1.1
[Chain D source organism]=Xenopus laevis
[Chain D UniProt accession]=P02281
[Chain D UniProt boundaries]=1-126
[Chain D UniProt coverage]=100%
[Chain D UniRef90 accession]=UniRef90_P57053
[Chain D UniRef90 boundaries]=1-126

[Entry]
[Accession]=MF2200003
[Name]=H2A-H2B histone dimer (human), containing histone variants H2A.Z and H2B type 1-J
[Source organism]=Homo sapiens
[Assembly]=Heterodimer
[Total number of proteins]=2
[Number of unique proteins]=2
[Class]=Histone-like interactions
[Subclass]=Histones
[PDB ID]=3wa9
[PDB chain IDs]=CD
[PDB note]=Chains A, B, E, F, G, H, I and J have been removed to highlight the basic interaction that forms the histone dimer composed of chains C and D.
[PDB experimental technique]=X-ray
[PDB resolution]=3.07
[Evidence global]=Histones form parts of the nucleosome particle by dimerization and subsequent multimerization (PMID:1946434). The dimer contains both histone subunits in a highly intertwined conformation reflecting the possible domain-swapped origins of the structure (PMID:17391511). Accordingly, this dimerization has been experimentally characterized to be coupled to the structure formation of both interacting partners (PMID:12779337); this synergistic folding has been shown separately for H2A-H2B dimers (PMID:15588829) and H3-H4 dimers as well (PMID:15096635). Histones containing various types of monomeric subunits can exhibit varying stability and folding kinetics. E.g. in the case of H3-H4 histones, the dimerization is a complex process with the two monomers first adopting an intermediate state upon encounter and then reaching the classical histone fold through restructurization (PMID:12779337). However, independent of composition and folding kinetics, all histones appear to fold in a cooperative fashion that is coupled to binding (PMID:11669650).
[Chain C name]=Histone H2A.Z
[Chain C source organism]=Homo sapiens
[Chain C UniProt accession]=P0C0S5
[Chain C UniProt boundaries]=1-128
[Chain C UniProt coverage]=100%
[Chain C UniRef90 accession]=UniRef90_P0C0S5
[Chain C UniRef90 boundaries]=1-128
[Chain D name]=Histone H2B type 1-J
[Chain D source organism]=Homo sapiens
[Chain D UniProt accession]=P06899
[Chain D UniProt boundaries]=1-126
[Chain D UniProt coverage]=100%
[Chain D UniRef90 accession]=UniRef90_P06899
[Chain D UniRef90 boundaries]=1-126
[Related structures]=4cay,5b31,5fug

[Entry]
[Accession]=MF2210001
[Name]=H2A-H2B histone dimer (Xenopus laevis), containing histone variants H2A type 1 and H2B 1.1
[Source organism]=Xenopus laevis
[Assembly]=Heterodimer
[Total number of proteins]=2
[Number of unique proteins]=2
[Class]=Histone-like interactions
[Subclass]=Histones
[PDB ID]=1aoi
[PDB chain IDs]=CD
[PDB note]=Chains A, B, E, F, G, H, I and J have been removed to highlight the basic interaction that forms the histone dimer composed of chains C and D.
[PDB experimental technique]=X-ray
[PDB resolution]=2.80
[Evidence global]=Histones form parts of the nucleosome particle by dimerization and subsequent multimerization (PMID:1946434). The dimer contains both histone subunits in a highly intertwined conformation reflecting the possible domain-swapped origins of the structure (PMID:17391511). Accordingly, this dimerization has been experimentally characterized to be coupled to the structure formation of both interacting partners (PMID:12779337); this synergistic folding has been shown separately for H2A-H2B dimers (PMID:15588829) and H3-H4 dimers as well (PMID:15096635). Histones containing various types of monomeric subunits can exhibit varying stability and folding kinetics. E.g. in the case of H3-H4 histones, the dimerization is a complex process with the two monomers first adopting an intermediate state upon encounter and then reaching the classical histone fold through restructurization (PMID:12779337). However, independent of composition and folding kinetics, all histones appear to fold in a cooperative fashion that is coupled to binding (PMID:11669650).
[Chain C name]=Histone H2A type 1
[Chain C source organism]=Xenopus laevis
[Chain C UniProt accession]=P06897
[Chain C UniProt boundaries]=5-120
[Chain C UniProt coverage]=89.2%
[Chain C UniRef90 accession]=UniRef90_Q00728
[Chain C UniRef90 boundaries]=6-120
[Chain D name]=Histone H2B 1.1
[Chain D source organism]=Xenopus laevis
[Chain D UniProt accession]=P02281
[Chain D UniProt boundaries]=28-126
[Chain D UniProt coverage]=78.6%
[Chain D UniRef90 accession]=UniRef90_P57053
[Chain D UniRef90 boundaries]=28-126
[Related structures]=2fj7,4j8u,1kx3,1kx4,1kx5,1m18,1m19,1m1a,3o62,1p34,1p3a,1p3b,1p3f,1p3g,1p3i,1p3k,1p3l,1p3m,1p3o,1p3p,3reh,3rei,3rej,3rek,3rel,1s32,4wu8,4wu9,3b6f,3b6g,4j8v,4j8w,4j8x,4kgc,3kuy,3kwq,3kxb,3lel,3lja,3lz0,3lz1,3mgp,3mgq,3mgr,3mgs,3mnn,2nzd,3ut9,3uta,3utb,4xzq,4ys3,4z66,1zbb,1zla,3tu4,4ld9,4xuj,4zux,5cp6,5dnm,5dnn,5e5a,5f99,5g2e,5hq2,5nl0,5x0x,5x0y

[Entry]
[Accession]=MF2210002
[Name]=H2A-H2B histone dimer (Gallus gallus), containing histone variants H2A-IV and H2B 5
[Source organism]=Gallus gallus
[Assembly]=Heterodimer
[Total number of proteins]=2
[Number of unique proteins]=2
[Class]=Histone-like interactions
[Subclass]=Histones
[PDB ID]=2aro
[PDB chain IDs]=AB
[PDB note]=Chains C, D, E, F, G and H have been removed to highlight the basic interaction that forms the histone dimer composed of chains A and B.
[PDB experimental technique]=X-ray
[PDB resolution]=2.10
[Evidence global]=Histones form parts of the nucleosome particle by dimerization and subsequent multimerization (PMID:1946434). The dimer contains both histone subunits in a highly intertwined conformation reflecting the possible domain-swapped origins of the structure (PMID:17391511). Accordingly, this dimerization has been experimentally characterized to be coupled to the structure formation of both interacting partners (PMID:12779337); this synergistic folding has been shown separately for H2A-H2B dimers (PMID:15588829) and H3-H4 dimers as well (PMID:15096635). Histones containing various types of monomeric subunits can exhibit varying stability and folding kinetics. E.g. in the case of H3-H4 histones, the dimerization is a complex process with the two monomers first adopting an intermediate state upon encounter and then reaching the classical histone fold through restructurization (PMID:12779337). However, independent of composition and folding kinetics, all histones appear to fold in a cooperative fashion that is coupled to binding (PMID:11669650).
[Chain A name]=Histone H2A-IV
[Chain A source organism]=Gallus gallus
[Chain A UniProt accession]=P02263
[Chain A UniProt boundaries]=1-129
[Chain A UniProt coverage]=100%
[Chain A UniRef90 accession]=UniRef90_P02263
[Chain A UniRef90 boundaries]=1-129
[Chain B name]=Histone H2B 5
[Chain B source organism]=Gallus gallus
[Chain B UniProt accession]=P0C1H4
[Chain B UniProt boundaries]=1-126
[Chain B UniProt coverage]=100%
[Chain B UniRef90 accession]=UniRef90_P0C1H4
[Chain B UniRef90 boundaries]=1-126
[Related structures]=1eqz,1hio,2hio,1hq3,1tzy

[Entry]
[Accession]=MF2201007
[Name]=H2A-H2B histone dimer (mouse/human), containing histone variants H2A and H2B type 1-B
[Source organism]=Mus musculus / Homo sapiens
[Assembly]=Heterodimer
[Total number of proteins]=2
[Number of unique proteins]=2
[Class]=Histone-like interactions
[Subclass]=Histones
[PDB ID]=3x1u
[PDB chain IDs]=CD
[PDB note]=Chains A, B, E, F, G, H, I and J have been removed to highlight the basic interaction that forms the histone dimer composed of chains C and D.
[PDB experimental technique]=X-ray
[PDB resolution]=3.25
[Evidence global]=Histones form parts of the nucleosome particle by dimerization and subsequent multimerization (PMID:1946434). The dimer contains both histone subunits in a highly intertwined conformation reflecting the possible domain-swapped origins of the structure (PMID:17391511). Accordingly, this dimerization has been experimentally characterized to be coupled to the structure formation of both interacting partners (PMID:12779337); this synergistic folding has been shown separately for H2A-H2B dimers (PMID:15588829) and H3-H4 dimers as well (PMID:15096635). Histones containing various types of monomeric subunits can exhibit varying stability and folding kinetics. E.g. in the case of H3-H4 histones, the dimerization is a complex process with the two monomers first adopting an intermediate state upon encounter and then reaching the classical histone fold through restructurization (PMID:12779337). However, independent of composition and folding kinetics, all histones appear to fold in a cooperative fashion that is coupled to binding (PMID:11669650).
[Chain C name]=Histone H2A
[Chain C source organism]=Mus musculus
[Chain C UniProt accession]=Q8CGP4
[Chain C UniProt boundaries]=2-129
[Chain C UniProt coverage]=99.2%
[Chain C UniRef90 accession]=UniRef90_Q93077
[Chain C UniRef90 boundaries]=2-124
[Chain D name]=Histone H2B type 1-B
[Chain D source organism]=Homo sapiens
[Chain D UniProt accession]=P33778
[Chain D UniProt boundaries]=3-126
[Chain D UniProt coverage]=98.4%
[Chain D UniRef90 accession]=UniRef90_P33778
[Chain D UniRef90 boundaries]=3-126

[Entry]
[Accession]=MF2210003
[Name]=H2A-H2B histone dimer (Drosophila melanogaster)
[Source organism]=Drosophila melanogaster
[Assembly]=Heterodimer
[Total number of proteins]=2
[Number of unique proteins]=2
[Class]=Histone-like interactions
[Subclass]=Histones
[PDB ID]=2nqb
[PDB chain IDs]=CD
[PDB note]=Chains A, B, E, F, G, H, I and J have been removed to highlight the basic interaction that forms the histone dimer composed of chains C and D.
[PDB experimental technique]=X-ray
[PDB resolution]=2.30
[Evidence global]=Histones form parts of the nucleosome particle by dimerization and subsequent multimerization (PMID:1946434). The dimer contains both histone subunits in a highly intertwined conformation reflecting the possible domain-swapped origins of the structure (PMID:17391511). Accordingly, this dimerization has been experimentally characterized to be coupled to the structure formation of both interacting partners (PMID:12779337); this synergistic folding has been shown separately for H2A-H2B dimers (PMID:15588829) and H3-H4 dimers as well (PMID:15096635). Histones containing various types of monomeric subunits can exhibit varying stability and folding kinetics. E.g. in the case of H3-H4 histones, the dimerization is a complex process with the two monomers first adopting an intermediate state upon encounter and then reaching the classical histone fold through restructurization (PMID:12779337). However, independent of composition and folding kinetics, all histones appear to fold in a cooperative fashion that is coupled to binding (PMID:11669650).
[Chain C name]=Histone H2A
[Chain C source organism]=Drosophila melanogaster
[Chain C UniProt accession]=P84051
[Chain C UniProt boundaries]=2-124
[Chain C UniProt coverage]=99.2%
[Chain C UniRef90 accession]=UniRef90_P84051
[Chain C UniRef90 boundaries]=2-124
[Chain D name]=Histone H2B
[Chain D source organism]=Drosophila melanogaster
[Chain D UniProt accession]=P02283
[Chain D UniProt boundaries]=1-123
[Chain D UniProt coverage]=100%
[Chain D UniRef90 accession]=UniRef90_P02283
[Chain D UniRef90 boundaries]=1-123
[Related structures]=2pyo,4qlc,4x23

[Entry]
[Accession]=MF2200004
[Name]=H2A-H2B histone dimer (human), containing histone variants H2A.V and H2B type 1-J
[Source organism]=Homo sapiens
[Assembly]=Heterodimer
[Total number of proteins]=2
[Number of unique proteins]=2
[Class]=Histone-like interactions
[Subclass]=Histones
[PDB ID]=3waa
[PDB chain IDs]=CD
[PDB note]=Chains A, B, E, F, G, H, I and J have been removed to highlight the basic interaction that forms the histone dimer composed of chains C and D.
[PDB experimental technique]=X-ray
[PDB resolution]=3.20
[Evidence global]=Histones form parts of the nucleosome particle by dimerization and subsequent multimerization (PMID:1946434). The dimer contains both histone subunits in a highly intertwined conformation reflecting the possible domain-swapped origins of the structure (PMID:17391511). Accordingly, this dimerization has been experimentally characterized to be coupled to the structure formation of both interacting partners (PMID:12779337); this synergistic folding has been shown separately for H2A-H2B dimers (PMID:15588829) and H3-H4 dimers as well (PMID:15096635). Histones containing various types of monomeric subunits can exhibit varying stability and folding kinetics. E.g. in the case of H3-H4 histones, the dimerization is a complex process with the two monomers first adopting an intermediate state upon encounter and then reaching the classical histone fold through restructurization (PMID:12779337). However, independent of composition and folding kinetics, all histones appear to fold in a cooperative fashion that is coupled to binding (PMID:11669650).
[Chain C name]=Histone H2A.V
[Chain C source organism]=Homo sapiens
[Chain C UniProt accession]=Q71UI9
[Chain C UniProt boundaries]=1-128
[Chain C UniProt coverage]=100%
[Chain C UniRef90 accession]=UniRef90_Q71UI9
[Chain C UniRef90 boundaries]=1-128
[Chain D name]=Histone H2B type 1-J
[Chain D source organism]=Homo sapiens
[Chain D UniProt accession]=P06899
[Chain D UniProt boundaries]=1-126
[Chain D UniProt coverage]=100%
[Chain D UniRef90 accession]=UniRef90_P06899
[Chain D UniRef90 boundaries]=1-126

[Entry]
[Accession]=MF2200005
[Name]=H3-H4 histone dimer (human), containing histone variant H3.1
[Source organism]=Homo sapiens
[Assembly]=Heterodimer
[Total number of proteins]=2
[Number of unique proteins]=2
[Class]=Histone-like interactions
[Subclass]=Histones
[PDB ID]=3afa
[PDB chain IDs]=AB
[PDB note]=Chains C, D, E, F, G, H, I and J have been removed to highlight the basic interaction that forms the histone dimer composed of chains A and B.
[PDB experimental technique]=X-ray
[PDB resolution]=2.50
[Evidence global]=Histones form parts of the nucleosome particle by dimerization and subsequent multimerization (PMID:1946434). The dimer contains both histone subunits in a highly intertwined conformation reflecting the possible domain-swapped origins of the structure (PMID:17391511). Accordingly, this dimerization has been experimentally characterized to be coupled to the structure formation of both interacting partners (PMID:12779337); this synergistic folding has been shown separately for H2A-H2B dimers (PMID:15588829) and H3-H4 dimers as well (PMID:15096635). Histones containing various types of monomeric subunits can exhibit varying stability and folding kinetics. E.g. in the case of H3-H4 histones, the dimerization is a complex process with the two monomers first adopting an intermediate state upon encounter and then reaching the classical histone fold through restructurization (PMID:12779337). However, independent of composition and folding kinetics, all histones appear to fold in a cooperative fashion that is coupled to binding (PMID:11669650).
[Chain A name]=Histone H3.1
[Chain A source organism]=Homo sapiens
[Chain A UniProt accession]=P68431
[Chain A UniProt boundaries]=1-136
[Chain A UniProt coverage]=100%
[Chain A UniRef90 accession]=UniRef90_P68431
[Chain A UniRef90 boundaries]=1-136
[Chain B name]=Histone H4
[Chain B source organism]=Homo sapiens
[Chain B UniProt accession]=P62805
[Chain B UniProt boundaries]=1-103
[Chain B UniProt coverage]=100%
[Chain B UniRef90 accession]=UniRef90_P62805
[Chain B UniRef90 boundaries]=1-103
[Related structures]=3ayw,3aze,3azf,3azg,3azh,3azi,3azj,3azk,3azl,3azm,3azn,5c3i,2cv5,1u35,3w96,3w97,3w98,3w99,3wa9,3waa,3wkj,3x1s,3x1t,3x1u,3x1v,4ym5,4ym6,4z2m,5av5,5av6,5av8,5av9,5avb,5avc,5b24,5b2i,5b2j,5cpi,5cpj,5cpk,5gse,5gsu,5jrg,5b1l,5b1m

[Entry]
[Accession]=MF2200006
[Name]=H3-H4 histone dimer (human), containing histone variant H3.2
[Source organism]=Homo sapiens
[Assembly]=Heterodimer
[Total number of proteins]=2
[Number of unique proteins]=2
[Class]=Histone-like interactions
[Subclass]=Histones
[PDB ID]=3av1
[PDB chain IDs]=AB
[PDB note]=Chains C, D, E, F, G and H have been removed to highlight the basic interaction that forms the histone dimer composed of chains A and B.
[PDB experimental technique]=X-ray
[PDB resolution]=2.50
[Evidence global]=Histones form parts of the nucleosome particle by dimerization and subsequent multimerization (PMID:1946434). The dimer contains both histone subunits in a highly intertwined conformation reflecting the possible domain-swapped origins of the structure (PMID:17391511). Accordingly, this dimerization has been experimentally characterized to be coupled to the structure formation of both interacting partners (PMID:12779337); this synergistic folding has been shown separately for H2A-H2B dimers (PMID:15588829) and H3-H4 dimers as well (PMID:15096635). Histones containing various types of monomeric subunits can exhibit varying stability and folding kinetics. E.g. in the case of H3-H4 histones, the dimerization is a complex process with the two monomers first adopting an intermediate state upon encounter and then reaching the classical histone fold through restructurization (PMID:12779337). However, independent of composition and folding kinetics, all histones appear to fold in a cooperative fashion that is coupled to binding (PMID:11669650).
[Chain A name]=Histone H3.2
[Chain A source organism]=Homo sapiens
[Chain A UniProt accession]=Q71DI3
[Chain A UniProt boundaries]=1-136
[Chain A UniProt coverage]=100%
[Chain A UniRef90 accession]=UniRef90_Q71DI3
[Chain A UniRef90 boundaries]=1-136
[Chain B name]=Histone H4
[Chain B source organism]=Homo sapiens
[Chain B UniProt accession]=P62805
[Chain B UniProt boundaries]=1-103
[Chain B UniProt coverage]=100%
[Chain B UniRef90 accession]=UniRef90_P62805
[Chain B UniRef90 boundaries]=1-103
[Related structures]=2aro,5bo0,4eo5,1hio,3b6f,3b6g,5bs7,5bsa,1eqz,1f66,2f8n,2fj7,2hio,1hq3,2io5,4j8u,4j8v,4j8w,4j8x,4kgc,3kuy,3kwq,1kx3,1kx4,1kx5,3kxb,3lel,3lja,3lz0,3lz1,3mgp,3mgq,3mgr,3mgs,3mnn,2nzd,3o62,1p34,1p3a,1p3b,1p3f,1p3g,1p3i,1p3k,1p3l,1p3m,1p3o,1p3p,3reh,3rei,3rej,3rek,3rel,1s32,1tzy,3ut9,3uta,3utb,4wu8,4wu9,4xzq,4ys3,4z66,5b0y,5b0z,5b40,3c9k,2hue,3mvd,4r8p,5kgf,5mlu

[Entry]
[Accession]=MF2200007
[Name]=H3-H4 histone dimer (human), containing histone variant H3.1t
[Source organism]=Homo sapiens
[Assembly]=Heterodimer
[Total number of proteins]=2
[Number of unique proteins]=2
[Class]=Histone-like interactions
[Subclass]=Histones
[PDB ID]=3a6n
[PDB chain IDs]=AB
[PDB note]=Chains C, D, E, F, G, H, I and J have been removed to highlight the basic interaction that forms the histone dimer composed of chains A and B.
[PDB experimental technique]=X-ray
[PDB resolution]=2.70
[Evidence global]=Histones form parts of the nucleosome particle by dimerization and subsequent multimerization (PMID:1946434). The dimer contains both histone subunits in a highly intertwined conformation reflecting the possible domain-swapped origins of the structure (PMID:17391511). Accordingly, this dimerization has been experimentally characterized to be coupled to the structure formation of both interacting partners (PMID:12779337); this synergistic folding has been shown separately for H2A-H2B dimers (PMID:15588829) and H3-H4 dimers as well (PMID:15096635). Histones containing various types of monomeric subunits can exhibit varying stability and folding kinetics. E.g. in the case of H3-H4 histones, the dimerization is a complex process with the two monomers first adopting an intermediate state upon encounter and then reaching the classical histone fold through restructurization (PMID:12779337). However, independent of composition and folding kinetics, all histones appear to fold in a cooperative fashion that is coupled to binding (PMID:11669650).
[Chain A name]=Histone H3.1t
[Chain A source organism]=Homo sapiens
[Chain A UniProt accession]=Q16695
[Chain A UniProt boundaries]=1-136
[Chain A UniProt coverage]=100%
[Chain A UniRef90 accession]=UniRef90_Q16695
[Chain A UniRef90 boundaries]=1-136
[Chain B name]=Histone H4
[Chain B source organism]=Homo sapiens
[Chain B UniProt accession]=P62805
[Chain B UniProt boundaries]=1-103
[Chain B UniProt coverage]=100%
[Chain B UniRef90 accession]=UniRef90_P62805
[Chain B UniRef90 boundaries]=1-103
[Related structures]=1aoi,3c1b,3c1c,1m18,1m19,1m1a

[Entry]
[Accession]=MF2200008
[Name]=H3-H4 histone dimer (human), containing histone variant H3.3
[Source organism]=Homo sapiens
[Assembly]=Heterodimer
[Total number of proteins]=2
[Number of unique proteins]=2
[Class]=Histone-like interactions
[Subclass]=Histones
[PDB ID]=3av2
[PDB chain IDs]=AB
[PDB note]=Chains C, D, E, F, G, H, I and J have been removed to highlight the basic interaction that forms the histone dimer composed of chains A and B.
[PDB experimental technique]=X-ray
[PDB resolution]=2.80
[Evidence global]=Histones form parts of the nucleosome particle by dimerization and subsequent multimerization (PMID:1946434). The dimer contains both histone subunits in a highly intertwined conformation reflecting the possible domain-swapped origins of the structure (PMID:17391511). Accordingly, this dimerization has been experimentally characterized to be coupled to the structure formation of both interacting partners (PMID:12779337); this synergistic folding has been shown separately for H2A-H2B dimers (PMID:15588829) and H3-H4 dimers as well (PMID:15096635). Histones containing various types of monomeric subunits can exhibit varying stability and folding kinetics. E.g. in the case of H3-H4 histones, the dimerization is a complex process with the two monomers first adopting an intermediate state upon encounter and then reaching the classical histone fold through restructurization (PMID:12779337). However, independent of composition and folding kinetics, all histones appear to fold in a cooperative fashion that is coupled to binding (PMID:11669650).
[Chain A name]=Histone H3.3
[Chain A source organism]=Homo sapiens
[Chain A UniProt accession]=P84243
[Chain A UniProt boundaries]=1-136
[Chain A UniProt coverage]=100%
[Chain A UniRef90 accession]=UniRef90_P84243
[Chain A UniRef90 boundaries]=1-136
[Chain B name]=Histone H4
[Chain B source organism]=Homo sapiens
[Chain B UniProt accession]=P62805
[Chain B UniProt boundaries]=1-103
[Chain B UniProt coverage]=100%
[Chain B UniRef90 accession]=UniRef90_P62805
[Chain B UniRef90 boundaries]=1-103
[Related structures]=4h9n,4h9o,4h9r,4h9s,4hga,3wtp,5b32,5b33,4h9p,4h9q,5ay8,5bnv,5bnx,5ja4,5kdm,5x7x,4zbj

[Entry]
[Accession]=MF2210004
[Name]=H3-H4 histone dimer (Drosophila melanogaster)
[Source organism]=Drosophila melanogaster
[Assembly]=Heterodimer
[Total number of proteins]=2
[Number of unique proteins]=2
[Class]=Histone-like interactions
[Subclass]=Histones
[PDB ID]=2nqb
[PDB chain IDs]=AB
[PDB note]=Chains C, D, E, F, G, H, I and J have been removed to highlight the basic interaction that forms the histone dimer composed of chains A and B.
[PDB experimental technique]=X-ray
[PDB resolution]=2.30
[Evidence global]=Histones form parts of the nucleosome particle by dimerization and subsequent multimerization (PMID:1946434). The dimer contains both histone subunits in a highly intertwined conformation reflecting the possible domain-swapped origins of the structure (PMID:17391511). Accordingly, this dimerization has been experimentally characterized to be coupled to the structure formation of both interacting partners (PMID:12779337); this synergistic folding has been shown separately for H2A-H2B dimers (PMID:15588829) and H3-H4 dimers as well (PMID:15096635). Histones containing various types of monomeric subunits can exhibit varying stability and folding kinetics. E.g. in the case of H3-H4 histones, the dimerization is a complex process with the two monomers first adopting an intermediate state upon encounter and then reaching the classical histone fold through restructurization (PMID:12779337). However, independent of composition and folding kinetics, all histones appear to fold in a cooperative fashion that is coupled to binding (PMID:11669650).
[Chain A name]=Histone H3
[Chain A source organism]=Drosophila melanogaster
[Chain A UniProt accession]=P02299
[Chain A UniProt boundaries]=2-136
[Chain A UniProt coverage]=99.3%
[Chain A UniRef90 accession]=UniRef90_Q71DI3
[Chain A UniRef90 boundaries]=2-136
[Chain B name]=Histone H4
[Chain B source organism]=Drosophila melanogaster
[Chain B UniProt accession]=P84040
[Chain B UniProt boundaries]=1-103
[Chain B UniProt coverage]=100%
[Chain B UniRef90 accession]=UniRef90_P84040
[Chain B UniRef90 boundaries]=1-103
[Related structures]=2pyo,4uuz,4qlc,4x23

[Entry]
[Accession]=MF2210005
[Name]=H3-H4 histone dimer (Saccharomyces cerevisiae)
[Source organism]=Saccharomyces cerevisiae
[Assembly]=Heterodimer
[Total number of proteins]=2
[Number of unique proteins]=2
[Class]=Histone-like interactions
[Subclass]=Histones
[PDB ID]=1id3
[PDB chain IDs]=AB
[PDB note]=Chains C, D, E, F, G, H, I and J have been removed to highlight the basic interaction that forms the histone dimer composed of chains A and B.
[PDB experimental technique]=X-ray
[PDB resolution]=3.10
[Evidence global]=Histones form parts of the nucleosome particle by dimerization and subsequent multimerization (PMID:1946434). The dimer contains both histone subunits in a highly intertwined conformation reflecting the possible domain-swapped origins of the structure (PMID:17391511). Accordingly, this dimerization has been experimentally characterized to be coupled to the structure formation of both interacting partners (PMID:12779337); this synergistic folding has been shown separately for H2A-H2B dimers (PMID:15588829) and H3-H4 dimers as well (PMID:15096635). Histones containing various types of monomeric subunits can exhibit varying stability and folding kinetics. E.g. in the case of H3-H4 histones, the dimerization is a complex process with the two monomers first adopting an intermediate state upon encounter and then reaching the classical histone fold through restructurization (PMID:12779337). However, independent of composition and folding kinetics, all histones appear to fold in a cooperative fashion that is coupled to binding (PMID:11669650).
[Chain A name]=Histone H3
[Chain A source organism]=Saccharomyces cerevisiae
[Chain A UniProt accession]=P61830
[Chain A UniProt boundaries]=2-136
[Chain A UniProt coverage]=99.3%
[Chain A UniRef90 accession]=UniRef90_Q757N1
[Chain A UniRef90 boundaries]=2-136
[Chain B name]=Histone H4
[Chain B source organism]=Saccharomyces cerevisiae
[Chain B UniProt accession]=P02309
[Chain B UniProt boundaries]=2-103
[Chain B UniProt coverage]=99%
[Chain B UniRef90 accession]=UniRef90_P02309
[Chain B UniRef90 boundaries]=2-103
[Related structures]=4jjn,4kud

[Entry]
[Accession]=MF4110005
[Name]=Transthyretin (Gallus gallus)
[Source organism]=Gallus gallus
[Assembly]=Homotetramer
[Total number of proteins]=4
[Number of unique proteins]=1
[Class]=Transthyretin-like folds
[Subclass]=Transthyretin
[PDB ID]=1tfp
[PDB chain IDs]=ABCD
[PDB note]=Chains C and D were generated from chains A and B respectively, using the biomatrices described in the original PDB file.
[PDB experimental technique]=X-ray
[PDB resolution]=2.90
[Evidence global]=Transthyretin was shown in calorimetrics experiments to follow two-state folding/binding kinetics with the emergence of structure being linked to oligomerization (PMID:11152276).
[Chain A name]=Transthyretin
[Chain A source organism]=Gallus gallus
[Chain A UniProt accession]=P27731
[Chain A UniProt boundaries]=21-150
[Chain A UniProt coverage]=86.7%
[Chain A UniRef90 accession]=UniRef90_P27731
[Chain A UniRef90 boundaries]=21-150
[Chain B name]=Transthyretin
[Chain B source organism]=Gallus gallus
[Chain B UniProt accession]=P27731
[Chain B UniProt boundaries]=21-150
[Chain B UniProt coverage]=86.7%
[Chain B UniRef90 accession]=UniRef90_P27731
[Chain B UniRef90 boundaries]=21-150
[Chain C name]=Transthyretin
[Chain C source organism]=Gallus gallus
[Chain C UniProt accession]=P27731
[Chain C UniProt boundaries]=21-150
[Chain C UniProt coverage]=86.7%
[Chain C UniRef90 accession]=UniRef90_P27731
[Chain C UniRef90 boundaries]=21-150
[Chain D name]=Transthyretin
[Chain D source organism]=Gallus gallus
[Chain D UniProt accession]=P27731
[Chain D UniProt boundaries]=21-150
[Chain D UniProt coverage]=86.7%
[Chain D UniRef90 accession]=UniRef90_P27731
[Chain D UniRef90 boundaries]=21-150

[Entry]
[Accession]=MF2202002
[Name]=GTPase binding domain of Wiskott-Aldrich syndrome protein in complex with E. coli EspF(U)
[Source organism]=Homo sapiens / Escherichia coli O157:H7
[Assembly]=Heterodimer
[Total number of proteins]=2
[Number of unique proteins]=2
[Class]=Other
[Subclass]=Other
[PDB ID]=2k42
[PDB chain IDs]=AB
[PDB note]=No modifications of the original PDB file. Chain identifiers are identical with the PDB's identifiers.
[PDB experimental technique]=NMR
[Evidence chain A]=The 230-249 region described in DisProt entry DP00215 and the 230-310 region described in IDEAL entry IID00269 cover 100% of the sequence present in the structure.
[Evidence chain B]=The 221-314 region described in IDEAL entry IID90008 covers 92% of the sequence present in the structure.
[Chain A name]=Wiskott-Aldrich syndrome protein
[Chain A source organism]=Homo sapiens
[Chain A UniProt accession]=P42768
[Chain A UniProt boundaries]=239-310
[Chain A UniProt coverage]=14.3%
[Chain A UniRef90 accession]=UniRef90_P42768
[Chain A UniRef90 boundaries]=239-310
[Chain B name]=Secreted effector protein EspF(U)
[Chain B source organism]=Escherichia coli O157:H7
[Chain B UniProt accession]=P0DJ89
[Chain B UniProt boundaries]=218-253
[Chain B UniProt coverage]=10.7%
[Chain B UniRef90 accession]=UniRef90_P0DJ88
[Chain B UniRef90 boundaries]=221-253

[Entry]
[Accession]=MF2110009
[Name]=HY5 leucine zipper homodimer
[Source organism]=Arabidopsis thaliana
[Assembly]=Homodimer
[Total number of proteins]=2
[Number of unique proteins]=1
[Class]=Coils and zippers
[Subclass]=Leucine zipper (dimeric)
[PDB ID]=2oqq
[PDB chain IDs]=AB
[PDB note]=No modifications of the original PDB file. Chain identifiers are identical with the PDB's identifiers.
[PDB experimental technique]=X-ray
[PDB resolution]=2.00
[Evidence global]=The subunits in the structure are bound via coiled coil interactions. Coiled coils are highly versatile folding units (PMID:11166216), where the formation of the structure and the interaction between subunits is almost ubiquitously linked. This cooperative nature of binding and folding that results in a two-step process has been demonstrated for coiled coils with varying oligomeric state from dimers (PMID:9811815) and trimers (PMID:10933510) up to heptamers (PMID:17030805). While the interaction and folding are linked, in certain cases there can be significant residual structure before association (PMID:8401212). However, these residual structural elements usually encompass 1-2 turns of helices that serve as a 'nucleation site' driving interaction and helix formation (zipping up) (PMID:17438295), thus even in these cases monomeric coiled coil subunits cannot be considered to have a stable structure. Leucine zippers, phenylalanine zippers and alanine zippers are subclasses of coiled coils where the hydrophobic interactions between subunits are predominantly formed by leucine, phenylalanine or alanine residues, respectively.
[Chain A name]=Transcription factor HY5
[Chain A source organism]=Arabidopsis thaliana
[Chain A UniProt accession]=O24646
[Chain A UniProt boundaries]=109-150
[Chain A UniProt coverage]=25%
[Chain A UniRef90 accession]=UniRef90_O24646
[Chain A UniRef90 boundaries]=111-150
[Chain B name]=Transcription factor HY5
[Chain B source organism]=Arabidopsis thaliana
[Chain B UniProt accession]=O24646
[Chain B UniProt boundaries]=109-150
[Chain B UniProt coverage]=25%
[Chain B UniRef90 accession]=UniRef90_O24646
[Chain B UniRef90 boundaries]=111-150

[Entry]
[Accession]=MF2211002
[Name]=c-Myc-Max heterodimeric leucine zipper
[Source organism]=Pan paniscus / Mus musculus
[Assembly]=Heterodimer
[Total number of proteins]=2
[Number of unique proteins]=2
[Class]=Coils and zippers
[Subclass]=Leucine zipper (dimeric)
[PDB ID]=1a93
[PDB chain IDs]=AB
[PDB note]=No modifications of the original PDB file. Chain identifiers are identical with the PDB's identifiers.
[PDB experimental technique]=NMR
[Evidence global]=The subunits in the structure are bound via coiled coil interactions (PMID:9680483). Coiled coils are highly versatile folding units (PMID:11166216), where the formation of the structure and the interaction between subunits is almost ubiquitously linked. This cooperative nature of binding and folding that results in a two-step process has been demonstrated for coiled coils with varying oligomeric state from dimers (PMID:9811815) and trimers (PMID:10933510) up to heptamers (PMID:17030805). While the interaction and folding are linked, in certain cases there can be significant residual structure before association (PMID:8401212). However, these residual structural elements usually encompass 1-2 turns of helices that serve as a 'nucleation site' driving interaction and helix formation (zipping up) (PMID:17438295), thus even in these cases monomeric coiled coil subunits cannot be considered to have a stable structure. Leucine zippers, phenylalanine zippers and alanine zippers are subclasses of coiled coils where the hydrophobic interactions between subunits are predominantly formed by leucine, phenylalanine or alanine residues, respectively.
[Evidence chain A]=The 406-434 region described in DisProt entry DP00260 covers 100% of a close homologue of the sequence present in the structure.
[Evidence chain B]=The 1-110 region described in DisProt entry DP00084 covers 100% of a close homologue of the sequence present in the structure.
[Chain A name]=Myc proto-oncogene protein
[Chain A source organism]=Pan paniscus
[Chain A UniProt accession]=A1YG22
[Chain A UniProt boundaries]=406-434
[Chain A UniProt coverage]=6.6%
[Chain A UniRef90 accession]=UniRef90_P01106
[Chain A UniRef90 boundaries]=406-434
[Chain B name]=Protein max
[Chain B source organism]=Mus musculus
[Chain B UniProt accession]=P28574
[Chain B UniProt boundaries]=74-102
[Chain B UniProt coverage]=18.1%
[Chain B UniRef90 accession]=UniRef90_P61244
[Chain B UniRef90 boundaries]=74-102
[Related structures]=2a93,1nkp

[Entry]
[Accession]=MF2201008
[Name]=Heterodimer of ATF-4 and C/EBP beta
[Source organism]=Homo sapiens / Mus musculus
[Assembly]=Heterodimer
[Total number of proteins]=2
[Number of unique proteins]=2
[Class]=Coils and zippers
[Subclass]=Leucine zipper (dimeric)
[PDB ID]=1ci6
[PDB chain IDs]=AB
[PDB note]=No modifications of the original PDB file. Chain identifiers are identical with the PDB's identifiers.
[PDB experimental technique]=X-ray
[PDB resolution]=2.60
[Evidence global]=The subunits of the dimer were shown to be disordered in their monomeric form with the structure arising as a result of the interaction (PMID:11018027). The subunits in the structure are bound via coiled coil interactions (PMID:11018027). Coiled coils are highly versatile folding units (PMID:11166216), where the formation of the structure and the interaction between subunits is almost ubiquitously linked. This cooperative nature of binding and folding that results in a two-step process has been demonstrated for coiled coils with varying oligomeric state from dimers (PMID:9811815) and trimers (PMID:10933510) up to heptamers (PMID:17030805). While the interaction and folding are linked, in certain cases there can be significant residual structure before association (PMID:8401212). However, these residual structural elements usually encompass 1-2 turns of helices that serve as a 'nucleation site' driving interaction and helix formation (zipping up) (PMID:17438295), thus even in these cases monomeric coiled coil subunits cannot be considered to have a stable structure. Leucine zippers, phenylalanine zippers and alanine zippers are subclasses of coiled coils where the hydrophobic interactions between subunits are predominantly formed by leucine, phenylalanine or alanine residues, respectively.
[Evidence chain B]=A homologue sharing the same Pfam domain (PF07716.12) has been experimentally characterized as disordered in DisProt entry DP00083.
[Chain A name]=Cyclic AMP-dependent transcription factor ATF-4
[Chain A source organism]=Homo sapiens
[Chain A UniProt accession]=P18848
[Chain A UniProt boundaries]=279-341
[Chain A UniProt coverage]=17.9%
[Chain A UniRef90 accession]=UniRef90_P18848
[Chain A UniRef90 boundaries]=280-341
[Chain B name]=CCAAT/enhancer-binding protein beta
[Chain B source organism]=Mus musculus
[Chain B UniProt accession]=P28033
[Chain B UniProt boundaries]=223-285
[Chain B UniProt coverage]=21.3%
[Chain B UniRef90 accession]=UniRef90_P28033
[Chain B UniRef90 boundaries]=224-285

[Entry]
[Accession]=MF4110006
[Name]=General corepressor Tup1p
[Source organism]=Saccharomyces cerevisiae
[Assembly]=Homotetramer
[Total number of proteins]=4
[Number of unique proteins]=1
[Class]=Coils and zippers
[Subclass]=Coiled coil (tetrameric)
[PDB ID]=3vp8
[PDB chain IDs]=ABCD
[PDB note]=No modifications of the original PDB file. Chain identifiers are identical with the PDB's identifiers.
[PDB experimental technique]=X-ray
[PDB resolution]=1.91
[Evidence global]=The subunits in the structure are bound via coiled coil interactions (PMID:22707714). Coiled coils are highly versatile folding units (PMID:11166216), where the formation of the structure and the interaction between subunits is almost ubiquitously linked. This cooperative nature of binding and folding that results in a two-step process has been demonstrated for coiled coils with varying oligomeric state from dimers (PMID:9811815) and trimers (PMID:10933510) up to heptamers (PMID:17030805). While the interaction and folding are linked, in certain cases there can be significant residual structure before association (PMID:8401212). However, these residual structural elements usually encompass 1-2 turns of helices that serve as a 'nucleation site' driving interaction and helix formation (zipping up) (PMID:17438295), thus even in these cases monomeric coiled coil subunits cannot be considered to have a stable structure.
[Chain A name]=General transcriptional corepressor TUP1
[Chain A source organism]=Saccharomyces cerevisiae
[Chain A UniProt accession]=P16649
[Chain A UniProt boundaries]=1-92
[Chain A UniProt coverage]=12.9%
[Chain A UniRef90 accession]=UniRef90_P16649
[Chain A UniRef90 boundaries]=1-92
[Chain B name]=General transcriptional corepressor TUP1
[Chain B source organism]=Saccharomyces cerevisiae
[Chain B UniProt accession]=P16649
[Chain B UniProt boundaries]=1-92
[Chain B UniProt coverage]=12.9%
[Chain B UniRef90 accession]=UniRef90_P16649
[Chain B UniRef90 boundaries]=1-92
[Chain C name]=General transcriptional corepressor TUP1
[Chain C source organism]=Saccharomyces cerevisiae
[Chain C UniProt accession]=P16649
[Chain C UniProt boundaries]=1-92
[Chain C UniProt coverage]=12.9%
[Chain C UniRef90 accession]=UniRef90_P16649
[Chain C UniRef90 boundaries]=1-92
[Chain D name]=General transcriptional corepressor TUP1
[Chain D source organism]=Saccharomyces cerevisiae
[Chain D UniProt accession]=P16649
[Chain D UniProt boundaries]=1-92
[Chain D UniProt coverage]=12.9%
[Chain D UniRef90 accession]=UniRef90_P16649
[Chain D UniRef90 boundaries]=1-92
[Related structures]=3vp9

[Entry]
[Accession]=MF2120017
[Name]=TrpR-like protein (Eubacterium eligens)
[Source organism]=Eubacterium eligens
[Assembly]=Homodimer
[Total number of proteins]=2
[Number of unique proteins]=1
[Class]=Other
[Subclass]=Trp repressor-like
[PDB ID]=3g1c
[PDB chain IDs]=AB
[PDB note]=Chain B was generated from chain A using the biomatrix described in the original PDB file.
[PDB experimental technique]=X-ray
[PDB resolution]=2.20
[Evidence global]=The folding and dimerization of the Trp repressor were shown to be linked by both experimental (PMID:10329154,PMID:2223756,PMID:7578063) and computational studies (PMID:10465773).
[Chain A name]=The TrpR like protein from Eubacterium eligens ATCC 27750
[Chain A source organism]=Eubacterium eligens
[Chain A UniProt accession]=C4Z2H9
[Chain A UniProt boundaries]=1-104
[Chain A UniProt coverage]=100%
[Chain A UniRef90 accession]=UniRef90_C4Z2H9
[Chain A UniRef90 boundaries]=1-104
[Chain B name]=The TrpR like protein from Eubacterium eligens ATCC 27750
[Chain B source organism]=Eubacterium eligens
[Chain B UniProt accession]=C4Z2H9
[Chain B UniProt boundaries]=1-104
[Chain B UniProt coverage]=100%
[Chain B UniRef90 accession]=UniRef90_C4Z2H9
[Chain B UniRef90 boundaries]=1-104

[Entry]
[Accession]=MF2120018
[Name]=Putative Trp repressor (Staphylococcus aureus)
[Source organism]=Staphylococcus aureus
[Assembly]=Homodimer
[Total number of proteins]=2
[Number of unique proteins]=1
[Class]=Other
[Subclass]=Trp repressor-like
[PDB ID]=3kor
[PDB chain IDs]=AD
[PDB note]=Chains B and C were removed as chains A and D represent the biologically active dimer.
[PDB experimental technique]=X-ray
[PDB resolution]=1.60
[Evidence global]=The folding and dimerization of the Trp repressor were shown to be linked by both experimental (PMID:10329154,PMID:2223756,PMID:7578063) and computational studies (PMID:10465773).
[Chain A name]=Uncharacterized protein
[Chain A source organism]=Staphylococcus aureus
[Chain A UniProt accession]=A0A0H3JS52
[Chain A UniProt boundaries]=1-100
[Chain A UniProt coverage]=100%
[Chain A UniRef90 accession]=UniRef90_Q49YV2
[Chain A UniRef90 boundaries]=1-98
[Chain D name]=Uncharacterized protein
[Chain D source organism]=Staphylococcus aureus
[Chain D UniProt accession]=A0A0H3JS52
[Chain D UniProt boundaries]=1-100
[Chain D UniProt coverage]=100%
[Chain D UniRef90 accession]=UniRef90_Q49YV2
[Chain D UniRef90 boundaries]=1-98

[Entry]
[Accession]=MF3300001
[Name]=Rb C-terminal domain bound to an E2F1-DP1 heterodimer
[Source organism]=Homo sapiens
[Assembly]=Heterotrimer
[Total number of proteins]=3
[Number of unique proteins]=3
[Class]=Other
[Subclass]=Other
[PDB ID]=2aze
[PDB chain IDs]=ABC
[PDB note]=No modifications of the original PDB file. Chain identifiers are identical with the PDB's identifiers.
[PDB experimental technique]=X-ray
[PDB resolution]=2.55
[Evidence global]=The interacting partners have been shown to adopt a stable structure as a result of the interaction (PMID:16360038).
[Evidence chain C]=The 772-874 region described in IDEAL entry IID00017 covers 100% of the sequence present in the structure.
[Chain A name]=Transcription factor Dp-1
[Chain A source organism]=Homo sapiens
[Chain A UniProt accession]=Q14186
[Chain A UniProt boundaries]=196-350
[Chain A UniProt coverage]=37.8%
[Chain A UniRef90 accession]=UniRef90_Q14186
[Chain A UniRef90 boundaries]=199-350
[Chain B name]=Transcription factor E2F1
[Chain B source organism]=Homo sapiens
[Chain B UniProt accession]=Q01094
[Chain B UniProt boundaries]=196-301
[Chain B UniProt coverage]=24.3%
[Chain B UniRef90 accession]=UniRef90_Q01094
[Chain B UniRef90 boundaries]=192-301
[Chain C name]=Retinoblastoma-associated protein
[Chain C source organism]=Homo sapiens
[Chain C UniProt accession]=P06400
[Chain C UniProt boundaries]=829-874
[Chain C UniProt coverage]=5%
[Chain C UniRef90 accession]=UniRef90_P06400
[Chain C UniRef90 boundaries]=829-874

[Entry]
[Accession]=MF2100006
[Name]=Rab11 binding domain of Rab11 family interacting protein 2
[Source organism]=Homo sapiens
[Assembly]=Homodimer
[Total number of proteins]=2
[Number of unique proteins]=1
[Class]=Coils and zippers
[Subclass]=Coiled coil (dimeric)
[PDB ID]=2k6s
[PDB chain IDs]=AB
[PDB note]=No modifications of the original PDB file. Chain identifiers are identical with the PDB's identifiers.
[PDB experimental technique]=NMR
[Evidence global]=The subunits in the structure are bound via coiled coil interactions (PMID:19119858). Coiled coils are highly versatile folding units (PMID:11166216), where the formation of the structure and the interaction between subunits is almost ubiquitously linked. This cooperative nature of binding and folding that results in a two-step process has been demonstrated for coiled coils with varying oligomeric state from dimers (PMID:9811815) and trimers (PMID:10933510) up to heptamers (PMID:17030805). While the interaction and folding are linked, in certain cases there can be significant residual structure before association (PMID:8401212). However, these residual structural elements usually encompass 1-2 turns of helices that serve as a 'nucleation site' driving interaction and helix formation (zipping up) (PMID:17438295), thus even in these cases monomeric coiled coil subunits cannot be considered to have a stable structure.
[Chain A name]=Rab11 family-interacting protein 2
[Chain A source organism]=Homo sapiens
[Chain A UniProt accession]=Q7L804
[Chain A UniProt boundaries]=449-489
[Chain A UniProt coverage]=8%
[Chain A UniRef90 accession]=UniRef90_Q7L804
[Chain A UniRef90 boundaries]=450-489
[Chain B name]=Rab11 family-interacting protein 2
[Chain B source organism]=Homo sapiens
[Chain B UniProt accession]=Q7L804
[Chain B UniProt boundaries]=449-489
[Chain B UniProt coverage]=8%
[Chain B UniRef90 accession]=UniRef90_Q7L804
[Chain B UniRef90 boundaries]=450-489
[Related structures]=3tso,4c4p

[Entry]
[Accession]=MF4100003
[Name]=p53 tetramerization domain (human)
[Source organism]=Homo sapiens
[Assembly]=Homotetramer
[Total number of proteins]=4
[Number of unique proteins]=1
[Class]=Other
[Subclass]=p53 tetramerization
[PDB ID]=2j0z
[PDB chain IDs]=ABCD
[PDB note]=No modifications of the original PDB file. Chain identifiers are identical with the PDB's identifiers.
[PDB experimental technique]=NMR
[Evidence global]=The tetramerization domain of p53 exhibits a four-helix bundle structure bound by hydrophobic and electrostatic interactions (PMID:8023159). The tetramer is formed as a dimer of dimers and follows a two state folding and binding process, demonstrated in several chemical and thermal denaturation/refolding experiments (PMID:9582268,PMID:18410249,PMID:19913028).
[Chain A name]=Cellular tumor antigen p53
[Chain A source organism]=Homo sapiens
[Chain A UniProt accession]=P04637
[Chain A UniProt boundaries]=326-356
[Chain A UniProt coverage]=7.9%
[Chain A UniRef90 accession]=UniRef90_P04637
[Chain A UniRef90 boundaries]=326-356
[Chain B name]=Cellular tumor antigen p53
[Chain B source organism]=Homo sapiens
[Chain B UniProt accession]=P04637
[Chain B UniProt boundaries]=326-356
[Chain B UniProt coverage]=7.9%
[Chain B UniRef90 accession]=UniRef90_P04637
[Chain B UniRef90 boundaries]=326-356
[Chain C name]=Cellular tumor antigen p53
[Chain C source organism]=Homo sapiens
[Chain C UniProt accession]=P04637
[Chain C UniProt boundaries]=326-356
[Chain C UniProt coverage]=7.9%
[Chain C UniRef90 accession]=UniRef90_P04637
[Chain C UniRef90 boundaries]=326-356
[Chain D name]=Cellular tumor antigen p53
[Chain D source organism]=Homo sapiens
[Chain D UniProt accession]=P04637
[Chain D UniProt boundaries]=326-356
[Chain D UniProt coverage]=7.9%
[Chain D UniRef90 accession]=UniRef90_P04637
[Chain D UniRef90 boundaries]=326-356
[Related structures]=1a1u,1aie,1c26,1hs5,2j10,2j11,1olg,1olh,1pes,1pet,1sae,1saf,1sak,1sal,3sak

[Entry]
[Accession]=MF4110007
[Name]=p53 tetramerization domain (Danio rerio)
[Source organism]=Danio rerio
[Assembly]=Homotetramer
[Total number of proteins]=4
[Number of unique proteins]=1
[Class]=Other
[Subclass]=p53 tetramerization
[PDB ID]=4d1l
[PDB chain IDs]=CDEF
[PDB note]=Chains A and B were removed as chains C, D, E and F represent the biologically relevant tetramer.
[PDB experimental technique]=X-ray
[PDB resolution]=1.97
[Evidence global]=The tetramerization domain of p53 exhibits a four-helix bundle structure bound by hydrophobic and electrostatic interactions (PMID:8023159). The tetramer is formed as a dimer of dimers and follows a two state folding and binding process, demonstrated in several chemical and thermal denaturation/refolding experiments (PMID:9582268,PMID:18410249,PMID:19913028).
[Chain C name]=Cellular tumor antigen p53
[Chain C source organism]=Danio rerio
[Chain C UniProt accession]=G1K2L5
[Chain C UniProt boundaries]=299-346
[Chain C UniProt coverage]=12.8%
[Chain C UniRef90 accession]=UniRef90_P79734
[Chain C UniRef90 boundaries]=301-345
[Chain D name]=Cellular tumor antigen p53
[Chain D source organism]=Danio rerio
[Chain D UniProt accession]=G1K2L5
[Chain D UniProt boundaries]=299-346
[Chain D UniProt coverage]=12.8%
[Chain D UniRef90 accession]=UniRef90_P79734
[Chain D UniRef90 boundaries]=301-345
[Chain E name]=Cellular tumor antigen p53
[Chain E source organism]=Danio rerio
[Chain E UniProt accession]=G1K2L5
[Chain E UniProt boundaries]=299-346
[Chain E UniProt coverage]=12.8%
[Chain E UniRef90 accession]=UniRef90_P79734
[Chain E UniRef90 boundaries]=301-345
[Chain F name]=Cellular tumor antigen p53
[Chain F source organism]=Danio rerio
[Chain F UniProt accession]=G1K2L5
[Chain F UniProt boundaries]=299-346
[Chain F UniProt coverage]=12.8%
[Chain F UniRef90 accession]=UniRef90_P79734
[Chain F UniRef90 boundaries]=301-345
[Related structures]=4d1m,4cz5,4cz6,4cz7

[Entry]
[Accession]=MF4100004
[Name]=p63 tetramerization domain (human)
[Source organism]=Homo sapiens
[Assembly]=Homotetramer
[Total number of proteins]=4
[Number of unique proteins]=1
[Class]=Other
[Subclass]=p53 tetramerization
[PDB ID]=3zy1
[PDB chain IDs]=ABCD
[PDB note]=Chains B, C and D were generated from chain A using the biomatrices described in the original PDB file.
[PDB experimental technique]=X-ray
[PDB resolution]=2.15
[Evidence global]=p63 is a member of the p53 protein family. The tetramerization region of p53, p63 and p73 are closely homologous to each other, having very similar sequences, structures and biological functions (PMID:25185827,PMID:18289041,PMID:20379196), all containing the same Pfam domain (PF07710). The tetramerization domain of p53 exhibits a four-helix bundle structure bound by hydrophobic and electrostatic interactions (PMID:8023159). The tetramer is formed as a dimer of dimers and follows a two state folding and binding process, demonstrated in several chemical and thermal denaturation/refolding experiments (PMID:9582268,PMID:18410249,PMID:19913028).
[Chain A name]=Tumor protein 63
[Chain A source organism]=Homo sapiens
[Chain A UniProt accession]=Q9H3D4
[Chain A UniProt boundaries]=396-441
[Chain A UniProt coverage]=6.8%
[Chain A UniRef90 accession]=UniRef90_Q9H3D4
[Chain A UniRef90 boundaries]=398-436
[Chain B name]=Tumor protein 63
[Chain B source organism]=Homo sapiens
[Chain B UniProt accession]=Q9H3D4
[Chain B UniProt boundaries]=396-441
[Chain B UniProt coverage]=6.8%
[Chain B UniRef90 accession]=UniRef90_Q9H3D4
[Chain B UniRef90 boundaries]=398-436
[Chain C name]=Tumor protein 63
[Chain C source organism]=Homo sapiens
[Chain C UniProt accession]=Q9H3D4
[Chain C UniProt boundaries]=396-441
[Chain C UniProt coverage]=6.8%
[Chain C UniRef90 accession]=UniRef90_Q9H3D4
[Chain C UniRef90 boundaries]=398-436
[Chain D name]=Tumor protein 63
[Chain D source organism]=Homo sapiens
[Chain D UniProt accession]=Q9H3D4
[Chain D UniProt boundaries]=396-441
[Chain D UniProt coverage]=6.8%
[Chain D UniRef90 accession]=UniRef90_Q9H3D4
[Chain D UniRef90 boundaries]=398-436
[Related structures]=3zy0,4a9z

[Entry]
[Accession]=MF4100005
[Name]=p73 tetramerization domain (human)
[Source organism]=Homo sapiens
[Assembly]=Homotetramer
[Total number of proteins]=4
[Number of unique proteins]=1
[Class]=Other
[Subclass]=p53 tetramerization
[PDB ID]=2kby
[PDB chain IDs]=ABCD
[PDB note]=No modifications of the original PDB file. Chain identifiers are identical with the PDB's identifiers.
[PDB experimental technique]=NMR
[Evidence global]=p73 is a member of the p53 protein family. The tetramerization region of p53, p63 and p73 are closely homologous to each other, having very similar sequences, structures and biological functions (PMID:25185827,PMID:18289041,PMID:20379196), all containing the same Pfam domain (PF07710). The tetramerization domain of p53 exhibits a four-helix bundle structure bound by hydrophobic and electrostatic interactions (PMID:8023159). The tetramer is formed as a dimer of dimers and follows a two state folding and binding process, demonstrated in several chemical and thermal denaturation/refolding experiments (PMID:9582268,PMID:18410249,PMID:19913028).
[Chain A name]=Tumor protein p73
[Chain A source organism]=Homo sapiens
[Chain A UniProt accession]=O15350
[Chain A UniProt boundaries]=349-398
[Chain A UniProt coverage]=7.9%
[Chain A UniRef90 accession]=UniRef90_O15350
[Chain A UniRef90 boundaries]=351-389
[Chain B name]=Tumor protein p73
[Chain B source organism]=Homo sapiens
[Chain B UniProt accession]=O15350
[Chain B UniProt boundaries]=349-398
[Chain B UniProt coverage]=7.9%
[Chain B UniRef90 accession]=UniRef90_O15350
[Chain B UniRef90 boundaries]=351-389
[Chain C name]=Tumor protein p73
[Chain C source organism]=Homo sapiens
[Chain C UniProt accession]=O15350
[Chain C UniProt boundaries]=349-398
[Chain C UniProt coverage]=7.9%
[Chain C UniRef90 accession]=UniRef90_O15350
[Chain C UniRef90 boundaries]=351-389
[Chain D name]=Tumor protein p73
[Chain D source organism]=Homo sapiens
[Chain D UniProt accession]=O15350
[Chain D UniProt boundaries]=349-398
[Chain D UniProt coverage]=7.9%
[Chain D UniRef90 accession]=UniRef90_O15350
[Chain D UniRef90 boundaries]=351-389
[Related structures]=2wqi,2wtt,2wqj,5hob,5hoc

[Entry]
[Accession]=MF2140005
[Name]=DNA binding domain of the E2 protein (Human papillomavirus type 16)
[Source organism]=Human papillomavirus type 16
[Assembly]=Homodimer
[Total number of proteins]=2
[Number of unique proteins]=1
[Class]=Other
[Subclass]=E2 dimer
[PDB ID]=1r8p
[PDB chain IDs]=AB
[PDB note]=No modifications of the original PDB file. Chain identifiers are identical with the PDB's identifiers.
[PDB experimental technique]=NMR
[Evidence global]=The DNA binding domain of E2 was shown to exhibit a two-state concerted unfolding and dissociation in denaturation/renaturation experiments (PMID:8745409,PMID:8756330).
[Chain A name]=Regulatory protein E2
[Chain A source organism]=Human papillomavirus type 16
[Chain A UniProt accession]=P03120
[Chain A UniProt boundaries]=285-365
[Chain A UniProt coverage]=22.2%
[Chain A UniRef90 accession]=UniRef90_P03120
[Chain A UniRef90 boundaries]=286-365
[Chain B name]=Regulatory protein E2
[Chain B source organism]=Human papillomavirus type 16
[Chain B UniProt accession]=P03120
[Chain B UniProt boundaries]=285-365
[Chain B UniProt coverage]=22.2%
[Chain B UniRef90 accession]=UniRef90_P03120
[Chain B UniRef90 boundaries]=286-365
[Related structures]=2q79,1zzf,1by9,3mi7

[Entry]
[Accession]=MF2140006
[Name]=DNA binding domain of the E2 protein (Human papillomavirus type 18)
[Source organism]=Human papillomavirus type 18
[Assembly]=Homodimer
[Total number of proteins]=2
[Number of unique proteins]=1
[Class]=Other
[Subclass]=E2 dimer
[PDB ID]=1f9f
[PDB chain IDs]=AB
[PDB note]=Chains C and D were removed as chains A and B represent the biologically active dimer.
[PDB experimental technique]=X-ray
[PDB resolution]=1.90
[Evidence global]=The DNA binding domain of E2 was shown to exhibit a two-state concerted unfolding and dissociation in denaturation/renaturation experiments (PMID:8745409,PMID:8756330).
[Chain A name]=Regulatory protein E2
[Chain A source organism]=Human papillomavirus type 18
[Chain A UniProt accession]=P06790
[Chain A UniProt boundaries]=283-365
[Chain A UniProt coverage]=22.7%
[Chain A UniRef90 accession]=UniRef90_P06790
[Chain A UniRef90 boundaries]=287-365
[Chain B name]=Regulatory protein E2
[Chain B source organism]=Human papillomavirus type 18
[Chain B UniProt accession]=P06790
[Chain B UniProt boundaries]=283-365
[Chain B UniProt coverage]=22.7%
[Chain B UniRef90 accession]=UniRef90_P06790
[Chain B UniRef90 boundaries]=287-365
[Related structures]=1jj4

[Entry]
[Accession]=MF2140007
[Name]=DNA binding domain of the E2 protein (Human papillomavirus type 31)
[Source organism]=Human papillomavirus type 31
[Assembly]=Homodimer
[Total number of proteins]=2
[Number of unique proteins]=1
[Class]=Other
[Subclass]=E2 dimer
[PDB ID]=1dhm
[PDB chain IDs]=AB
[PDB note]=No modifications of the original PDB file. Chain identifiers are identical with the PDB's identifiers.
[PDB experimental technique]=NMR
[Evidence global]=The DNA binding domain of E2 was shown to exhibit a two-state concerted unfolding and dissociation in denaturation/renaturation experiments (PMID:8745409,PMID:8756330).
[Chain A name]=Regulatory protein E2
[Chain A source organism]=Human papillomavirus type 31
[Chain A UniProt accession]=P17383
[Chain A UniProt boundaries]=290-372
[Chain A UniProt coverage]=22.3%
[Chain A UniRef90 accession]=UniRef90_P17383
[Chain A UniRef90 boundaries]=291-372
[Chain B name]=Regulatory protein E2
[Chain B source organism]=Human papillomavirus type 31
[Chain B UniProt accession]=P17383
[Chain B UniProt boundaries]=290-372
[Chain B UniProt coverage]=22.3%
[Chain B UniRef90 accession]=UniRef90_P17383
[Chain B UniRef90 boundaries]=291-372
[Related structures]=1a7g

[Entry]
[Accession]=MF2140008
[Name]=DNA binding domain of the E2 protein (Human papillomavirus type 6a)
[Source organism]=Human papillomavirus type 6a
[Assembly]=Homodimer
[Total number of proteins]=2
[Number of unique proteins]=1
[Class]=Other
[Subclass]=E2 dimer
[PDB ID]=2aye
[PDB chain IDs]=AB
[PDB note]=Chains C, D, E and F were removed as chains A and B represent the biologically active dimer.
[PDB experimental technique]=X-ray
[PDB resolution]=2.30
[Evidence global]=The DNA binding domain of E2 was shown to exhibit a two-state concerted unfolding and dissociation in denaturation/renaturation experiments (PMID:8745409,PMID:8756330).
[Chain A name]=Regulatory protein E2
[Chain A source organism]=Human papillomavirus type 6a
[Chain A UniProt accession]=Q84294
[Chain A UniProt boundaries]=282-368
[Chain A UniProt coverage]=23.6%
[Chain A UniRef90 accession]=UniRef90_Q84294
[Chain A UniRef90 boundaries]=282-368
[Chain B name]=Regulatory protein E2
[Chain B source organism]=Human papillomavirus type 6a
[Chain B UniProt accession]=Q84294
[Chain B UniProt boundaries]=282-368
[Chain B UniProt coverage]=23.6%
[Chain B UniRef90 accession]=UniRef90_Q84294
[Chain B UniRef90 boundaries]=282-368
[Related structures]=2ayb,2ayg,1r8h

[Entry]
[Accession]=MF2140009
[Name]=DNA binding domain of the E2 protein (Bovine papillomavirus type 1)
[Source organism]=Bovine papillomavirus type 1
[Assembly]=Homodimer
[Total number of proteins]=2
[Number of unique proteins]=1
[Class]=Other
[Subclass]=E2 dimer
[PDB ID]=1dbd
[PDB chain IDs]=AB
[PDB note]=No modifications of the original PDB file. Chain identifiers are identical with the PDB's identifiers.
[PDB experimental technique]=NMR
[Evidence global]=The DNA binding domain of E2 was shown to exhibit a two-state concerted unfolding and dissociation in denaturation/renaturation experiments (PMID:8745409,PMID:8756330).
[Chain A name]=Regulatory protein E2
[Chain A source organism]=Bovine papillomavirus type 1
[Chain A UniProt accession]=P03122
[Chain A UniProt boundaries]=311-410
[Chain A UniProt coverage]=24.4%
[Chain A UniRef90 accession]=UniRef90_P03122
[Chain A UniRef90 boundaries]=311-410
[Chain B name]=Regulatory protein E2
[Chain B source organism]=Bovine papillomavirus type 1
[Chain B UniProt accession]=P03122
[Chain B UniProt boundaries]=311-410
[Chain B UniProt coverage]=24.4%
[Chain B UniRef90 accession]=UniRef90_P03122
[Chain B UniRef90 boundaries]=311-410
[Related structures]=1jjh,2bop

[Entry]
[Accession]=MF6100001
[Name]=Heat shock factor binding protein 1 (HSBP1) 
[Source organism]=Homo sapiens
[Assembly]=Homohexamer
[Total number of proteins]=6
[Number of unique proteins]=1
[Class]=Coils and zippers
[Subclass]=Coiled coil (hexameric)
[PDB ID]=3ci9
[PDB chain IDs]=ABCDEF
[PDB note]=Chains C and E were generated from chain A and chains D and F were generated from chain B using the biomatrices described in the original PDB file.
[PDB experimental technique]=X-ray
[PDB resolution]=1.80
[Evidence global]=The subunits in the structure are bound via coiled coil interactions (PMID:18767159). Coiled coils are highly versatile folding units (PMID:11166216), where the formation of the structure and the interaction between subunits is almost ubiquitously linked. This cooperative nature of binding and folding that results in a two-step process has been demonstrated for coiled coils with varying oligomeric state from dimers (PMID:9811815) and trimers (PMID:10933510) up to heptamers (PMID:17030805). While the interaction and folding are linked, in certain cases there can be significant residual structure before association (PMID:8401212). However, these residual structural elements usually encompass 1-2 turns of helices that serve as a 'nucleation site' driving interaction and helix formation (zipping up) (PMID:17438295), thus even in these cases monomeric coiled coil subunits cannot be considered to have a stable structure.
[Chain A name]=Heat shock factor-binding protein 1
[Chain A source organism]=Homo sapiens
[Chain A UniProt accession]=O75506
[Chain A UniProt boundaries]=6-53
[Chain A UniProt coverage]=63.2%
[Chain A UniRef90 accession]=UniRef90_O75506
[Chain A UniRef90 boundaries]=6-53
[Chain B name]=Heat shock factor-binding protein 1
[Chain B source organism]=Homo sapiens
[Chain B UniProt accession]=O75506
[Chain B UniProt boundaries]=6-53
[Chain B UniProt coverage]=63.2%
[Chain B UniRef90 accession]=UniRef90_O75506
[Chain B UniRef90 boundaries]=6-53
[Chain C name]=Heat shock factor-binding protein 1
[Chain C source organism]=Homo sapiens
[Chain C UniProt accession]=O75506
[Chain C UniProt boundaries]=6-53
[Chain C UniProt coverage]=63.2%
[Chain C UniRef90 accession]=UniRef90_O75506
[Chain C UniRef90 boundaries]=6-53
[Chain D name]=Heat shock factor-binding protein 1
[Chain D source organism]=Homo sapiens
[Chain D UniProt accession]=O75506
[Chain D UniProt boundaries]=6-53
[Chain D UniProt coverage]=63.2%
[Chain D UniRef90 accession]=UniRef90_O75506
[Chain D UniRef90 boundaries]=6-53
[Chain E name]=Heat shock factor-binding protein 1
[Chain E source organism]=Homo sapiens
[Chain E UniProt accession]=O75506
[Chain E UniProt boundaries]=6-53
[Chain E UniProt coverage]=63.2%
[Chain E UniRef90 accession]=UniRef90_O75506
[Chain E UniRef90 boundaries]=6-53
[Chain F name]=Heat shock factor-binding protein 1
[Chain F source organism]=Homo sapiens
[Chain F UniProt accession]=O75506
[Chain F UniProt boundaries]=6-53
[Chain F UniProt coverage]=63.2%
[Chain F UniRef90 accession]=UniRef90_O75506
[Chain F UniRef90 boundaries]=6-53

[Entry]
[Accession]=MF6120001
[Name]=4-oxalocrotonate tautomerase
[Source organism]=Pseudomonas putida
[Assembly]=Homohexamer
[Total number of proteins]=6
[Number of unique proteins]=1
[Class]=Homooligomeric enzymes
[Subclass]=Homohexameric enzymes
[PDB ID]=4x19
[PDB chain IDs]=ABCDEF
[PDB note]=Chains G, H, I, J, K, L, M, N, O, P, Q, R, S, T, U, V, W, X, Y, Z, a, b, c and d were removed as chains A, B, C, D, E and F represent the biologically active hexamer.
[PDB experimental technique]=X-ray
[PDB resolution]=1.94
[Evidence global]=4-oxalocrotonate tautomerase hexamer from Pseudomonas putida was shown by DSC to follow a two-state folding with the hexameric, dimeric and secondary structure all melting at the same temperature (PMID:20465238).
[Chain A name]=2-hydroxymuconate tautomerase
[Chain A source organism]=Pseudomonas putida
[Chain A UniProt accession]=Q01468
[Chain A UniProt boundaries]=2-63
[Chain A UniProt coverage]=98.4%
[Chain A UniRef90 accession]=UniRef90_Q01468
[Chain A UniRef90 boundaries]=2-63
[Chain B name]=2-hydroxymuconate tautomerase
[Chain B source organism]=Pseudomonas putida
[Chain B UniProt accession]=Q01468
[Chain B UniProt boundaries]=2-63
[Chain B UniProt coverage]=98.4%
[Chain B UniRef90 accession]=UniRef90_Q01468
[Chain B UniRef90 boundaries]=2-63
[Chain C name]=2-hydroxymuconate tautomerase
[Chain C source organism]=Pseudomonas putida
[Chain C UniProt accession]=Q01468
[Chain C UniProt boundaries]=2-63
[Chain C UniProt coverage]=98.4%
[Chain C UniRef90 accession]=UniRef90_Q01468
[Chain C UniRef90 boundaries]=2-63
[Chain D name]=2-hydroxymuconate tautomerase
[Chain D source organism]=Pseudomonas putida
[Chain D UniProt accession]=Q01468
[Chain D UniProt boundaries]=2-63
[Chain D UniProt coverage]=98.4%
[Chain D UniRef90 accession]=UniRef90_Q01468
[Chain D UniRef90 boundaries]=2-63
[Chain E name]=2-hydroxymuconate tautomerase
[Chain E source organism]=Pseudomonas putida
[Chain E UniProt accession]=Q01468
[Chain E UniProt boundaries]=2-63
[Chain E UniProt coverage]=98.4%
[Chain E UniRef90 accession]=UniRef90_Q01468
[Chain E UniRef90 boundaries]=2-63
[Chain F name]=2-hydroxymuconate tautomerase
[Chain F source organism]=Pseudomonas putida
[Chain F UniProt accession]=Q01468
[Chain F UniProt boundaries]=2-63
[Chain F UniProt coverage]=98.4%
[Chain F UniRef90 accession]=UniRef90_Q01468
[Chain F UniRef90 boundaries]=2-63
[Related structures]=1bjp,2fm7,4ota,4otb,4otc,4x1c,5cln,5clo

[Entry]
[Accession]=MF2120019
[Name]=Escherichia coli met repressor (MetJ)
[Source organism]=Escherichia coli
[Assembly]=Homodimer
[Total number of proteins]=2
[Number of unique proteins]=1
[Class]=Other
[Subclass]=Other
[PDB ID]=1cmb
[PDB chain IDs]=AB
[PDB note]=No modifications of the original PDB file. Chain identifiers are identical with the PDB's identifiers.
[PDB experimental technique]=X-ray
[PDB resolution]=1.80
[Evidence global]=MetJ was shown by differential scanning calorimetry to follow a two-state folding and dimerization (PMID:1390748).
[Chain A name]=Met repressor
[Chain A source organism]=Escherichia coli
[Chain A UniProt accession]=P0A8U6
[Chain A UniProt boundaries]=2-105
[Chain A UniProt coverage]=99%
[Chain A UniRef90 accession]=UniRef90_A7ZUF7
[Chain A UniRef90 boundaries]=2-105
[Chain B name]=Met repressor
[Chain B source organism]=Escherichia coli
[Chain B UniProt accession]=P0A8U6
[Chain B UniProt boundaries]=2-105
[Chain B UniProt coverage]=99%
[Chain B UniRef90 accession]=UniRef90_A7ZUF7
[Chain B UniRef90 boundaries]=2-105
[Related structures]=1cma,1cmc,1mj2,1mjk,1mjl,1mjm,1mjo,1mjp,1mjq

[Entry]
[Accession]=MF2110010
[Name]=Nerve growth factor (NGF)
[Source organism]=Mus musculus
[Assembly]=Homodimer
[Total number of proteins]=2
[Number of unique proteins]=1
[Class]=NGF-like proteins
[Subclass]=Homodimeric NGF-like proteins
[PDB ID]=1bet
[PDB chain IDs]=AB
[PDB note]=Chain B was generated from chain A using the biomatrices described in the original PDB file.
[PDB experimental technique]=X-ray
[PDB resolution]=2.30
[Evidence global]=Various dimeric members of neurotrophic factors (including human/mouse nerve growth factor, human brain-derived neurotrophic factor (BDNF), neurotrophin 3 (NT-3), and neurotrophin 4/5 (NT-4/5)) have been shown to fold and dimerize at the same time via a two-state process (PMID:8161524). While the members of this family show a significant variance in sequence, they adopt a highly similar structure upon binding and behave almost identically in unfolding/refolding experiments. Thus the two-state folding/binding nature seems to be a hallmark of NGF and closely related proteins.
[Chain A name]=Beta-nerve growth factor
[Chain A source organism]=Mus musculus
[Chain A UniProt accession]=P01139
[Chain A UniProt boundaries]=131-237
[Chain A UniProt coverage]=44.4%
[Chain A UniRef90 accession]=UniRef90_P01139
[Chain A UniRef90 boundaries]=131-237
[Chain B name]=Beta-nerve growth factor
[Chain B source organism]=Mus musculus
[Chain B UniProt accession]=P01139
[Chain B UniProt boundaries]=131-237
[Chain B UniProt coverage]=44.4%
[Chain B UniRef90 accession]=UniRef90_P01139
[Chain B UniRef90 boundaries]=131-237
[Related structures]=1btg,4eax,1sgf,4xpj

[Entry]
[Accession]=MF2100007
[Name]=Neurotrophin 3 homodimer
[Source organism]=Homo sapiens
[Assembly]=Homodimer
[Total number of proteins]=2
[Number of unique proteins]=1
[Class]=NGF-like proteins
[Subclass]=Homodimeric NGF-like proteins
[PDB ID]=1b8k
[PDB chain IDs]=AB
[PDB note]=Chain B was generated from chain A using the biomatrices described in the original PDB file.
[PDB experimental technique]=X-ray
[PDB resolution]=2.15
[Evidence global]=Various dimeric members of neurotrophic factors (including human/mouse nerve growth factor, human brain-derived neurotrophic factor (BDNF), neurotrophin 3 (NT-3), and neurotrophin 4/5 (NT-4/5)) have been shown to fold and dimerize at the same time via a two-state process (PMID:8161524). While the members of this family show a significant variance in sequence, they adopt a highly similar structure upon binding and behave almost identically in unfolding/refolding experiments. Thus the two-state folding/binding nature seems to be a hallmark of NGF and closely related proteins.
[Chain A name]=Neurotrophin-3
[Chain A source organism]=Homo sapiens
[Chain A UniProt accession]=P20783
[Chain A UniProt boundaries]=139-257
[Chain A UniProt coverage]=46.3%
[Chain A UniRef90 accession]=UniRef90_P20783
[Chain A UniRef90 boundaries]=139-257
[Chain B name]=Neurotrophin-3
[Chain B source organism]=Homo sapiens
[Chain B UniProt accession]=P20783
[Chain B UniProt boundaries]=139-257
[Chain B UniProt coverage]=46.3%
[Chain B UniRef90 accession]=UniRef90_P20783
[Chain B UniRef90 boundaries]=139-257
[Related structures]=1nt3,3buk

[Entry]
[Accession]=MF2100008
[Name]=Neurotrophin 4 homodimer
[Source organism]=Homo sapiens
[Assembly]=Homodimer
[Total number of proteins]=2
[Number of unique proteins]=1
[Class]=NGF-like proteins
[Subclass]=Homodimeric NGF-like proteins
[PDB ID]=1b98
[PDB chain IDs]=AM
[PDB note]=No modifications of the original PDB file. Chain identifiers are identical with the PDB's identifiers.
[PDB experimental technique]=X-ray
[PDB resolution]=2.75
[Evidence global]=Various dimeric members of neurotrophic factors (including human/mouse nerve growth factor, human brain-derived neurotrophic factor (BDNF), neurotrophin 3 (NT-3), and neurotrophin 4/5 (NT-4/5)) have been shown to fold and dimerize at the same time via a two-state process (PMID:8161524). While the members of this family show a significant variance in sequence, they adopt a highly similar structure upon binding and behave almost identically in unfolding/refolding experiments. Thus the two-state folding/binding nature seems to be a hallmark of NGF and closely related proteins.
[Chain A name]=Neurotrophin-4
[Chain A source organism]=Homo sapiens
[Chain A UniProt accession]=P34130
[Chain A UniProt boundaries]=81-210
[Chain A UniProt coverage]=61.9%
[Chain A UniRef90 accession]=UniRef90_P34130
[Chain A UniRef90 boundaries]=81-210
[Chain M name]=Neurotrophin-4
[Chain M source organism]=Homo sapiens
[Chain M UniProt accession]=P34130
[Chain M UniProt boundaries]=81-210
[Chain M UniProt coverage]=61.9%
[Chain M UniRef90 accession]=UniRef90_P34130
[Chain M UniRef90 boundaries]=81-210
[Related structures]=1hcf

[Entry]
[Accession]=MF2200009
[Name]=Brain-derived neurotrophic factor/neurotrophin 3 heterodimer
[Source organism]=Homo sapiens
[Assembly]=Heterodimer
[Total number of proteins]=2
[Number of unique proteins]=2
[Class]=NGF-like proteins
[Subclass]=Heterodimeric NGF-like proteins
[PDB ID]=1bnd
[PDB chain IDs]=AB
[PDB note]=No modifications of the original PDB file. Chain identifiers are identical with the PDB's identifiers.
[PDB experimental technique]=X-ray
[PDB resolution]=2.30
[Evidence global]=Various dimeric members of neurotrophic factors (including human/mouse nerve growth factor, human brain-derived neurotrophic factor (BDNF), neurotrophin 3 (NT-3), and neurotrophin 4/5 (NT-4/5)) have been shown to fold and dimerize at the same time via a two-state process (PMID:8161524). While the members of this family show a significant variance in sequence, they adopt a highly similar structure upon binding and behave almost identically in unfolding/refolding experiments. Thus the two-state folding/binding nature seems to be a hallmark of NGF and closely related proteins.
[Chain A name]=Brain-derived neurotrophic factor
[Chain A source organism]=Homo sapiens
[Chain A UniProt accession]=P23560
[Chain A UniProt boundaries]=129-247
[Chain A UniProt coverage]=48.2%
[Chain A UniRef90 accession]=UniRef90_P23560
[Chain A UniRef90 boundaries]=129-247
[Chain B name]=Neurotrophin-3
[Chain B source organism]=Homo sapiens
[Chain B UniProt accession]=P20783
[Chain B UniProt boundaries]=139-257
[Chain B UniProt coverage]=46.3%
[Chain B UniRef90 accession]=UniRef90_P20783
[Chain B UniRef90 boundaries]=139-257

[Entry]
[Accession]=MF2201009
[Name]=Brain-derived neurotrophic factor/neurotrophin 4 heterodimer
[Source organism]=Sus scrofa / Homo sapiens
[Assembly]=Heterodimer
[Total number of proteins]=2
[Number of unique proteins]=2
[Class]=NGF-like proteins
[Subclass]=Heterodimeric NGF-like proteins
[PDB ID]=1b8m
[PDB chain IDs]=AB
[PDB note]=No modifications of the original PDB file. Chain identifiers are identical with the PDB's identifiers.
[PDB experimental technique]=X-ray
[PDB resolution]=2.75
[Evidence global]=Various dimeric members of neurotrophic factors (including human/mouse nerve growth factor, human brain-derived neurotrophic factor (BDNF), neurotrophin 3 (NT-3), and neurotrophin 4/5 (NT-4/5)) have been shown to fold and dimerize at the same time via a two-state process (PMID:8161524). While the members of this family show a significant variance in sequence, they adopt a highly similar structure upon binding and behave almost identically in unfolding/refolding experiments. Thus the two-state folding/binding nature seems to be a hallmark of NGF and closely related proteins.
[Chain A name]=Brain-derived neurotrophic factor
[Chain A source organism]=Sus scrofa
[Chain A UniProt accession]=P14082
[Chain A UniProt boundaries]=134-252
[Chain A UniProt coverage]=47.2%
[Chain A UniRef90 accession]=UniRef90_P23560-3
[Chain A UniRef90 boundaries]=144-262
[Chain B name]=Neurotrophin-4
[Chain B source organism]=Homo sapiens
[Chain B UniProt accession]=P34130
[Chain B UniProt boundaries]=81-210
[Chain B UniProt coverage]=61.9%
[Chain B UniRef90 accession]=UniRef90_P34130
[Chain B UniRef90 boundaries]=81-210

[Entry]
[Accession]=MF2110011
[Name]=Ovulation-inducing factor (OIF) from llama seminal plasma
[Source organism]=Saimiri boliviensis boliviensis
[Assembly]=Homodimer
[Total number of proteins]=2
[Number of unique proteins]=1
[Class]=NGF-like proteins
[Subclass]=Homodimeric NGF-like proteins
[PDB ID]=4efv
[PDB chain IDs]=AB
[PDB note]=No modifications of the original PDB file. Chain identifiers are identical with the PDB's identifiers.
[PDB experimental technique]=X-ray
[PDB resolution]=2.32
[Evidence global]=Various dimeric members of neurotrophic factors (including human/mouse nerve growth factor, human brain-derived neurotrophic factor (BDNF), neurotrophin 3 (NT-3), and neurotrophin 4/5 (NT-4/5)) have been shown to fold and dimerize at the same time via a two-state process (PMID:8161524). While the members of this family show a significant variance in sequence, they adopt a highly similar structure upon binding and behave almost identically in unfolding/refolding experiments. Thus the two-state folding/binding nature seems to be a hallmark of NGF and closely related proteins. While OIF plays a different biological role than NGF, they share a 97% sequence identity and have virtually identical structures.
[Chain A name]=Beta-nerve growth factor
[Chain A source organism]=Saimiri boliviensis boliviensis
[Chain A UniProt accession]=Q5ISB0
[Chain A UniProt boundaries]=124-238
[Chain A UniProt coverage]=47.7%
[Chain A UniRef90 accession]=UniRef90_P13600
[Chain A UniRef90 boundaries]=124-236
[Chain B name]=Beta-nerve growth factor
[Chain B source organism]=Saimiri boliviensis boliviensis
[Chain B UniProt accession]=Q5ISB0
[Chain B UniProt boundaries]=124-238
[Chain B UniProt coverage]=47.7%
[Chain B UniRef90 accession]=UniRef90_P13600
[Chain B UniRef90 boundaries]=124-236

[Entry]
[Accession]=MF2110012
[Name]=Dimerization domain of HNF-1alpha
[Source organism]=Mus musculus
[Assembly]=Homodimer
[Total number of proteins]=2
[Number of unique proteins]=1
[Class]=Coils and zippers
[Subclass]=Coiled coil (dimeric, forming a 4-helix bundle)
[PDB ID]=1jb6
[PDB chain IDs]=AC
[PDB note]=Chain C was generated from chain A using the biomatrix described in the original PDB file. Chain B was removed as chains A and C represent the biologically active dimer.
[PDB experimental technique]=X-ray
[PDB resolution]=1.70
[Evidence global]=HNF dimer The thermal and chemical equilibrium unfolding of a 32-residue alpha-helical peptide comprising the dimerization domain of HNF-1 was monitored by circular dichroism spectroscopy. The conformational stability of this peptide was shown to be concentration dependent, and the unfolding reaction is described as a two-state transition between folded dimers and unfolded monomers (PMID:1988015).
[Chain A name]=Hepatocyte nuclear factor 1-alpha
[Chain A source organism]=Mus musculus
[Chain A UniProt accession]=P22361
[Chain A UniProt boundaries]=1-33
[Chain A UniProt coverage]=5.3%
[Chain A UniRef90 accession]=UniRef90_P22361
[Chain A UniRef90 boundaries]=2-32
[Chain C name]=Hepatocyte nuclear factor 1-alpha
[Chain C source organism]=Mus musculus
[Chain C UniProt accession]=P22361
[Chain C UniProt boundaries]=1-33
[Chain C UniProt coverage]=5.3%
[Chain C UniRef90 accession]=UniRef90_P22361
[Chain C UniRef90 boundaries]=2-32
[Related structures]=1f93,1g2y,1g2z,1g39,2gyp

[Entry]
[Accession]=MF2120020
[Name]=Factor for inversion stimulation (FIS)
[Source organism]=Escherichia coli
[Assembly]=Homodimer
[Total number of proteins]=2
[Number of unique proteins]=1
[Class]=Other
[Subclass]=Other
[PDB ID]=1ety
[PDB chain IDs]=AB
[PDB note]=No modifications of the original PDB file. Chain identifiers are identical with the PDB's identifiers.
[PDB experimental technique]=X-ray
[PDB resolution]=2.00
[Evidence global]=FIS forms an intertwined homodimer. Equilibrium and kinetic methods have shown that FIS follows a two-step folding reaction where the two unfolded monomers associate to a dimeric intermediate during a fast phase, which is followed by a slower, subsequent folding of the dimeric intermediate to the native dimer (PMID:14698300).
[Chain A name]=DNA-binding protein Fis
[Chain A source organism]=Escherichia coli
[Chain A UniProt accession]=P0A6R3
[Chain A UniProt boundaries]=10-98
[Chain A UniProt coverage]=90.8%
[Chain A UniRef90 accession]=UniRef90_A8AQG0
[Chain A UniRef90 boundaries]=10-98
[Chain B name]=DNA-binding protein Fis
[Chain B source organism]=Escherichia coli
[Chain B UniProt accession]=P0A6R3
[Chain B UniProt boundaries]=6-98
[Chain B UniProt coverage]=94.9%
[Chain B UniRef90 accession]=UniRef90_A8AQG0
[Chain B UniRef90 boundaries]=6-98
[Related structures]=1etk,1eto,1etq,1etv,1etw,1etx,1f36,1fia,1fip,3fis,4fis,4ihv,4ihw,4ihx,4ihy,3iv5,3jr9,3jra,3jrb,3jrc,3jrd,3jre,3jrf,3jrg,3jrh,3jri,5ds9,5dtd,5e3l,5e3m,5e3n,5e3o

[Entry]
[Accession]=MF4410001
[Name]=Neuronal SNARE core complex (Vamp2 / Syntaxin-1A / SNAP25)
[Source organism]=Rattus norvegicus
[Assembly]=Heterotetramer
[Total number of proteins]=4
[Number of unique proteins]=4
[Class]=Coils and zippers
[Subclass]=Coiled coil (tetrameric, 4-helix bundle)
[PDB ID]=1n7s
[PDB chain IDs]=ABCD
[PDB note]=No modifications of the original PDB file. Chain identifiers are identical with the PDB's identifiers.
[PDB experimental technique]=X-ray
[PDB resolution]=1.45
[Evidence global]=The structure shows the core domain of a SNARE complex (PMID:12496247). SNARE complexes are formed by the parallel arrangement of four protein chains bound by coiled-coil interactions forming a four helix bundle (PMID:9390521). Coiled coils are highly versatile folding units (PMID:11166216), where the formation of the structure and the interaction between subunits is almost ubiquitously linked. This cooperative nature of binding and folding that results in a two-step process has been demonstrated for coiled coils with varying oligomeric state from dimers (PMID:9811815) and trimers (PMID:10933510) up to heptamers (PMID:17030805). While the interaction and folding are linked, in certain cases there can be significant residual structure before association (PMID:8401212). However, these residual structural elements usually encompass 1-2 turns of helices that serve as a 'nucleation site' driving interaction and helix formation (zipping up) (PMID:17438295), thus even in these cases monomeric coiled coil subunits cannot be considered to have a stable structure.
[Chain A name]=Vesicle-associated membrane protein 2
[Chain A source organism]=Rattus norvegicus
[Chain A UniProt accession]=P63045
[Chain A UniProt boundaries]=27-89
[Chain A UniProt coverage]=54.3%
[Chain A UniRef90 accession]=UniRef90_P63044
[Chain A UniRef90 boundaries]=28-89
[Chain B name]=Syntaxin-1A
[Chain B source organism]=Rattus norvegicus
[Chain B UniProt accession]=P32851
[Chain B UniProt boundaries]=189-256
[Chain B UniProt coverage]=23.6%
[Chain B UniRef90 accession]=UniRef90_P32851
[Chain B UniRef90 boundaries]=191-256
[Chain C name]=Synaptosomal-associated protein 25
[Chain C source organism]=Rattus norvegicus
[Chain C UniProt accession]=P60881
[Chain C UniProt boundaries]=7-83
[Chain C UniProt coverage]=37.4%
[Chain C UniRef90 accession]=UniRef90_P60880
[Chain C UniRef90 boundaries]=7-83
[Chain D name]=Synaptosomal-associated protein 25
[Chain D source organism]=Rattus norvegicus
[Chain D UniProt accession]=P60881
[Chain D UniProt boundaries]=139-204
[Chain D UniProt coverage]=32%
[Chain D UniRef90 accession]=UniRef90_P60880
[Chain D UniRef90 boundaries]=141-204
[Related structures]=1kil,1sfc,2n1t,3hd7,3ipd,3rk2,3rk3,3rl0,5cch,5cci,5ccg

[Entry]
[Accession]=MF4400001
[Name]=Autophagic SNARE core complex (Vamp8 / Syntaxin-17 / SNAP29)
[Source organism]=Homo sapiens
[Assembly]=Heterotetramer
[Total number of proteins]=4
[Number of unique proteins]=4
[Class]=Coils and zippers
[Subclass]=Coiled coil (tetrameric, 4-helix bundle)
[PDB ID]=4wy4
[PDB chain IDs]=ABCD
[PDB note]=No modifications of the original PDB file. Chain identifiers are identical with the PDB's identifiers.
[PDB experimental technique]=X-ray
[PDB resolution]=1.40
[Evidence global]=The structure shows the core domain of a SNARE complex (PMID:25686604). SNARE complexes are formed by the parallel arrangement of four protein chains bound by coiled-coil interactions forming a four helix bundle (PMID:9390521). Coiled coils are highly versatile folding units (PMID:11166216), where the formation of the structure and the interaction between subunits is almost ubiquitously linked. This cooperative nature of binding and folding that results in a two-step process has been demonstrated for coiled coils with varying oligomeric state from dimers (PMID:9811815) and trimers (PMID:10933510) up to heptamers (PMID:17030805). While the interaction and folding are linked, in certain cases there can be significant residual structure before association (PMID:8401212). However, these residual structural elements usually encompass 1-2 turns of helices that serve as a 'nucleation site' driving interaction and helix formation (zipping up) (PMID:17438295), thus even in these cases monomeric coiled coil subunits cannot be considered to have a stable structure.
[Chain A name]=Vesicle-associated membrane protein 8
[Chain A source organism]=Homo sapiens
[Chain A UniProt accession]=Q9BV40
[Chain A UniProt boundaries]=11-74
[Chain A UniProt coverage]=64%
[Chain A UniRef90 accession]=UniRef90_Q9BV40
[Chain A UniRef90 boundaries]=11-74
[Chain B name]=Syntaxin-17
[Chain B source organism]=Homo sapiens
[Chain B UniProt accession]=P56962
[Chain B UniProt boundaries]=170-227
[Chain B UniProt coverage]=19.2%
[Chain B UniRef90 accession]=UniRef90_P56962
[Chain B UniRef90 boundaries]=170-227
[Chain C name]=Synaptosomal-associated protein 29
[Chain C source organism]=Homo sapiens
[Chain C UniProt accession]=O95721
[Chain C UniProt boundaries]=39-116
[Chain C UniProt coverage]=30.2%
[Chain C UniRef90 accession]=UniRef90_O95721
[Chain C UniRef90 boundaries]=39-116
[Chain D name]=Synaptosomal-associated protein 29
[Chain D source organism]=Homo sapiens
[Chain D UniProt accession]=O95721
[Chain D UniProt boundaries]=194-258
[Chain D UniProt coverage]=25.2%
[Chain D UniRef90 accession]=UniRef90_O95721
[Chain D UniRef90 boundaries]=194-258

[Entry]
[Accession]=MF4411001
[Name]=Endosomal SNARE core complex (Vamp4 / Vti1-rp2 / Syntaxin-6 / Syntaxin-13)
[Source organism]=Mus musculus / Rattus norvegicus / Pongo abelii
[Assembly]=Heterotetramer
[Total number of proteins]=4
[Number of unique proteins]=4
[Class]=Coils and zippers
[Subclass]=Coiled coil (tetrameric, 4-helix bundle)
[PDB ID]=2nps
[PDB chain IDs]=ABCD
[PDB note]=No modifications of the original PDB file. Chain identifiers are identical with the PDB's identifiers.
[PDB experimental technique]=X-ray
[PDB resolution]=2.50
[Evidence global]=The structure shows the core domain of a SNARE complex (PMID:17159904). SNARE complexes are formed by the parallel arrangement of four protein chains bound by coiled-coil interactions forming a four helix bundle (PMID:9390521). Coiled coils are highly versatile folding units (PMID:11166216), where the formation of the structure and the interaction between subunits is almost ubiquitously linked. This cooperative nature of binding and folding that results in a two-step process has been demonstrated for coiled coils with varying oligomeric state from dimers (PMID:9811815) and trimers (PMID:10933510) up to heptamers (PMID:17030805). While the interaction and folding are linked, in certain cases there can be significant residual structure before association (PMID:8401212). However, these residual structural elements usually encompass 1-2 turns of helices that serve as a 'nucleation site' driving interaction and helix formation (zipping up) (PMID:17438295), thus even in these cases monomeric coiled coil subunits cannot be considered to have a stable structure.
[Chain A name]=Vesicle-associated membrane protein 4
[Chain A source organism]=Mus musculus
[Chain A UniProt accession]=O70480
[Chain A UniProt boundaries]=44-117
[Chain A UniProt coverage]=52.5%
[Chain A UniRef90 accession]=UniRef90_O75379
[Chain A UniRef90 boundaries]=46-117
[Chain B name]=Syntaxin-12
[Chain B source organism]=Rattus norvegicus
[Chain B UniProt accession]=G3V7P1
[Chain B UniProt boundaries]=181-251
[Chain B UniProt coverage]=25.9%
[Chain B UniRef90 accession]=UniRef90_Q86Y82
[Chain B UniRef90 boundaries]=184-251
[Chain C name]=Vesicle transport through interaction with t-SNAREs homolog 1A
[Chain C source organism]=Rattus norvegicus
[Chain C UniProt accession]=Q9JI51
[Chain C UniProt boundaries]=119-199
[Chain C UniProt coverage]=36.2%
[Chain C UniRef90 accession]=UniRef90_Q9JI51
[Chain C UniRef90 boundaries]=122-199
[Chain D name]=Syntaxin-6
[Chain D source organism]=Pongo abelii
[Chain D UniProt accession]=Q5R6Q2
[Chain D UniProt boundaries]=169-234
[Chain D UniProt coverage]=25.9%
[Chain D UniRef90 accession]=UniRef90_O43752
[Chain D UniRef90 boundaries]=169-234

[Entry]
[Accession]=MF4411002
[Name]=Endosomal SNARE core complex (Vamp8 / Vti1-rp1 / Syntaxin-7 / Syntaxin-8)
[Source organism]=Rattus norvegicus / Mus musculus
[Assembly]=Heterotetramer
[Total number of proteins]=4
[Number of unique proteins]=4
[Class]=Coils and zippers
[Subclass]=Coiled coil (tetrameric, 4-helix bundle)
[PDB ID]=1gl2
[PDB chain IDs]=ABCD
[PDB note]=No modifications of the original PDB file. Chain identifiers are identical with the PDB's identifiers.
[PDB experimental technique]=X-ray
[PDB resolution]=1.9
[Evidence global]=The structure shows the core domain of a SNARE complex (PMID:11786915). SNARE complexes are formed by the parallel arrangement of four protein chains bound by coiled-coil interactions forming a four helix bundle (PMID:9390521). Coiled coils are highly versatile folding units (PMID:11166216), where the formation of the structure and the interaction between subunits is almost ubiquitously linked. This cooperative nature of binding and folding that results in a two-step process has been demonstrated for coiled coils with varying oligomeric state from dimers (PMID:9811815) and trimers (PMID:10933510) up to heptamers (PMID:17030805). While the interaction and folding are linked, in certain cases there can be significant residual structure before association (PMID:8401212). However, these residual structural elements usually encompass 1-2 turns of helices that serve as a 'nucleation site' driving interaction and helix formation (zipping up) (PMID:17438295), thus even in these cases monomeric coiled coil subunits cannot be considered to have a stable structure.
[Chain A name]=Vesicle-associated membrane protein 8
[Chain A source organism]=Rattus norvegicus
[Chain A UniProt accession]=Q9WUF4
[Chain A UniProt boundaries]=2-66
[Chain A UniProt coverage]=65%
[Chain A UniRef90 accession]=UniRef90_O70404
[Chain A UniRef90 boundaries]=7-67
[Chain B name]=Syntaxin-7
[Chain B source organism]=Mus musculus
[Chain B UniProt accession]=O70439
[Chain B UniProt boundaries]=165-229
[Chain B UniProt coverage]=24.9%
[Chain B UniRef90 accession]=UniRef90_O15400
[Chain B UniRef90 boundaries]=168-229
[Chain C name]=Vesicle transport through interaction with t-SNAREs homolog 1B
[Chain C source organism]=Mus musculus
[Chain C UniProt accession]=O88384
[Chain C UniProt boundaries]=136-200
[Chain C UniProt coverage]=28%
[Chain C UniRef90 accession]=UniRef90_O88384
[Chain C UniRef90 boundaries]=139-200
[Chain D name]=Syntaxin-8
[Chain D source organism]=Rattus norvegicus
[Chain D UniProt accession]=Q9Z2Q7
[Chain D UniProt boundaries]=145-209
[Chain D UniProt coverage]=27.5%
[Chain D UniRef90 accession]=UniRef90_Q9Z2Q7
[Chain D UniRef90 boundaries]=152-209

[Entry]
[Accession]=MF4411003
[Name]=Neuronal SNARE core complex (Syntaxin-binding protein 5 / Syntaxin-1A / SNAP25)
[Source organism]=Rattus norvegicus / Macaca mulatta
[Assembly]=Heterotetramer
[Total number of proteins]=4
[Number of unique proteins]=4
[Class]=Coils and zippers
[Subclass]=Coiled coil (tetrameric, 4-helix bundle)
[PDB ID]=1urq
[PDB chain IDs]=ABCD
[PDB note]=No modifications of the original PDB file. Chain identifiers are identical with the PDB's identifiers.
[PDB experimental technique]=X-ray
[PDB resolution]=2.0
[Evidence global]=The structure shows the core domain of a SNARE complex (PMID:15316007). SNARE complexes are formed by the parallel arrangement of four protein chains bound by coiled-coil interactions forming a four helix bundle (PMID:9390521). Coiled coils are highly versatile folding units (PMID:11166216), where the formation of the structure and the interaction between subunits is almost ubiquitously linked. This cooperative nature of binding and folding that results in a two-step process has been demonstrated for coiled coils with varying oligomeric state from dimers (PMID:9811815) and trimers (PMID:10933510) up to heptamers (PMID:17030805). While the interaction and folding are linked, in certain cases there can be significant residual structure before association (PMID:8401212). However, these residual structural elements usually encompass 1-2 turns of helices that serve as a 'nucleation site' driving interaction and helix formation (zipping up) (PMID:17438295), thus even in these cases monomeric coiled coil subunits cannot be considered to have a stable structure.
[Chain A name]=Syntaxin-binding protein 5
[Chain A source organism]=Rattus norvegicus
[Chain A UniProt accession]=Q9WU70
[Chain A UniProt boundaries]=1083-1145
[Chain A UniProt coverage]=5.5%
[Chain A UniRef90 accession]=UniRef90_Q9WU70
[Chain A UniRef90 boundaries]=1086-1145
[Chain B name]=Syntaxin-1A
[Chain B source organism]=Rattus norvegicus
[Chain B UniProt accession]=P32851
[Chain B UniProt boundaries]=185-259
[Chain B UniProt coverage]=26%
[Chain B UniRef90 accession]=UniRef90_P32851
[Chain B UniRef90 boundaries]=186-259
[Chain C name]=Synaptosomal-associated protein 25
[Chain C source organism]=Rattus norvegicus
[Chain C UniProt accession]=P60881
[Chain C UniProt boundaries]=5-83
[Chain C UniProt coverage]=38.3%
[Chain C UniRef90 accession]=UniRef90_P60880
[Chain C UniRef90 boundaries]=5-83
[Chain D name]=Synaptosomal-associated protein 25
[Chain D source organism]=Macaca mulatta
[Chain D UniProt accession]=P60881
[Chain D UniProt boundaries]=141-204
[Chain D UniProt coverage]=31.1%
[Chain D UniRef90 accession]=UniRef90_P60880
[Chain D UniRef90 boundaries]=141-204

[Entry]
[Accession]=MF4410002
[Name]=Exocytotic SNARE core complex (Synaptobrevin homolog 1 / SSO1 / Protein transport protein SEC9)
[Source organism]=Saccharomyces cerevisiae
[Assembly]=Heterotetramer
[Total number of proteins]=4
[Number of unique proteins]=4
[Class]=Coils and zippers
[Subclass]=Coiled coil (tetrameric, 4-helix bundle)
[PDB ID]=3b5n
[PDB chain IDs]=ABCD
[PDB note]=Chains E, F, G, H, I, J, K and L were removed as chains A, B, C and D represent the biologically active tetramer.
[PDB experimental technique]=X-ray
[PDB resolution]=1.60
[Evidence global]=The structure shows the core domain of a SNARE complex (PMID:17956869). SNARE complexes are formed by the parallel arrangement of four protein chains bound by coiled-coil interactions forming a four helix bundle (PMID:9390521). Coiled coils are highly versatile folding units (PMID:11166216), where the formation of the structure and the interaction between subunits is almost ubiquitously linked. This cooperative nature of binding and folding that results in a two-step process has been demonstrated for coiled coils with varying oligomeric state from dimers (PMID:9811815) and trimers (PMID:10933510) up to heptamers (PMID:17030805). While the interaction and folding are linked, in certain cases there can be significant residual structure before association (PMID:8401212). However, these residual structural elements usually encompass 1-2 turns of helices that serve as a 'nucleation site' driving interaction and helix formation (zipping up) (PMID:17438295), thus even in these cases monomeric coiled coil subunits cannot be considered to have a stable structure.
[Chain A name]=Synaptobrevin homolog 1
[Chain A source organism]=Saccharomyces cerevisiae
[Chain A UniProt accession]=P31109
[Chain A UniProt boundaries]=26-86
[Chain A UniProt coverage]=52.1%
[Chain A UniRef90 accession]=UniRef90_P31109
[Chain A UniRef90 boundaries]=27-86
[Chain B name]=Protein SSO1
[Chain B source organism]=Saccharomyces cerevisiae
[Chain B UniProt accession]=P32867
[Chain B UniProt boundaries]=189-257
[Chain B UniProt coverage]=23.8%
[Chain B UniRef90 accession]=UniRef90_P32867
[Chain B UniRef90 boundaries]=189-257
[Chain C name]=Protein transport protein SEC9
[Chain C source organism]=Saccharomyces cerevisiae
[Chain C UniProt accession]=P40357
[Chain C UniProt boundaries]=431-500
[Chain C UniProt coverage]=10.8%
[Chain C UniRef90 accession]=UniRef90_P40357
[Chain C UniRef90 boundaries]=433-499
[Chain D name]=Protein transport protein SEC9
[Chain D source organism]=Saccharomyces cerevisiae
[Chain D UniProt accession]=P40357
[Chain D UniProt boundaries]=587-650
[Chain D UniProt coverage]=9.8%
[Chain D UniRef90 accession]=UniRef90_P40357
[Chain D UniRef90 boundaries]=596-650

[Entry]
[Accession]=MF4210003
[Name]=Endosomal SNARE core complex (Syntaxin-1A / SNAP25)
[Source organism]=Rattus norvegicus
[Assembly]=Heterotetramer
[Total number of proteins]=4
[Number of unique proteins]=2
[Class]=Coils and zippers
[Subclass]=Coiled coil (tetrameric, 4-helix bundle)
[PDB ID]=1jth
[PDB chain IDs]=ABCD
[PDB note]=No modifications of the original PDB file. Chain identifiers are identical with the PDB's identifiers.
[PDB experimental technique]=X-ray
[PDB resolution]=2.00
[Evidence global]=The structure shows the core domain of a SNARE complex (PMID:11533035). SNARE complexes are formed by the parallel arrangement of four protein chains bound by coiled-coil interactions forming a four helix bundle (PMID:9390521). Coiled coils are highly versatile folding units (PMID:11166216), where the formation of the structure and the interaction between subunits is almost ubiquitously linked. This cooperative nature of binding and folding that results in a two-step process has been demonstrated for coiled coils with varying oligomeric state from dimers (PMID:9811815) and trimers (PMID:10933510) up to heptamers (PMID:17030805). While the interaction and folding are linked, in certain cases there can be significant residual structure before association (PMID:8401212). However, these residual structural elements usually encompass 1-2 turns of helices that serve as a 'nucleation site' driving interaction and helix formation (zipping up) (PMID:17438295), thus even in these cases monomeric coiled coil subunits cannot be considered to have a stable structure.
[Chain A name]=Synaptosomal-associated protein 25
[Chain A source organism]=Rattus norvegicus
[Chain A UniProt accession]=P60881
[Chain A UniProt boundaries]=1-82
[Chain A UniProt coverage]=39.8%
[Chain A UniRef90 accession]=UniRef90_P60880
[Chain A UniRef90 boundaries]=1-82
[Chain B name]=Syntaxin-1A
[Chain B source organism]=Rattus norvegicus
[Chain B UniProt accession]=P32851
[Chain B UniProt boundaries]=191-267
[Chain B UniProt coverage]=26.7%
[Chain B UniRef90 accession]=UniRef90_P32851
[Chain B UniRef90 boundaries]=191-267
[Chain C name]=Synaptosomal-associated protein 25
[Chain C source organism]=Rattus norvegicus
[Chain C UniProt accession]=P60881
[Chain C UniProt boundaries]=1-82
[Chain C UniProt coverage]=39.8%
[Chain C UniRef90 accession]=UniRef90_P60880
[Chain C UniRef90 boundaries]=1-82
[Chain D name]=Syntaxin-1A
[Chain D source organism]=Rattus norvegicus
[Chain D UniProt accession]=P32851
[Chain D UniProt boundaries]=191-267
[Chain D UniProt coverage]=26.7%
[Chain D UniRef90 accession]=UniRef90_P32851
[Chain D UniRef90 boundaries]=191-267

[Entry]
[Accession]=MF2200010
[Name]=CENP-A/histone H4 dimer (human)
[Source organism]=Homo sapiens
[Assembly]=Heterodimer
[Total number of proteins]=2
[Number of unique proteins]=2
[Class]=Histone-like interactions
[Subclass]=Histone-like complexes
[PDB ID]=3nqj
[PDB chain IDs]=AB
[PDB note]=No modifications of the original PDB file. Chain identifiers are identical with the PDB's identifiers.
[PDB experimental technique]=X-ray
[PDB resolution]=2.10
[Evidence global]=The structure shows a dimer adopting the histone fold with Centromere protein A (CENP-A) substituting histone H3 in a classical H3/H4 dimer (PMID:20739937). While CENP-A containing dimers show slight structural differences compared to H3/H4 dimers, the overall dimer and nucleosomal structure (and based on these presumably the folding kinetics) are essentially the same (PMID:22127263). Histone dimerization has been experimentally characterized to be coupled to the structure formation of both interacting partners (PMID:12779337); this synergistic folding has been shown separately for various histone dimers (PMID:15588829, PMID:15096635). Histones containing various types of monomeric subunits can exhibit varying stability and folding kinetics; however, independent of composition and folding kinetics, all histones appear to fold in a cooperative fashion that is coupled to binding (PMID:11669650).
[Chain A name]=Histone H3-like centromeric protein A
[Chain A source organism]=Homo sapiens
[Chain A UniProt accession]=P49450
[Chain A UniProt boundaries]=59-140
[Chain A UniProt coverage]=58.6%
[Chain A UniRef90 accession]=UniRef90_P49450
[Chain A UniRef90 boundaries]=60-140
[Chain B name]=Histone H4
[Chain B source organism]=Homo sapiens
[Chain B UniProt accession]=P62805
[Chain B UniProt boundaries]=20-103
[Chain B UniProt coverage]=81.6%
[Chain B UniRef90 accession]=UniRef90_P62805
[Chain B UniRef90 boundaries]=21-103
[Related structures]=3an2,3nqu,3r45,3wtp

[Entry]
[Accession]=MF2210006
[Name]=CENP-A/histone H4 dimer (Kluyveromyces lactis)
[Source organism]=Kluyveromyces lactis
[Assembly]=Heterodimer
[Total number of proteins]=2
[Number of unique proteins]=2
[Class]=Histone-like interactions
[Subclass]=Histone-like complexes
[PDB ID]=2yfw
[PDB chain IDs]=AB
[PDB note]=Chains C, D, E, F, G and H were removed as chains A and B represent the biologically relevant dimer.
[PDB experimental technique]=X-ray
[PDB resolution]=2.60
[Evidence global]=The structure shows a dimer adopting the histone fold with Centromere protein A (CENP-A) substituting histone H3 in a classical H3/H4 dimer (PMID:21606327). While CENP-A containing dimers show slight structural differences compared to H3/H4 dimers, the overall dimer and nucleosomal structure (and based on these presumably the folding kinetics) are essentially the same (PMID:22127263). Histone dimerization has been experimentally characterized to be coupled to the structure formation of both interacting partners (PMID:12779337); this synergistic folding has been shown separately for various histone dimers (PMID:15588829, PMID:15096635). Histones containing various types of monomeric subunits can exhibit varying stability and folding kinetics; however, independent of composition and folding kinetics, all histones appear to fold in a cooperative fashion that is coupled to binding (PMID:11669650).
[Chain A name]=Histone H3-like centromeric protein CSE4
[Chain A source organism]=Kluyveromyces lactis
[Chain A UniProt accession]=Q6CTI2
[Chain A UniProt boundaries]=93-184
[Chain A UniProt coverage]=50%
[Chain A UniRef90 accession]=UniRef90_Q6CTI2
[Chain A UniRef90 boundaries]=93-184
[Chain B name]=Histone H4
[Chain B source organism]=Kluyveromyces lactis
[Chain B UniProt accession]=Q6CMU6
[Chain B UniProt boundaries]=1-103
[Chain B UniProt coverage]=100%
[Chain B UniRef90 accession]=UniRef90_P02309
[Chain B UniRef90 boundaries]=18-103
[Related structures]=2yfv

[Entry]
[Accession]=MF2200011
[Name]=CENP-S/CENP-X dimer (human)
[Source organism]=Homo sapiens
[Assembly]=Heterodimer
[Total number of proteins]=2
[Number of unique proteins]=2
[Class]=Histone-like interactions
[Subclass]=Histone-like complexes
[PDB ID]=4ne3
[PDB chain IDs]=AB
[PDB note]=No modifications of the original PDB file. Chain identifiers are identical with the PDB's identifiers.
[PDB experimental technique]=X-ray
[PDB resolution]=1.80
[Evidence global]=Centromere proteins S and X (CENP-S and CENP-X), also called MHF1 and MHF2 form histone-like heterodimers (PMID:20347428). These dimers further associate with heterodimers formed by CENP-T and CENP-W and these tetrameric structures share a high degree of similarity with canonical histone multimers within the nucleosome (PMID:22304917). CENP-T-W-S-X tetramers - similarly to nucleosomes formed by histones - are able to bind and supercoil DNA (PMID:24234442). Apart from some structural differences leading to different functions (e.g. CENP-T-W-S-X tetramers show a preference for branched DNA as opposed to nucleosomes, PMID:24390579), both the overall and the underlying basic structures of nucleosomes and CENP-T-W-S-X tetramers are essentially the same with both CENP-S/CENP-X and CENP-T/W dimers forming structures nearly identical to that of histone dimers (PMID:20347428 and PMID:19070575). Histone dimerization has been experimentally characterized to be coupled to the structure formation of both interacting partners (PMID:12779337); this synergistic folding has been shown separately for various histone dimers (PMID:15588829, PMID:15096635). Histones containing various types of monomeric subunits can exhibit varying stability and folding kinetics; however, independent of composition and folding kinetics, all histones appear to fold in a cooperative fashion that is coupled to binding (PMID:11669650).
[Chain A name]=Centromere protein S
[Chain A source organism]=Homo sapiens
[Chain A UniProt accession]=Q8N2Z9
[Chain A UniProt boundaries]=14-106
[Chain A UniProt coverage]=67.4%
[Chain A UniRef90 accession]=UniRef90_Q8N2Z9
[Chain A UniRef90 boundaries]=14-105
[Chain B name]=Centromere protein X
[Chain B source organism]=Homo sapiens
[Chain B UniProt accession]=A8MT69
[Chain B UniProt boundaries]=8-81
[Chain B UniProt coverage]=91.4%
[Chain B UniRef90 accession]=UniRef90_A8MT69
[Chain B UniRef90 boundaries]=8-81
[Related structures]=4dra,4drb,4e44,4e45,4ne5,4ne6,4ndy,4ne1

[Entry]
[Accession]=MF2210007
[Name]=CENP-S/CENP-X dimer (Gallus gallus)
[Source organism]=Gallus gallus
[Assembly]=Heterodimer
[Total number of proteins]=2
[Number of unique proteins]=2
[Class]=Histone-like interactions
[Subclass]=Histone-like complexes
[PDB ID]=3b0b
[PDB chain IDs]=AD
[PDB note]=Chains B and C were removed as chains A and D represent the biologically relevant dimer.
[PDB experimental technique]=X-ray
[PDB resolution]=2.15
[Evidence global]=Centromere proteins S and X (CENP-S and CENP-X), also called MHF1 and MHF2 form histone-like heterodimers (PMID:20347428). These dimers further associate with heterodimers formed by CENP-T and CENP-W and these tetrameric structures share a high degree of similarity with canonical histone multimers within the nucleosome (PMID:22304917). CENP-T-W-S-X tetramers - similarly to nucleosomes formed by histones - are able to bind and supercoil DNA (PMID:24234442). Apart from some structural differences leading to different functions (e.g. CENP-T-W-S-X tetramers show a preference for branched DNA as opposed to nucleosomes, PMID:24390579), both the overall and the underlying basic structures of nucleosomes and CENP-T-W-S-X tetramers are essentially the same with both CENP-S/CENP-X and CENP-T/W dimers forming structures nearly identical to that of histone dimers (PMID:20347428 and PMID:19070575). Histone dimerization has been experimentally characterized to be coupled to the structure formation of both interacting partners (PMID:12779337); this synergistic folding has been shown separately for various histone dimers (PMID:15588829, PMID:15096635). Histones containing various types of monomeric subunits can exhibit varying stability and folding kinetics; however, independent of composition and folding kinetics, all histones appear to fold in a cooperative fashion that is coupled to binding (PMID:11669650).
[Chain A name]=Centromere protein S
[Chain A source organism]=Gallus gallus
[Chain A UniProt accession]=E1BSW7
[Chain A UniProt boundaries]=2-106
[Chain A UniProt coverage]=75.5%
[Chain A UniRef90 accession]=UniRef90_E1BSW7
[Chain A UniRef90 boundaries]=2-106
[Chain D name]=Centromere protein X
[Chain D source organism]=Gallus gallus
[Chain D UniProt accession]=P0DJH7
[Chain D UniProt boundaries]=2-80
[Chain D UniProt coverage]=98.8%
[Chain D UniRef90 accession]=UniRef90_P0DJH7
[Chain D UniRef90 boundaries]=2-80
[Related structures]=3vh5,3vh6

[Entry]
[Accession]=MF2210008
[Name]=MHF complex (Saccharomyces cerevisiae)
[Source organism]=Saccharomyces cerevisiae
[Assembly]=Heterodimer
[Total number of proteins]=2
[Number of unique proteins]=2
[Class]=Histone-like interactions
[Subclass]=Histone-like complexes
[PDB ID]=3v9r
[PDB chain IDs]=AB
[PDB note]=Chains C and D were removed as chains A and B represent the biologically relevant dimer.
[PDB experimental technique]=X-ray
[PDB resolution]=2.40
[Evidence global]=Centromere proteins S and X (CENP-S and CENP-X), also called MHF1 and MHF2 form histone-like heterodimers (MHF complex, PMID:20347428). These dimers further associate with heterodimers formed by CENP-T and CENP-W and these tetrameric structures share a high degree of similarity with canonical histone multimers within the nucleosome (PMID:22304917). CENP-T-W-S-X tetramers - similarly to nucleosomes formed by histones - are able to bind and supercoil DNA (PMID:24234442). Apart from some structural differences leading to different functions (e.g. CENP-T-W-S-X tetramers show a preference for branched DNA as opposed to nucleosomes, PMID:24390579), both the overall and the underlying basic structures of nucleosomes and CENP-T-W-S-X tetramers are essentially the same with both CENP-S/CENP-X and CENP-T/W dimers forming structures nearly identical to that of histone dimers (PMID:20347428 and PMID:19070575). Histone dimerization has been experimentally characterized to be coupled to the structure formation of both interacting partners (PMID:12779337); this synergistic folding has been shown separately for various histone dimers (PMID:15588829, PMID:15096635). Histones containing various types of monomeric subunits can exhibit varying stability and folding kinetics; however, independent of composition and folding kinetics, all histones appear to fold in a cooperative fashion that is coupled to binding (PMID:11669650).
[Chain A name]=Uncharacterized protein YOL086W-A
[Chain A source organism]=Saccharomyces cerevisiae
[Chain A UniProt accession]=Q3E835
[Chain A UniProt boundaries]=1-90
[Chain A UniProt coverage]=100%
[Chain A UniRef90 accession]=UniRef90_Q3E835
[Chain A UniRef90 boundaries]=1-90
[Chain B name]=Uncharacterized protein YDL160C-A
[Chain B source organism]=Saccharomyces cerevisiae
[Chain B UniProt accession]=Q3E829
[Chain B UniProt boundaries]=1-80
[Chain B UniProt coverage]=100%
[Chain B UniRef90 accession]=UniRef90_Q3E829
[Chain B UniRef90 boundaries]=1-80

[Entry]
[Accession]=MF2210009
[Name]=CENP-T/CENP-W dimer (Gallus gallus)
[Source organism]=Gallus gallus
[Assembly]=Heterodimer
[Total number of proteins]=2
[Number of unique proteins]=2
[Class]=Histone-like interactions
[Subclass]=Histone-like complexes
[PDB ID]=3b0c
[PDB chain IDs]=TW
[PDB note]=No modifications of the original PDB file. Chain identifiers are identical with the PDB's identifiers.
[PDB experimental technique]=X-ray
[PDB resolution]=2.20
[Evidence global]=Centromere proteins T and W (CENP-T and CENP-W) form histone-like heterodimers (PMID:19070575). These dimers further associate with heterodimers formed by CENP-S and CENP-X and these tetrameric structures share a high degree of similarity with canonical histone multimers within the nucleosome (PMID:22304917). CENP-T-W-S-X tetramers - similarly to nucleosomes formed by histones - are able to bind and supercoil DNA (PMID:24234442). Apart from some structural differences leading to different functions (e.g. CENP-T-W-S-X tetramers show a preference for branched DNA as opposed to nucleosomes, PMID:24390579), both the overall and the underlying basic structures of nucleosomes and CENP-T-W-S-X tetramers are essentially the same with both CENP-S/CENP-X and CENP-T/W dimers forming structures nearly identical to that of histone dimers (PMID:20347428 and PMID:19070575). Histone dimerization has been experimentally characterized to be coupled to the structure formation of both interacting partners (PMID:12779337); this synergistic folding has been shown separately for various histone dimers (PMID:15588829, PMID:15096635). Histones containing various types of monomeric subunits can exhibit varying stability and folding kinetics; however, independent of composition and folding kinetics, all histones appear to fold in a cooperative fashion that is coupled to binding (PMID:11669650).
[Chain T name]=Centromere protein T
[Chain T source organism]=Gallus gallus
[Chain T UniProt accession]=F1NPG5
[Chain T UniProt boundaries]=529-639
[Chain T UniProt coverage]=17.4%
[Chain T UniRef90 accession]=UniRef90_F1NPG5
[Chain T UniRef90 boundaries]=531-639
[Chain W name]=Centromere protein W
[Chain W source organism]=Gallus gallus
[Chain W UniProt accession]=P0DJH6
[Chain W UniProt boundaries]=2-76
[Chain W UniProt coverage]=98.7%
[Chain W UniRef90 accession]=UniRef90_P0DJH6
[Chain W UniRef90 boundaries]=2-76
[Related structures]=3b0d,3vh5,3vh6

[Entry]
[Accession]=MF4110008
[Name]=Oligomerization domain of Drosophila melanogaster p53
[Source organism]=Drosophila melanogaster
[Assembly]=Homotetramer
[Total number of proteins]=4
[Number of unique proteins]=1
[Class]=Other
[Subclass]=p53 tetramerization
[PDB ID]=2rp4
[PDB chain IDs]=ABCD
[PDB note]=No modifications of the original PDB file. Chain identifiers are identical with the PDB's identifiers.
[PDB experimental technique]=NMR
[Evidence global]=While the C-terminal region of p53 from humans and D. melanogaster do not share a high degree of sequential identity, they are structurally and functionally similar (PMID:10778859). The oligomerization domain (OD) of D. melanogaster p53 (Dmp53) includes the structural elements of that of human p53 exhibiting a four-helix bundle structure bound by hydrophobic and electrostatic interactions (PMID:8023159). Human p53 tetramer is formed as a dimer of dimers and follows a two state folding and binding process, demonstrated in several chemical and thermal denaturation/refolding experiments (PMID:9582268,PMID:18410249,PMID:19913028). The main difference between the two p53 variants are the additional structural elements in Dmp53 OD which comprise an additional helix and a beta-strand. The deletion of these structural elements destabilize the oligomer hinting at a suboptimal binding of the core structural elements compared to the human counterpart (PMID:17581633).
[Chain A name]=GH11591p
[Chain A source organism]=Drosophila melanogaster
[Chain A UniProt accession]=Q9N6D8
[Chain A UniProt boundaries]=310-385
[Chain A UniProt coverage]=19.7%
[Chain A UniRef90 accession]=UniRef90_Q9N6D8
[Chain A UniRef90 boundaries]=315-385
[Chain B name]=GH11591p
[Chain B source organism]=Drosophila melanogaster
[Chain B UniProt accession]=Q9N6D8
[Chain B UniProt boundaries]=310-385
[Chain B UniProt coverage]=19.7%
[Chain B UniRef90 accession]=UniRef90_Q9N6D8
[Chain B UniRef90 boundaries]=315-385
[Chain C name]=GH11591p
[Chain C source organism]=Drosophila melanogaster
[Chain C UniProt accession]=Q9N6D8
[Chain C UniProt boundaries]=310-385
[Chain C UniProt coverage]=19.7%
[Chain C UniRef90 accession]=UniRef90_Q9N6D8
[Chain C UniRef90 boundaries]=315-385
[Chain D name]=GH11591p
[Chain D source organism]=Drosophila melanogaster
[Chain D UniProt accession]=Q9N6D8
[Chain D UniProt boundaries]=310-385
[Chain D UniProt coverage]=19.7%
[Chain D UniRef90 accession]=UniRef90_Q9N6D8
[Chain D UniRef90 boundaries]=315-385

[Entry]
[Accession]=MF2210010
[Name]=Bulb-type mannose-binding lectin (Allium sativum)
[Source organism]=Allium sativum
[Assembly]=Heterodimer
[Total number of proteins]=2
[Number of unique proteins]=2
[Class]=Bulb-type lectin domain
[Subclass]=Heterodimeric lectin
[PDB ID]=1kj1
[PDB chain IDs]=AD
[PDB note]=Chains P and Q were removed as chains A and D represent the biologically relevant dimer.
[PDB experimental technique]=X-ray
[PDB resolution]=2.20
[Evidence global]=The association between the two subunits of mannose-binding lectin from garlic bulbs was shown to be highly reversible and can be defined as a two-state process in which the folded dimer is converted directly into the unfolded monomers (PMID:11401577).
[Chain A name]=I lectin (Precursor)
[Chain A source organism]=Allium sativum
[Chain A UniProt accession]=Q38789
[Chain A UniProt boundaries]=177-285
[Chain A UniProt coverage]=36%
[Chain A UniRef90 accession]=UniRef90_Q38789
[Chain A UniRef90 boundaries]=177-285
[Chain D name]=II lectin (Precursor)
[Chain D source organism]=Allium sativum
[Chain D UniProt accession]=Q38783
[Chain D UniProt boundaries]=29-137
[Chain D UniProt coverage]=70.3%
[Chain D UniRef90 accession]=UniRef90_Q38784
[Chain D UniRef90 boundaries]=18-126
[Related structures]=1bwu

[Entry]
[Accession]=MF2110013
[Name]=Bulb-type lectin (Allium sativum)
[Source organism]=Allium sativum
[Assembly]=Homodimer
[Total number of proteins]=2
[Number of unique proteins]=1
[Class]=Bulb-type lectin domain
[Subclass]=Homodimeric lectin
[PDB ID]=4h3o
[PDB chain IDs]=AB
[PDB note]=No modifications of the original PDB file. Chain identifiers are identical with the PDB's identifiers.
[PDB experimental technique]=X-ray
[PDB resolution]=2.17
[Evidence global]=A very closely homologous lectin of the same type from the same organism sharing a high degree of sequence and structural similarity has been shown to follow a two-state folding process (PMID:11401577).
[Chain A name]=Lectin
[Chain A source organism]=Allium sativum
[Chain A UniProt accession]=K4DIE9
[Chain A UniProt boundaries]=1-105
[Chain A UniProt coverage]=100%
[Chain A UniRef90 accession]=UniRef90_K4DIE9
[Chain A UniRef90 boundaries]=1-105
[Chain B name]=Lectin
[Chain B source organism]=Allium sativum
[Chain B UniProt accession]=K4DIE9
[Chain B UniProt boundaries]=1-105
[Chain B UniProt coverage]=100%
[Chain B UniRef90 accession]=UniRef90_K4DIE9
[Chain B UniRef90 boundaries]=1-105

[Entry]
[Accession]=MF2110014
[Name]=Mannose-binding lectin (Narcissus pseudonarcissus)
[Source organism]=Galanthus nivalis
[Assembly]=Homodimer
[Total number of proteins]=2
[Number of unique proteins]=1
[Class]=Bulb-type lectin domain
[Subclass]=Homodimeric lectin
[PDB ID]=3dzw
[PDB chain IDs]=AC
[PDB note]=Chain C was generated from chain A using the biomatrix described in the original PDB file. Chain B was removed as chains A and C represent the biologically relevant dimer.
[PDB experimental technique]=X-ray
[PDB resolution]=1.70
[Evidence global]=A closely homologous lectin of the same type sharing a high degree of sequence and structural similarity has been shown to follow a two-state folding process (PMID:11401577).
[Chain A name]=Mannose-specific lectin
[Chain A source organism]=Galanthus nivalis
[Chain A UniProt accession]=P30617
[Chain A UniProt boundaries]=24-130
[Chain A UniProt coverage]=68.2%
[Chain A UniRef90 accession]=UniRef90_P30617
[Chain A UniRef90 boundaries]=24-130
[Chain C name]=Mannose-specific lectin
[Chain C source organism]=Galanthus nivalis
[Chain C UniProt accession]=P30617
[Chain C UniProt boundaries]=24-130
[Chain C UniProt coverage]=68.2%
[Chain C UniRef90 accession]=UniRef90_P30617
[Chain C UniRef90 boundaries]=24-130
[Related structures]=1jpc,1msa,1niv,1npl

[Entry]
[Accession]=MF2110015
[Name]=Mannose-binding lectin (Polygonatum cyrtonema)
[Source organism]=Polygonatum cyrtonema
[Assembly]=Homodimer
[Total number of proteins]=2
[Number of unique proteins]=1
[Class]=Bulb-type lectin domain
[Subclass]=Homodimeric lectin
[PDB ID]=3a0e
[PDB chain IDs]=AB
[PDB note]=Chain B was generated from chain A using the biomatrix described in the original PDB file.
[PDB experimental technique]=X-ray
[PDB resolution]=2.00
[Evidence global]=A closely homologous lectin of the same type sharing a high degree of sequence and structural similarity has been shown to follow a two-state folding process (PMID:11401577).
[Chain A name]=Mannose/sialic acid-binding lectin
[Chain A source organism]=Polygonatum cyrtonema
[Chain A UniProt accession]=Q8L568
[Chain A UniProt boundaries]=29-138
[Chain A UniProt coverage]=68.8%
[Chain A UniRef90 accession]=UniRef90_Q8L568
[Chain A UniRef90 boundaries]=29-138
[Chain B name]=Mannose/sialic acid-binding lectin
[Chain B source organism]=Polygonatum cyrtonema
[Chain B UniProt accession]=Q8L568
[Chain B UniProt boundaries]=29-138
[Chain B UniProt coverage]=68.8%
[Chain B UniRef90 accession]=UniRef90_Q8L568
[Chain B UniRef90 boundaries]=29-138
[Related structures]=3a0c,3a0d

[Entry]
[Accession]=MF2210011
[Name]=Tuber agglutinin (Colocasia esculenta)
[Source organism]=Colocasia esculenta
[Assembly]=Heterodimer
[Total number of proteins]=2
[Number of unique proteins]=2
[Class]=Bulb-type lectin domain
[Subclass]=Heterodimeric lectin
[PDB ID]=5d5g
[PDB chain IDs]=AB
[PDB note]=Chains C and D were removed as chains A and B represent the biologically relevant dimer.
[PDB experimental technique]=X-ray
[PDB resolution]=1.74
[Evidence global]=A closely homologous lectin of the same type sharing a high degree of sequence and structural similarity has been shown to follow a two-state folding process (PMID:11401577).
[Chain A name]=Tuber agglutinin
[Chain A source organism]=Colocasia esculenta
[Chain A UniProt accession]=R9RL27
[Chain A UniProt boundaries]=24-132
[Chain A UniProt coverage]=41.3%
[Chain A UniRef90 accession]=UniRef90_R9RL27
[Chain A UniRef90 boundaries]=24-132
[Chain B name]=Tuber agglutinin
[Chain B source organism]=Colocasia esculenta
[Chain B UniProt accession]=R9RL27
[Chain B UniProt boundaries]=140-250
[Chain B UniProt coverage]=42%
[Chain B UniRef90 accession]=UniRef90_R9RL27
[Chain B UniRef90 boundaries]=140-250
[Related structures]=5d9z,3r0e,5t1x,5t20

[Entry]
[Accession]=MF2210012
[Name]=Neoculin heterodimer (Molineria latifolia)
[Source organism]=Molineria latifolia
[Assembly]=Heterodimer
[Total number of proteins]=2
[Number of unique proteins]=2
[Class]=Bulb-type lectin domain
[Subclass]=Heterodimeric lectin
[PDB ID]=2d04
[PDB chain IDs]=AB
[PDB note]=Chains C, D, E, F, G and H were removed as chains A and B represent the biologically relevant dimer.
[PDB experimental technique]=X-ray
[PDB resolution]=2.76
[Evidence global]=A closely homologous protein (bulb-type lectin) sharing a high degree of sequence and structural similarity has been shown to follow a two-state folding process (PMID:11401577).
[Chain A name]=Curculin-2
[Chain A source organism]=Molineria latifolia
[Chain A UniProt accession]=Q6F495
[Chain A UniProt boundaries]=23-135
[Chain A UniProt coverage]=71.5%
[Chain A UniRef90 accession]=UniRef90_Q6F495
[Chain A UniRef90 boundaries]=23-135
[Chain B name]=Curculin-1
[Chain B source organism]=Molineria latifolia
[Chain B UniProt accession]=P19667
[Chain B UniProt boundaries]=23-136
[Chain B UniProt coverage]=72.2%
[Chain B UniRef90 accession]=UniRef90_P19667
[Chain B UniRef90 boundaries]=23-136
[Related structures]=2dpf

[Entry]
[Accession]=MF2210013
[Name]=Mannose-binding lectin (Crocus vernus)
[Source organism]=Crocus vernus
[Assembly]=Heterodimer
[Total number of proteins]=2
[Number of unique proteins]=2
[Class]=Bulb-type lectin domain
[Subclass]=Heterodimeric lectin
[PDB ID]=3mez
[PDB chain IDs]=AB
[PDB note]=Chains C and D were removed as chains A and B represent the biologically relevant dimer.
[PDB experimental technique]=X-ray
[PDB resolution]=1.94
[Evidence global]=A closely homologous protein (bulb-type lectin) sharing a high degree of sequence and structural similarity has been shown to follow a two-state folding process (PMID:11401577).
[Chain A name]=Mannose-specific lectin 3
[Chain A source organism]=Crocus vernus
[Chain A UniProt accession]=P86626
[Chain A UniProt boundaries]=1-111
[Chain A UniProt coverage]=49.6%
[Chain A UniRef90 accession]=UniRef90_P86626
[Chain A UniRef90 boundaries]=1-111
[Chain B name]=Mannose-specific lectin 3
[Chain B source organism]=Crocus vernus
[Chain B UniProt accession]=P86626
[Chain B UniProt boundaries]=112-224
[Chain B UniProt coverage]=50.4%
[Chain B UniRef90 accession]=UniRef90_P86626
[Chain B UniRef90 boundaries]=112-224

[Entry]
[Accession]=MF2100009
[Name]=Basic HLH/leucine zipper domain of Max
[Source organism]=Homo sapiens
[Assembly]=Homodimer
[Total number of proteins]=2
[Number of unique proteins]=1
[Class]=Other
[Subclass]=Basic helix-loop-helix (bHLH)
[PDB ID]=1r05
[PDB chain IDs]=AB
[PDB note]=No modifications of the original PDB file. Chain identifiers are identical with the PDB's identifiers.
[PDB experimental technique]=NMR
[Evidence global]=Monomeric elements of basic helix-loop-helix domains were shown to be natively unfolded with a pH-dependent premolten globule conformation, as shown by several spectroscopic techniques (NMR, fluorescence, FTIR, and circular dichroism) (PMID:20102160,PMID:8303294).
[Evidence chain A]=The 1-110 region described in DisProt entry DP00084 covers 100% of the sequence present in the structure.
[Evidence chain B]=The 1-110 region described in DisProt entry DP00084 covers 100% of the sequence present in the structure.
[Chain A name]=Protein max
[Chain A source organism]=Homo sapiens
[Chain A UniProt accession]=P61244
[Chain A UniProt boundaries]=21-107
[Chain A UniProt coverage]=54.4%
[Chain A UniRef90 accession]=UniRef90_P61244
[Chain A UniRef90 boundaries]=22-103
[Chain B name]=Protein max
[Chain B source organism]=Homo sapiens
[Chain B UniProt accession]=P61244
[Chain B UniProt boundaries]=21-107
[Chain B UniProt coverage]=54.4%
[Chain B UniRef90 accession]=UniRef90_P61244
[Chain B UniRef90 boundaries]=22-103
[Related structures]=1nlw,1an2,1hlo,5eyo

[Entry]
[Accession]=MF2100010
[Name]=Transcription factor HES-1 dimer
[Source organism]=Homo sapiens
[Assembly]=Homodimer
[Total number of proteins]=2
[Number of unique proteins]=1
[Class]=Other
[Subclass]=Basic helix-loop-helix (bHLH)
[PDB ID]=2mh3
[PDB chain IDs]=AB
[PDB note]=No modifications of the original PDB file. Chain identifiers are identical with the PDB's identifiers.
[PDB experimental technique]=NMR
[Evidence global]=Monomeric elements of basic helix-loop-helix domains were shown to be natively unfolded with a pH-dependent premolten globule conformation, as shown by several spectroscopic techniques (NMR, fluorescence, FTIR, and circular dichroism) (PMID:20102160,PMID:8303294).
[Evidence chain A]=A close homologue sharing the same Pfam domain (PF00010.23) has been experimentally characterized as disordered in DisProt entries DP00084 and DP00672, and IDEAL entry IID00121.
[Evidence chain B]=A close homologue sharing the same Pfam domain (PF00010.23) has been experimentally characterized as disordered in DisProt entries DP00084 and DP00672, and IDEAL entry IID00121.
[Chain A name]=Transcription factor HES-1
[Chain A source organism]=Homo sapiens
[Chain A UniProt accession]=Q14469
[Chain A UniProt boundaries]=26-95
[Chain A UniProt coverage]=25%
[Chain A UniRef90 accession]=UniRef90_P35428
[Chain A UniRef90 boundaries]=27-95
[Chain B name]=Transcription factor HES-1
[Chain B source organism]=Homo sapiens
[Chain B UniProt accession]=Q14469
[Chain B UniProt boundaries]=26-95
[Chain B UniProt coverage]=25%
[Chain B UniRef90 accession]=UniRef90_P35428
[Chain B UniRef90 boundaries]=27-95

[Entry]
[Accession]=MF2100011
[Name]=DNA-binding protein inhibitor ID-3
[Source organism]=Homo sapiens
[Assembly]=Homodimer
[Total number of proteins]=2
[Number of unique proteins]=1
[Class]=Other
[Subclass]=Basic helix-loop-helix (bHLH)
[PDB ID]=2lfh
[PDB chain IDs]=AB
[PDB note]=No modifications of the original PDB file. Chain identifiers are identical with the PDB's identifiers.
[PDB experimental technique]=NMR
[Evidence global]=Monomeric elements of basic helix-loop-helix domains were shown to be natively unfolded with a pH-dependent premolten globule conformation, as shown by several spectroscopic techniques (NMR, fluorescence, FTIR, and circular dichroism) (PMID:20102160,PMID:8303294).
[Evidence chain A]=A close homologue sharing the same Pfam domain (PF00010.23) has been experimentally characterized as disordered in DisProt entries DP00084 and DP00672, and IDEAL entry IID00121.
[Evidence chain B]=A close homologue sharing the same Pfam domain (PF00010.23) has been experimentally characterized as disordered in DisProt entries DP00084 and DP00672, and IDEAL entry IID00121.
[Chain A name]=DNA-binding protein inhibitor ID-3
[Chain A source organism]=Homo sapiens
[Chain A UniProt accession]=Q02535
[Chain A UniProt boundaries]=27-83
[Chain A UniProt coverage]=47.9%
[Chain A UniRef90 accession]=UniRef90_P41133
[Chain A UniRef90 boundaries]=27-83
[Chain B name]=DNA-binding protein inhibitor ID-3
[Chain B source organism]=Homo sapiens
[Chain B UniProt accession]=Q02535
[Chain B UniProt boundaries]=27-83
[Chain B UniProt coverage]=47.9%
[Chain B UniRef90 accession]=UniRef90_P41133
[Chain B UniRef90 boundaries]=27-83

[Entry]
[Accession]=MF2120021
[Name]=CesAB chaperone homodimer
[Source organism]=Escherichia coli
[Assembly]=Homodimer
[Total number of proteins]=2
[Number of unique proteins]=1
[Class]=Coils and zippers
[Subclass]=Other
[PDB ID]=2lhk
[PDB chain IDs]=AB
[PDB note]=No modifications of the original PDB file. Chain identifiers are identical with the PDB's identifiers.
[PDB experimental technique]=NMR
[Evidence global]=E. coli CesAB was shown to form a loosely packed four-helix bundle stabilized by coiled-coil interactions that are partially disrupted by packing irregularities. Thus native CesAB adopts a molted globule-like structure even in its dimeric state (PMID:22152477).
[Chain A name]=L0052
[Chain A source organism]=Escherichia coli
[Chain A UniProt accession]=O52124
[Chain A UniProt boundaries]=1-107
[Chain A UniProt coverage]=100%
[Chain A UniRef90 accession]=UniRef90_O52124
[Chain A UniRef90 boundaries]=1-107
[Chain B name]=L0052
[Chain B source organism]=Escherichia coli
[Chain B UniProt accession]=O52124
[Chain B UniProt boundaries]=1-107
[Chain B UniProt coverage]=100%
[Chain B UniRef90 accession]=UniRef90_O52124
[Chain B UniRef90 boundaries]=1-107
[Related structures]=2m1n

[Entry]
[Accession]=MF2120022
[Name]=Quorum-sensing antiactivator TraM
[Source organism]=Rhizobium radiobacter
[Assembly]=Homodimer
[Total number of proteins]=2
[Number of unique proteins]=1
[Class]=Coils and zippers
[Subclass]=Other
[PDB ID]=1rfy
[PDB chain IDs]=AC
[PDB note]=Chain C was generated from chain A using the biomatrix described in the original PDB file. Chain B was removed as chains A and C represent the biologically relevant dimer.
[PDB experimental technique]=X-ray
[PDB resolution]=1.60
[Evidence global]=TraM dimers were shown to fold/refold in a single step via a two-state mechanism using thermal unfolding experiments monitored by CD (PMID:16997969).
[Chain A name]=Transcriptional repressor TraM
[Chain A source organism]=Rhizobium radiobacter
[Chain A UniProt accession]=Q57471
[Chain A UniProt boundaries]=1-102
[Chain A UniProt coverage]=100%
[Chain A UniRef90 accession]=UniRef90_Q57471
[Chain A UniRef90 boundaries]=1-102
[Chain C name]=Transcriptional repressor TraM
[Chain C source organism]=Rhizobium radiobacter
[Chain C UniProt accession]=Q57471
[Chain C UniProt boundaries]=1-102
[Chain C UniProt coverage]=100%
[Chain C UniRef90 accession]=UniRef90_Q57471
[Chain C UniRef90 boundaries]=1-102
[Related structures]=1upg,1us6

[Entry]
[Accession]=MF2120023
[Name]=Quorum-sensing antiactivator TraM2
[Source organism]=Rhizobium radiobacter
[Assembly]=Homodimer
[Total number of proteins]=2
[Number of unique proteins]=1
[Class]=Coils and zippers
[Subclass]=Other
[PDB ID]=2hjd
[PDB chain IDs]=AB
[PDB note]=Chains C and D were removed as chains A and B represent the biologically relevant dimer.
[PDB experimental technique]=X-ray
[PDB resolution]=2.10
[Evidence global]=TraM dimers were shown to fold/refold in a single step via a two-state mechanism using thermal unfolding experiments monitored by CD (PMID:16997969).
[Chain A name]=Quorum-sensing antiactivator
[Chain A source organism]=Rhizobium radiobacter
[Chain A UniProt accession]=Q20HX4
[Chain A UniProt boundaries]=1-102
[Chain A UniProt coverage]=100%
[Chain A UniRef90 accession]=UniRef90_Q20HX4
[Chain A UniRef90 boundaries]=1-102
[Chain B name]=Quorum-sensing antiactivator
[Chain B source organism]=Rhizobium radiobacter
[Chain B UniProt accession]=Q20HX4
[Chain B UniProt boundaries]=1-102
[Chain B UniProt coverage]=100%
[Chain B UniRef90 accession]=UniRef90_Q20HX4
[Chain B UniRef90 boundaries]=1-102

[Entry]
[Accession]=MF5200001
[Name]=The synaptic acetylcholinesterase tetramer assembled around a polyproline-II helix
[Source organism]=Homo sapiens
[Assembly]=Heteropentamer
[Total number of proteins]=5
[Number of unique proteins]=2
[Class]=Coils and zippers
[Subclass]=Other
[PDB ID]=1vzj
[PDB chain IDs]=ABCDI
[PDB note]=Chains E, F, G, H and J were removed as chains A, B, C, D and I represent the biologically relevant oligomer.
[PDB experimental technique]=X-ray
[PDB resolution]=2.35
[Evidence global]=The subunits in the structure are bound via coiled coil interactions (PMID:15526038). Coiled coils are highly versatile folding units (PMID:11166216), where the formation of the structure and the interaction between subunits is almost ubiquitously linked. This cooperative nature of binding and folding that results in a two-step process has been demonstrated for coiled coils with varying oligomeric state from dimers (PMID:9811815) and trimers (PMID:10933510) up to heptamers (PMID:17030805). While the interaction and folding are linked, in certain cases there can be significant residual structure before association (PMID:8401212). However, these residual structural elements usually encompass 1-2 turns of helices that serve as a 'nucleation site' driving interaction and helix formation (zipping up) (PMID:17438295), thus even in these cases monomeric coiled coil subunits cannot be considered to have a stable structure.
[Chain A name]=Acetylcholinesterase
[Chain A source organism]=Homo sapiens
[Chain A UniProt accession]=P22303
[Chain A UniProt boundaries]=575-614
[Chain A UniProt coverage]=6.5%
[Chain A UniRef90 accession]=UniRef90_P22303
[Chain A UniRef90 boundaries]=575-614
[Chain B name]=Acetylcholinesterase
[Chain B source organism]=Homo sapiens
[Chain B UniProt accession]=P22303
[Chain B UniProt boundaries]=575-614
[Chain B UniProt coverage]=6.5%
[Chain B UniRef90 accession]=UniRef90_P22303
[Chain B UniRef90 boundaries]=575-614
[Chain C name]=Acetylcholinesterase
[Chain C source organism]=Homo sapiens
[Chain C UniProt accession]=P22303
[Chain C UniProt boundaries]=575-614
[Chain C UniProt coverage]=6.5%
[Chain C UniRef90 accession]=UniRef90_P22303
[Chain C UniRef90 boundaries]=575-614
[Chain D name]=Acetylcholinesterase
[Chain D source organism]=Homo sapiens
[Chain D UniProt accession]=P22303
[Chain D UniProt boundaries]=575-614
[Chain D UniProt coverage]=6.5%
[Chain D UniRef90 accession]=UniRef90_P22303
[Chain D UniRef90 boundaries]=575-614
[Chain I name]=Acetylcholinesterase collagenic tail peptide
[Chain I source organism]=Homo sapiens
[Chain I UniProt accession]=Q9Y215
[Chain I UniProt boundaries]=53-67
[Chain I UniProt coverage]=3.3%
[Chain I UniRef90 accession]=UniRef90_Q9Y215
[Chain I UniRef90 boundaries]=?-?

[Entry]
[Accession]=MF2140010
[Name]=Antitoxin phd dimer (Escherichia virus P1)
[Source organism]=Enterobacteria phage P1
[Assembly]=Homodimer
[Total number of proteins]=2
[Number of unique proteins]=1
[Class]=Other
[Subclass]=Phd antitoxin
[PDB ID]=3hs2
[PDB chain IDs]=AB
[PDB note]=Chains C, D, E, F, G and H were removed as chains A and B represent the biologically relevant dimer.
[PDB experimental technique]=X-ray
[PDB resolution]=2.20
[Evidence global]=The dimerization of the prevents host death (phd) antitoxin from Escherichia virus P1 has been shown with differential scanning calorimetry to fit well to a two-state model consisting of a dimer unfolding into monomer species (PMID:20603017).
[Evidence chain A]=The 1-73 region described in DisProt entry DP00288 covers 100% of the sequence present in the structure.
[Evidence chain B]=The 1-73 region described in DisProt entry DP00288 covers 100% of the sequence present in the structure.
[Chain A name]=Antitoxin phd
[Chain A source organism]=Enterobacteria phage P1
[Chain A UniProt accession]=Q06253
[Chain A UniProt boundaries]=1-58
[Chain A UniProt coverage]=79.5%
[Chain A UniRef90 accession]=UniRef90_Q06253
[Chain A UniRef90 boundaries]=1-58
[Chain B name]=Antitoxin phd
[Chain B source organism]=Enterobacteria phage P1
[Chain B UniProt accession]=Q06253
[Chain B UniProt boundaries]=1-58
[Chain B UniProt coverage]=79.5%
[Chain B UniRef90 accession]=UniRef90_Q06253
[Chain B UniRef90 boundaries]=1-58
[Related structures]=3k33,3kh2,4zlx,4zm0,4zm2

[Entry]
[Accession]=MF2120024
[Name]=Antitoxin phd dimer (Mycobacterium tuberculosis)
[Source organism]=Mycobacterium tuberculosis
[Assembly]=Homodimer
[Total number of proteins]=2
[Number of unique proteins]=1
[Class]=Other
[Subclass]=Phd antitoxin
[PDB ID]=3g5o
[PDB chain IDs]=AD
[PDB note]=Chains B and C were removed as chains A and D represent the biologically relevant dimer. Chains A and D were truncated to exclude the regions in contact with chains B and C.
[PDB experimental technique]=X-ray
[PDB resolution]=2.00
[Evidence global]=The dimerization of the prevents host death (phd) antitoxin from Escherichia virus P1 has been shown with differential scanning calorimetry to fit well to a two-state model consisting of a dimer unfolding into monomer species (PMID:20603017).
[Evidence chain A]=A homologue sharing the same Pfam domain (PF02604.16) has been experimentally characterized as disordered in DisProt entry DP00288.
[Evidence chain D]=A homologue sharing the same Pfam domain (PF02604.16) has been experimentally characterized as disordered in DisProt entry DP00288.
[Chain A name]=Antitoxin RelF
[Chain A source organism]=Mycobacterium tuberculosis
[Chain A UniProt accession]=O33347
[Chain A UniProt boundaries]=1-93
[Chain A UniProt coverage]=100%
[Chain A UniRef90 accession]=UniRef90_O33347
[Chain A UniRef90 boundaries]=1-93
[Chain D name]=Antitoxin RelF
[Chain D source organism]=Mycobacterium tuberculosis
[Chain D UniProt accession]=O33347
[Chain D UniProt boundaries]=1-93
[Chain D UniProt coverage]=100%
[Chain D UniRef90 accession]=UniRef90_O33347
[Chain D UniRef90 boundaries]=1-93

[Entry]
[Accession]=MF2120025
[Name]=Docking domain A of the erythronolide synthase
[Source organism]=Saccharopolyspora erythraea
[Assembly]=Homodimer
[Total number of proteins]=2
[Number of unique proteins]=1
[Class]=Coils and zippers
[Subclass]=Coiled coil (dimeric, forming a 4-helix bundle)
[PDB ID]=1pzq
[PDB chain IDs]=AB
[PDB note]=No modifications of the original PDB file. Chain identifiers are identical with the PDB's identifiers.
[PDB experimental technique]=NMR
[Evidence global]=The subunits in the structure are bound via coiled coil interactions (PMID:12954331). Coiled coils are highly versatile folding units (PMID:11166216), where the formation of the structure and the interaction between subunits is almost ubiquitously linked. This cooperative nature of binding and folding that results in a two-step process has been demonstrated for coiled coils with varying oligomeric state from dimers (PMID:9811815) and trimers (PMID:10933510) up to heptamers (PMID:17030805). While the interaction and folding are linked, in certain cases there can be significant residual structure before association (PMID:8401212). However, these residual structural elements usually encompass 1-2 turns of helices that serve as a 'nucleation site' driving interaction and helix formation (zipping up) (PMID:17438295), thus even in these cases monomeric coiled coil subunits cannot be considered to have a stable structure.
[Chain A name]=Erythronolide synthase, modules 3 and 4
[Chain A source organism]=Saccharopolyspora erythraea
[Chain A UniProt accession]=Q03132
[Chain A UniProt boundaries]=3488-3547
[Chain A UniProt coverage]=1.7%
[Chain A UniRef90 accession]=UniRef90_Q03132
[Chain A UniRef90 boundaries]=3490-3547
[Chain B name]=Erythronolide synthase, modules 3 and 4
[Chain B source organism]=Saccharopolyspora erythraea
[Chain B UniProt accession]=Q03132
[Chain B UniProt boundaries]=3488-3547
[Chain B UniProt coverage]=1.7%
[Chain B UniRef90 accession]=UniRef90_Q03132
[Chain B UniRef90 boundaries]=3490-3547

[Entry]
[Accession]=MF2100012
[Name]=Human glutathione S-transferase A1
[Source organism]=Homo sapiens
[Assembly]=Homodimer
[Total number of proteins]=2
[Number of unique proteins]=1
[Class]=Homooligomeric enzymes
[Subclass]=Homodimeric enzymes
[PDB ID]=1k3y
[PDB chain IDs]=AB
[PDB note]=No modifications of the original PDB file. Chain identifiers are identical with the PDB's identifiers.
[PDB experimental technique]=X-ray
[PDB resolution]=1.30
[Evidence global]=The urea-induced unfolding/refolding of human glutathione S-transferase A1 dimer has been shown to be a two-state process (PMID:9548764) with the association of disordered monomers forming a structured dimer. While there may be some structuring of the monomers before dimerization, this partial structure does not fully stabilize the protein (PMID:10600132).
[Chain A name]=Glutathione S-transferase A1
[Chain A source organism]=Homo sapiens
[Chain A UniProt accession]=P08263
[Chain A UniProt boundaries]=2-222
[Chain A UniProt coverage]=99.5%
[Chain A UniRef90 accession]=UniRef90_P08263
[Chain A UniRef90 boundaries]=2-222
[Chain B name]=Glutathione S-transferase A1
[Chain B source organism]=Homo sapiens
[Chain B UniProt accession]=P08263
[Chain B UniProt boundaries]=2-222
[Chain B UniProt coverage]=99.5%
[Chain B UniRef90 accession]=UniRef90_P08263
[Chain B UniRef90 boundaries]=2-222
[Related structures]=1gsd,1gse,1gsf,1guh,1k3l,1k3o,1lbk,1pkw,1pkz,1pl1,1pl2,1usb,1xwg,1ydk,2r3x,2r6k,3i69,3i6a,3ik9,3ktl,3l0h,3q74,3u6v,3zfb,3zfl,4hj2,5jcu,5lcz,5ld0

[Entry]
[Accession]=MF2130001
[Name]=Archaeal histone hMfB
[Source organism]=Methanothermus fervidus
[Assembly]=Homodimer
[Total number of proteins]=2
[Number of unique proteins]=1
[Class]=Histone-like interactions
[Subclass]=Histone-like complexes
[PDB ID]=1bfm
[PDB chain IDs]=AB
[PDB note]=No modifications of the original PDB file. Chain identifiers are identical with the PDB's identifiers.
[PDB experimental technique]=NMR
[Evidence global]=The GdmCl-induced unfolding and refolding transitions of the dimer (monitored by stopped-flow far UV CD) provide support for a two-state equilibrium reaction with no populated intermediates. The data sets were well described by the global fits to a two-state model (PMID:15313621).
[Chain A name]=DNA-binding protein HMf-2
[Chain A source organism]=Methanothermus fervidus
[Chain A UniProt accession]=P19267
[Chain A UniProt boundaries]=1-69
[Chain A UniProt coverage]=100%
[Chain A UniRef90 accession]=UniRef90_P19267
[Chain A UniRef90 boundaries]=1-69
[Chain B name]=DNA-binding protein HMf-2
[Chain B source organism]=Methanothermus fervidus
[Chain B UniProt accession]=P19267
[Chain B UniProt boundaries]=1-69
[Chain B UniProt coverage]=100%
[Chain B UniRef90 accession]=UniRef90_P19267
[Chain B UniRef90 boundaries]=1-69
[Related structures]=1a7w,1b6w

[Entry]
[Accession]=MF2100013
[Name]=S100B
[Source organism]=Homo sapiens
[Assembly]=Homodimer
[Total number of proteins]=2
[Number of unique proteins]=1
[Class]=Other
[Subclass]=Other
[PDB ID]=1uwo
[PDB chain IDs]=AB
[PDB note]=No modifications of the original PDB file. Chain identifiers are identical with the PDB's identifiers.
[PDB experimental technique]=NMR
[Evidence global]=GuHCl-induced denaturation of the S100B protein dimer showed that it follows a two-state unfolding/refolding process (PMID:11888280).
[Chain A name]=Protein S100-B
[Chain A source organism]=Homo sapiens
[Chain A UniProt accession]=P04271
[Chain A UniProt boundaries]=2-92
[Chain A UniProt coverage]=98.9%
[Chain A UniRef90 accession]=UniRef90_P04271
[Chain A UniRef90 boundaries]=2-92
[Chain B name]=Protein S100-B
[Chain B source organism]=Homo sapiens
[Chain B UniProt accession]=P04271
[Chain B UniProt boundaries]=2-92
[Chain B UniProt coverage]=98.9%
[Chain B UniRef90 accession]=UniRef90_P04271
[Chain B UniRef90 boundaries]=2-92
[Related structures]=3czt,3d0y,3d10,2h61,3hcm,2m49,1mq1,2pru,4xyn,5csf,5csi,5csj,5csn,5d7f

[Entry]
[Accession]=MF2110016
[Name]=Dynein light chain TcTex-1
[Source organism]=Drosophila melanogaster
[Assembly]=Homodimer
[Total number of proteins]=2
[Number of unique proteins]=1
[Class]=Other
[Subclass]=Other
[PDB ID]=1ygt
[PDB chain IDs]=AB
[PDB note]=Chain B was generated from chain A using the biomatrix described in the original PDB file.
[PDB experimental technique]=X-ray
[PDB resolution]=1.70
[Evidence global]=The equilibrium unfolding transition of the dynein light chain TcTex-1 dimer was monitored by intrinsic fluorescence intensity, fluorescence anisotropy, and circular dichroism and was modeled as a two-state mechanism where a folded dimer dissociates to two unfolded monomers without populating thermodynamically stable monomeric or dimeric intermediates (PMID:16734416).
[Chain A name]=Dynein light chain Tctex-type
[Chain A source organism]=Drosophila melanogaster
[Chain A UniProt accession]=Q94524
[Chain A UniProt boundaries]=1-111
[Chain A UniProt coverage]=100%
[Chain A UniRef90 accession]=UniRef90_Q94524
[Chain A UniRef90 boundaries]=1-111
[Chain B name]=Dynein light chain Tctex-type
[Chain B source organism]=Drosophila melanogaster
[Chain B UniProt accession]=Q94524
[Chain B UniProt boundaries]=1-111
[Chain B UniProt coverage]=100%
[Chain B UniRef90 accession]=UniRef90_Q94524
[Chain B UniRef90 boundaries]=1-111
[Related structures]=3fm7,2pg1

[Entry]
[Accession]=MF2120026
[Name]=Dihydrofolate reductase
[Source organism]=Thermotoga maritima
[Assembly]=Homodimer
[Total number of proteins]=2
[Number of unique proteins]=1
[Class]=Homooligomeric enzymes
[Subclass]=Homodimeric enzymes
[PDB ID]=1cz3
[PDB chain IDs]=AB
[PDB note]=No modifications of the original PDB file. Chain identifiers are identical with the PDB's identifiers.
[PDB experimental technique]=X-ray
[PDB resolution]=2.10
[Evidence global]=The enzyme DHFR from the hyperthermophilic bacterium Thermotoga maritima represents an extremely stable dimer; no isolated structured monomers could be detected in equilibrium or during unfolding. The equilibrium unfolding strictly follows the two-state model for the dimer (PMID:10413491).
[Chain A name]=Dihydrofolate reductase
[Chain A source organism]=Thermotoga maritima
[Chain A UniProt accession]=Q60034
[Chain A UniProt boundaries]=2-165
[Chain A UniProt coverage]=97%
[Chain A UniRef90 accession]=UniRef90_Q60034
[Chain A UniRef90 boundaries]=2-165
[Chain B name]=Dihydrofolate reductase
[Chain B source organism]=Thermotoga maritima
[Chain B UniProt accession]=Q60034
[Chain B UniProt boundaries]=2-165
[Chain B UniProt coverage]=97%
[Chain B UniRef90 accession]=UniRef90_Q60034
[Chain B UniRef90 boundaries]=2-165
[Related structures]=1d1g

[Entry]
[Accession]=MF4120007
[Name]=Type II dihydrofolate reductase
[Source organism]=Escherichia coli
[Assembly]=Homotetramer
[Total number of proteins]=4
[Number of unique proteins]=1
[Class]=Homooligomeric enzymes
[Subclass]=Homotetrameric enzymes
[PDB ID]=2rh2
[PDB chain IDs]=ABCD
[PDB note]=Chains B, C and D were generated from chain A using the biomatrices described in the original PDB file.
[PDB experimental technique]=X-ray
[PDB resolution]=0.96
[Evidence global]=Using absorbance, fluorescence, and circular dichroism the unfolding of type II DHFR is protein concentration dependent and  can be described by a two-state model involving native dimer and unfolded monomer (PMID:1932013).
[Chain A name]=Dihydrofolate reductase type 2
[Chain A source organism]=Escherichia coli
[Chain A UniProt accession]=P00383
[Chain A UniProt boundaries]=17-78
[Chain A UniProt coverage]=79.5%
[Chain A UniRef90 accession]=UniRef90_P00383
[Chain A UniRef90 boundaries]=17-78
[Chain B name]=Dihydrofolate reductase type 2
[Chain B source organism]=Escherichia coli
[Chain B UniProt accession]=P00383
[Chain B UniProt boundaries]=17-78
[Chain B UniProt coverage]=79.5%
[Chain B UniRef90 accession]=UniRef90_P00383
[Chain B UniRef90 boundaries]=17-78
[Chain C name]=Dihydrofolate reductase type 2
[Chain C source organism]=Escherichia coli
[Chain C UniProt accession]=P00383
[Chain C UniProt boundaries]=17-78
[Chain C UniProt coverage]=79.5%
[Chain C UniRef90 accession]=UniRef90_P00383
[Chain C UniRef90 boundaries]=17-78
[Chain D name]=Dihydrofolate reductase type 2
[Chain D source organism]=Escherichia coli
[Chain D UniProt accession]=P00383
[Chain D UniProt boundaries]=17-78
[Chain D UniProt coverage]=79.5%
[Chain D UniRef90 accession]=UniRef90_P00383
[Chain D UniRef90 boundaries]=17-78
[Related structures]=2gqv,2p4t,2rk1,2rk2,3sfm,1vie,1vif

[Entry]
[Accession]=MF2110017
[Name]=Class pi glutathione S-transferase (Sus scrofa)
[Source organism]=Sus scrofa
[Assembly]=Homodimer
[Total number of proteins]=2
[Number of unique proteins]=1
[Class]=Homooligomeric enzymes
[Subclass]=Homodimeric enzymes
[PDB ID]=2gsr
[PDB chain IDs]=AB
[PDB note]=No modifications of the original PDB file. Chain identifiers are identical with the PDB's identifiers.
[PDB experimental technique]=X-ray
[PDB resolution]=2.11
[Evidence global]=Guanidine hydrochloride and urea induced denaturation of the dimer is well described by a two-state model involving significant populations of only the folded dimer and unfolded monomer. Neither a folded, active monomeric form nor stable unfolding intermediates were detected (PMID:1930226).
[Chain A name]=Glutathione S-transferase P
[Chain A source organism]=Sus scrofa
[Chain A UniProt accession]=P80031
[Chain A UniProt boundaries]=1-206
[Chain A UniProt coverage]=99.5%
[Chain A UniRef90 accession]=UniRef90_P80031
[Chain A UniRef90 boundaries]=1-206
[Chain B name]=Glutathione S-transferase P
[Chain B source organism]=Sus scrofa
[Chain B UniProt accession]=P80031
[Chain B UniProt boundaries]=1-206
[Chain B UniProt coverage]=99.5%
[Chain B UniRef90 accession]=UniRef90_P80031
[Chain B UniRef90 boundaries]=1-206

[Entry]
[Accession]=MF2110018
[Name]=Glutathione S-transferase (Schistosoma japonicum)
[Source organism]=Schistosoma japonicum
[Assembly]=Homodimer
[Total number of proteins]=2
[Number of unique proteins]=1
[Class]=Homooligomeric enzymes
[Subclass]=Homodimeric enzymes
[PDB ID]=4wr4
[PDB chain IDs]=AB
[PDB note]=Chain B was generated from chain A using the biomatrix described in the original PDB file.
[PDB experimental technique]=X-ray
[PDB resolution]=1.60
[Evidence global]=Data of the urea- and temperature-induced unfolding of the dimer indicate the absence of thermodynamically stable intermediates and that the unfolding/refolding transition is a two-state process involving folded native dimer and unfolded monomer. Thermograms obtained by differential scanning microcalorimetry also fitted a two-state unfolding transition model (PMID:9041642).
[Chain A name]=Glutathione S-transferase class-mu 26 kDa isozyme
[Chain A source organism]=Schistosoma japonicum
[Chain A UniProt accession]=P08515
[Chain A UniProt boundaries]=2-217
[Chain A UniProt coverage]=99.1%
[Chain A UniRef90 accession]=UniRef90_P08515
[Chain A UniRef90 boundaries]=2-217
[Chain B name]=Glutathione S-transferase class-mu 26 kDa isozyme
[Chain B source organism]=Schistosoma japonicum
[Chain B UniProt accession]=P08515
[Chain B UniProt boundaries]=2-217
[Chain B UniProt coverage]=99.1%
[Chain B UniRef90 accession]=UniRef90_P08515
[Chain B UniRef90 boundaries]=2-217
[Related structures]=1b8x,1bg5,1dug,1gne,1gta,1gtb,1m99,1m9a,1m9b,1u87,1u88,1ua5,1y6e,3crt,3cru,3d0z,3qmz,4ai6,4akg,4akh,4aki,4ecb,4ecc,4wr5,5gzz

[Entry]
[Accession]=MF2210014
[Name]=Monellin
[Source organism]=Dioscoreophyllum cumminsii
[Assembly]=Heterodimer
[Total number of proteins]=2
[Number of unique proteins]=2
[Class]=Other
[Subclass]=Other
[PDB ID]=1krl
[PDB chain IDs]=AB
[PDB note]=Chains C and D were removed as chains A and B represent the biologically active dimer.
[PDB experimental technique]=X-ray
[PDB resolution]=1.90
[Evidence global]=The two chains of monellin have been shown to be unstructured prior to assembly of the dimer. While the native dimeric structure is reached through various competing pathways entailing different intermediates, these partially structured states can only arise after the encounter complex has been formed (PMID:22542529).
[Chain A name]=Monellin chain A
[Chain A source organism]=Dioscoreophyllum cumminsii
[Chain A UniProt accession]=P02881
[Chain A UniProt boundaries]=2-45
[Chain A UniProt coverage]=97.8%
[Chain A UniRef90 accession]=UniRef90_P02881
[Chain A UniRef90 boundaries]=2-45
[Chain B name]=Monellin chain B
[Chain B source organism]=Dioscoreophyllum cumminsii
[Chain B UniProt accession]=P02882
[Chain B UniProt boundaries]=1-50
[Chain B UniProt coverage]=100%
[Chain B UniRef90 accession]=UniRef90_P02882
[Chain B UniRef90 boundaries]=1-50
[Related structures]=3mon,4mon,3pxm,3pyj,3q2p,5lc6,5lc7

[Entry]
[Accession]=MF2120027
[Name]=Bacterial antitoxin CcdA
[Source organism]=Escherichia coli
[Assembly]=Homodimer
[Total number of proteins]=2
[Number of unique proteins]=1
[Class]=Other
[Subclass]=Ribbon-helix-helix (RHH)
[PDB ID]=2adl
[PDB chain IDs]=AB
[PDB note]=No modifications of the original PDB file. Chain identifiers are identical with the PDB's identifiers.
[PDB experimental technique]=NMR
[Evidence global]=The interacting chains form a ribbon-helix-helix (RHH) structure (PMID:17007877). These structures in general have been described with the two monomers adopting a stable conformation upon the interaction (PMID:17676053). The hydrophobic core stabilizing the complex is formed by both interactors and is thus absent prior to the interaction (PMID:25713077).
[Chain A name]=Antitoxin CcdA
[Chain A source organism]=Escherichia coli
[Chain A UniProt accession]=P62552
[Chain A UniProt boundaries]=1-72
[Chain A UniProt coverage]=100%
[Chain A UniRef90 accession]=UniRef90_P62553
[Chain A UniRef90 boundaries]=1-72
[Chain B name]=Antitoxin CcdA
[Chain B source organism]=Escherichia coli
[Chain B UniProt accession]=P62552
[Chain B UniProt boundaries]=1-72
[Chain B UniProt coverage]=100%
[Chain B UniRef90 accession]=UniRef90_P62553
[Chain B UniRef90 boundaries]=1-72
[Related structures]=2adn,2h3a,2h3c,3g7z,3hpw,3tcj

[Entry]
[Accession]=MF6110001
[Name]=Nucleoside diphosphate kinase (Dictyostelium discoideum)
[Source organism]=Dictyostelium discoideum
[Assembly]=Homohexamer
[Total number of proteins]=6
[Number of unique proteins]=1
[Class]=Homooligomeric enzymes
[Subclass]=Homohexameric enzymes
[PDB ID]=1npk
[PDB chain IDs]=ABCDEF
[PDB note]=Chains B, C, D, E and F were generated from chain A using the biomatrices described in the original PDB file.
[PDB experimental technique]=X-ray
[PDB resolution]=1.80
[Evidence global]=The hexameric NDP kinase from Dictyostelium discoideum displays one single, irreversible differential scanning calorimetry peak (Tm=62°C) over a broad protein concentration, indicating a single step denaturation. However, the P105G substitution, which affects a loop implicated in subunit contacts, yields a protein that reversibly dissociates to folded monomers at 38°C before the irreversible denaturation occurs (Tm=47°C). These data indicate a “coupling” of the quaternary structure with the tertiary structure in the wild-type, but not in the mutated protein (PMID:8663370).
[Chain A name]=Nucleoside diphosphate kinase, cytosolic
[Chain A source organism]=Dictyostelium discoideum
[Chain A UniProt accession]=P22887
[Chain A UniProt boundaries]=2-155
[Chain A UniProt coverage]=99.4%
[Chain A UniRef90 accession]=UniRef90_P22887
[Chain A UniRef90 boundaries]=2-155
[Chain B name]=Nucleoside diphosphate kinase, cytosolic
[Chain B source organism]=Dictyostelium discoideum
[Chain B UniProt accession]=P22887
[Chain B UniProt boundaries]=2-155
[Chain B UniProt coverage]=99.4%
[Chain B UniRef90 accession]=UniRef90_P22887
[Chain B UniRef90 boundaries]=2-155
[Chain C name]=Nucleoside diphosphate kinase, cytosolic
[Chain C source organism]=Dictyostelium discoideum
[Chain C UniProt accession]=P22887
[Chain C UniProt boundaries]=2-155
[Chain C UniProt coverage]=99.4%
[Chain C UniRef90 accession]=UniRef90_P22887
[Chain C UniRef90 boundaries]=2-155
[Chain D name]=Nucleoside diphosphate kinase, cytosolic
[Chain D source organism]=Dictyostelium discoideum
[Chain D UniProt accession]=P22887
[Chain D UniProt boundaries]=2-155
[Chain D UniProt coverage]=99.4%
[Chain D UniRef90 accession]=UniRef90_P22887
[Chain D UniRef90 boundaries]=2-155
[Chain E name]=Nucleoside diphosphate kinase, cytosolic
[Chain E source organism]=Dictyostelium discoideum
[Chain E UniProt accession]=P22887
[Chain E UniProt boundaries]=2-155
[Chain E UniProt coverage]=99.4%
[Chain E UniRef90 accession]=UniRef90_P22887
[Chain E UniRef90 boundaries]=2-155
[Chain F name]=Nucleoside diphosphate kinase, cytosolic
[Chain F source organism]=Dictyostelium discoideum
[Chain F UniProt accession]=P22887
[Chain F UniProt boundaries]=2-155
[Chain F UniProt coverage]=99.4%
[Chain F UniRef90 accession]=UniRef90_P22887
[Chain F UniRef90 boundaries]=2-155
[Related structures]=1b4s,1b99,1bux,1f3f,1f6t,1hhq,1hiy,1hlw,1kdn,1leo,1lwx,1mn7,1mn9,1ncl,1ndc,1ndk,1ndp,1nsp,1pae,1s5z,2bef,3fkb,4c6a,4cp5

[Entry]
[Accession]=MF2100014
[Name]=Superoxide dismutase (SOD)
[Source organism]=Homo sapiens
[Assembly]=Homodimer
[Total number of proteins]=2
[Number of unique proteins]=1
[Class]=Homooligomeric enzymes
[Subclass]=Homodimeric enzymes
[PDB ID]=2c9v
[PDB chain IDs]=AF
[PDB note]=No modifications of the original PDB file. Chain identifiers are identical with the PDB's identifiers.
[PDB experimental technique]=X-ray
[PDB resolution]=1.07
[Evidence global]=CD measurements and a global analysis decomposition of the time-resolved fluorescence decay over denaturant concentration shows the presence of an intermediate in the unfolding of human SOD by guanidinium hydrochloride. Considering previous measurements of partially denatured HSOD as a function of protein concentration (PMID:1510915), these results strongly suggest that the unfolding intermediate is a monomer that displays a molten globule state (PMID:8298055).
[Chain A name]=Superoxide dismutase [Cu-Zn]
[Chain A source organism]=Homo sapiens
[Chain A UniProt accession]=P00441
[Chain A UniProt boundaries]=2-154
[Chain A UniProt coverage]=99.4%
[Chain A UniRef90 accession]=UniRef90_P00441
[Chain A UniRef90 boundaries]=2-154
[Chain F name]=Superoxide dismutase [Cu-Zn]
[Chain F source organism]=Homo sapiens
[Chain F UniProt accession]=P00441
[Chain F UniProt boundaries]=2-154
[Chain F UniProt coverage]=99.4%
[Chain F UniRef90 accession]=UniRef90_P00441
[Chain F UniRef90 boundaries]=2-154
[Related structures]=1azv,1ba9,1dsw,1fun,1hl4,1hl5,1kmg,1l3n,1mfm,1n18,1n19,1oez,1ozt,1ozu,1p1v,1ptz,1pu0,1rk7,1sos,1spd,1uxl,1uxm,2af2,2c9s,2c9u,2gbt,2gbu,2gbv,2lu5,2mp3,2nnx,2r27,2v0a,2vr6,2vr7,2vr8,2wko,2wyt,2wyz,2wz0,2wz5,2wz6,2xjk,2xjl,2zkw,2zkx,2zky,3cqp,3cqq,3ecu,3ecv,3ecw,3gqf,3gtv,3gzo,3gzp,3gzq,3h2p,3h2q,3hff,3k91,3kh3,3kh4,3ltv,3qqd,3re0,3t5w,4a7g,4a7q,4a7s,4a7t,4a7u,4a7v,4b3e,4bcy,4bcz,4bd4,4ff9,4mcm,4mcn,4nin,4nio,4nip,4oh2,4sod,4xcr,5dli,2nam,5j0f,5j0g,5k02

[Entry]
[Accession]=MF2120028
[Name]=Subtilisin inhibitor (SSI)
[Source organism]=Streptomyces albogriseolus
[Assembly]=Homodimer
[Total number of proteins]=2
[Number of unique proteins]=1
[Class]=Other
[Subclass]=Other
[PDB ID]=3ssi
[PDB chain IDs]=AB
[PDB note]=Chain B was generated from chain A using the biomatrix described in the original PDB file.
[PDB experimental technique]=X-ray
[PDB resolution]=2.30
[Evidence global]=The thermal unfolding of SSI has been studied by differential scanning calorimetry (DSC). The DSC data show that dimeric SSI remains dimeric as the temperature is raised until it unfolds and that it then dissociates during the unfolding process (PMID:7030385).
[Chain A name]=Subtilisin inhibitor
[Chain A source organism]=Streptomyces albogriseolus
[Chain A UniProt accession]=P01006
[Chain A UniProt boundaries]=32-144
[Chain A UniProt coverage]=78.5%
[Chain A UniRef90 accession]=UniRef90_P01006
[Chain A UniRef90 boundaries]=32-144
[Chain B name]=Subtilisin inhibitor
[Chain B source organism]=Streptomyces albogriseolus
[Chain B UniProt accession]=P01006
[Chain B UniProt boundaries]=32-144
[Chain B UniProt coverage]=78.5%
[Chain B UniRef90 accession]=UniRef90_P01006
[Chain B UniRef90 boundaries]=32-144
[Related structures]=2sic,3sic,5sic

[Entry]
[Accession]=MF2110019
[Name]=4-aminobutyrate aminotransferase
[Source organism]=Sus scrofa
[Assembly]=Homodimer
[Total number of proteins]=2
[Number of unique proteins]=1
[Class]=Homooligomeric enzymes
[Subclass]=Homodimeric enzymes
[PDB ID]=1ohv
[PDB chain IDs]=AB
[PDB note]=Chains C and D were removed as chains A and B represent the biologically active dimer.
[PDB experimental technique]=X-ray
[PDB resolution]=2.30
[Evidence global]=The unfolding of pig liver 4-aminobutyrate aminotransferase by urea has been investigated at equilibrium. Unfolding of the enzyme was monitored by circular dichroism and fluorescence spectroscopy. The steepness of the fluorescence and CD changes between 2 and 8 M urea, and the lack of any discernible plateau suggests that unfolding of the protein is a cooperative process. The unfolding of 4-aminobutyrate aminotransferase as a function of urea concentration was monitored by fluorescence measurements of the tryptophanyl residues. The kinetic results indicate that the aminotransferase unfolds in a single kinetic phase (PMID:8075151).
[Chain A name]=4-aminobutyrate aminotransferase, mitochondrial
[Chain A source organism]=Sus scrofa
[Chain A UniProt accession]=P80147
[Chain A UniProt boundaries]=39-499
[Chain A UniProt coverage]=92.2%
[Chain A UniRef90 accession]=UniRef90_P80147
[Chain A UniRef90 boundaries]=39-499
[Chain B name]=4-aminobutyrate aminotransferase, mitochondrial
[Chain B source organism]=Sus scrofa
[Chain B UniProt accession]=P80147
[Chain B UniProt boundaries]=39-499
[Chain B UniProt coverage]=92.2%
[Chain B UniRef90 accession]=UniRef90_P80147
[Chain B UniRef90 boundaries]=39-499
[Related structures]=1ohw,1ohy,4y0d,4y0h,4y0i,4zsw,4zsy

[Entry]
[Accession]=MF2140011
[Name]=Dimeric Mnt repressor
[Source organism]=Enterobacteria phage P22
[Assembly]=Homodimer
[Total number of proteins]=2
[Number of unique proteins]=1
[Class]=Other
[Subclass]=Ribbon-helix-helix (RHH)
[PDB ID]=1mnt
[PDB chain IDs]=AB
[PDB note]=No modifications of the original PDB file. Chain identifiers are identical with the PDB's identifiers.
[PDB experimental technique]=NMR
[Evidence global]=The Mnt repressor shows a high degree of sequential and structural similarity with the Arc and MetJ repressors (PMID:7999761). Both of these close homologues of Mnt repressor have been shown to adopt a stable structure only via dimerization (PMID:8110744,PMID:1390748)
[Chain A name]=Regulatory protein mnt
[Chain A source organism]=Enterobacteria phage P22
[Chain A UniProt accession]=P03049
[Chain A UniProt boundaries]=2-77
[Chain A UniProt coverage]=91.6%
[Chain A UniRef90 accession]=UniRef90_P03049
[Chain A UniRef90 boundaries]=2-77
[Chain B name]=Regulatory protein mnt
[Chain B source organism]=Enterobacteria phage P22
[Chain B UniProt accession]=P03049
[Chain B UniProt boundaries]=2-77
[Chain B UniProt coverage]=91.6%
[Chain B UniRef90 accession]=UniRef90_P03049
[Chain B UniRef90 boundaries]=2-77

[Entry]
[Accession]=MF2140012
[Name]=Dimeric serine proteinase from Semliki Forest virus core protein
[Source organism]=Semliki forest virus
[Assembly]=Homodimer
[Total number of proteins]=2
[Number of unique proteins]=1
[Class]=Homooligomeric enzymes
[Subclass]=Homodimeric enzymes
[PDB ID]=1vcq
[PDB chain IDs]=AB
[PDB note]=No modifications of the original PDB file. Chain identifiers are identical with the PDB's identifiers.
[PDB experimental technique]=X-ray
[PDB resolution]=3.10
[Evidence chain A]=The 119-260 region described in DisProt entry DP00999 covers 95.3% of the sequence present in the structure.
[Evidence chain B]=The 119-260 region described in DisProt entry DP00999 covers 95.3% of the sequence present in the structure.
[Chain A name]=Structural polyprotein
[Chain A source organism]=Semliki forest virus
[Chain A UniProt accession]=P03315
[Chain A UniProt boundaries]=119-267
[Chain A UniProt coverage]=11.9%
[Chain A UniRef90 accession]=UniRef90_P03315
[Chain A UniRef90 boundaries]=119-267
[Chain B name]=Structural polyprotein
[Chain B source organism]=Semliki forest virus
[Chain B UniProt accession]=P03315
[Chain B UniProt boundaries]=119-267
[Chain B UniProt coverage]=11.9%
[Chain B UniRef90 accession]=UniRef90_P03315
[Chain B UniRef90 boundaries]=119-267
[Related structures]=1dyl,1vcp

[Entry]
[Accession]=MF2140013
[Name]=Influenza A NEP M1-binding domain
[Source organism]=Influenza A virus
[Assembly]=Homodimer
[Total number of proteins]=2
[Number of unique proteins]=1
[Class]=Coils and zippers
[Subclass]=Coiled coil (dimeric, forming a 4-helix bundle)
[PDB ID]=1pd3
[PDB chain IDs]=AB
[PDB note]=No modifications of the original PDB file. Chain identifiers are identical with the PDB's identifiers.
[PDB experimental technique]=X-ray
[PDB resolution]=2.60
[Evidence chain A]=The 1-121 region described in DisProt entry DP00871 covers 100% of a close homologue of the sequence present in the structure.
[Evidence chain B]=The 1-121 region described in DisProt entry DP00871 covers 100% of a close homologue of the sequence present in the structure.
[Chain A name]=Nuclear export protein
[Chain A source organism]=Influenza A virus
[Chain A UniProt accession]=P03508
[Chain A UniProt boundaries]=59-116
[Chain A UniProt coverage]=47.9%
[Chain A UniRef90 accession]=UniRef90_P03506
[Chain A UniRef90 boundaries]=59-116
[Chain B name]=Nuclear export protein
[Chain B source organism]=Influenza A virus
[Chain B UniProt accession]=P03508
[Chain B UniProt boundaries]=59-116
[Chain B UniProt coverage]=47.9%
[Chain B UniRef90 accession]=UniRef90_P03506
[Chain B UniRef90 boundaries]=59-116

[Entry]
[Accession]=MF2120029
[Name]=SinR dimerization domain
[Source organism]=Bacillus subtilis
[Assembly]=Homodimer
[Total number of proteins]=2
[Number of unique proteins]=1
[Class]=Other
[Subclass]=Other
[PDB ID]=2yal
[PDB chain IDs]=AB
[PDB note]=No modifications of the original PDB file. Chain identifiers are identical with the PDB's identifiers.
[PDB experimental technique]=X-ray
[PDB resolution]=2.27
[Evidence chain A]=The C-terminal dimerization regions of SirR is highly mobile evading structure determination by X-ray (PMID:23430750).
[Evidence chain B]=The C-terminal dimerization regions of SirR is highly mobile evading structure determination by X-ray (PMID:23430750).
[Chain A name]=HTH-type transcriptional regulator SinR
[Chain A source organism]=Bacillus subtilis
[Chain A UniProt accession]=P06533
[Chain A UniProt boundaries]=71-111
[Chain A UniProt coverage]=36.9%
[Chain A UniRef90 accession]=UniRef90_P06533
[Chain A UniRef90 boundaries]=74-111
[Chain B name]=HTH-type transcriptional regulator SinR
[Chain B source organism]=Bacillus subtilis
[Chain B UniProt accession]=P06533
[Chain B UniProt boundaries]=71-111
[Chain B UniProt coverage]=36.9%
[Chain B UniRef90 accession]=UniRef90_P06533
[Chain B UniRef90 boundaries]=74-111
[Related structures]=3zkc

[Entry]
[Accession]=MF2110020
[Name]=The mid-region of tropomyosin
[Source organism]=Bos taurus
[Assembly]=Homodimer
[Total number of proteins]=2
[Number of unique proteins]=1
[Class]=Coils and zippers
[Subclass]=Coiled coil (dimeric)
[PDB ID]=2b9c
[PDB chain IDs]=AB
[PDB note]=No modifications of the original PDB file. Chain identifiers are identical with the PDB's identifiers.
[PDB experimental technique]=X-ray
[PDB resolution]=2.30
[Evidence global]=The subunits in the structure are bound via coiled coil interactions (PMID:16365313). Coiled coils are highly versatile folding units (PMID:11166216), where the formation of the structure and the interaction between subunits is almost ubiquitously linked. This cooperative nature of binding and folding that results in a two-step process has been demonstrated for coiled coils with varying oligomeric state from dimers (PMID:9811815) and trimers (PMID:10933510) up to heptamers (PMID:17030805). While the interaction and folding are linked, in certain cases there can be significant residual structure before association (PMID:8401212). However, these residual structural elements usually encompass 1-2 turns of helices that serve as a 'nucleation site' driving interaction and helix formation (zipping up) (PMID:17438295), thus even in these cases monomeric coiled coil subunits cannot be considered to have a stable structure.
[Chain A name]=Tropomyosin alpha-1 chain
[Chain A source organism]=Bos taurus
[Chain A UniProt accession]=Q5KR49
[Chain A UniProt boundaries]=88-225
[Chain A UniProt coverage]=48.6%
[Chain A UniRef90 accession]=UniRef90_P09493
[Chain A UniRef90 boundaries]=88-225
[Chain B name]=Tropomyosin alpha-1 chain
[Chain B source organism]=Bos taurus
[Chain B UniProt accession]=Q5KR49
[Chain B UniProt boundaries]=88-225
[Chain B UniProt coverage]=48.6%
[Chain B UniRef90 accession]=UniRef90_P09493
[Chain B UniRef90 boundaries]=88-225
[Related structures]=2d3e,2efr,2efs,2tma

[Entry]
[Accession]=MF2120030
[Name]=Antitoxin RelB
[Source organism]=Escherichia coli
[Assembly]=Homodimer
[Total number of proteins]=2
[Number of unique proteins]=1
[Class]=Other
[Subclass]=Ribbon-helix-helix (RHH)
[PDB ID]=2k29
[PDB chain IDs]=AB
[PDB note]=No modifications of the original PDB file. Chain identifiers are identical with the PDB's identifiers.
[PDB experimental technique]=NMR
[Evidence global]=The interacting chains form a ribbon-helix-helix (RHH) structure (PMID:18501926). These structures in general have been described with the two monomers adopting a stable conformation upon the interaction (PMID:17676053). The hydrophobic core stabilizing the complex is formed by both interactors and is thus absent prior to the interaction (PMID:25713077).
[Chain A name]=Antitoxin RelB
[Chain A source organism]=Escherichia coli
[Chain A UniProt accession]=P0C079
[Chain A UniProt boundaries]=1-50
[Chain A UniProt coverage]=63.3%
[Chain A UniRef90 accession]=UniRef90_P0C079
[Chain A UniRef90 boundaries]=1-50
[Chain B name]=Antitoxin RelB
[Chain B source organism]=Escherichia coli
[Chain B UniProt accession]=P0C079
[Chain B UniProt boundaries]=1-50
[Chain B UniProt coverage]=63.3%
[Chain B UniRef90 accession]=UniRef90_P0C079
[Chain B UniRef90 boundaries]=1-50
[Related structures]=4fxe

[Entry]
[Accession]=MF2140014
[Name]=Dimerization domain of the rabies virus phosphoprotein 
[Source organism]=Rabies virus
[Assembly]=Homodimer
[Total number of proteins]=2
[Number of unique proteins]=1
[Class]=Other
[Subclass]=Other
[PDB ID]=3l32
[PDB chain IDs]=AB
[PDB note]=No modifications of the original PDB file. Chain identifiers are identical with the PDB's identifiers.
[PDB experimental technique]=X-ray
[PDB resolution]=1.50
[Evidence chain A]=The C-terminal dimerization region of SirR is highly mobile evading structure determination by X-ray (PDB:3oa1).
[Evidence chain B]=The C-terminal dimerization region of SirR is highly mobile evading structure determination by X-ray (PDB:3oa1).
[Chain A name]=Phosphoprotein
[Chain A source organism]=Rabies virus
[Chain A UniProt accession]=Q0GBY3
[Chain A UniProt boundaries]=89-133
[Chain A UniProt coverage]=15.2%
[Chain A UniRef90 accession]=UniRef90_P22363
[Chain A UniRef90 boundaries]=90-133
[Chain B name]=Phosphoprotein
[Chain B source organism]=Rabies virus
[Chain B UniProt accession]=Q0GBY3
[Chain B UniProt boundaries]=89-133
[Chain B UniProt coverage]=15.2%
[Chain B UniRef90 accession]=UniRef90_P22363
[Chain B UniRef90 boundaries]=90-133

[Entry]
[Accession]=MF2140015
[Name]=Capsid protein C fragment from dengue virus capsid protein
[Source organism]=Dengue virus type 2
[Assembly]=Homodimer
[Total number of proteins]=2
[Number of unique proteins]=1
[Class]=Other
[Subclass]=Other
[PDB ID]=1r6r
[PDB chain IDs]=AB
[PDB note]=No modifications of the original PDB file. Chain identifiers are identical with the PDB's identifiers.
[PDB experimental technique]=NMR
[Evidence chain A]=The 1-100 region described in DisProt entry DP00876 covers 100% of a close homologue of the sequence present in the structure.
[Evidence chain B]=The 1-100 region described in DisProt entry DP00876 covers 100% of a close homologue of the sequence present in the structure.
[Chain A name]=Genome polyprotein
[Chain A source organism]=Dengue virus type 2
[Chain A UniProt accession]=P12823
[Chain A UniProt boundaries]=1-100
[Chain A UniProt coverage]=3%
[Chain A UniRef90 accession]=UniRef90_P29991
[Chain A UniRef90 boundaries]=1-100
[Chain B name]=Genome polyprotein
[Chain B source organism]=Dengue virus type 2
[Chain B UniProt accession]=P12823
[Chain B UniProt boundaries]=1-100
[Chain B UniProt coverage]=3%
[Chain B UniRef90 accession]=UniRef90_P29991
[Chain B UniRef90 boundaries]=1-100

[Entry]
[Accession]=MF2110021
[Name]=ID2 HLH homodimer
[Source organism]=Sus scrofa
[Assembly]=Homodimer
[Total number of proteins]=2
[Number of unique proteins]=1
[Class]=Other
[Subclass]=Basic helix-loop-helix (bHLH)
[PDB ID]=4aya
[PDB chain IDs]=AB
[PDB note]=No modifications of the original PDB file. Chain identifiers are identical with the PDB's identifiers.
[PDB experimental technique]=X-ray
[PDB resolution]=2.10
[Evidence global]=Monomeric elements of basic helix-loop-helix domains were shown to be natively unfolded with a pH-dependent premolten globule conformation, as shown by several spectroscopic techniques (NMR, fluorescence, FTIR, and circular dichroism) (PMID:20102160,PMID:8303294).
[Chain A name]=DNA-binding protein inhibitor ID-2
[Chain A source organism]=Sus scrofa
[Chain A UniProt accession]=Q2VIU1
[Chain A UniProt boundaries]=1-82
[Chain A UniProt coverage]=61.2%
[Chain A UniRef90 accession]=UniRef90_P41136
[Chain A UniRef90 boundaries]=1-82
[Chain B name]=DNA-binding protein inhibitor ID-2
[Chain B source organism]=Sus scrofa
[Chain B UniProt accession]=Q2VIU1
[Chain B UniProt boundaries]=1-82
[Chain B UniProt coverage]=61.2%
[Chain B UniRef90 accession]=UniRef90_P41136
[Chain B UniRef90 boundaries]=1-82

[Entry]
[Accession]=MF2110022
[Name]=Cobra venom nerve growth factor (NGF)
[Source organism]=Naja atra
[Assembly]=Homodimer
[Total number of proteins]=2
[Number of unique proteins]=1
[Class]=NGF-like proteins
[Subclass]=Homodimeric NGF-like proteins
[PDB ID]=4ec7
[PDB chain IDs]=AB
[PDB note]=No modifications of the original PDB file. Chain identifiers are identical with the PDB's identifiers.
[PDB experimental technique]=X-ray
[PDB resolution]=2.60
[Evidence global]=Various dimeric members of neurotrophic factors (including human/mouse nerve growth factor, human brain-derived neurotrophic factor (BDNF), neurotrophin 3 (NT-3), and neurotrophin 4/5 (NT-4/5)) have been shown to fold and dimerize at the same time via a two-state process (PMID:8161524). While the members of this family show a significant variance in sequence, they adopt a highly similar structure upon binding and behave almost identically in unfolding/refolding experiments. Thus the two-state folding/binding nature seems to be a hallmark of NGF and closely related proteins.
[Chain A name]=Venom nerve growth factor
[Chain A source organism]=Naja atra
[Chain A UniProt accession]=P61898
[Chain A UniProt boundaries]=1-116
[Chain A UniProt coverage]=100%
[Chain A UniRef90 accession]=UniRef90_P61898
[Chain A UniRef90 boundaries]=1-116
[Chain B name]=Venom nerve growth factor
[Chain B source organism]=Naja atra
[Chain B UniProt accession]=P61898
[Chain B UniProt boundaries]=1-116
[Chain B UniProt coverage]=100%
[Chain B UniRef90 accession]=UniRef90_P61898
[Chain B UniRef90 boundaries]=1-116

[Entry]
[Accession]=MF2120031
[Name]=SopB dimerization domain
[Source organism]=Escherichia coli
[Assembly]=Homodimer
[Total number of proteins]=2
[Number of unique proteins]=1
[Class]=Other
[Subclass]=Other
[PDB ID]=3kz5
[PDB chain IDs]=BE
[PDB note]=Chain A was removed as chains B and E represent the biologically relevant dimer.
[PDB experimental technique]=X-ray
[PDB resolution]=1.58
[Evidence chain B]=The C-terminal dimerization region of SopB is highly mobile evading structure determination by X-ray (PMID:20236989).
[Evidence chain E]=The C-terminal dimerization region of SopB is highly mobile evading structure determination by X-ray (PMID:20236989).
[Chain B name]=Protein SopB
[Chain B source organism]=Escherichia coli
[Chain B UniProt accession]=P62558
[Chain B UniProt boundaries]=272-323
[Chain B UniProt coverage]=16.1%
[Chain B UniRef90 accession]=UniRef90_P62559
[Chain B UniRef90 boundaries]=279-323
[Chain E name]=Protein SopB
[Chain E source organism]=Escherichia coli
[Chain E UniProt accession]=P62558
[Chain E UniProt boundaries]=272-323
[Chain E UniProt coverage]=16.1%
[Chain E UniRef90 accession]=UniRef90_P62559
[Chain E UniRef90 boundaries]=279-323

[Entry]
[Accession]=MF2110023
[Name]=Basic HLH/leucine zipper domain of apo MITF
[Source organism]=Mus musculus
[Assembly]=Homodimer
[Total number of proteins]=2
[Number of unique proteins]=1
[Class]=Other
[Subclass]=Basic helix-loop-helix (bHLH)
[PDB ID]=4ath
[PDB chain IDs]=AB
[PDB note]=No modifications of the original PDB file. Chain identifiers are identical with the PDB's identifiers.
[PDB experimental technique]=X-ray
[PDB resolution]=1.95
[Evidence global]=Monomeric elements of basic helix-loop-helix domains were shown to be natively unfolded with a pH-dependent premolten globule conformation, as shown by several spectroscopic techniques (NMR, fluorescence, FTIR, and circular dichroism) (PMID:20102160,PMID:8303294).
[Chain A name]=Microphthalmia-associated transcription factor
[Chain A source organism]=Mus musculus
[Chain A UniProt accession]=Q08874
[Chain A UniProt boundaries]=321-403
[Chain A UniProt coverage]=15.8%
[Chain A UniRef90 accession]=UniRef90_O75030
[Chain A UniRef90 boundaries]=324-403
[Chain B name]=Microphthalmia-associated transcription factor
[Chain B source organism]=Mus musculus
[Chain B UniProt accession]=Q08874
[Chain B UniProt boundaries]=321-403
[Chain B UniProt coverage]=15.8%
[Chain B UniRef90 accession]=UniRef90_O75030
[Chain B UniRef90 boundaries]=324-403
[Related structures]=4ati,4atk

[Entry]
[Accession]=MF3100003
[Name]=Vimentin coil 1B fragment (trimeric)
[Source organism]=Homo sapiens
[Assembly]=Homotrimer
[Total number of proteins]=3
[Number of unique proteins]=1
[Class]=Coils and zippers
[Subclass]=Coiled coil (trimeric)
[PDB ID]=4ypc
[PDB chain IDs]=ABC
[PDB note]=Chains B and C were generated from chain A using the biomatrices described in the original PDB file.
[PDB experimental technique]=X-ray
[PDB resolution]=1.44
[Evidence global]=The subunits in the structure are bound via coiled coil interactions (PMID:26795465). Coiled coils are highly versatile folding units (PMID:11166216), where the formation of the structure and the interaction between subunits is almost ubiquitously linked. This cooperative nature of binding and folding that results in a two-step process has been demonstrated for coiled coils with varying oligomeric state from dimers (PMID:9811815) and trimers (PMID:10933510) up to heptamers (PMID:17030805). While the interaction and folding are linked, in certain cases there can be significant residual structure before association (PMID:8401212). However, these residual structural elements usually encompass 1-2 turns of helices that serve as a 'nucleation site' driving interaction and helix formation (zipping up) (PMID:17438295), thus even in these cases monomeric coiled coil subunits cannot be considered to have a stable structure.
[Chain A name]=Vimentin
[Chain A source organism]=Homo sapiens
[Chain A UniProt accession]=P08670
[Chain A UniProt boundaries]=161-243
[Chain A UniProt coverage]=17.8%
[Chain A UniRef90 accession]=UniRef90_P08670
[Chain A UniRef90 boundaries]=161-243
[Chain B name]=Vimentin
[Chain B source organism]=Homo sapiens
[Chain B UniProt accession]=P08670
[Chain B UniProt boundaries]=161-243
[Chain B UniProt coverage]=17.8%
[Chain B UniRef90 accession]=UniRef90_P08670
[Chain B UniRef90 boundaries]=161-243
[Chain C name]=Vimentin
[Chain C source organism]=Homo sapiens
[Chain C UniProt accession]=P08670
[Chain C UniProt boundaries]=161-243
[Chain C UniProt coverage]=17.8%
[Chain C UniRef90 accession]=UniRef90_P08670
[Chain C UniRef90 boundaries]=161-243
[Related structures]=4yv3

[Entry]
[Accession]=MF2130002
[Name]=Methionyl-tRNA synthetase from Pyrococcus abyssi
[Source organism]=Pyrococcus abyssi
[Assembly]=Homodimer
[Total number of proteins]=2
[Number of unique proteins]=1
[Class]=Other
[Subclass]=Other
[PDB ID]=1mkh
[PDB chain IDs]=AB
[PDB note]=Chain B was generated from chain A using the biomatrix described in the original PDB file.
[PDB experimental technique]=X-ray
[PDB resolution]=2.01
[Evidence chain A]=The C-terminal dimerization region of methionyl-tRNA synthetase is highly mobile evading structure determination by X-ray (PMID:14992601).
[Evidence chain B]=The C-terminal dimerization region of methionyl-tRNA synthetase is highly mobile evading structure determination by X-ray (PMID:14992601).
[Chain A name]=Methionine--tRNA ligase
[Chain A source organism]=Pyrococcus abyssi
[Chain A UniProt accession]=Q9V011
[Chain A UniProt boundaries]=616-722
[Chain A UniProt coverage]=14.8%
[Chain A UniRef90 accession]=UniRef90_Q9V011
[Chain A UniRef90 boundaries]=616-722
[Chain B name]=Methionine--tRNA ligase
[Chain B source organism]=Pyrococcus abyssi
[Chain B UniProt accession]=Q9V011
[Chain B UniProt boundaries]=616-722
[Chain B UniProt coverage]=14.8%
[Chain B UniRef90 accession]=UniRef90_Q9V011
[Chain B UniRef90 boundaries]=616-722

[Entry]
[Accession]=MF2220002
[Name]=PE25-PPE41 heterodimer from M. tuberculosis
[Source organism]=Mycobacterium tuberculosis
[Assembly]=Heterodimer
[Total number of proteins]=2
[Number of unique proteins]=2
[Class]=Other
[Subclass]=Other
[PDB ID]=4w4k
[PDB chain IDs]=AB
[PDB note]=Chains C and D were removed as chains A and B represent the biologically relevant dimer.
[PDB experimental technique]=X-ray
[PDB resolution]=1.95
[Evidence global]=Both proteins involved in the interaction evade successful expression, purification and crystallization in their monomeric form, owing to the fact that both proteins are disordered and are extremely susceptible to degradation (PMID:16690741).
[Chain A name]=PE family protein
[Chain A source organism]=Mycobacterium tuberculosis
[Chain A UniProt accession]=A0A0H3LBR3
[Chain A UniProt boundaries]=5-98
[Chain A UniProt coverage]=94.9%
[Chain A UniRef90 accession]=UniRef90_UPI0005092AC7
[Chain A UniRef90 boundaries]=1-107
[Chain B name]=PPE family protein
[Chain B source organism]=Mycobacterium tuberculosis
[Chain B UniProt accession]=A0A0H3LBN6
[Chain B UniProt boundaries]=1-174
[Chain B UniProt coverage]=89.7%
[Chain B UniRef90 accession]=UniRef90_Q79FE1
[Chain B UniRef90 boundaries]=1-174
[Related structures]=2g38,4w4l,4kxr

[Entry]
[Accession]=MF2100015
[Name]=Vimentin coil 1B fragment (dimeric)
[Source organism]=Homo sapiens
[Assembly]=Homodimer
[Total number of proteins]=2
[Number of unique proteins]=1
[Class]=Coils and zippers
[Subclass]=Coiled coil (dimeric)
[PDB ID]=3ssu
[PDB chain IDs]=AB
[PDB note]=No modifications of the original PDB file. Chain identifiers are identical with the PDB's identifiers.
[PDB experimental technique]=X-ray
[PDB resolution]=2.60
[Evidence global]=The subunits in the structure are bound via coiled coil interactions (PMID:22869704). Coiled coils are highly versatile folding units (PMID:11166216), where the formation of the structure and the interaction between subunits is almost ubiquitously linked. This cooperative nature of binding and folding that results in a two-step process has been demonstrated for coiled coils with varying oligomeric state from dimers (PMID:9811815) and trimers (PMID:10933510) up to heptamers (PMID:17030805). While the interaction and folding are linked, in certain cases there can be significant residual structure before association (PMID:8401212). However, these residual structural elements usually encompass 1-2 turns of helices that serve as a 'nucleation site' driving interaction and helix formation (zipping up) (PMID:17438295), thus even in these cases monomeric coiled coil subunits cannot be considered to have a stable structure.
[Chain A name]=Vimentin
[Chain A source organism]=Homo sapiens
[Chain A UniProt accession]=P08670
[Chain A UniProt boundaries]=97-189
[Chain A UniProt coverage]=20%
[Chain A UniRef90 accession]=UniRef90_P08670
[Chain A UniRef90 boundaries]=99-189
[Chain B name]=Vimentin
[Chain B source organism]=Homo sapiens
[Chain B UniProt accession]=P08670
[Chain B UniProt boundaries]=97-189
[Chain B UniProt coverage]=20%
[Chain B UniRef90 accession]=UniRef90_P08670
[Chain B UniRef90 boundaries]=99-189
[Related structures]=3s4r,3g1e,3swk,3uf1

[Entry]
[Accession]=MF2100016
[Name]=TRIM25 coiled-coil
[Source organism]=Homo sapiens
[Assembly]=Homodimer
[Total number of proteins]=2
[Number of unique proteins]=1
[Class]=Coils and zippers
[Subclass]=Coiled coil (dimeric)
[PDB ID]=4cfg
[PDB chain IDs]=AB
[PDB note]=No modifications of the original PDB file. Chain identifiers are identical with the PDB's identifiers.
[PDB experimental technique]=X-ray
[PDB resolution]=2.80
[Evidence global]=The subunits in the structure are bound via coiled coil interactions (PMID:24550273). Coiled coils are highly versatile folding units (PMID:11166216), where the formation of the structure and the interaction between subunits is almost ubiquitously linked. This cooperative nature of binding and folding that results in a two-step process has been demonstrated for coiled coils with varying oligomeric state from dimers (PMID:9811815) and trimers (PMID:10933510) up to heptamers (PMID:17030805). While the interaction and folding are linked, in certain cases there can be significant residual structure before association (PMID:8401212). However, these residual structural elements usually encompass 1-2 turns of helices that serve as a 'nucleation site' driving interaction and helix formation (zipping up) (PMID:17438295), thus even in these cases monomeric coiled coil subunits cannot be considered to have a stable structure.
[Chain A name]=E3 ubiquitin/ISG15 ligase TRIM25
[Chain A source organism]=Homo sapiens
[Chain A UniProt accession]=Q14258
[Chain A UniProt boundaries]=194-357
[Chain A UniProt coverage]=26%
[Chain A UniRef90 accession]=UniRef90_Q14258
[Chain A UniRef90 boundaries]=194-357
[Chain B name]=E3 ubiquitin/ISG15 ligase TRIM25
[Chain B source organism]=Homo sapiens
[Chain B UniProt accession]=Q14258
[Chain B UniProt boundaries]=194-357
[Chain B UniProt coverage]=26%
[Chain B UniRef90 accession]=UniRef90_Q14258
[Chain B UniRef90 boundaries]=194-357
[Related structures]=4ltb

[Entry]
[Accession]=MF4200001
[Name]=OPTN:TBK1 complex
[Source organism]=Homo sapiens
[Assembly]=Heterotetramer
[Total number of proteins]=4
[Number of unique proteins]=2
[Class]=Coils and zippers
[Subclass]=Coiled coil (tetrameric)
[PDB ID]=5eof
[PDB chain IDs]=ABCD
[PDB note]=No modifications of the original PDB file. Chain identifiers are identical with the PDB's identifiers.
[PDB experimental technique]=X-ray
[PDB resolution]=2.05
[Evidence global]=The subunits in the structure are bound via coiled coil interactions (PMID:27620379). Coiled coils are highly versatile folding units (PMID:11166216), where the formation of the structure and the interaction between subunits is almost ubiquitously linked. This cooperative nature of binding and folding that results in a two-step process has been demonstrated for coiled coils with varying oligomeric state from dimers (PMID:9811815) and trimers (PMID:10933510) up to heptamers (PMID:17030805). While the interaction and folding are linked, in certain cases there can be significant residual structure before association (PMID:8401212). However, these residual structural elements usually encompass 1-2 turns of helices that serve as a 'nucleation site' driving interaction and helix formation (zipping up) (PMID:17438295), thus even in these cases monomeric coiled coil subunits cannot be considered to have a stable structure.
[Chain A name]=Optineurin
[Chain A source organism]=Homo sapiens
[Chain A UniProt accession]=Q96CV9
[Chain A UniProt boundaries]=26-103
[Chain A UniProt coverage]=13.5%
[Chain A UniRef90 accession]=UniRef90_Q96CV9
[Chain A UniRef90 boundaries]=26-103
[Chain B name]=Optineurin
[Chain B source organism]=Homo sapiens
[Chain B UniProt accession]=Q96CV9
[Chain B UniProt boundaries]=26-103
[Chain B UniProt coverage]=13.5%
[Chain B UniRef90 accession]=UniRef90_Q96CV9
[Chain B UniRef90 boundaries]=26-103
[Chain C name]=Serine/threonine-protein kinase TBK1
[Chain C source organism]=Homo sapiens
[Chain C UniProt accession]=Q9UHD2
[Chain C UniProt boundaries]=677-729
[Chain C UniProt coverage]=7.3%
[Chain C UniRef90 accession]=UniRef90_Q9UHD2
[Chain C UniRef90 boundaries]=677-729
[Chain D name]=Serine/threonine-protein kinase TBK1
[Chain D source organism]=Homo sapiens
[Chain D UniProt accession]=Q9UHD2
[Chain D UniProt boundaries]=677-729
[Chain D UniProt coverage]=7.3%
[Chain D UniRef90 accession]=UniRef90_Q9UHD2
[Chain D UniRef90 boundaries]=677-729
[Related structures]=5eoa

[Entry]
[Accession]=MF4200002
[Name]=p63/p73 hetero-tetramerization domain (human)
[Source organism]=Homo sapiens
[Assembly]=Heterotetramer
[Total number of proteins]=4
[Number of unique proteins]=2
[Class]=Other
[Subclass]=p53 tetramerization
[PDB ID]=2nb1
[PDB chain IDs]=ABCD
[PDB note]=No modifications of the original PDB file. Chain identifiers are identical with the PDB's identifiers.
[PDB experimental technique]=NMR
[Evidence global]=p63 and p73 are members of the p53 protein family. The tetramerization region of p53, p63 and p73 are closely homologous to each other, having very similar sequences, structures and biological functions (PMID:25185827,PMID:18289041,PMID:20379196), all containing the same Pfam domain (PF07710). The tetramerization domain of p53 exhibits a four-helix bundle structure bound by hydrophobic and electrostatic interactions (PMID:8023159). The tetramer is formed as a dimer of dimers and follows a two state folding and binding process, demonstrated in several chemical and thermal denaturation/refolding experiments (PMID:9582268,PMID:18410249,PMID:19913028).
[Chain A name]=Tumor protein 63
[Chain A source organism]=Homo sapiens
[Chain A UniProt accession]=Q9H3D4
[Chain A UniProt boundaries]=397-455
[Chain A UniProt coverage]=8.7%
[Chain A UniRef90 accession]=UniRef90_Q9H3D4
[Chain A UniRef90 boundaries]=397-455
[Chain B name]=Tumor protein p73
[Chain B source organism]=Homo sapiens
[Chain B UniProt accession]=O15350
[Chain B UniProt boundaries]=351-398
[Chain B UniProt coverage]=7.5%
[Chain B UniRef90 accession]=UniRef90_O15350
[Chain B UniRef90 boundaries]=351-398
[Chain C name]=Tumor protein 63
[Chain C source organism]=Homo sapiens
[Chain C UniProt accession]=Q9H3D4
[Chain C UniProt boundaries]=397-455
[Chain C UniProt coverage]=8.7%
[Chain C UniRef90 accession]=UniRef90_Q9H3D4
[Chain C UniRef90 boundaries]=397-455
[Chain D name]=Tumor protein p73
[Chain D source organism]=Homo sapiens
[Chain D UniProt accession]=O15350
[Chain D UniProt boundaries]=351-398
[Chain D UniProt coverage]=7.5%
[Chain D UniRef90 accession]=UniRef90_O15350
[Chain D UniRef90 boundaries]=351-398

[Entry]
[Accession]=MF2200012
[Name]=Leukemia Fusion Target AF9 in complex with AF4
[Source organism]=Homo sapiens
[Assembly]=Heterodimer
[Total number of proteins]=2
[Number of unique proteins]=2
[Class]=Other
[Subclass]=Other
[PDB ID]=2lm0
[PDB chain IDs]=AB
[PDB note]=Chain A has been split into two chains to reflect the real biological assembly. The newly generated chain A corresponds to residues 738-779, while chain B corresponds to residues 1490-1568. Linker residues and expression tags were removed.
[PDB experimental technique]=NMR
[Evidence global]=AF9 is an intrinsically disordered protein, which binds competing disordered partners, most notably AF4, Dot1L, BCoR and hPC3. The two interacting protein regions undergo mutual synergistic folding (PMID:23260655).
[Chain A name]=AF4/FMR2 family member 1
[Chain A source organism]=Homo sapiens
[Chain A UniProt accession]=P51825
[Chain A UniProt boundaries]=738-779
[Chain A UniProt coverage]=3.5%
[Chain A UniRef90 accession]=UniRef90_P51825
[Chain A UniRef90 boundaries]=738-779
[Chain B name]=Protein AF-9
[Chain B source organism]=Homo sapiens
[Chain B UniProt accession]=P42568
[Chain B UniProt boundaries]=490-568
[Chain B UniProt coverage]=13.9%
[Chain B UniRef90 accession]=UniRef90_P42568
[Chain B UniRef90 boundaries]=490-568

[Entry]
[Accession]=MF2200013
[Name]=Leukemia Fusion Target AF9 in complex with hPC3
[Source organism]=Homo sapiens
[Assembly]=Heterodimer
[Total number of proteins]=2
[Number of unique proteins]=2
[Class]=Other
[Subclass]=Other
[PDB ID]=2n4q
[PDB chain IDs]=AB
[PDB note]=No modifications of the original PDB file. Chain identifiers are identical with the PDB's identifiers.
[PDB experimental technique]=NMR
[Evidence global]=AF9 is an intrinsically disordered protein, which binds competing disordered partners, most notably AF4, Dot1L, BCoR and hPC3. The two interacting protein regions undergo mutual synergistic folding (PMID:23260655).
[Chain A name]=Chromobox protein homolog 8
[Chain A source organism]=Homo sapiens
[Chain A UniProt accession]=Q9HC52
[Chain A UniProt boundaries]=327-349
[Chain A UniProt coverage]=5.9%
[Chain A UniRef90 accession]=UniRef90_Q9HC52
[Chain A UniRef90 boundaries]=327-349
[Chain B name]=Protein AF-9
[Chain B source organism]=Homo sapiens
[Chain B UniProt accession]=P42568
[Chain B UniProt boundaries]=500-568
[Chain B UniProt coverage]=12.1%
[Chain B UniRef90 accession]=UniRef90_P42568
[Chain B UniRef90 boundaries]=500-568

[Entry]
[Accession]=MF2200014
[Name]=Leukemia Fusion Target AF9 in complex with Dot1L
[Source organism]=Homo sapiens
[Assembly]=Heterodimer
[Total number of proteins]=2
[Number of unique proteins]=2
[Class]=Other
[Subclass]=Other
[PDB ID]=2mv7
[PDB chain IDs]=AB
[PDB note]=No modifications of the original PDB file. Chain identifiers are identical with the PDB's identifiers.
[PDB experimental technique]=NMR
[Evidence global]=AF9 is an intrinsically disordered protein, which binds competing disordered partners, most notably AF4, Dot1L, BCoR and hPC3. The two interacting protein regions undergo mutual synergistic folding (PMID:23260655).
[Chain A name]=Protein AF-9
[Chain A source organism]=Homo sapiens
[Chain A UniProt accession]=P42568
[Chain A UniProt boundaries]=500-568
[Chain A UniProt coverage]=12.1%
[Chain A UniRef90 accession]=UniRef90_P42568
[Chain A UniRef90 boundaries]=500-568
[Chain B name]=Histone-lysine N-methyltransferase, H3 lysine-79 specific
[Chain B source organism]=Homo sapiens
[Chain B UniProt accession]=Q8TEK3
[Chain B UniProt boundaries]=876-900
[Chain B UniProt coverage]=1.4%
[Chain B UniRef90 accession]=UniRef90_Q8TEK3
[Chain B UniRef90 boundaries]=877-900

[Entry]
[Accession]=MF3140002
[Name]=SARS-Coronavirus HR2 Domain (prefusion, trimeric form)
[Source organism]=Human SARS coronavirus
[Assembly]=Homotrimer
[Total number of proteins]=3
[Number of unique proteins]=1
[Class]=Coils and zippers
[Subclass]=Coiled coil (trimeric)
[PDB ID]=2fxp
[PDB chain IDs]=ABC
[PDB note]=No modifications of the original PDB file. Chain identifiers are identical with the PDB's identifiers.
[PDB experimental technique]=NMR
[Evidence global]=The subunits in the structure are bound via coiled coil interactions (PMID:16507566). Coiled coils are highly versatile folding units (PMID:11166216), where the formation of the structure and the interaction between subunits is almost ubiquitously linked. This cooperative nature of binding and folding that results in a two-step process has been demonstrated for coiled coils with varying oligomeric state from dimers (PMID:9811815) and trimers (PMID:10933510) up to heptamers (PMID:17030805). While the interaction and folding are linked, in certain cases there can be significant residual structure before association (PMID:8401212). However, these residual structural elements usually encompass 1-2 turns of helices that serve as a 'nucleation site' driving interaction and helix formation (zipping up) (PMID:17438295), thus even in these cases monomeric coiled coil subunits cannot be considered to have a stable structure.
[Chain A name]=Spike glycoprotein
[Chain A source organism]=Human SARS coronavirus
[Chain A UniProt accession]=P59594
[Chain A UniProt boundaries]=1139-1193
[Chain A UniProt coverage]=4.4%
[Chain A UniRef90 accession]=UniRef90_P59594
[Chain A UniRef90 boundaries]=1140-1193
[Chain B name]=Spike glycoprotein
[Chain B source organism]=Human SARS coronavirus
[Chain B UniProt accession]=P59594
[Chain B UniProt boundaries]=1139-1193
[Chain B UniProt coverage]=4.4%
[Chain B UniRef90 accession]=UniRef90_P59594
[Chain B UniRef90 boundaries]=1140-1193
[Chain C name]=Spike glycoprotein
[Chain C source organism]=Human SARS coronavirus
[Chain C UniProt accession]=P59594
[Chain C UniProt boundaries]=1139-1193
[Chain C UniProt coverage]=4.4%
[Chain C UniRef90 accession]=UniRef90_P59594
[Chain C UniRef90 boundaries]=1140-1193

[Entry]
[Accession]=MF3100004
[Name]=C-terminal coiled coil domain of Transient receptor potential (TRP) channel subfamily P member 2
[Source organism]=Homo sapiens
[Assembly]=Homotrimer
[Total number of proteins]=3
[Number of unique proteins]=1
[Class]=Coils and zippers
[Subclass]=Coiled coil (trimeric)
[PDB ID]=3hrn
[PDB chain IDs]=ABC
[PDB note]=Chains B and C were generated from chain A using the biomatrices described in the original PDB file.
[PDB experimental technique]=X-ray
[PDB resolution]=1.90
[Evidence global]=The subunits in the structure are bound via coiled coil interactions (PMID:19556541). Coiled coils are highly versatile folding units (PMID:11166216), where the formation of the structure and the interaction between subunits is almost ubiquitously linked. This cooperative nature of binding and folding that results in a two-step process has been demonstrated for coiled coils with varying oligomeric state from dimers (PMID:9811815) and trimers (PMID:10933510) up to heptamers (PMID:17030805). While the interaction and folding are linked, in certain cases there can be significant residual structure before association (PMID:8401212). However, these residual structural elements usually encompass 1-2 turns of helices that serve as a 'nucleation site' driving interaction and helix formation (zipping up) (PMID:17438295), thus even in these cases monomeric coiled coil subunits cannot be considered to have a stable structure.
[Chain A name]=Polycystin-2
[Chain A source organism]=Homo sapiens
[Chain A UniProt accession]=Q13563
[Chain A UniProt boundaries]=832-895
[Chain A UniProt coverage]=6.6%
[Chain A UniRef90 accession]=UniRef90_Q13563
[Chain A UniRef90 boundaries]=833-895
[Chain B name]=Polycystin-2
[Chain B source organism]=Homo sapiens
[Chain B UniProt accession]=Q13563
[Chain B UniProt boundaries]=832-895
[Chain B UniProt coverage]=6.6%
[Chain B UniRef90 accession]=UniRef90_Q13563
[Chain B UniRef90 boundaries]=833-895
[Chain C name]=Polycystin-2
[Chain C source organism]=Homo sapiens
[Chain C UniProt accession]=Q13563
[Chain C UniProt boundaries]=832-895
[Chain C UniProt coverage]=6.6%
[Chain C UniRef90 accession]=UniRef90_Q13563
[Chain C UniRef90 boundaries]=833-895
[Related structures]=3hro

[Entry]
[Accession]=MF2110024
[Name]=L27 domain complex (D. melanogaster)
[Source organism]=Drosophila melanogaster
[Assembly]=Homodimer
[Total number of proteins]=2
[Number of unique proteins]=1
[Class]=L27 domains
[Subclass]=L27_1 type
[PDB ID]=4rp3
[PDB chain IDs]=AB
[PDB note]=No modifications of the original PDB file. Chain identifiers are identical with the PDB's identifiers.
[PDB experimental technique]=X-ray
[PDB resolution]=1.36
[Evidence global]=The interacting chains form half of a heterotetrameric L27 complex (a dimer of dimers) (PMID:16147993). L27 complexes formed by Lin-2 and Lin-7 proteins were shown to function as obligate heterodimers/tetramers undergoing a cooperative unfolding transition. Circular dichroism studies reveal that the individual monomers are largely unfolded outside the complex form (PMID:12110687).
[Chain A name]=Disks large 1 tumor suppressor protein
[Chain A source organism]=Drosophila melanogaster
[Chain A UniProt accession]=P31007
[Chain A UniProt boundaries]=1-97
[Chain A UniProt coverage]=10%
[Chain A UniRef90 accession]=UniRef90_P31007
[Chain A UniRef90 boundaries]=1-97
[Chain B name]=Disks large 1 tumor suppressor protein
[Chain B source organism]=Drosophila melanogaster
[Chain B UniProt accession]=P31007
[Chain B UniProt boundaries]=1-97
[Chain B UniProt coverage]=10%
[Chain B UniRef90 accession]=UniRef90_P31007
[Chain B UniRef90 boundaries]=1-97
[Related structures]=4rp4,4rp5

[Entry]
[Accession]=MF2110025
[Name]=Tropomyosin dimer (Gallus gallus)
[Source organism]=Gallus gallus
[Assembly]=Homodimer
[Total number of proteins]=2
[Number of unique proteins]=1
[Class]=Coils and zippers
[Subclass]=Coiled coil (dimeric)
[PDB ID]=1ic2
[PDB chain IDs]=AB
[PDB note]=Chains C and D were removed as chains A and B represent the biologically relevant dimer.
[PDB experimental technique]=X-ray
[PDB resolution]=2.00
[Evidence global]=The subunits in the structure are bound via coiled coil interactions (PMID:11438684). Coiled coils are highly versatile folding units (PMID:11166216), where the formation of the structure and the interaction between subunits is almost ubiquitously linked. This cooperative nature of binding and folding that results in a two-step process has been demonstrated for coiled coils with varying oligomeric state from dimers (PMID:9811815) and trimers (PMID:10933510) up to heptamers (PMID:17030805). While the interaction and folding are linked, in certain cases there can be significant residual structure before association (PMID:8401212). However, these residual structural elements usually encompass 1-2 turns of helices that serve as a 'nucleation site' driving interaction and helix formation (zipping up) (PMID:17438295), thus even in these cases monomeric coiled coil subunits cannot be considered to have a stable structure.
[Chain A name]=Tropomyosin alpha-1 chain
[Chain A source organism]=Gallus gallus
[Chain A UniProt accession]=P04268
[Chain A UniProt boundaries]=1-81
[Chain A UniProt coverage]=28.5%
[Chain A UniRef90 accession]=UniRef90_P09493
[Chain A UniRef90 boundaries]=1-81
[Chain B name]=Tropomyosin alpha-1 chain
[Chain B source organism]=Gallus gallus
[Chain B UniProt accession]=P04268
[Chain B UniProt boundaries]=1-81
[Chain B UniProt coverage]=28.5%
[Chain B UniRef90 accession]=UniRef90_P09493
[Chain B UniRef90 boundaries]=1-81
[Related structures]=3mtu,3u1a,3u1c,1c1g

[Entry]
[Accession]=MF2110026
[Name]=N-Terminal dimerization domain Lis1
[Source organism]=Rattus norvegicus
[Assembly]=Homodimer
[Total number of proteins]=2
[Number of unique proteins]=1
[Class]=Other
[Subclass]=Other
[PDB ID]=1uuj
[PDB chain IDs]=AB
[PDB note]=Chains C and D were removed as chains A and B represent the biologically relevant dimer.
[PDB experimental technique]=X-ray
[PDB resolution]=1.75
[Evidence global]=Lis1 was shown to be a dimer under native conditions. Monitoring the chemically induced unfolding of the protein by fluorescence and by circular dichroism revealed that the reaction follows a single and coincident transition.
[Chain A name]=Platelet-activating factor acetylhydrolase IB subunit alpha
[Chain A source organism]=Rattus norvegicus
[Chain A UniProt accession]=P63004
[Chain A UniProt boundaries]=1-86
[Chain A UniProt coverage]=21%
[Chain A UniRef90 accession]=UniRef90_P63005
[Chain A UniRef90 boundaries]=1-86
[Chain B name]=Platelet-activating factor acetylhydrolase IB subunit alpha
[Chain B source organism]=Rattus norvegicus
[Chain B UniProt accession]=P63004
[Chain B UniProt boundaries]=1-86
[Chain B UniProt coverage]=21%
[Chain B UniRef90 accession]=UniRef90_P63005
[Chain B UniRef90 boundaries]=1-86

[Entry]
[Accession]=MF2110027
[Name]=Mannose-binding lectin (Hyacinthoides hispanica)
[Source organism]=Hyacinthoides hispanica
[Assembly]=Homodimer
[Total number of proteins]=2
[Number of unique proteins]=1
[Class]=Bulb-type lectin domain
[Subclass]=Homodimeric lectin
[PDB ID]=1b2p
[PDB chain IDs]=AB
[PDB note]=No modifications of the original PDB file. Chain identifiers are identical with the PDB's identifiers.
[PDB experimental technique]=X-ray
[PDB resolution]=1.70
[Evidence global]=A closely homologous lectin of the same type sharing a high degree of sequence and structural similarity has been shown to follow a two-state folding process (PMID:11401577).
[Chain A name]=Lectin SCAman (Fragment)
[Chain A source organism]=Hyacinthoides hispanica
[Chain A UniProt accession]=Q9ZP49
[Chain A UniProt boundaries]=22-140
[Chain A UniProt coverage]=76.8%
[Chain A UniRef90 accession]=UniRef90_Q9ZP49
[Chain A UniRef90 boundaries]=22-140
[Chain B name]=Lectin SCAman (Fragment)
[Chain B source organism]=Hyacinthoides hispanica
[Chain B UniProt accession]=Q9ZP49
[Chain B UniProt boundaries]=22-140
[Chain B UniProt coverage]=76.8%
[Chain B UniRef90 accession]=UniRef90_Q9ZP49
[Chain B UniRef90 boundaries]=22-140

[Entry]
[Accession]=MF2110028
[Name]=Dimerization domain of the type I alpha regulatory subunit of protein kinase A
[Source organism]=Bos taurus
[Assembly]=Homodimer
[Total number of proteins]=2
[Number of unique proteins]=1
[Class]=Other
[Subclass]=Other
[PDB ID]=2ezw
[PDB chain IDs]=AB
[PDB note]=No modifications of the original PDB file. Chain identifiers are identical with the PDB's identifiers.
[PDB experimental technique]=NMR
[Evidence chain A]=The N-terminal dimerization region of RIalpha is highly mobile evading structure determination by X-ray (PMID:24316401).
[Evidence chain B]=The N-terminal dimerization region of RIalpha is highly mobile evading structure determination by X-ray (PMID:24316401).
[Chain A name]=cAMP-dependent protein kinase type I-alpha regulatory subunit
[Chain A source organism]=Bos taurus
[Chain A UniProt accession]=P00514
[Chain A UniProt boundaries]=13-62
[Chain A UniProt coverage]=13.2%
[Chain A UniRef90 accession]=UniRef90_P10644
[Chain A UniRef90 boundaries]=14-63
[Chain B name]=cAMP-dependent protein kinase type I-alpha regulatory subunit
[Chain B source organism]=Bos taurus
[Chain B UniProt accession]=P00514
[Chain B UniProt boundaries]=13-62
[Chain B UniProt coverage]=13.2%
[Chain B UniRef90 accession]=UniRef90_P10644
[Chain B UniRef90 boundaries]=14-63
[Related structures]=3im3,3im4,5hvz

[Entry]
[Accession]=MF2110029
[Name]=Coiled Coil Domain of Pawr
[Source organism]=Rattus norvegicus
[Assembly]=Homodimer
[Total number of proteins]=2
[Number of unique proteins]=1
[Class]=Coils and zippers
[Subclass]=Coiled coil (dimeric)
[PDB ID]=5fiy
[PDB chain IDs]=AB
[PDB note]=Chains C, D, E, F and G were removed as chains A and B represent the biologically relevant dimer.
[PDB experimental technique]=X-ray
[PDB resolution]=3.00
[Evidence global]=The subunits in the structure are bound via coiled coil interactions. Coiled coils are highly versatile folding units (PMID:11166216), where the formation of the structure and the interaction between subunits is almost ubiquitously linked. This cooperative nature of binding and folding that results in a two-step process has been demonstrated for coiled coils with varying oligomeric state from dimers (PMID:9811815) and trimers (PMID:10933510) up to heptamers (PMID:17030805). While the interaction and folding are linked, in certain cases there can be significant residual structure before association (PMID:8401212). However, these residual structural elements usually encompass 1-2 turns of helices that serve as a 'nucleation site' driving interaction and helix formation (zipping up) (PMID:17438295), thus even in these cases monomeric coiled coil subunits cannot be considered to have a stable structure.
[Chain A name]=PRKC apoptosis WT1 regulator protein
[Chain A source organism]=Rattus norvegicus
[Chain A UniProt accession]=Q62627
[Chain A UniProt boundaries]=240-332
[Chain A UniProt coverage]=28%
[Chain A UniRef90 accession]=UniRef90_Q62627
[Chain A UniRef90 boundaries]=240-332
[Chain B name]=PRKC apoptosis WT1 regulator protein
[Chain B source organism]=Rattus norvegicus
[Chain B UniProt accession]=Q62627
[Chain B UniProt boundaries]=240-332
[Chain B UniProt coverage]=28%
[Chain B UniRef90 accession]=UniRef90_Q62627
[Chain B UniRef90 boundaries]=240-332

[Entry]
[Accession]=MF4110009
[Name]=p53/p73-b homo-tetramerization domain (Ciona intestinalis)
[Source organism]=Ciona intestinalis
[Assembly]=Homotetramer
[Total number of proteins]=4
[Number of unique proteins]=1
[Class]=Other
[Subclass]=p53 tetramerization
[PDB ID]=2mw4
[PDB chain IDs]=ABCD
[PDB note]=No modifications of the original PDB file. Chain identifiers are identical with the PDB's identifiers.
[PDB experimental technique]=NMR
[Evidence global]=p53, p63, p73 and their homologues are all members of the p53 protein family. The tetramerization region of p53, p63 and p73 are closely homologous to each other, having very similar sequences, structures and biological functions (PMID:25185827,PMID:18289041,PMID:20379196), all containing the same Pfam domain (PF07710). The tetramerization domain of p53 exhibits a four-helix bundle structure bound by hydrophobic and electrostatic interactions (PMID:8023159). The tetramer is formed as a dimer of dimers and follows a two state folding and binding process, demonstrated in several chemical and thermal denaturation/refolding experiments (PMID:9582268,PMID:18410249,PMID:19913028).
[Chain A name]=Uncharacterized protein
[Chain A source organism]=Ciona intestinalis
[Chain A UniProt accession]=F6SSG7
[Chain A UniProt boundaries]=374-419
[Chain A UniProt coverage]=11%
[Chain A UniRef90 accession]=UniRef90_F6SSG7
[Chain A UniRef90 boundaries]=374-419
[Chain B name]=Uncharacterized protein
[Chain B source organism]=Ciona intestinalis
[Chain B UniProt accession]=F6SSG7
[Chain B UniProt boundaries]=374-419
[Chain B UniProt coverage]=11%
[Chain B UniRef90 accession]=UniRef90_F6SSG7
[Chain B UniRef90 boundaries]=374-419
[Chain C name]=Uncharacterized protein
[Chain C source organism]=Ciona intestinalis
[Chain C UniProt accession]=F6SSG7
[Chain C UniProt boundaries]=374-419
[Chain C UniProt coverage]=11%
[Chain C UniRef90 accession]=UniRef90_F6SSG7
[Chain C UniRef90 boundaries]=374-419
[Chain D name]=Uncharacterized protein
[Chain D source organism]=Ciona intestinalis
[Chain D UniProt accession]=F6SSG7
[Chain D UniProt boundaries]=374-419
[Chain D UniProt coverage]=11%
[Chain D UniRef90 accession]=UniRef90_F6SSG7
[Chain D UniRef90 boundaries]=374-419

[Entry]
[Accession]=MF6240001
[Name]=Human respiratory syncytial virus fusion protein core
[Source organism]=Human respiratory syncytial virus A
[Assembly]=Heterohexamer
[Total number of proteins]=6
[Number of unique proteins]=2
[Class]=Coils and zippers
[Subclass]=Coiled coil (hexameric)
[PDB ID]=1g2c
[PDB chain IDs]=ABCDEF
[PDB note]=Chains G, H, I, J, K, L, M, N, O, P, Q, R, S, T, U, V, W and X were removed as chains A, B, C, D, E and F represent the biologically relevant dimer.
[PDB experimental technique]=X-ray
[PDB resolution]=2.30
[Evidence global]=The subunits in the structure are bound via coiled coil interactions (PMID:11106388). Coiled coils are highly versatile folding units (PMID:11166216), where the formation of the structure and the interaction between subunits is almost ubiquitously linked. This cooperative nature of binding and folding that results in a two-step process has been demonstrated for coiled coils with varying oligomeric state from dimers (PMID:9811815) and trimers (PMID:10933510) up to heptamers (PMID:17030805). While the interaction and folding are linked, in certain cases there can be significant residual structure before association (PMID:8401212). However, these residual structural elements usually encompass 1-2 turns of helices that serve as a 'nucleation site' driving interaction and helix formation (zipping up) (PMID:17438295), thus even in these cases monomeric coiled coil subunits cannot be considered to have a stable structure.
[Chain A name]=Fusion glycoprotein F0
[Chain A source organism]=Human respiratory syncytial virus A
[Chain A UniProt accession]=P11209
[Chain A UniProt boundaries]=158-209
[Chain A UniProt coverage]=9.1%
[Chain A UniRef90 accession]=UniRef90_P03420
[Chain A UniRef90 boundaries]=158-209
[Chain B name]=Fusion glycoprotein F0
[Chain B source organism]=Human respiratory syncytial virus A
[Chain B UniProt accession]=P11209
[Chain B UniProt boundaries]=477-519
[Chain B UniProt coverage]=7.5%
[Chain B UniRef90 accession]=UniRef90_P03420
[Chain B UniRef90 boundaries]=477-519
[Chain C name]=Fusion glycoprotein F0
[Chain C source organism]=Human respiratory syncytial virus A
[Chain C UniProt accession]=P11209
[Chain C UniProt boundaries]=158-209
[Chain C UniProt coverage]=9.1%
[Chain C UniRef90 accession]=UniRef90_P03420
[Chain C UniRef90 boundaries]=158-209
[Chain D name]=Fusion glycoprotein F0
[Chain D source organism]=Human respiratory syncytial virus A
[Chain D UniProt accession]=P11209
[Chain D UniProt boundaries]=477-519
[Chain D UniProt coverage]=7.5%
[Chain D UniRef90 accession]=UniRef90_P03420
[Chain D UniRef90 boundaries]=477-519
[Chain E name]=Fusion glycoprotein F0
[Chain E source organism]=Human respiratory syncytial virus A
[Chain E UniProt accession]=P11209
[Chain E UniProt boundaries]=158-209
[Chain E UniProt coverage]=9.1%
[Chain E UniRef90 accession]=UniRef90_P03420
[Chain E UniRef90 boundaries]=158-209
[Chain F name]=Fusion glycoprotein F0
[Chain F source organism]=Human respiratory syncytial virus A
[Chain F UniProt accession]=P11209
[Chain F UniProt boundaries]=477-519
[Chain F UniProt coverage]=7.5%
[Chain F UniRef90 accession]=UniRef90_P03420
[Chain F UniRef90 boundaries]=477-519
[Related structures]=3kpe,3rrr,3rrt,4jhw,4zyp,5j3d,5toj,5tok,5u68

[Entry]
[Accession]=MF4140003
[Name]=Measles virus phosphoprotein tetramerization domain
[Source organism]=Measles virus
[Assembly]=Homotetramer
[Total number of proteins]=4
[Number of unique proteins]=1
[Class]=Coils and zippers
[Subclass]=Coiled coil (tetrameric)
[PDB ID]=4bhv
[PDB chain IDs]=ABCD
[PDB note]=No modifications of the original PDB file. Chain identifiers are identical with the PDB's identifiers.
[PDB experimental technique]=X-ray
[PDB resolution]=2.10
[Evidence global]=The subunits in the structure are bound via coiled coil interactions (PMID:23576502). Coiled coils are highly versatile folding units (PMID:11166216), where the formation of the structure and the interaction between subunits is almost ubiquitously linked. This cooperative nature of binding and folding that results in a two-step process has been demonstrated for coiled coils with varying oligomeric state from dimers (PMID:9811815) and trimers (PMID:10933510) up to heptamers (PMID:17030805). While the interaction and folding are linked, in certain cases there can be significant residual structure before association (PMID:8401212). However, these residual structural elements usually encompass 1-2 turns of helices that serve as a 'nucleation site' driving interaction and helix formation (zipping up) (PMID:17438295), thus even in these cases monomeric coiled coil subunits cannot be considered to have a stable structure.
[Chain A name]=Phosphoprotein
[Chain A source organism]=Measles virus
[Chain A UniProt accession]=P03422
[Chain A UniProt boundaries]=304-360
[Chain A UniProt coverage]=11.2%
[Chain A UniRef90 accession]=UniRef90_P35974
[Chain A UniRef90 boundaries]=304-360
[Chain B name]=Phosphoprotein
[Chain B source organism]=Measles virus
[Chain B UniProt accession]=P03422
[Chain B UniProt boundaries]=304-360
[Chain B UniProt coverage]=11.2%
[Chain B UniRef90 accession]=UniRef90_P35974
[Chain B UniRef90 boundaries]=304-360
[Chain C name]=Phosphoprotein
[Chain C source organism]=Measles virus
[Chain C UniProt accession]=P03422
[Chain C UniProt boundaries]=304-360
[Chain C UniProt coverage]=11.2%
[Chain C UniRef90 accession]=UniRef90_P35974
[Chain C UniRef90 boundaries]=304-360
[Chain D name]=Phosphoprotein
[Chain D source organism]=Measles virus
[Chain D UniProt accession]=P03422
[Chain D UniProt boundaries]=304-360
[Chain D UniProt coverage]=11.2%
[Chain D UniRef90 accession]=UniRef90_P35974
[Chain D UniRef90 boundaries]=304-360
[Related structures]=4c5q,3zdo

[Entry]
[Accession]=MF4140004
[Name]=Core (C) protein from West Nile Virus
[Source organism]=Kunjin virus
[Assembly]=Homotetramer
[Total number of proteins]=4
[Number of unique proteins]=1
[Class]=Other
[Subclass]=Other
[PDB ID]=1sfk
[PDB chain IDs]=ABCD
[PDB note]=Chains E, F, G and H were removed as chains A, B, C and D represent the biologically relevant dimer.
[PDB experimental technique]=X-ray
[PDB resolution]=3.20
[Evidence chain A]=The 1-105 region described in DisProt entry DP00673 covers 100% of the sequence present in the structure.
[Evidence chain B]=The 1-105 region described in DisProt entry DP00673 covers 100% of the sequence present in the structure.
[Evidence chain C]=The 1-105 region described in DisProt entry DP00673 covers 100% of the sequence present in the structure.
[Evidence chain D]=The 1-105 region described in DisProt entry DP00673 covers 100% of the sequence present in the structure.
[Chain A name]=Genome polyprotein
[Chain A source organism]=Kunjin virus
[Chain A UniProt accession]=P14335
[Chain A UniProt boundaries]=23-98
[Chain A UniProt coverage]=2.2%
[Chain A UniRef90 accession]=UniRef90_P06935
[Chain A UniRef90 boundaries]=23-98
[Chain B name]=Genome polyprotein
[Chain B source organism]=Kunjin virus
[Chain B UniProt accession]=P14335
[Chain B UniProt boundaries]=23-98
[Chain B UniProt coverage]=2.2%
[Chain B UniRef90 accession]=UniRef90_P06935
[Chain B UniRef90 boundaries]=23-98
[Chain C name]=Genome polyprotein
[Chain C source organism]=Kunjin virus
[Chain C UniProt accession]=P14335
[Chain C UniProt boundaries]=23-98
[Chain C UniProt coverage]=2.2%
[Chain C UniRef90 accession]=UniRef90_P06935
[Chain C UniRef90 boundaries]=23-98
[Chain D name]=Genome polyprotein
[Chain D source organism]=Kunjin virus
[Chain D UniProt accession]=P14335
[Chain D UniProt boundaries]=23-98
[Chain D UniProt coverage]=2.2%
[Chain D UniRef90 accession]=UniRef90_P06935
[Chain D UniRef90 boundaries]=23-98

[Entry]
[Accession]=MF2100017
[Name]=C-terminal domain of the end-binding protein 1 (EB1)
[Source organism]=Homo sapiens
[Assembly]=Homodimer
[Total number of proteins]=2
[Number of unique proteins]=1
[Class]=Coils and zippers
[Subclass]=Coiled coil (dimeric)
[PDB ID]=1wu9
[PDB chain IDs]=AB
[PDB note]=No modifications of the original PDB file. Chain identifiers are identical with the PDB's identifiers.
[PDB experimental technique]=X-ray
[PDB resolution]=1.54
[Evidence global]=EB1 is a stable dimer with a parallel coiled coil and show that dimerization is essential for the formation of its C-terminal domain (EB1-C) (PMID:15616574).
[Chain A name]=Microtubule-associated protein RP/EB family member 1
[Chain A source organism]=Homo sapiens
[Chain A UniProt accession]=Q15691
[Chain A UniProt boundaries]=189-268
[Chain A UniProt coverage]=29.9%
[Chain A UniRef90 accession]=UniRef90_Q15691
[Chain A UniRef90 boundaries]=189-268
[Chain B name]=Microtubule-associated protein RP/EB family member 1
[Chain B source organism]=Homo sapiens
[Chain B UniProt accession]=Q15691
[Chain B UniProt boundaries]=189-268
[Chain B UniProt coverage]=29.9%
[Chain B UniRef90 accession]=UniRef90_Q15691
[Chain B UniRef90 boundaries]=189-268
[Related structures]=1txq,1yib,1yig,2hkq,2hl5,2r8u,3gjo,3tq7,4xa3,4xa6,5jv3,5jvm,5jvp,5jvr,5jvs,5jvu,5jx1

[Entry]
[Accession]=MF6140001
[Name]=SARS-Coronavirus HR2 Domain (post-fusion, hexameric form)
[Source organism]=Human SARS coronavirus
[Assembly]=Homohexamer
[Total number of proteins]=6
[Number of unique proteins]=1
[Class]=Coils and zippers
[Subclass]=Coiled coil (tetrameric)
[PDB ID]=1zv8
[PDB chain IDs]=ABCDEF
[PDB note]=Chains G, H, I, J, K and L were removed as chains A, B, C, D, E and F represent the biologically relevant hexamer.
[PDB experimental technique]=X-ray
[PDB resolution]=1.94
[Evidence global]=The subunits in the structure are bound via coiled coil interactions (PMID:16698550). Coiled coils are highly versatile folding units (PMID:11166216), where the formation of the structure and the interaction between subunits is almost ubiquitously linked. This cooperative nature of binding and folding that results in a two-step process has been demonstrated for coiled coils with varying oligomeric state from dimers (PMID:9811815) and trimers (PMID:10933510) up to heptamers (PMID:17030805). While the interaction and folding are linked, in certain cases there can be significant residual structure before association (PMID:8401212). However, these residual structural elements usually encompass 1-2 turns of helices that serve as a 'nucleation site' driving interaction and helix formation (zipping up) (PMID:17438295), thus even in these cases monomeric coiled coil subunits cannot be considered to have a stable structure.
[Chain A name]=Spike glycoprotein
[Chain A source organism]=Human SARS coronavirus
[Chain A UniProt accession]=P59594
[Chain A UniProt boundaries]=901-950
[Chain A UniProt coverage]=4%
[Chain A UniRef90 accession]=UniRef90_P59594
[Chain A UniRef90 boundaries]=901-950
[Chain B name]=Spike glycoprotein
[Chain B source organism]=Human SARS coronavirus
[Chain B UniProt accession]=P59594
[Chain B UniProt boundaries]=1150-1185
[Chain B UniProt coverage]=2.9%
[Chain B UniRef90 accession]=UniRef90_P59594
[Chain B UniRef90 boundaries]=1150-1185
[Chain C name]=Spike glycoprotein
[Chain C source organism]=Human SARS coronavirus
[Chain C UniProt accession]=P59594
[Chain C UniProt boundaries]=901-950
[Chain C UniProt coverage]=4%
[Chain C UniRef90 accession]=UniRef90_P59594
[Chain C UniRef90 boundaries]=901-950
[Chain D name]=Spike glycoprotein
[Chain D source organism]=Human SARS coronavirus
[Chain D UniProt accession]=P59594
[Chain D UniProt boundaries]=1150-1185
[Chain D UniProt coverage]=2.9%
[Chain D UniRef90 accession]=UniRef90_P59594
[Chain D UniRef90 boundaries]=1150-1185
[Chain E name]=Spike glycoprotein
[Chain E source organism]=Human SARS coronavirus
[Chain E UniProt accession]=P59594
[Chain E UniProt boundaries]=901-950
[Chain E UniProt coverage]=4%
[Chain E UniRef90 accession]=UniRef90_P59594
[Chain E UniRef90 boundaries]=901-950
[Chain F name]=Spike glycoprotein
[Chain F source organism]=Human SARS coronavirus
[Chain F UniProt accession]=P59594
[Chain F UniProt boundaries]=1150-1185
[Chain F UniProt coverage]=2.9%
[Chain F UniRef90 accession]=UniRef90_P59594
[Chain F UniRef90 boundaries]=1150-1185
[Related structures]=2beq,2bez

[Entry]
[Accession]=MF2120032
[Name]=BenM DNA binding domain dimer
[Source organism]=Acinetobacter baylyi
[Assembly]=Homodimer
[Total number of proteins]=2
[Number of unique proteins]=1
[Class]=Other
[Subclass]=Other
[PDB ID]=3m1e
[PDB chain IDs]=AB
[PDB note]=Chain B was generated from chain A using the biomatrices described in the original PDB file.
[PDB experimental technique]=X-ray
[PDB resolution]=1.80
[Evidence chain A]=The N-terminal dimerization regions of BenM is highly mobile evading structure determination by X-ray (PMID:19400783).
[Evidence chain B]=The N-terminal dimerization regions of BenM is highly mobile evading structure determination by X-ray (PMID:19400783).
[Chain A name]=HTH-type transcriptional regulator BenM
[Chain A source organism]=Acinetobacter baylyi
[Chain A UniProt accession]=O68014
[Chain A UniProt boundaries]=1-94
[Chain A UniProt coverage]=30.9%
[Chain A UniRef90 accession]=UniRef90_O68014
[Chain A UniRef90 boundaries]=1-87
[Chain B name]=HTH-type transcriptional regulator BenM
[Chain B source organism]=Acinetobacter baylyi
[Chain B UniProt accession]=O68014
[Chain B UniProt boundaries]=1-94
[Chain B UniProt coverage]=30.9%
[Chain B UniRef90 accession]=UniRef90_O68014
[Chain B UniRef90 boundaries]=1-87
[Related structures]=4ihs,4iht,3k1m,3k1n,3k1p

[Entry]
[Accession]=MF2210015
[Name]=H2A-H2B histone dimer (S. cerevisiae), containing histone variants H2A.2 and H2B.1
[Source organism]=Saccharomyces cerevisiae
[Assembly]=Heterodimer
[Total number of proteins]=2
[Number of unique proteins]=2
[Class]=Histone-like interactions
[Subclass]=Histones
[PDB ID]=4kud
[PDB chain IDs]=CD
[PDB note]=Chains A, B, E, F, G, H, I, J, K and L have been removed to highlight the basic interaction that forms the histone dimer composed of chains C and D.
[PDB experimental technique]=X-ray
[PDB resolution]=3.20
[Evidence global]=Histones form parts of the nucleosome particle by dimerization and subsequent multimerization (PMID:1946434). The dimer contains both histone subunits in a highly intertwined conformation reflecting the possible domain-swapped origins of the structure (PMID:17391511). Accordingly, this dimerization has been experimentally characterized to be coupled to the structure formation of both interacting partners (PMID:12779337); this synergistic folding has been shown separately for H2A-H2B dimers (PMID:15588829) and H3-H4 dimers as well (PMID:15096635). Histones containing various types of monomeric subunits can exhibit varying stability and folding kinetics. E.g. in the case of H3-H4 histones, the dimerization is a complex process with the two monomers first adopting an intermediate state upon encounter and then reaching the classical histone fold through restructurization (PMID:12779337). However, independent of composition and folding kinetics, all histones appear to fold in a cooperative fashion that is coupled to binding (PMID:11669650).
[Chain C name]=Histone H2A.2
[Chain C source organism]=Saccharomyces cerevisiae
[Chain C UniProt accession]=P04912
[Chain C UniProt boundaries]=1-132
[Chain C UniProt coverage]=100%
[Chain C UniRef90 accession]=UniRef90_P04911
[Chain C UniRef90 boundaries]=1-132
[Chain D name]=Histone H2B.1
[Chain D source organism]=Saccharomyces cerevisiae
[Chain D UniProt accession]=P02293
[Chain D UniProt boundaries]=1-131
[Chain D UniProt coverage]=100%
[Chain D UniRef90 accession]=UniRef90_P02293
[Chain D UniRef90 boundaries]=1-131
[Related structures]=4wnn,5bt1

[Entry]
[Accession]=MF2120033
[Name]=E. coli proline utilization A (PutA) DNA-binding domain
[Source organism]=Escherichia coli
[Assembly]=Homodimer
[Total number of proteins]=2
[Number of unique proteins]=1
[Class]=Other
[Subclass]=Ribbon-helix-helix (RHH)
[PDB ID]=2ay0
[PDB chain IDs]=AB
[PDB note]=Chains C, D, E and F were removed as chains A and B represent the biologically relevant dimer.
[PDB experimental technique]=X-ray
[PDB resolution]=2.10
[Evidence global]=The interacting chains form a ribbon-helix-helix (RHH) structure (PMID:17001030). These structures in general have been described with the two monomers adopting a stable conformation upon the interaction (PMID:17676053). The hydrophobic core stabilizing the complex is formed by both interactors and is thus absent prior to the interaction (PMID:25713077).
[Chain A name]=Bifunctional protein PutA
[Chain A source organism]=Escherichia coli
[Chain A UniProt accession]=P09546
[Chain A UniProt boundaries]=1-52
[Chain A UniProt coverage]=3.9%
[Chain A UniRef90 accession]=UniRef90_P09546
[Chain A UniRef90 boundaries]=1-52
[Chain B name]=Bifunctional protein PutA
[Chain B source organism]=Escherichia coli
[Chain B UniProt accession]=P09546
[Chain B UniProt boundaries]=1-52
[Chain B UniProt coverage]=3.9%
[Chain B UniRef90 accession]=UniRef90_P09546
[Chain B UniRef90 boundaries]=1-52
[Related structures]=2gpe,2rbf

[Entry]
[Accession]=MF4140005
[Name]=SARS-Coronavirus HR2 Domain (post-fusion, tetrameric form)
[Source organism]=Human SARS coronavirus
[Assembly]=Homotetramer
[Total number of proteins]=4
[Number of unique proteins]=1
[Class]=Coils and zippers
[Subclass]=Coiled coil (tetrameric)
[PDB ID]=1zv7
[PDB chain IDs]=ABCD
[PDB note]=Chains C and D were generated from chains A and B, respectively, using the biomatrices described in the original PDB file.
[PDB experimental technique]=X-ray
[PDB resolution]=1.70
[Evidence global]=The subunits in the structure are bound via coiled coil interactions (PMID:16698550). Coiled coils are highly versatile folding units (PMID:11166216), where the formation of the structure and the interaction between subunits is almost ubiquitously linked. This cooperative nature of binding and folding that results in a two-step process has been demonstrated for coiled coils with varying oligomeric state from dimers (PMID:9811815) and trimers (PMID:10933510) up to heptamers (PMID:17030805). While the interaction and folding are linked, in certain cases there can be significant residual structure before association (PMID:8401212). However, these residual structural elements usually encompass 1-2 turns of helices that serve as a 'nucleation site' driving interaction and helix formation (zipping up) (PMID:17438295), thus even in these cases monomeric coiled coil subunits cannot be considered to have a stable structure.
[Chain A name]=Spike glycoprotein
[Chain A source organism]=Human SARS coronavirus
[Chain A UniProt accession]=P59594
[Chain A UniProt boundaries]=1150-1193
[Chain A UniProt coverage]=3.5%
[Chain A UniRef90 accession]=UniRef90_P59594
[Chain A UniRef90 boundaries]=1150-1193
[Chain B name]=Spike glycoprotein
[Chain B source organism]=Human SARS coronavirus
[Chain B UniProt accession]=P59594
[Chain B UniProt boundaries]=1150-1193
[Chain B UniProt coverage]=3.5%
[Chain B UniRef90 accession]=UniRef90_P59594
[Chain B UniRef90 boundaries]=1150-1193
[Chain C name]=Spike glycoprotein
[Chain C source organism]=Human SARS coronavirus
[Chain C UniProt accession]=P59594
[Chain C UniProt boundaries]=1150-1193
[Chain C UniProt coverage]=3.5%
[Chain C UniRef90 accession]=UniRef90_P59594
[Chain C UniRef90 boundaries]=1150-1193
[Chain D name]=Spike glycoprotein
[Chain D source organism]=Human SARS coronavirus
[Chain D UniProt accession]=P59594
[Chain D UniProt boundaries]=1150-1193
[Chain D UniProt coverage]=3.5%
[Chain D UniRef90 accession]=UniRef90_P59594
[Chain D UniRef90 boundaries]=1150-1193

[Entry]
[Accession]=MF2200015
[Name]=H2A-H2B histone dimer (human), containing histone variants H2A type 1-A and H2B type 1-J
[Source organism]=Homo sapiens
[Assembly]=Heterodimer
[Total number of proteins]=2
[Number of unique proteins]=2
[Class]=Histone-like interactions
[Subclass]=Histones
[PDB ID]=5gt0
[PDB chain IDs]=CD
[PDB note]=Chains A, B, E, F, G, H, I and J have been removed to highlight the basic interaction that forms the histone dimer composed of chains C and D.
[PDB experimental technique]=X-ray
[PDB resolution]=2.82
[Evidence global]=Histones form parts of the nucleosome particle by dimerization and subsequent multimerization (PMID:1946434). The dimer contains both histone subunits in a highly intertwined conformation reflecting the possible domain-swapped origins of the structure (PMID:17391511). Accordingly, this dimerization has been experimentally characterized to be coupled to the structure formation of both interacting partners (PMID:12779337); this synergistic folding has been shown separately for H2A-H2B dimers (PMID:15588829) and H3-H4 dimers as well (PMID:15096635). Histones containing various types of monomeric subunits can exhibit varying stability and folding kinetics. E.g. in the case of H3-H4 histones, the dimerization is a complex process with the two monomers first adopting an intermediate state upon encounter and then reaching the classical histone fold through restructurization (PMID:12779337). However, independent of composition and folding kinetics, all histones appear to fold in a cooperative fashion that is coupled to binding (PMID:11669650).
[Chain C name]=Histone H2A type 1-A
[Chain C source organism]=Homo sapiens
[Chain C UniProt accession]=Q96QV6
[Chain C UniProt boundaries]=2-131
[Chain C UniProt coverage]=99.2%
[Chain C UniRef90 accession]=UniRef90_P04908
[Chain C UniRef90 boundaries]=2-131
[Chain D name]=Histone H2B type 1-C/E/F/G/I
[Chain D source organism]=Homo sapiens
[Chain D UniProt accession]=P62807
[Chain D UniProt boundaries]=2-126
[Chain D UniProt coverage]=99.2%
[Chain D UniRef90 accession]=UniRef90_P62807
[Chain D UniRef90 boundaries]=2-126

[Entry]
[Accession]=MF2200016
[Name]=H2A-H2B histone dimer (human), containing histone variants H2A type 1-D and H2B type 1-A
[Source organism]=Homo sapiens
[Assembly]=Heterodimer
[Total number of proteins]=2
[Number of unique proteins]=2
[Class]=Histone-like interactions
[Subclass]=Histones
[PDB ID]=5gt3
[PDB chain IDs]=CD
[PDB note]=Chains A, B, E, F, G, H, I and J have been removed to highlight the basic interaction that forms the histone dimer composed of chains C and D.
[PDB experimental technique]=X-ray
[PDB resolution]=2.91
[Evidence global]=Histones form parts of the nucleosome particle by dimerization and subsequent multimerization (PMID:1946434). The dimer contains both histone subunits in a highly intertwined conformation reflecting the possible domain-swapped origins of the structure (PMID:17391511). Accordingly, this dimerization has been experimentally characterized to be coupled to the structure formation of both interacting partners (PMID:12779337); this synergistic folding has been shown separately for H2A-H2B dimers (PMID:15588829) and H3-H4 dimers as well (PMID:15096635). Histones containing various types of monomeric subunits can exhibit varying stability and folding kinetics. E.g. in the case of H3-H4 histones, the dimerization is a complex process with the two monomers first adopting an intermediate state upon encounter and then reaching the classical histone fold through restructurization (PMID:12779337). However, independent of composition and folding kinetics, all histones appear to fold in a cooperative fashion that is coupled to binding (PMID:11669650).
[Chain C name]=Histone H2A type 1-D
[Chain C source organism]=Homo sapiens
[Chain C UniProt accession]=P20671
[Chain C UniProt boundaries]=2-130
[Chain C UniProt coverage]=99.2%
[Chain C UniRef90 accession]=UniRef90_P20671
[Chain C UniRef90 boundaries]=2-130
[Chain D name]=Histone H2B type 1-A
[Chain D source organism]=Homo sapiens
[Chain D UniProt accession]=Q96A08
[Chain D UniProt boundaries]=2-127
[Chain D UniProt coverage]=99.2%
[Chain D UniRef90 accession]=UniRef90_P70696
[Chain D UniRef90 boundaries]=2-127

[Entry]
[Accession]=MF2200017
[Name]=H3-H4 histone dimer (human), containing histone variant H3.3C
[Source organism]=Homo sapiens
[Assembly]=Heterodimer
[Total number of proteins]=2
[Number of unique proteins]=2
[Class]=Histone-like interactions
[Subclass]=Histones
[PDB ID]=4z5t
[PDB chain IDs]=AB
[PDB note]=Chains C, D, E, F, G, H, I and J have been removed to highlight the basic interaction that forms the histone dimer composed of chains A and B.
[PDB experimental technique]=X-ray
[PDB resolution]=2.80
[Evidence global]=Histones form parts of the nucleosome particle by dimerization and subsequent multimerization (PMID:1946434). The dimer contains both histone subunits in a highly intertwined conformation reflecting the possible domain-swapped origins of the structure (PMID:17391511). Accordingly, this dimerization has been experimentally characterized to be coupled to the structure formation of both interacting partners (PMID:12779337); this synergistic folding has been shown separately for H2A-H2B dimers (PMID:15588829) and H3-H4 dimers as well (PMID:15096635). Histones containing various types of monomeric subunits can exhibit varying stability and folding kinetics. E.g. in the case of H3-H4 histones, the dimerization is a complex process with the two monomers first adopting an intermediate state upon encounter and then reaching the classical histone fold through restructurization (PMID:12779337). However, independent of composition and folding kinetics, all histones appear to fold in a cooperative fashion that is coupled to binding (PMID:11669650).
[Chain A name]=Histone H3.3C
[Chain A source organism]=Homo sapiens
[Chain A UniProt accession]=Q6NXT2
[Chain A UniProt boundaries]=1-135
[Chain A UniProt coverage]=100%
[Chain A UniRef90 accession]=UniRef90_Q6NXT2
[Chain A UniRef90 boundaries]=1-135
[Chain B name]=Histone H4
[Chain B source organism]=Homo sapiens
[Chain B UniProt accession]=P62805
[Chain B UniProt boundaries]=1-103
[Chain B UniProt coverage]=100%
[Chain B UniRef90 accession]=UniRef90_P62805
[Chain B UniRef90 boundaries]=1-103

[Entry]
[Accession]=MF2120034
[Name]=Bacillus subtilis antitoxin MazE
[Source organism]=Bacillus subtilis
[Assembly]=Homodimer
[Total number of proteins]=2
[Number of unique proteins]=1
[Class]=Other
[Subclass]=Ribbon-helix-helix (RHH)
[PDB ID]=4me7
[PDB chain IDs]=EF
[PDB note]=Chains A, B, C and D were removed and chains E and F were truncated to include residues 6-52 and 7-52, respectively, to highlight the dimeric interaction.
[PDB experimental technique]=X-ray
[PDB resolution]=2.92
[Evidence global]=The interacting chains form a ribbon-helix-helix (RHH) structure (PMID:17007877). These structures in general have been described with the two monomers adopting a stable conformation upon the interaction (PMID:17676053). The hydrophobic core stabilizing the complex is formed by both interactors and is thus absent prior to the interaction (PMID:25713077).
[Chain E name]=Antitoxin EndoAI
[Chain E source organism]=Bacillus subtilis
[Chain E UniProt accession]=P96621
[Chain E UniProt boundaries]=1-93
[Chain E UniProt coverage]=100%
[Chain E UniRef90 accession]=UniRef90_P96621
[Chain E UniRef90 boundaries]=1-93
[Chain F name]=Antitoxin EndoAI
[Chain F source organism]=Bacillus subtilis
[Chain F UniProt accession]=P96621
[Chain F UniProt boundaries]=1-93
[Chain F UniProt coverage]=100%
[Chain F UniRef90 accession]=UniRef90_P96621
[Chain F UniRef90 boundaries]=1-93

[Entry]
[Accession]=MF2100018
[Name]=Dimeric cytoplasmic domain of syndecan-4
[Source organism]=Homo sapiens
[Assembly]=Homodimer
[Total number of proteins]=2
[Number of unique proteins]=1
[Class]=Other
[Subclass]=Other
[PDB ID]=1ejp
[PDB chain IDs]=AB
[PDB note]=No modifications of the original PDB file. Chain identifiers are identical with the PDB's identifiers.
[PDB experimental technique]=NMR
[Evidence chain A]=The cytoplasmic domain of Syndecan-4 has been shown to adopt a stable structure upon binding to a partner protein (either through binding to an ordered domain PMID:16533050 or through dimerization PMID:11456484).
[Evidence chain B]=The cytoplasmic domain of Syndecan-4 has been shown to adopt a stable structure upon binding to a partner protein (either through binding to an ordered domain PMID:16533050 or through dimerization PMID:11456484).
[Chain A name]=Syndecan-4
[Chain A source organism]=Homo sapiens
[Chain A UniProt accession]=P31431
[Chain A UniProt boundaries]=171-198
[Chain A UniProt coverage]=14.1%
[Chain A UniRef90 accession]=UniRef90_P31431
[Chain A UniRef90 boundaries]=171-198
[Chain B name]=Syndecan-4
[Chain B source organism]=Homo sapiens
[Chain B UniProt accession]=P31431
[Chain B UniProt boundaries]=171-198
[Chain B UniProt coverage]=14.1%
[Chain B UniRef90 accession]=UniRef90_P31431
[Chain B UniRef90 boundaries]=171-198
[Related structures]=1ejq

[Entry]
[Accession]=MF2211003
[Name]=Yeast elongin C in complex with a von Hippel-Lindau peptide
[Source organism]=Saccharomyces cerevisiae / Mus musculus
[Assembly]=Heterodimer
[Total number of proteins]=2
[Number of unique proteins]=2
[Class]=Other
[Subclass]=Other
[PDB ID]=1hv2
[PDB chain IDs]=AB
[PDB note]=No modifications of the original PDB file. Chain identifiers are identical with the PDB's identifiers.
[PDB experimental technique]=NMR
[Evidence global]=Both elongin C and the interacting region of VHL are dynamically unstable in isolation and only adopt a stable conformation upon interaction (PMID:11545595).
[Chain A name]=Elongin-C
[Chain A source organism]=Saccharomyces cerevisiae
[Chain A UniProt accession]=Q03071
[Chain A UniProt boundaries]=1-99
[Chain A UniProt coverage]=100%
[Chain A UniRef90 accession]=UniRef90_Q03071
[Chain A UniRef90 boundaries]=1-99
[Chain B name]=Von Hippel-Lindau disease tumor suppressor
[Chain B source organism]=Mus musculus
[Chain B UniProt accession]=P40338
[Chain B UniProt boundaries]=123-137
[Chain B UniProt coverage]=8.3%
[Chain B UniRef90 accession]=UniRef90_P40338
[Chain B UniRef90 boundaries]=123-137

[Entry]
[Accession]=MF2200018
[Name]=T-cell surface glycoprotein CD4 and proto-oncogene tyrosine-protein kinase LCK fragments
[Source organism]=Homo sapiens
[Assembly]=Heterodimer
[Total number of proteins]=2
[Number of unique proteins]=2
[Class]=Other
[Subclass]=Other
[PDB ID]=1q68
[PDB chain IDs]=AB
[PDB note]=No modifications of the original PDB file. Chain identifiers are identical with the PDB's identifiers.
[PDB experimental technique]=NMR
[Evidence global]=The interacting regions of CD4 and Lck were shown using NMR to undergo cooperative folding as a result of the binding (PMID:14500983).
[Chain A name]=T-cell surface glycoprotein CD4
[Chain A source organism]=Homo sapiens
[Chain A UniProt accession]=P01730
[Chain A UniProt boundaries]=421-458
[Chain A UniProt coverage]=8.3%
[Chain A UniRef90 accession]=UniRef90_P01730
[Chain A UniRef90 boundaries]=421-458
[Chain B name]=Tyrosine-protein kinase Lck
[Chain B source organism]=Homo sapiens
[Chain B UniProt accession]=P06239
[Chain B UniProt boundaries]=7-35
[Chain B UniProt coverage]=5.7%
[Chain B UniRef90 accession]=UniRef90_P06239
[Chain B UniRef90 boundaries]=7-35