LEUCINE ZIPPER MONOMER
Saccharomyces cerevisiae
State in the Current Structure
| Assembly | Oligomeric State | Construct | Mutations and Modifications | Ligands, Ions and Associated Components | Method and Experimental Conditions | Structure Quality |
|---|---|---|---|---|---|---|
| 1 | Protein monomer Monomer Protein × 1 PDB declaration: monomeric（1） Consistent with protein copy count | Chain A； UniProt 247–281 | Not recorded | No other associated polymer | SOLUTION NMR mmCIF provides none of the parsed experimental conditions | Resolution not provided |
Other States of the Same Protein in the Database
Each row is a biological assembly of the same UniProt protein in another PDB entry. The “Difference from current entry” column identifies evidence-level differences; no tag means the currently parsed fields agree.
| Other PDB | Difference from Current Entry 1ZTA | Assembly / Oligomeric State | Construct | Mutations and Modifications | Ligands, Ions and Non-polymers | Method and Experimental Conditions | Structure Quality |
|---|---|---|---|---|---|---|---|
| 1CE9 HELIX CAPPING IN THE GCN4 LEUCINE ZIPPER Deposited 1999-03-18 | Different construct Different mutation/modification Different oligomeric state Different experimental method Different experimental conditions Different structure-quality metrics | Assembly 1 Protein homooligomer Homooligomer；Protein × 4 PDB declaration: tetrameric |
Chain A
251–281（31 aa）
Chain B
251–281（31 aa）
Chain C
251–281（31 aa）
Chain D
251–281（31 aa）
|
Mutation：R2S,M3V,Q5E Mutation：R2S,M3V,Q5E Mutation：R2S,M3V,Q5E Mutation：R2S,M3V,Q5E | No recorded non-water small molecule |
X-RAY DIFFRACTION
X-ray crystallization conditions
pH 4.6；SEE REFERENCE, pH 4.6
|
Resolution 1.80 Å R-free 0.283 |
| 1CE9 HELIX CAPPING IN THE GCN4 LEUCINE ZIPPER Deposited 1999-03-18 | Different construct Different mutation/modification Different oligomeric state Different experimental method Different experimental conditions Different structure-quality metrics | Assembly 2 Protein homooligomer Homooligomer；Protein × 2 PDB declaration: dimeric |
Chain C
251–281（31 aa）
Chain D
251–281（31 aa）
|
Mutation：R2S,M3V,Q5E Mutation：R2S,M3V,Q5E | No recorded non-water small molecule |
X-RAY DIFFRACTION
X-ray crystallization conditions
pH 4.6；SEE REFERENCE, pH 4.6
|
Resolution 1.80 Å R-free 0.283 |
| 1CE9 HELIX CAPPING IN THE GCN4 LEUCINE ZIPPER Deposited 1999-03-18 | Different construct Different mutation/modification Different oligomeric state Different experimental method Different experimental conditions Different structure-quality metrics | Assembly 3 Protein homooligomer Homooligomer；Protein × 2 PDB declaration: dimeric |
Chain A
251–281（31 aa）
Chain B
251–281（31 aa）
|
Mutation：R2S,M3V,Q5E Mutation：R2S,M3V,Q5E | No recorded non-water small molecule |
X-RAY DIFFRACTION
X-ray crystallization conditions
pH 4.6；SEE REFERENCE, pH 4.6
|
Resolution 1.80 Å R-free 0.283 |
| 1DGC THE X-RAY STRUCTURE OF THE GCN4-BZIP BOUND TO ATF/CREB SITE DNA SHOWS THE COMPLEX DEPENDS ON DNA FLEXIBILITY Deposited 1993-07-15 | Different construct Different oligomeric state Different experimental method Different experimental conditions Different structure-quality metrics | Assembly 1 Protein–DNA Homooligomer；Protein × 2 PDB declaration: tetrameric |
Chain A
220–281（62 aa）
|
Not recorded | No recorded non-water small molecule |
X-RAY DIFFRACTION
X-ray crystallization conditions
VAPOR DIFFUSION, HANGING DROP；pH 5.25；277 K；pH 5.25, VAPOR DIFFUSION, HANGING DROP, temperature 277.00K
|
Resolution 3.00 Å |
| 1FAV THE STRUCTURE OF AN HIV-1 SPECIFIC CELL ENTRY INHIBITOR IN COMPLEX WITH THE HIV-1 GP41 TRIMERIC CORE Deposited 2000-07-13 | Different construct Different mutation/modification Different oligomeric state Different experimental method Different experimental conditions Different structure-quality metrics | Assembly 1 Insufficient information Heteromer；Protein × 6 PDB declaration: hexameric |
Chain A
252–280（29 aa）
|
Mutation：L2I, V6I, L9I, N13I, L16I, V20I, L23I, V27I | No recorded non-water small molecule |
X-RAY DIFFRACTION
X-ray crystallization conditions
VAPOR DIFFUSION, HANGING DROP；pH 6.9；298 K；25mM PIPES, 0.25M MgAc, 2.5% isopropanol, 10mM Hepes, 37.5mM NaCl, pH 6.9, VAPOR DIFFUSION, HANGING DROP, temperature 298.0K
|
Resolution 3.00 Å R-free 0.295 |
| 1FMH NMR SOLUTION STRUCTURE OF A DESIGNED HETERODIMERIC LEUCINE ZIPPER Deposited 2000-08-17 | Different construct Different mutation/modification Different oligomeric state Different experimental conditions | Assembly 1 Protein homooligomer Homooligomer；Protein × 2 PDB declaration: dimeric |
Chain A
249–279（31 aa）
Fragment：LEUCINE ZIPPER ACIDIC CHAIN
Chain B
249–279（31 aa）
Fragment：LEUCINE ZIPPER BASIC CHAIN
|
Mutation：R249E M250V K251A D255K K256E E258A E259Q L260A L261E S262A K263E H266Q N269Q R273Q K275E K276H L277E V278C Non-standard monomer：Yes (specific site not provided by mmCIF) Mutation：;R249E M250V K251Q Q252A E254K D255K K256R E258Q E259A L261K S262A K263R H266A L267A E268K N269Q E270K A272Q R273A K275R K276H L277K V278C ; Non-standard monomer：Yes (specific site not provided by mmCIF) | No recorded non-water small molecule |
SOLUTION NMR
NMR measurement conditions
pH 5.65；310 K；Ionic strength (raw mmCIF value) 10 mM；Pressure ambient
NMR sample composition
2.1 mM AB zipper; 90% H2O, 10% D2O | 90% H2O/10% D2O
|
Resolution not provided |
| 1GCL GCN4 LEUCINE ZIPPER CORE MUTANT P-LI Deposited 1993-10-20 | Different construct Different mutation/modification Different oligomeric state Different experimental method Different structure-quality metrics | Assembly 1 Protein homooligomer Homooligomer；Protein × 4 PDB declaration: tetrameric |
Chain A
249–281（33 aa）
Chain B
249–281（33 aa）
Chain C
249–281（33 aa）
Chain D
249–281（33 aa）
|
Mutation：L5I,V9L,L12I,N16L,L19I,V23L,L26I,V30L Non-standard monomer：Yes (specific site not provided by mmCIF) Mutation：L5I,V9L,L12I,N16L,L19I,V23L,L26I,V30L Non-standard monomer：Yes (specific site not provided by mmCIF) Mutation：L5I,V9L,L12I,N16L,L19I,V23L,L26I,V30L Non-standard monomer：Yes (specific site not provided by mmCIF) Mutation：L5I,V9L,L12I,N16L,L19I,V23L,L26I,V30L Non-standard monomer：Yes (specific site not provided by mmCIF) | No recorded non-water small molecule | X-RAY DIFFRACTION mmCIF provides none of the parsed conditions | Resolution 2.10 Å |
| 1GCM GCN4 LEUCINE ZIPPER CORE MUTANT P-LI Deposited 1995-04-25 | Different construct Different mutation/modification Different oligomeric state Different experimental method Different structure-quality metrics | Assembly 1 Protein homooligomer Homooligomer；Protein × 3 PDB declaration: trimeric |
Chain A
249–281（33 aa）
Chain B
249–281（33 aa）
Chain C
249–281（33 aa）
|
Mutation：L5I, V9I, L12I, N16I, L19I, V23I, L26I, V30I (I AT HEPTAD A POSITIONS, I AT HEPTAD D POSITIONS) Non-standard monomer：Yes (specific site not provided by mmCIF) Mutation：L5I, V9I, L12I, N16I, L19I, V23I, L26I, V30I (I AT HEPTAD A POSITIONS, I AT HEPTAD D POSITIONS) Non-standard monomer：Yes (specific site not provided by mmCIF) Mutation：L5I, V9I, L12I, N16I, L19I, V23I, L26I, V30I (I AT HEPTAD A POSITIONS, I AT HEPTAD D POSITIONS) Non-standard monomer：Yes (specific site not provided by mmCIF) | No recorded non-water small molecule | X-RAY DIFFRACTION mmCIF provides none of the parsed conditions | Resolution 1.80 Å |
| 1GK6 Human vimentin coil 2B fragment linked to GCN4 leucine zipper (Z2B) Deposited 2001-08-08 | Different construct Different mutation/modification Different oligomeric state Different experimental method Different experimental conditions Different structure-quality metrics | Assembly 1 Insufficient information Homooligomer；Protein × 2 PDB declaration: dimeric |
Chain A
249–279（31 aa）
Fragment：Z2B FUSION CONSTRUCT CONTAINING THE GCN4 LEUCINE ZIPPER LINKED TO VIMENTIN RESIDUES 385 - 412
Chain B
249–279（31 aa）
Fragment：Z2B FUSION CONSTRUCT CONTAINING THE GCN4 LEUCINE ZIPPER LINKED TO VIMENTIN RESIDUES 385 - 412
|
Not recorded | No recorded non-water small molecule |
X-RAY DIFFRACTION
X-ray crystallization conditions
VAPOR DIFFUSION, HANGING DROP；pH 8.5；HANGING DROPS WITH 12.5MG/ML PROTEIN AND 0.55M (NH4)2HPO4, PH ADJUSTED TO 9.0 WITH NAOH, AS PRECIPITANT
|
Resolution 1.90 Å R-free 0.227 |
| 1GZL Crystal structure of C14linkmid/IQN17: a cross-linked inhibitor of HIV-1 entry bound to the gp41 hydrophobic pocket Deposited 2002-05-23 | Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental method Different experimental conditions Different structure-quality metrics | Assembly 1 Insufficient information Heteromer；Protein × 6 PDB declaration: hexameric |
Chain A
249–276（28 aa）
Fragment：GP41 HYDROPHOBIC POCKET, RESIDUES 565-581, GCN4, RESIDUES 249-276
|
Non-standard monomer：Yes (specific site not provided by mmCIF) | CL CHLORIDE ION × 3 N2P PENTANE-1,5-DIAMINE × 3 |
X-RAY DIFFRACTION
X-ray crystallization conditions
pH 8.6；16% ISOPROPANOL, 0.1 M TRIS, PH 8.6, 1 M (NH4)2SO4
|
Resolution 1.80 Å R-free 0.243 |
| 1GZL Crystal structure of C14linkmid/IQN17: a cross-linked inhibitor of HIV-1 entry bound to the gp41 hydrophobic pocket Deposited 2002-05-23 | Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental method Different experimental conditions Different structure-quality metrics | Assembly 2 Insufficient information Heteromer；Protein × 6 PDB declaration: hexameric |
Chain B
249–276（28 aa）
Fragment：GP41 HYDROPHOBIC POCKET, RESIDUES 565-581, GCN4, RESIDUES 249-276
|
Non-standard monomer：Yes (specific site not provided by mmCIF) | CL CHLORIDE ION × 3 N2P PENTANE-1,5-DIAMINE × 3 |
X-RAY DIFFRACTION
X-ray crystallization conditions
pH 8.6；16% ISOPROPANOL, 0.1 M TRIS, PH 8.6, 1 M (NH4)2SO4
|
Resolution 1.80 Å R-free 0.243 |
| 1IHQ GLYTM1BZIP: A CHIMERIC PEPTIDE MODEL OF THE N-TERMINUS OF A RAT SHORT ALPHA TROPOMYOSIN WITH THE N-TERMINUS ENCODED BY EXON 1B Deposited 2001-04-19 | Different construct Different mutation/modification Different oligomeric state Different experimental conditions | Assembly 1 Insufficient information Homooligomer；Protein × 2 PDB declaration: dimeric |
Chain A
264–281（18 aa）
Chain B
264–281（18 aa）
|
Not recorded | No recorded non-water small molecule |
SOLUTION NMR
NMR measurement conditions
pH 6.4；281 K；Ionic strength (raw mmCIF value) 0.12 N；Pressure atmospheric
NMR sample composition
1-2 mM | 100 mM NaCl, 10 mM phosphate, 10% Deuterium Oxide, pH 6.4
|
Resolution not provided |
| 1IJ0 Coiled Coil Trimer GCN4-pVLS Ser at Buried D Position Deposited 2001-04-24 | Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental method Different experimental conditions Different structure-quality metrics | Assembly 1 Protein homooligomer Homooligomer；Protein × 3 PDB declaration: trimeric |
Chain A
249–281（33 aa）
Fragment：Coiled coil region
Chain B
249–281（33 aa）
Fragment：Coiled coil region
Chain C
249–281（33 aa）
Fragment：Coiled coil region
|
Mutation：L12S, N16V Non-standard monomer：Yes (specific site not provided by mmCIF) Mutation：L12S, N16V Non-standard monomer：Yes (specific site not provided by mmCIF) Mutation：L12S, N16V Non-standard monomer：Yes (specific site not provided by mmCIF) | ZN ZINC ION × 3 |
X-RAY DIFFRACTION
X-ray crystallization conditions
VAPOR DIFFUSION, HANGING DROP；pH 7；297 K；0.1 M Na Cacodylate,
16% PEG 8000,
0.1 M Zn Acetate, pH 7.0, VAPOR DIFFUSION, HANGING DROP, temperature 297K
|
Resolution 1.86 Å R-free 0.258 |
| 1IJ1 GCN4-pVLT Coiled-coil Trimer with Threonine at the d(12) Position Deposited 2001-04-24 | Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental method Different experimental conditions Different structure-quality metrics | Assembly 1 Protein homooligomer Homooligomer；Protein × 3 PDB declaration: trimeric |
Chain A
249–281（33 aa）
Fragment：COILED COIL REGION
Chain B
249–281（33 aa）
Fragment：COILED COIL REGION
Chain C
249–281（33 aa）
Fragment：COILED COIL REGION
|
Mutation：L12T, N16V Non-standard monomer：Yes (specific site not provided by mmCIF) Mutation：L12T, N16V Non-standard monomer：Yes (specific site not provided by mmCIF) Mutation：L12T, N16V Non-standard monomer：Yes (specific site not provided by mmCIF) | ZN ZINC ION × 3 |
X-RAY DIFFRACTION
X-ray crystallization conditions
VAPOR DIFFUSION, HANGING DROP；pH 6；298 K；0.1 M Na Cacodylate,
20% PEG 8000,
0.2 M Zn Acetate, pH 6.0, VAPOR DIFFUSION, HANGING DROP, temperature 298K
|
Resolution 1.86 Å R-free 0.278 |
| 1IJ2 GCN4-pVTL Coiled-coil Trimer with Threonine at the a(16) position Deposited 2001-04-24 | Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental method Different experimental conditions Different structure-quality metrics | Assembly 1 Protein homooligomer Homooligomer；Protein × 3 PDB declaration: trimeric |
Chain A
249–281（33 aa）
Fragment：COILED COIL REGION
Chain B
249–281（33 aa）
Fragment：COILED COIL REGION
Chain C
249–281（33 aa）
Fragment：COILED COIL REGION
|
Mutation：N16T Non-standard monomer：Yes (specific site not provided by mmCIF) Mutation：N16T Non-standard monomer：Yes (specific site not provided by mmCIF) Mutation：N16T Non-standard monomer：Yes (specific site not provided by mmCIF) | CD CADMIUM ION × 3 |
X-RAY DIFFRACTION
X-ray crystallization conditions
VAPOR DIFFUSION, HANGING DROP；pH 7；298 K；0.1 M HEPES, 25 mM cadmium sulfate, 1 M sodium acetate, pH 7.0, VAPOR DIFFUSION, HANGING DROP, temperature 298K
|
Resolution 1.70 Å R-free 0.279 |
| 1IJ3 GCN4-pVSL Coiled-coil trimer with Serine at the a(16) position Deposited 2001-04-24 | Different construct Different mutation/modification Different oligomeric state Different experimental method Different experimental conditions Different structure-quality metrics | Assembly 1 Protein homooligomer Homooligomer；Protein × 3 PDB declaration: trimeric |
Chain A
249–281（33 aa）
Fragment：coiled coil region
Chain B
249–281（33 aa）
Fragment：coiled coil region
Chain C
249–281（33 aa）
Fragment：coiled coil region
|
Mutation：N16S Non-standard monomer：Yes (specific site not provided by mmCIF) Mutation：N16S Non-standard monomer：Yes (specific site not provided by mmCIF) Mutation：N16S Non-standard monomer：Yes (specific site not provided by mmCIF) | No recorded non-water small molecule |
X-RAY DIFFRACTION
X-ray crystallization conditions
VAPOR DIFFUSION, HANGING DROP；pH 6.5；298 K；0.1 M MES, 50 mM cesium chloride, 10% PEG 20000, pH 6.5, VAPOR DIFFUSION, HANGING DROP, temperature 298K
|
Resolution 1.80 Å R-free 0.269 |
| 1KQL Crystal structure of the C-terminal region of striated muscle alpha-tropomyosin at 2.7 angstrom resolution Deposited 2002-01-07 | Different construct Different mutation/modification Different oligomeric state Different experimental method Different experimental conditions Different structure-quality metrics | Assembly 1 Protein homooligomer Homooligomer；Protein × 2 PDB declaration: dimeric |
Chain A
255–278（24 aa）
Chain B
255–278（24 aa）
|
Not recorded | No recorded non-water small molecule |
X-RAY DIFFRACTION
X-ray crystallization conditions
VAPOR DIFFUSION, SITTING DROP；pH 8.3；295 K；PEG 550 monomethylether, glycerol, sodium chloride, magnesium acetate, bicine, tris buffer, dithiothreitol, pH 8.3, VAPOR DIFFUSION, SITTING DROP, temperature 295K
|
Resolution 2.70 Å R-free 0.289 |
| 1KQL Crystal structure of the C-terminal region of striated muscle alpha-tropomyosin at 2.7 angstrom resolution Deposited 2002-01-07 | Different construct Different mutation/modification Different oligomeric state Different experimental method Different experimental conditions Different structure-quality metrics | Assembly 2 Protein homooligomer Homooligomer；Protein × 4 PDB declaration: tetrameric |
Chain A
255–278（24 aa）
Chain B
255–278（24 aa）
|
Not recorded | No recorded non-water small molecule |
X-RAY DIFFRACTION
X-ray crystallization conditions
VAPOR DIFFUSION, SITTING DROP；pH 8.3；295 K；PEG 550 monomethylether, glycerol, sodium chloride, magnesium acetate, bicine, tris buffer, dithiothreitol, pH 8.3, VAPOR DIFFUSION, SITTING DROP, temperature 295K
|
Resolution 2.70 Å R-free 0.289 |
| 1LD4 Placement of the Structural Proteins in Sindbis Virus Deposited 2002-04-08 | Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental method Different experimental conditions Different structure-quality metrics | Assembly 1 Protein heterocomplex Heteromer；Protein × 960 PDB declaration: 960-MERIC |
Chain E
225–281（57 aa）
Fragment：LEUCINE-ZIPPER (residues 225-281)
Chain F
225–281（57 aa）
Fragment：LEUCINE-ZIPPER (residues 225-281)
Chain G
225–281（57 aa）
Fragment：LEUCINE-ZIPPER (residues 225-281)
Chain H
225–281（57 aa）
Fragment：LEUCINE-ZIPPER (residues 225-281)
Chain I
225–281（57 aa）
Fragment：LEUCINE-ZIPPER (residues 225-281)
Chain J
225–281（57 aa）
Fragment：LEUCINE-ZIPPER (residues 225-281)
Chain K
225–281（57 aa）
Fragment：LEUCINE-ZIPPER (residues 225-281)
Chain L
225–281（57 aa）
Fragment：LEUCINE-ZIPPER (residues 225-281)
|
Not recorded | UNX UNKNOWN LIGAND × 1920 |
ELECTRON MICROSCOPY
cryo-EM buffer
50mM Tris-HCl, 200mM NaCl, 0.1mM EDTA；pH 7.5；50mM Tris-HCl, 200mM NaCl, 0.1mM EDTA
|
Resolution 11.40 Å |
| 1LD4 Placement of the Structural Proteins in Sindbis Virus Deposited 2002-04-08 | Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental method Different experimental conditions Different structure-quality metrics | Assembly 2 Protein heterocomplex Heteromer；Protein × 16 PDB declaration: hexadecameric |
Chain E
225–281（57 aa）
Fragment：LEUCINE-ZIPPER (residues 225-281)
Chain F
225–281（57 aa）
Fragment：LEUCINE-ZIPPER (residues 225-281)
Chain G
225–281（57 aa）
Fragment：LEUCINE-ZIPPER (residues 225-281)
Chain H
225–281（57 aa）
Fragment：LEUCINE-ZIPPER (residues 225-281)
Chain I
225–281（57 aa）
Fragment：LEUCINE-ZIPPER (residues 225-281)
Chain J
225–281（57 aa）
Fragment：LEUCINE-ZIPPER (residues 225-281)
Chain K
225–281（57 aa）
Fragment：LEUCINE-ZIPPER (residues 225-281)
Chain L
225–281（57 aa）
Fragment：LEUCINE-ZIPPER (residues 225-281)
|
Not recorded | UNX UNKNOWN LIGAND × 32 |
ELECTRON MICROSCOPY
cryo-EM buffer
50mM Tris-HCl, 200mM NaCl, 0.1mM EDTA；pH 7.5；50mM Tris-HCl, 200mM NaCl, 0.1mM EDTA
|
Resolution 11.40 Å |
| 1LD4 Placement of the Structural Proteins in Sindbis Virus Deposited 2002-04-08 | Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental method Different experimental conditions Different structure-quality metrics | Assembly 3 Protein heterocomplex Heteromer；Protein × 80 PDB declaration: 80-meric |
Chain E
225–281（57 aa）
Fragment：LEUCINE-ZIPPER (residues 225-281)
Chain F
225–281（57 aa）
Fragment：LEUCINE-ZIPPER (residues 225-281)
Chain G
225–281（57 aa）
Fragment：LEUCINE-ZIPPER (residues 225-281)
Chain H
225–281（57 aa）
Fragment：LEUCINE-ZIPPER (residues 225-281)
Chain I
225–281（57 aa）
Fragment：LEUCINE-ZIPPER (residues 225-281)
Chain J
225–281（57 aa）
Fragment：LEUCINE-ZIPPER (residues 225-281)
Chain K
225–281（57 aa）
Fragment：LEUCINE-ZIPPER (residues 225-281)
Chain L
225–281（57 aa）
Fragment：LEUCINE-ZIPPER (residues 225-281)
|
Not recorded | UNX UNKNOWN LIGAND × 160 |
ELECTRON MICROSCOPY
cryo-EM buffer
50mM Tris-HCl, 200mM NaCl, 0.1mM EDTA；pH 7.5；50mM Tris-HCl, 200mM NaCl, 0.1mM EDTA
|
Resolution 11.40 Å |
| 1LD4 Placement of the Structural Proteins in Sindbis Virus Deposited 2002-04-08 | Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental method Different experimental conditions Different structure-quality metrics | Assembly 4 Protein heterocomplex Heteromer；Protein × 96 PDB declaration: 96-meric |
Chain E
225–281（57 aa）
Fragment：LEUCINE-ZIPPER (residues 225-281)
Chain F
225–281（57 aa）
Fragment：LEUCINE-ZIPPER (residues 225-281)
Chain G
225–281（57 aa）
Fragment：LEUCINE-ZIPPER (residues 225-281)
Chain H
225–281（57 aa）
Fragment：LEUCINE-ZIPPER (residues 225-281)
Chain I
225–281（57 aa）
Fragment：LEUCINE-ZIPPER (residues 225-281)
Chain J
225–281（57 aa）
Fragment：LEUCINE-ZIPPER (residues 225-281)
Chain K
225–281（57 aa）
Fragment：LEUCINE-ZIPPER (residues 225-281)
Chain L
225–281（57 aa）
Fragment：LEUCINE-ZIPPER (residues 225-281)
|
Not recorded | UNX UNKNOWN LIGAND × 192 |
ELECTRON MICROSCOPY
cryo-EM buffer
50mM Tris-HCl, 200mM NaCl, 0.1mM EDTA；pH 7.5；50mM Tris-HCl, 200mM NaCl, 0.1mM EDTA
|
Resolution 11.40 Å |
| 1LD4 Placement of the Structural Proteins in Sindbis Virus Deposited 2002-04-08 | Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental method Different experimental conditions Different structure-quality metrics | Assembly 5 Protein heterocomplex Heteromer；Protein × 16 PDB declaration: hexadecameric |
Chain E
225–281（57 aa）
Fragment：LEUCINE-ZIPPER (residues 225-281)
Chain F
225–281（57 aa）
Fragment：LEUCINE-ZIPPER (residues 225-281)
Chain G
225–281（57 aa）
Fragment：LEUCINE-ZIPPER (residues 225-281)
Chain H
225–281（57 aa）
Fragment：LEUCINE-ZIPPER (residues 225-281)
Chain I
225–281（57 aa）
Fragment：LEUCINE-ZIPPER (residues 225-281)
Chain J
225–281（57 aa）
Fragment：LEUCINE-ZIPPER (residues 225-281)
Chain K
225–281（57 aa）
Fragment：LEUCINE-ZIPPER (residues 225-281)
Chain L
225–281（57 aa）
Fragment：LEUCINE-ZIPPER (residues 225-281)
|
Not recorded | UNX UNKNOWN LIGAND × 32 |
ELECTRON MICROSCOPY
cryo-EM buffer
50mM Tris-HCl, 200mM NaCl, 0.1mM EDTA；pH 7.5；50mM Tris-HCl, 200mM NaCl, 0.1mM EDTA
|
Resolution 11.40 Å |
| 1LLM Crystal Structure of a Zif23-GCN4 Chimera Bound to DNA Deposited 2002-04-29 | Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental method Different experimental conditions Different structure-quality metrics | Assembly 1 Insufficient information Homooligomer；Protein × 2 PDB declaration: tetrameric |
Chain C
253–281（29 aa）
Chain D
253–281（29 aa）
|
Not recorded | ZN ZINC ION × 4 |
X-RAY DIFFRACTION
X-ray crystallization conditions
VAPOR DIFFUSION, HANGING DROP；pH 8；298 K；bis-tris propane, magnesium chloride, ammonium acetate, pH 8, VAPOR DIFFUSION, HANGING DROP, temperature 298K
|
Resolution 1.50 Å R-free 0.234 |
| 1NKN VISUALIZING AN UNSTABLE COILED COIL: THE CRYSTAL STRUCTURE OF AN N-TERMINAL SEGMENT OF THE SCALLOP MYOSIN ROD Deposited 2003-01-03 | Different construct Different mutation/modification Different oligomeric state Different experimental method Different experimental conditions Different structure-quality metrics | Assembly 1 Protein homooligomer Homooligomer；Protein × 2 PDB declaration: dimeric |
Chain A
250–281（32 aa）
Chain B
250–281（32 aa）
|
Not recorded | No recorded non-water small molecule |
X-RAY DIFFRACTION
X-ray crystallization conditions
VAPOR DIFFUSION, HANGING DROP；pH 6.9；289 K；sodium chloride, sodium azide, MOPS, PEG 200 MME, pH 6.9, VAPOR DIFFUSION, HANGING DROP, temperature 289K
|
Resolution 2.50 Å R-free 0.289 |
| 1NKN VISUALIZING AN UNSTABLE COILED COIL: THE CRYSTAL STRUCTURE OF AN N-TERMINAL SEGMENT OF THE SCALLOP MYOSIN ROD Deposited 2003-01-03 | Different construct Different mutation/modification Different oligomeric state Different experimental method Different experimental conditions Different structure-quality metrics | Assembly 2 Protein homooligomer Homooligomer；Protein × 2 PDB declaration: dimeric |
Chain C
250–281（32 aa）
Chain D
250–281（32 aa）
|
Not recorded | No recorded non-water small molecule |
X-RAY DIFFRACTION
X-ray crystallization conditions
VAPOR DIFFUSION, HANGING DROP；pH 6.9；289 K；sodium chloride, sodium azide, MOPS, PEG 200 MME, pH 6.9, VAPOR DIFFUSION, HANGING DROP, temperature 289K
|
Resolution 2.50 Å R-free 0.289 |
| 1PIQ CRYSTAL STRUCTURE OF GCN4-PIQ, A TRIMERIC COILED COIL WITH BURIED POLAR RESIDUES Deposited 1998-09-25 | Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental method Different experimental conditions Different structure-quality metrics | Assembly 1 Protein homooligomer Homooligomer；Protein × 3 PDB declaration: trimeric |
Chain A
249–279（31 aa）
Fragment：COILED-COIL DOMAIN
|
Mutation：L5I, V9I, L12I, N16Q, L19I, V23I, L26I, V30I Non-standard monomer：Yes (specific site not provided by mmCIF) | CL CHLORIDE ION × 3 |
X-RAY DIFFRACTION
X-ray crystallization conditions
pH 4.5；PROTEIN WAS CRYSTALLIZED FROM: 75 MM NAAC PH4.5, 20 MM MGCL2 AND 23% MPD
|
Resolution 1.80 Å R-free 0.236 |
| 1RB4 ANTIPARALLEL TRIMER OF GCN4-LEUCINE ZIPPER CORE MUTANT AS N16A TETRAGONAL AUTOMATIC SOLUTION Deposited 2003-11-01 | Different construct Different mutation/modification Different oligomeric state Different experimental method Different experimental conditions Different structure-quality metrics | Assembly 1 Protein homooligomer Homooligomer；Protein × 3 PDB declaration: trimeric |
Chain A
249–281（33 aa）
Fragment：LEUCINE-ZIPPER (RESIDUES 249-281)
Chain B
249–281（33 aa）
Fragment：LEUCINE-ZIPPER (RESIDUES 249-281)
Chain C
249–281（33 aa）
Fragment：LEUCINE-ZIPPER (RESIDUES 249-281)
|
Mutation：N16A Mutation：N16A Mutation：N16A | No recorded non-water small molecule |
X-RAY DIFFRACTION
X-ray crystallization conditions
VAPOR DIFFUSION, SITTING DROP；pH 7.3；298 K；25 mM phosphate pH 7.3 400 mM NaCl 15% PEG8000, VAPOR DIFFUSION, SITTING DROP, temperature 298K
|
Resolution 1.90 Å R-free 0.307 |
| 1RB5 ANTIPARALLEL TRIMER OF GCN4-LEUCINE ZIPPER CORE MUTANT AS N16A TRIGONAL FORM Deposited 2003-11-01 | Different construct Different mutation/modification Different oligomeric state Different experimental method Different experimental conditions Different structure-quality metrics | Assembly 1 Protein homooligomer Homooligomer；Protein × 3 PDB declaration: trimeric |
Chain A
249–281（33 aa）
Fragment：LEUCINE-ZIPPER (RESIDUES 249-281)
Chain B
249–281（33 aa）
Fragment：LEUCINE-ZIPPER (RESIDUES 249-281)
Chain C
249–281（33 aa）
Fragment：LEUCINE-ZIPPER (RESIDUES 249-281)
|
Mutation：N16A Non-standard monomer：Yes (specific site not provided by mmCIF) Mutation：N16A Non-standard monomer：Yes (specific site not provided by mmCIF) Mutation：N16A Non-standard monomer：Yes (specific site not provided by mmCIF) | No recorded non-water small molecule |
X-RAY DIFFRACTION
X-ray crystallization conditions
VAPOR DIFFUSION, SITTING DROP；pH 7.3；298 K；100mM bis-tris, pH 7.3, VAPOR DIFFUSION, SITTING DROP, temperature 298K
|
Resolution 1.90 Å R-free 0.257 |
| 1RB6 ANTIPARALLEL TRIMER OF GCN4-LEUCINE ZIPPER CORE MUTANT AS N16A TETRAGONAL FORM Deposited 2003-11-01 | Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental method Different experimental conditions Different structure-quality metrics | Assembly 1 Protein homooligomer Homooligomer；Protein × 3 PDB declaration: trimeric |
Chain A
249–281（33 aa）
Fragment：LEUCINE-ZIPPER (RESIDUES 249-281)
Chain B
249–281（33 aa）
Fragment：LEUCINE-ZIPPER (RESIDUES 249-281)
Chain C
249–281（33 aa）
Fragment：LEUCINE-ZIPPER (RESIDUES 249-281)
|
Mutation：N16A Non-standard monomer：Yes (specific site not provided by mmCIF) Mutation：N16A Non-standard monomer：Yes (specific site not provided by mmCIF) Mutation：N16A Non-standard monomer：Yes (specific site not provided by mmCIF) | CL CHLORIDE ION × 8 K POTASSIUM ION × 2 |
X-RAY DIFFRACTION
X-ray crystallization conditions
VAPOR DIFFUSION, SITTING DROP；pH 7.3；298 K；25 mM phosphate 400 mM NaCl 15% PEG8000, pH 7.3, VAPOR DIFFUSION, SITTING DROP, temperature 298K
|
Resolution 1.90 Å R-free 0.241 |
| 1SWI GCN4-LEUCINE ZIPPER CORE MUTANT AS N16A COMPLEXED WITH BENZENE Deposited 1996-05-09 | Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental method Different structure-quality metrics | Assembly 1 Protein homooligomer Homooligomer；Protein × 3 PDB declaration: trimeric |
Chain A
249–281（33 aa）
Chain B
249–281（33 aa）
Chain C
249–281（33 aa）
|
Mutation：N16A Mutation：N16A Mutation：N16A | BNZ BENZENE × 1 | X-RAY DIFFRACTION mmCIF provides none of the parsed conditions | Resolution 2.60 Å |
| 1TMZ TMZIP: A CHIMERIC PEPTIDE MODEL OF THE N-TERMINUS OF ALPHA TROPOMYOSIN, NMR, 15 STRUCTURES Deposited 1998-04-20 | Different construct Different mutation/modification Different oligomeric state Different experimental conditions | Assembly 1 Protein homooligomer Homooligomer；Protein × 2 PDB declaration: dimeric |
Chain A
250–281（32 aa）
Chain B
250–281（32 aa）
|
Not recorded | No recorded non-water small molecule |
SOLUTION NMR
NMR measurement conditions
pH 6.4；288 K
|
Resolution not provided |
| 1UNT Structure Based Engineering of Internal Molecular Surfaces Of Four Helix Bundles Deposited 2003-09-15 | Different construct Different mutation/modification Different oligomeric state Different experimental method Different experimental conditions Different structure-quality metrics | Assembly 1 Protein homooligomer Homooligomer；Protein × 4 PDB declaration: tetrameric |
Chain A
249–281（33 aa）
Chain B
249–281（33 aa）
|
Mutation：YES Non-standard monomer：Yes (specific site not provided by mmCIF) Mutation：YES Non-standard monomer：Yes (specific site not provided by mmCIF) | No recorded non-water small molecule |
X-RAY DIFFRACTION
X-ray crystallization conditions
VAPOR DIFFUSION, HANGING DROP；pH 7；HANGING DROP, RESERVOIR: 10%W/V PEG 6K, 2 M NACL, PH 7.0
|
Resolution 2.07 Å R-free 0.286 |
| 1UNU Structure Based Engineering of Internal Molecular Surfaces Of Four Helix Bundles Deposited 2003-09-15 | Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental method Different experimental conditions Different structure-quality metrics | Assembly 1 Protein homooligomer Homooligomer；Protein × 4 PDB declaration: tetrameric |
Chain A
249–281（33 aa）
Chain B
249–281（33 aa）
|
Mutation：YES Non-standard monomer：Yes (specific site not provided by mmCIF) Mutation：YES Non-standard monomer：Yes (specific site not provided by mmCIF) | CL CHLORIDE ION × 2 |
X-RAY DIFFRACTION
X-ray crystallization conditions
VAPOR DIFFUSION, HANGING DROP；pH 7；HANGING DROP, RESERVOIR: 10%W/V PEG 6K, 2 M NACL, PH 7.0
|
Resolution 2.07 Å R-free 0.273 |
| 1UNV Structure Based Engineering of Internal Molecular Surfaces Of Four Helix Bundles Deposited 2003-09-15 | Different construct Different mutation/modification Different oligomeric state Different experimental method Different experimental conditions Different structure-quality metrics | Assembly 1 Protein homooligomer Homooligomer；Protein × 4 PDB declaration: tetrameric |
Chain A
249–281（33 aa）
Chain B
249–281（33 aa）
|
Mutation：YES Non-standard monomer：Yes (specific site not provided by mmCIF) Mutation：YES Non-standard monomer：Yes (specific site not provided by mmCIF) | No recorded non-water small molecule |
X-RAY DIFFRACTION
X-ray crystallization conditions
VAPOR DIFFUSION, HANGING DROP；pH 7；HANGING DROP, RESERVOIR: 10%W/V PEG 6K, 2 M NACL, PH 7.0
|
Resolution 2.14 Å R-free 0.302 |
| 1UNW Structure Based Engineering of Internal Molecular Surfaces Of Four Helix Bundles Deposited 2003-09-15 | Different construct Different mutation/modification Different oligomeric state Different experimental method Different experimental conditions Different structure-quality metrics | Assembly 1 Protein homooligomer Homooligomer；Protein × 4 PDB declaration: tetrameric |
Chain A
249–281（33 aa）
Chain B
249–281（33 aa）
|
Mutation：YES Non-standard monomer：Yes (specific site not provided by mmCIF) Mutation：YES Non-standard monomer：Yes (specific site not provided by mmCIF) | No recorded non-water small molecule |
X-RAY DIFFRACTION
X-ray crystallization conditions
pH 7；10% W/V PEG 8K, 100 MM TRIS, 200 MM MGCL2, PH 7.0
|
Resolution 2.20 Å R-free 0.284 |
| 1UNX Structure Based Engineering of Internal Molecular Surfaces Of Four Helix Bundles Deposited 2003-09-15 | Different construct Different mutation/modification Different oligomeric state Different experimental method Different experimental conditions Different structure-quality metrics | Assembly 1 Protein homooligomer Homooligomer；Protein × 4 PDB declaration: tetrameric |
Chain A
249–281（33 aa）
Chain B
249–281（33 aa）
|
Mutation：YES Non-standard monomer：Yes (specific site not provided by mmCIF) Mutation：YES Non-standard monomer：Yes (specific site not provided by mmCIF) | No recorded non-water small molecule |
X-RAY DIFFRACTION
X-ray crystallization conditions
pH 7；2.5 M NACL, 100 MM NAAC, 200 MM LI2SO4, pH 7.00
|
Resolution 2.40 Å R-free 0.306 |
| 1UNY Structure Based Engineering of Internal Molecular Surfaces Of Four Helix Bundles Deposited 2003-09-15 | Different construct Different mutation/modification Different oligomeric state Different experimental method Different experimental conditions Different structure-quality metrics | Assembly 1 Protein homooligomer Homooligomer；Protein × 4 PDB declaration: tetrameric |
Chain A
249–281（33 aa）
Chain B
249–281（33 aa）
|
Mutation：YES Non-standard monomer：Yes (specific site not provided by mmCIF) Mutation：YES Non-standard monomer：Yes (specific site not provided by mmCIF) | No recorded non-water small molecule |
X-RAY DIFFRACTION
X-ray crystallization conditions
pH 7；2.5 M NACL, 100 MM NAAC, 200 MM LI2SO4, PH 4.5
|
Resolution 2.30 Å R-free 0.322 |
| 1UNZ Structure Based Engineering of Internal Molecular Surfaces Of Four Helix Bundles Deposited 2003-09-15 | Different construct Different mutation/modification Different oligomeric state Different experimental method Different experimental conditions Different structure-quality metrics | Assembly 1 Protein homooligomer Homooligomer；Protein × 4 PDB declaration: tetrameric |
Chain A
249–281（33 aa）
Chain B
249–281（33 aa）
|
Mutation：YES Non-standard monomer：Yes (specific site not provided by mmCIF) Mutation：YES Non-standard monomer：Yes (specific site not provided by mmCIF) | No recorded non-water small molecule |
X-RAY DIFFRACTION
X-ray crystallization conditions
pH 7；2.5 M NACL, 100 MM NAAC, 200 MM LI2SO4, PH 4.5
|
Resolution 2.30 Å R-free 0.314 |
| 1UO0 Structure Based Engineering of Internal Molecular Surfaces Of Four Helix Bundles Deposited 2003-09-15 | Different construct Different mutation/modification Different oligomeric state Different experimental method Different experimental conditions Different structure-quality metrics | Assembly 1 Protein homooligomer Homooligomer；Protein × 4 PDB declaration: tetrameric |
Chain A
249–281（33 aa）
Chain B
249–281（33 aa）
|
Mutation：YES Non-standard monomer：Yes (specific site not provided by mmCIF) Mutation：YES Non-standard monomer：Yes (specific site not provided by mmCIF) | No recorded non-water small molecule |
X-RAY DIFFRACTION
X-ray crystallization conditions
pH 7；2.5 M NACL, 100 MM NAAC, 200 MM LI2SO4, PH 4.5
|
Resolution 2.40 Å R-free 0.299 |
| 1UO1 Structure Based Engineering of Internal Molecular Surfaces Of Four Helix Bundles Deposited 2003-09-15 | Different construct Different mutation/modification Different oligomeric state Different experimental method Different experimental conditions Different structure-quality metrics | Assembly 1 Protein homooligomer Homooligomer；Protein × 4 PDB declaration: tetrameric |
Chain A
249–281（33 aa）
Chain B
249–281（33 aa）
|
Mutation：YES Non-standard monomer：Yes (specific site not provided by mmCIF) Mutation：YES Non-standard monomer：Yes (specific site not provided by mmCIF) | No recorded non-water small molecule |
X-RAY DIFFRACTION
X-ray crystallization conditions
pH 7；2.5 M NACL, 100 MM NAAC, 200 MM LI2SO4, PH 4.5
|
Resolution 2.50 Å R-free 0.302 |
| 1UO2 Structure Based Engineering of Internal Molecular Surfaces Of Four Helix Bundles Deposited 2003-09-15 | Different construct Different mutation/modification Different oligomeric state Different experimental method Different experimental conditions Different structure-quality metrics | Assembly 1 Protein homooligomer Homooligomer；Protein × 4 PDB declaration: tetrameric |
Chain A
249–281（33 aa）
Chain B
249–281（33 aa）
|
Non-standard monomer：Yes (specific site not provided by mmCIF) Non-standard monomer：Yes (specific site not provided by mmCIF) | No recorded non-water small molecule |
X-RAY DIFFRACTION
X-ray crystallization conditions
VAPOR DIFFUSION, HANGING DROP；pH 7；HANGING DROP, RESERVOIR: 2.5 M NACL, 100 MM NAAC, 200 MM LI2SO4, PH 4.5
|
Resolution 1.99 Å R-free 0.286 |
| 1UO3 Structure Based Engineering of Internal Molecular Surfaces Of Four Helix Bundles Deposited 2003-09-15 | Different construct Different mutation/modification Different oligomeric state Different experimental method Different experimental conditions Different structure-quality metrics | Assembly 1 Protein homooligomer Homooligomer；Protein × 4 PDB declaration: tetrameric |
Chain A
249–281（33 aa）
Chain B
249–281（33 aa）
|
Mutation：YES Non-standard monomer：Yes (specific site not provided by mmCIF) Mutation：YES Non-standard monomer：Yes (specific site not provided by mmCIF) | No recorded non-water small molecule |
X-RAY DIFFRACTION
X-ray crystallization conditions
VAPOR DIFFUSION, HANGING DROP；pH 7；HANGING DROP, RESERVOIR: 10%W/V PEG 6K, 2 M NACL, PH 7.0
|
Resolution 1.92 Å R-free 0.284 |
| 1UO4 Structure Based Engineering of Internal Molecular Surfaces Of Four Helix Bundles Deposited 2003-09-15 | Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental method Different experimental conditions Different structure-quality metrics | Assembly 1 Protein homooligomer Homooligomer；Protein × 4 PDB declaration: tetrameric |
Chain A
249–281（33 aa）
Chain B
249–281（33 aa）
|
Mutation：YES Non-standard monomer：Yes (specific site not provided by mmCIF) Mutation：YES Non-standard monomer：Yes (specific site not provided by mmCIF) | CL CHLORIDE ION × 2 PIH iodobenzene × 2 |
X-RAY DIFFRACTION
X-ray crystallization conditions
VAPOR DIFFUSION, HANGING DROP；pH 7；HANGING DROP, RESERVOIR: 10%W/V PEG 6K, 2 M NACL, PH 7.0
|
Resolution 1.70 Å R-free 0.257 |
| 1UO5 Structure Based Engineering of Internal Molecular Surfaces Of Four Helix Bundles Deposited 2003-09-15 | Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental method Different experimental conditions Different structure-quality metrics | Assembly 1 Protein homooligomer Homooligomer；Protein × 4 PDB declaration: tetrameric |
Chain A
249–281（33 aa）
Chain B
249–281（33 aa）
|
Mutation：YES Non-standard monomer：Yes (specific site not provided by mmCIF) Mutation：YES Non-standard monomer：Yes (specific site not provided by mmCIF) | CL CHLORIDE ION × 2 PIH iodobenzene × 2 |
X-RAY DIFFRACTION
X-ray crystallization conditions
VAPOR DIFFUSION, HANGING DROP；pH 7；HANGING DROP, RESERVOIR: 10%W/V PEG 6K, 2 M NACL, PH 7.0
|
Resolution 2.07 Å R-free 0.283 |
| 1W5G An anti-parallel four helix bundle (acetimide modification). Deposited 2004-08-06 | Different construct Different mutation/modification Different oligomeric state Different experimental method Different experimental conditions Different structure-quality metrics | Assembly 1 Protein homooligomer Homooligomer；Protein × 4 PDB declaration: tetrameric |
Chain A
249–281（33 aa）
Chain B
249–281（33 aa）
|
Mutation：YES Mutation：YES | No recorded non-water small molecule |
X-RAY DIFFRACTION
X-ray crystallization conditions
VAPOR DIFFUSION, HANGING DROP；pH 10；HANGING DROP, 1UL OF 1MG/ML PEPTIDE IN WATER, 1UL 100MM CAPS, 30% PEG 400, PH 10.5.
|
Resolution 2.16 Å R-free 0.337 |
| 1W5H An anti-parallel four helix bundle. Deposited 2004-08-06 | Different construct Different mutation/modification Different oligomeric state Different experimental method Different experimental conditions Different structure-quality metrics | Assembly 1 Protein homooligomer Homooligomer；Protein × 4 PDB declaration: tetrameric |
Chain A
249–281（33 aa）
Chain B
249–281（33 aa）
|
Mutation：YES Mutation：YES | No recorded non-water small molecule |
X-RAY DIFFRACTION
X-ray crystallization conditions
VAPOR DIFFUSION, HANGING DROP；pH 10.5；HANGING DROP, 1UL OF 1MG/ML PEPTIDE IN WATER, 1UL 100MM CAPS, 30% PEG 400, PH 10.5.
|
Resolution 2.50 Å R-free 0.344 |
| 1W5I ABA does not affect topology of pLI. Deposited 2004-08-07 | Different construct Different mutation/modification Different oligomeric state Different experimental method Different experimental conditions Different structure-quality metrics | Assembly 1 Protein homooligomer Homooligomer；Protein × 4 PDB declaration: tetrameric |
Chain A
249–281（33 aa）
Chain B
249–281（33 aa）
|
Not recorded | No recorded non-water small molecule |
X-RAY DIFFRACTION
X-ray crystallization conditions
VAPOR DIFFUSION, HANGING DROP；HANGING DROP, 1 UL OF 10MG/ML PEPTIDE IN WATER TO 1UL OF 2M NACL 10% PEG 6K.
|
Resolution 2.30 Å R-free 0.295 |
| 1W5J AN ANTI-PARALLEL FOUR HELIX BUNDLE Deposited 2004-08-07 | Different construct Different mutation/modification Different oligomeric state Different experimental method Different experimental conditions Different structure-quality metrics | Assembly 1 Protein homooligomer Homooligomer；Protein × 4 PDB declaration: tetrameric |
Chain A
249–281（33 aa）
Chain B
249–281（33 aa）
|
Mutation：YES Non-standard monomer：Yes (specific site not provided by mmCIF) Mutation：YES Non-standard monomer：Yes (specific site not provided by mmCIF) | No recorded non-water small molecule |
X-RAY DIFFRACTION
X-ray crystallization conditions
VAPOR DIFFUSION, HANGING DROP；pH 5.6；HANGING DROP, 1 UL OF 10 MG/ML PEPTIDE IN WATER TO 1UL OF 0.07M TRI-SODIUM CITRATE DIHYDRATE PH 5.6 0.7M AMMONIUM DIHYDROGEN PHOSPHATE %30 V/V GLYCEROL, HAMPTON CRYSTAL SCREEN CRYO NUMBER 11
|
Resolution 2.20 Å R-free 0.285 |
| 1W5J AN ANTI-PARALLEL FOUR HELIX BUNDLE Deposited 2004-08-07 | Different construct Different mutation/modification Different oligomeric state Different experimental method Different experimental conditions Different structure-quality metrics | Assembly 2 Protein homooligomer Homooligomer；Protein × 4 PDB declaration: tetrameric |
Chain C
249–281（33 aa）
Chain D
249–281（33 aa）
|
Mutation：YES Non-standard monomer：Yes (specific site not provided by mmCIF) Mutation：YES Non-standard monomer：Yes (specific site not provided by mmCIF) | No recorded non-water small molecule |
X-RAY DIFFRACTION
X-ray crystallization conditions
VAPOR DIFFUSION, HANGING DROP；pH 5.6；HANGING DROP, 1 UL OF 10 MG/ML PEPTIDE IN WATER TO 1UL OF 0.07M TRI-SODIUM CITRATE DIHYDRATE PH 5.6 0.7M AMMONIUM DIHYDROGEN PHOSPHATE %30 V/V GLYCEROL, HAMPTON CRYSTAL SCREEN CRYO NUMBER 11
|
Resolution 2.20 Å R-free 0.285 |
| 1W5K AN ANTI-PARALLEL FOUR HELIX BUNDLE Deposited 2004-08-07 | Different construct Different mutation/modification Different oligomeric state Different experimental method Different experimental conditions Different structure-quality metrics | Assembly 1 Protein homooligomer Homooligomer；Protein × 4 PDB declaration: tetrameric |
Chain A
249–281（33 aa）
Chain B
249–281（33 aa）
|
Mutation：YES Non-standard monomer：Yes (specific site not provided by mmCIF) Mutation：YES Non-standard monomer：Yes (specific site not provided by mmCIF) | No recorded non-water small molecule |
X-RAY DIFFRACTION
X-ray crystallization conditions
VAPOR DIFFUSION, HANGING DROP；pH 5；HANGING DROP, 1UL OF 10MG/ML PEPTIDE IN WATER, 1UL 100MM CAPS, 30% PEG 400, PH 10.5, 1UL OF 50MM TCEP IN WATER
|
Resolution 1.92 Å R-free 0.307 |
| 1W5K AN ANTI-PARALLEL FOUR HELIX BUNDLE Deposited 2004-08-07 | Different construct Different mutation/modification Different oligomeric state Different experimental method Different experimental conditions Different structure-quality metrics | Assembly 2 Protein homooligomer Homooligomer；Protein × 4 PDB declaration: tetrameric |
Chain C
249–281（33 aa）
Chain D
249–281（33 aa）
|
Mutation：YES Non-standard monomer：Yes (specific site not provided by mmCIF) Mutation：YES Non-standard monomer：Yes (specific site not provided by mmCIF) | No recorded non-water small molecule |
X-RAY DIFFRACTION
X-ray crystallization conditions
VAPOR DIFFUSION, HANGING DROP；pH 5；HANGING DROP, 1UL OF 10MG/ML PEPTIDE IN WATER, 1UL 100MM CAPS, 30% PEG 400, PH 10.5, 1UL OF 50MM TCEP IN WATER
|
Resolution 1.92 Å R-free 0.307 |
| 1W5L An anti-parallel to parallel switch. Deposited 2004-08-07 | Different construct Different mutation/modification Different oligomeric state Different experimental method Different experimental conditions Different structure-quality metrics | Assembly 1 Protein homooligomer Homooligomer；Protein × 4 PDB declaration: tetrameric |
Chain A
249–281（33 aa）
Chain B
249–281（33 aa）
|
Mutation：YES Mutation：YES | No recorded non-water small molecule |
X-RAY DIFFRACTION
X-ray crystallization conditions
VAPOR DIFFUSION, HANGING DROP；HANGING DROP, 1 UL OF 10 MG/ML PEPTIDE IN WATER TO 1 UL OF 2M NACL 10% PEG 6K.
|
Resolution 2.17 Å R-free 0.292 |
| 1YSA THE GCN4 BASIC REGION LEUCINE ZIPPER BINDS DNA AS A DIMER OF UNINTERRUPTED ALPHA HELICES: CRYSTAL STRUCTURE OF THE PROTEIN-DNA COMPLEX Deposited 1993-08-09 | Different construct Different mutation/modification Different oligomeric state Different experimental method Different experimental conditions Different structure-quality metrics | Assembly 1 Protein–DNA Homooligomer；Protein × 2 PDB declaration: tetrameric |
Chain C
226–281（56 aa）
Chain D
226–281（56 aa）
|
Not recorded | No recorded non-water small molecule |
X-RAY DIFFRACTION
X-ray crystallization conditions
VAPOR DIFFUSION, HANGING DROP；pH 5.75；295 K；pH 5.75, VAPOR DIFFUSION, HANGING DROP, temperature 295.00K
TWO ADENINES, B22 AND B23, WHICH ARE NEAR THE 5-PRIME END
OF DNA CHAIN B ARE LOOPED OUT OF THE DNA HELIX. THIS
CONFORMATION IS PRESENT IN CRYSTALS THAT WERE SOAKED IN
35% (VOL/VOL) POLYETHYLENE GLYCOL MW 400, FOLLOWED BY
RAPID FREEZING AND X-RAY DATA COLLECTION AT -155 DEG.
CENTIGRADE.
|
Resolution 2.90 Å |
| 1ZII GCN4-LEUCINE ZIPPER CORE MUTANT ASN16ABA IN THE DIMERIC STATE Deposited 1996-10-30 | Different construct Different mutation/modification Different oligomeric state Different experimental method Different structure-quality metrics | Assembly 1 Protein homooligomer Homooligomer；Protein × 2 PDB declaration: dimeric |
Chain A
249–281（33 aa）
Chain B
249–281（33 aa）
|
Mutation：ASN 16 REPLACED WITH AMINOBUTYRIC ACID (ABA) Non-standard monomer：Yes (specific site not provided by mmCIF) Mutation：ASN 16 REPLACED WITH AMINOBUTYRIC ACID (ABA) Non-standard monomer：Yes (specific site not provided by mmCIF) | No recorded non-water small molecule | X-RAY DIFFRACTION mmCIF provides none of the parsed conditions | Resolution 1.80 Å |
| 1ZIJ GCN4-LEUCINE ZIPPER CORE MUTANT ASN16ABA IN THE TRIMERIC STATE Deposited 1996-10-30 | Different construct Different mutation/modification Different oligomeric state Different experimental method Different structure-quality metrics | Assembly 1 Protein homooligomer Homooligomer；Protein × 3 PDB declaration: trimeric |
Chain A
249–281（33 aa）
Chain B
249–281（33 aa）
Chain C
249–281（33 aa）
|
Mutation：ASN 16 REPLACED WITH AMINOBUTYRIC ACID (ABA) Non-standard monomer：Yes (specific site not provided by mmCIF) Mutation：ASN 16 REPLACED WITH AMINOBUTYRIC ACID (ABA) Non-standard monomer：Yes (specific site not provided by mmCIF) Mutation：ASN 16 REPLACED WITH AMINOBUTYRIC ACID (ABA) Non-standard monomer：Yes (specific site not provided by mmCIF) | No recorded non-water small molecule | X-RAY DIFFRACTION mmCIF provides none of the parsed conditions | Resolution 2.00 Å |
| 1ZIK GCN4-LEUCINE ZIPPER CORE MUTANT ASN16LYS IN THE DIMERIC STATE Deposited 1996-10-30 | Different construct Different mutation/modification Different oligomeric state Different experimental method Different structure-quality metrics | Assembly 1 Protein homooligomer Homooligomer；Protein × 2 PDB declaration: dimeric |
Chain A
249–281（33 aa）
Chain B
249–281（33 aa）
|
Mutation：N16K Mutation：N16K | No recorded non-water small molecule | X-RAY DIFFRACTION mmCIF provides none of the parsed conditions | Resolution 1.80 Å |
| 1ZIL GCN4-LEUCINE ZIPPER CORE MUTANT ASN16GLN IN THE DIMERIC STATE Deposited 1996-10-30 | Different construct Different mutation/modification Different oligomeric state Different experimental method Different structure-quality metrics | Assembly 1 Protein homooligomer Homooligomer；Protein × 2 PDB declaration: dimeric |
Chain A
249–281（33 aa）
Chain B
249–281（33 aa）
|
Mutation：N16Q Mutation：N16Q | No recorded non-water small molecule | X-RAY DIFFRACTION mmCIF provides none of the parsed conditions | Resolution 2.25 Å |
| 1ZIM GCN4-LEUCINE ZIPPER CORE MUTANT ASN16GLN IN THE TRIMERIC STATE Deposited 1996-10-30 | Different construct Different mutation/modification Different oligomeric state Different experimental method Different structure-quality metrics | Assembly 1 Protein homooligomer Homooligomer；Protein × 3 PDB declaration: trimeric |
Chain A
249–281（33 aa）
Chain B
249–281（33 aa）
Chain C
249–281（33 aa）
|
Mutation：N16Q Non-standard monomer：Yes (specific site not provided by mmCIF) Mutation：N16Q Non-standard monomer：Yes (specific site not provided by mmCIF) Mutation：N16Q Non-standard monomer：Yes (specific site not provided by mmCIF) | No recorded non-water small molecule | X-RAY DIFFRACTION mmCIF provides none of the parsed conditions | Resolution 2.00 Å |
| 2AHP GCN4 leucine zipper, mutation of Lys15 to epsilon-azido-Lys Deposited 2005-07-28 | Different construct Different mutation/modification Different oligomeric state Different experimental method Different experimental conditions Different structure-quality metrics | Assembly 1 Protein homooligomer Homooligomer；Protein × 2 PDB declaration: dimeric |
Chain A
249–281（33 aa）
Fragment：residues 249-281
Chain B
249–281（33 aa）
Fragment：residues 249-281
|
Non-standard monomer：Yes (specific site not provided by mmCIF) Non-standard monomer：Yes (specific site not provided by mmCIF) | No recorded non-water small molecule |
X-RAY DIFFRACTION
X-ray crystallization conditions
VAPOR DIFFUSION, HANGING DROP；pH 8.5；295 K；0.065 M Tris, 5.2% w/v PEG 8000, 35% v/v anhydrous glycerol, pH 8.5, VAPOR DIFFUSION, HANGING DROP, temperature 295K
|
Resolution 2.00 Å R-free 0.263 |
| 2B1F Antiparallel four-stranded coiled coil specified by a 3-3-1 hydrophobic heptad repeat Deposited 2005-09-15 | Different construct Different mutation/modification Different oligomeric state Different experimental method Different experimental conditions Different structure-quality metrics | Assembly 1 Protein homooligomer Homooligomer；Protein × 4 PDB declaration: tetrameric |
Chain A
251–281（31 aa）
Chain B
251–281（31 aa）
Chain C
251–281（31 aa）
Chain D
251–281（31 aa）
|
Not recorded | No recorded non-water small molecule |
X-RAY DIFFRACTION
X-ray crystallization conditions
VAPOR DIFFUSION, HANGING DROP；pH 8.2；295 K；Ethanol, Tris-HCl, pH 8.2, VAPOR DIFFUSION, HANGING DROP, temperature 295.0K
|
Resolution 1.50 Å R-free 0.283 |
| 2B22 Antiparallel four-stranded coiled coil specified by a 3-3-1 hydrophobic heptad repeat Deposited 2005-09-16 | Different construct Different oligomeric state Different ligand/ion Different experimental method Different experimental conditions Different structure-quality metrics | Assembly 1 Protein homooligomer Homooligomer；Protein × 4 PDB declaration: tetrameric |
Chain A
251–281（31 aa）
|
Not recorded | NA SODIUM ION × 8 |
X-RAY DIFFRACTION
X-ray crystallization conditions
VAPOR DIFFUSION, HANGING DROP；pH 4.6；295 K；PEG 400, cadmium chloride, sodium acetate, pH 4.6, VAPOR DIFFUSION, HANGING DROP, temperature 295K
|
Resolution 2.00 Å R-free 0.276 |
| 2BNI pLI mutant E20C L16G Y17H, antiparallel Deposited 2005-03-24 | Different construct Different mutation/modification Different oligomeric state Different experimental method Different experimental conditions Different structure-quality metrics | Assembly 1 Protein homooligomer Homooligomer；Protein × 4 PDB declaration: tetrameric |
Chain A
249–281（33 aa）
Chain B
249–281（33 aa）
Chain C
249–281（33 aa）
Chain D
249–281（33 aa）
|
Mutation：YES Non-standard monomer：Yes (specific site not provided by mmCIF) Mutation：YES Non-standard monomer：Yes (specific site not provided by mmCIF) Mutation：YES Non-standard monomer：Yes (specific site not provided by mmCIF) Mutation：YES Non-standard monomer：Yes (specific site not provided by mmCIF) | No recorded non-water small molecule |
X-RAY DIFFRACTION
X-ray crystallization conditions
VAPOR DIFFUSION, SITTING DROP；SITTING DROP WITH 200NL 20% PEG 3350 0.2M POTASSIUM THIOCYANATE AND 200NL 20MG/ML PEPTIDE STOCK IN WATER.
|
Resolution 1.50 Å R-free 0.276 |
| 2CCE Parallel Configuration of pLI E20S Deposited 2006-01-16 | Different construct Different mutation/modification Different oligomeric state Different experimental method Different experimental conditions Different structure-quality metrics | Assembly 1 Protein homooligomer Homooligomer；Protein × 4 PDB declaration: tetrameric |
Chain A
249–281（33 aa）
Fragment：RESIDUES 249-281
Chain B
249–281（33 aa）
Fragment：RESIDUES 249-281
|
Mutation：YES Non-standard monomer：Yes (specific site not provided by mmCIF) Mutation：YES Non-standard monomer：Yes (specific site not provided by mmCIF) | No recorded non-water small molecule |
X-RAY DIFFRACTION
X-ray crystallization conditions
pH 0；2M NACL, 10% PEG 6K, pH 0.00
|
Resolution 1.90 Å R-free 0.319 |
| 2CCF Antiparallel Configuration of pLI E20S Deposited 2006-01-16 | Different construct Different mutation/modification Different oligomeric state Different experimental method Different experimental conditions Different structure-quality metrics | Assembly 1 Protein homooligomer Homooligomer；Protein × 4 PDB declaration: tetrameric |
Chain A
249–281（33 aa）
Fragment：RESIDUES 249-281
Chain B
249–281（33 aa）
Fragment：RESIDUES 249-281
|
Mutation：YES Non-standard monomer：Yes (specific site not provided by mmCIF) Mutation：YES Non-standard monomer：Yes (specific site not provided by mmCIF) | No recorded non-water small molecule |
X-RAY DIFFRACTION
X-ray crystallization conditions
pH 10；100MM CAPS PH 10.5, 30% PEG 400
|
Resolution 1.70 Å R-free 0.316 |
| 2CCN pLI E20C is antiparallel Deposited 2006-01-16 | Different construct Different mutation/modification Different oligomeric state Different experimental method Different experimental conditions Different structure-quality metrics | Assembly 1 Protein homooligomer Homooligomer；Protein × 4 PDB declaration: tetrameric |
Chain A
249–281（33 aa）
Fragment：RESIDUES 249-281
Chain B
249–281（33 aa）
Fragment：RESIDUES 249-281
|
Mutation：YES Non-standard monomer：Yes (specific site not provided by mmCIF) Mutation：YES Non-standard monomer：Yes (specific site not provided by mmCIF) | No recorded non-water small molecule |
X-RAY DIFFRACTION
X-ray crystallization conditions
pH 10.5；100MM CAPS PH 10.5, 30% PEG 400
|
Resolution 1.60 Å R-free 0.259 |
| 2D3E Crystal structure of the C-Terminal fragment of rabbit skeletal alpha-tropomyosin Deposited 2005-09-27 | Different construct Different mutation/modification Different oligomeric state Different experimental method Different experimental conditions Different structure-quality metrics | Assembly 1 Insufficient information Homooligomer；Protein × 4 PDB declaration: tetrameric |
Chain A
254–277（24 aa）
Fragment：residues 151-175, residues 176-284
Chain B
254–277（24 aa）
Fragment：residues 151-175, residues 176-284
Chain C
254–277（24 aa）
Fragment：residues 151-175, residues 176-284
Chain D
254–277（24 aa）
Fragment：residues 151-175, residues 176-284
|
Not recorded | No recorded non-water small molecule |
X-RAY DIFFRACTION
X-ray crystallization conditions
VAPOR DIFFUSION, SITTING DROP；pH 5.2；293 K；MPD, AMMONIUM ACETATE, SODIUM CITRATE, pH 5.20, VAPOR DIFFUSION, SITTING DROP, temperature 293.0K
|
Resolution 2.60 Å R-free 0.309 |
| 2DGC GCN4 BASIC DOMAIN, LEUCINE ZIPPER COMPLEXED WITH ATF/CREB SITE DNA Deposited 1995-09-28 | Different construct Different oligomeric state Different experimental method Different experimental conditions Different structure-quality metrics | Assembly 1 Protein–DNA Homooligomer；Protein × 2 PDB declaration: tetrameric |
Chain A
220–281（62 aa）
|
Not recorded | No recorded non-water small molecule |
X-RAY DIFFRACTION
X-ray crystallization conditions
VAPOR DIFFUSION；pH 4.6；pH 4.60, VAPOR DIFFUSION
|
Resolution 2.20 Å R-free 0.316 |
| 2EFR Crystal structure of the c-terminal tropomyosin fragment with N- and C-terminal extensions of the leucine zipper at 1.8 angstroms resolution Deposited 2007-02-23 | Different construct Different mutation/modification Different oligomeric state Different experimental method Different experimental conditions Different structure-quality metrics | Assembly 1 Insufficient information Homooligomer；Protein × 2 PDB declaration: dimeric |
Chain A
249–277（29 aa）
Fragment：residues 147-175, residues 176-301
Chain B
249–277（29 aa）
Fragment：residues 147-175, residues 176-301
|
Mutation：C190S Mutation：C190S | No recorded non-water small molecule |
X-RAY DIFFRACTION
X-ray crystallization conditions
VAPOR DIFFUSION, SITTING DROP；pH 7.5；2.2M 1,6-HEXANEDIOL, 0.2M AMMONIUM ACETATE, 0.1M HEPES, PH7.5, pH 7.50, VAPOR DIFFUSION, SITTING DROP
|
Resolution 1.80 Å R-free 0.316 |
| 2EFR Crystal structure of the c-terminal tropomyosin fragment with N- and C-terminal extensions of the leucine zipper at 1.8 angstroms resolution Deposited 2007-02-23 | Different construct Different mutation/modification Different oligomeric state Different experimental method Different experimental conditions Different structure-quality metrics | Assembly 2 Insufficient information Homooligomer；Protein × 2 PDB declaration: dimeric |
Chain C
249–277（29 aa）
Fragment：residues 147-175, residues 176-301
Chain D
249–277（29 aa）
Fragment：residues 147-175, residues 176-301
|
Mutation：C190S Mutation：C190S | No recorded non-water small molecule |
X-RAY DIFFRACTION
X-ray crystallization conditions
VAPOR DIFFUSION, SITTING DROP；pH 7.5；2.2M 1,6-HEXANEDIOL, 0.2M AMMONIUM ACETATE, 0.1M HEPES, PH7.5, pH 7.50, VAPOR DIFFUSION, SITTING DROP
|
Resolution 1.80 Å R-free 0.316 |
| 2EFS Crystal structure of the C-terminal tropomyosin fragment with N- and C-terminal extensions of the leucine zipper at 2.0 angstroms resolution Deposited 2007-02-23 | Different construct Different mutation/modification Different oligomeric state Different experimental method Different experimental conditions Different structure-quality metrics | Assembly 1 Insufficient information Homooligomer；Protein × 2 PDB declaration: dimeric |
Chain A
249–277（29 aa）
Fragment：residues 147-175, residues 176-301
Chain B
249–277（29 aa）
Fragment：residues 147-175, residues 176-301
|
Mutation：C190S Mutation：C190S | No recorded non-water small molecule |
X-RAY DIFFRACTION
X-ray crystallization conditions
VAPOR DIFFUSION, SITTING DROP；pH 8.5；293 K；40% MPD, 0.4M AMMONIUM ACETATE 0.1M TRIS-HCL, pH 8.50, VAPOR DIFFUSION, SITTING DROP, temperature 293K
|
Resolution 2.00 Å R-free 0.304 |
| 2EFS Crystal structure of the C-terminal tropomyosin fragment with N- and C-terminal extensions of the leucine zipper at 2.0 angstroms resolution Deposited 2007-02-23 | Different construct Different mutation/modification Different oligomeric state Different experimental method Different experimental conditions Different structure-quality metrics | Assembly 2 Insufficient information Homooligomer；Protein × 2 PDB declaration: dimeric |
Chain C
249–277（29 aa）
Fragment：residues 147-175, residues 176-301
Chain D
249–277（29 aa）
Fragment：residues 147-175, residues 176-301
|
Mutation：C190S Mutation：C190S | No recorded non-water small molecule |
X-RAY DIFFRACTION
X-ray crystallization conditions
VAPOR DIFFUSION, SITTING DROP；pH 8.5；293 K；40% MPD, 0.4M AMMONIUM ACETATE 0.1M TRIS-HCL, pH 8.50, VAPOR DIFFUSION, SITTING DROP, temperature 293K
|
Resolution 2.00 Å R-free 0.304 |
| 2G9J Complex of TM1a(1-14)Zip with TM9a(251-284): a model for the polymerization domain ("overlap region") of tropomyosin, Northeast Structural Genomics Target OR9 Deposited 2006-03-06 | Different construct Different mutation/modification Different oligomeric state Different experimental conditions | Assembly 1 Insufficient information Heteromer；Protein × 4 PDB declaration: tetrameric |
Chain A
264–281（18 aa）
Fragment：TM1a(1-14)Zip
Chain B
264–281（18 aa）
Fragment：TM1a(1-14)Zip
|
Not recorded | No recorded non-water small molecule |
SOLUTION NMR
NMR measurement conditions
pH 6.5；10 K；Ionic strength (raw mmCIF value) 0.14；Pressure ambient
NMR sample composition
1mM complex of TM1a(1-14)Zip U-15N withTM9a(251-284)U15N, 100 mM NaCl, 10 mM sodium phospate 10% deuterium oxide pH 6.5 | 100 mM NaCl, 10 mM sodium phospate 10% deuterium oxide pH 6.5
NMR sample composition
1mM complex of TM1a(1-14)Zip U15N/U13C with TM9a(251-284) unlabled, 100 mM NaCl, 10 mM sodium phospate 10% deuterium oxide pH 6.5 | 100 mM NaCl, 10 mM sodium phospate 10% deuterium oxide pH 6.5
NMR sample composition
1mM complex of TM1a(1-14)Zip U15N/U13C with TM9a(251-284) unlabled, 100 mM NaCl, 10 mM sodium phospate 99.9% deuterium oxide pH 6.5 | 100 mM NaCl, 10 mM sodium phospate 99.9% deuterium oxide pH 6.5
NMR sample composition
1mM complex of TM1a(1-14)Zip unlabeled with TM9a(251-284)U15N/U13C, 100 mM NaCl, 10 mM sodium phospate 10% deuterium oxide pH 6.5 or in 99.9% deuterium oxide | 100 mM NaCl, 10 mM sodium phospate 10% deuterium oxide pH 6.5 or in 99.9% deuterium oxide
NMR sample composition
1mM complex of TM1a(1-14)Zip unlabeled with TM9a(251-284)U15N/U13C, 100 mM NaCl, 10 mM sodium phospate 10% deuterium oxide 99.9% deuterium oxide, pH 6.5 | 100 mM NaCl, 10 mM sodium phospate 10% deuterium oxide 99.9% deuterium oxide, pH 6.5
NMR sample composition
1mM complex of TM1a(1-14), one chain labeled U15N/U13C the other chain unlabeled, with unlabeled TM9a(251-284), 100 mM NaCl, 10 mM sodium phospate 10% deuterium oxide pH 6.5 | 100 mM NaCl, 10 mM sodium phospate 10% deuterium oxide pH 6.5
NMR sample composition
1mM complex of TM9a(251-284), one chain labeled U15N/U13C the other chain unlabeled, with unlabele TM1a(1-14)Zip, 100 mM NaCl, 10 mM sodium phospate 10% deuterium oxide pH 6.5 | 100 mM NaCl, 10 mM sodium phospate 10% deuterium oxide pH 6.5
|
Resolution not provided |
| 2HY6 A seven-helix coiled coil Deposited 2006-08-04 | Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental method Different experimental conditions Different structure-quality metrics | Assembly 1 Protein homooligomer Homooligomer；Protein × 7 PDB declaration: heptameric |
Chain A
250–281（32 aa）
Fragment：residues 250-281
Chain B
250–281（32 aa）
Fragment：residues 250-281
Chain C
250–281（32 aa）
Fragment：residues 250-281
Chain D
250–281（32 aa）
Fragment：residues 250-281
Chain E
250–281（32 aa）
Fragment：residues 250-281
Chain F
250–281（32 aa）
Fragment：residues 250-281
Chain G
250–281（32 aa）
Fragment：residues 250-281
|
Mutation：E7A, K9A, L14A, K16A, E21A, E23A, K28A, L30A Mutation：E7A, K9A, L14A, K16A, E21A, E23A, K28A, L30A Mutation：E7A, K9A, L14A, K16A, E21A, E23A, K28A, L30A Mutation：E7A, K9A, L14A, K16A, E21A, E23A, K28A, L30A Mutation：E7A, K9A, L14A, K16A, E21A, E23A, K28A, L30A Mutation：E7A, K9A, L14A, K16A, E21A, E23A, K28A, L30A Mutation：E7A, K9A, L14A, K16A, E21A, E23A, K28A, L30A | HEZ HEXANE-1,6-DIOL × 8 |
X-RAY DIFFRACTION
X-ray crystallization conditions
VAPOR DIFFUSION, HANGING DROP；pH 5.4；295 K；0.1M potassium dihydrogen phosphate, 1.4M hexanediol, pH 5.4, VAPOR DIFFUSION, HANGING DROP, temperature 295K
|
Resolution 1.25 Å R-free 0.209 |
| 2IPZ A Parallel Coiled-Coil Tetramer with Offset Helices Deposited 2006-10-12 | Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental method Different experimental conditions Different structure-quality metrics | Assembly 1 Protein homooligomer Homooligomer；Protein × 4 PDB declaration: tetrameric |
Chain A
250–281（32 aa）
Chain B
250–281（32 aa）
Chain C
250–281（32 aa）
Chain D
250–281（32 aa）
|
Not recorded | GOL GLYCEROL × 1 IPA ISOPROPYL ALCOHOL × 1 |
X-RAY DIFFRACTION
X-ray crystallization conditions
VAPOR DIFFUSION, HANGING DROP；pH 7.8；295 K；10% Iso-propanol, 20% PEG 4000, 0.1M sodium bromide, 0.1M sodium HEPES, pH 7.8, VAPOR DIFFUSION, HANGING DROP, temperature 295.0K
|
Resolution 1.35 Å R-free 0.237 |
| 2LPB Structure of the complex of the central activation domain of Gcn4 bound to the mediator co-activator domain 1 of Gal11/med15 Deposited 2012-02-07 | Different construct Different oligomeric state Different experimental conditions | Assembly 1 Protein heterocomplex Heteromer；Protein × 2 PDB declaration: dimeric |
Chain B
101–134（34 aa）
Fragment：Transcriptional activation region, residues 101-134
|
Not recorded | No recorded non-water small molecule |
SOLUTION NMR
NMR measurement conditions
pH 6.5；298 K；Ionic strength (raw mmCIF value) 150；Pressure ambient
NMR sample composition
1-1.2 mM [U-15N] Gal11, 2-2.4 mM Gcn4, 20 mM Sodium phosphate, 150 mM Sodium chloride, 1 mM PMSF, 5 mM DTT, 90% H2O/10% D2O | 90% H2O/10% D2O
NMR sample composition
2-2.4 mM Gal11, 1-1.2 mM [U-15N] Gcn4, 20 mM Sodium phosphate, 150 mM Sodium chloride, 1 mM PMSF, 5 mM DTT, 90% H2O/10% D2O | 90% H2O/10% D2O
NMR sample composition
1-1.2 mM [U-13C; U-15N] Gal11, 2-2.4 mM Gcn4, 20 mM Sodium phosphate, 150 mM Sodium chloride, 1 mM PMSF, 5 mM DTT, 90% H2O/10% D2O | 90% H2O/10% D2O
NMR sample composition
1-1.2 mM [U-13C; U-15N] Gal11, 2-2.4 mM Gcn4, 20 mM Sodium phosphate, 150 mM Sodium chloride, 1 mM PMSF, 5 mM DTT, 100% D2O | 100% D2O
NMR sample composition
2-2.4 mM Gal11, 1-1.2 mM [U-13C; U-15N] Gcn4, 20 mM Sodium phosphate, 150 mM Sodium chloride, 1 mM PMSF, 5 mM DTT, 90% H2O/10% D2O | 90% H2O/10% D2O
|
Resolution not provided |
| 2N9B Solution NMR Structure of Antiparallel Myosin-10:GCN4 Tandem Coiled-Coil Deposited 2015-11-12 | Different construct Different mutation/modification Different oligomeric state Different experimental conditions | Assembly 1 Insufficient information Homooligomer；Protein × 2 PDB declaration: dimeric |
Chain A
253–280（28 aa）
Chain B
253–280（28 aa）
|
Not recorded | No recorded non-water small molecule |
SOLUTION NMR
NMR measurement conditions
pH 6.5；308 K；Ionic strength (raw mmCIF value) 0.6；Pressure ambient
NMR sample composition
1.1 mM [U-100% 13C; U-100% 15N] entity-1, 100 mM potassium phosphate-2, 1 mM EDTA-3, 0.03 % sodium azide-4, 90% H2O/10% D2O | 90% H2O/10% D2O
|
Resolution not provided |
| 2NRN Self-assembly of coiled-coil tetramers in the 1.40 A structure of a leucine-zipper mutant Deposited 2006-11-02 | Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental method Different experimental conditions Different structure-quality metrics | Assembly 1 Protein homooligomer Homooligomer；Protein × 4 PDB declaration: tetrameric |
Chain A
251–281（31 aa）
Fragment：GCN4 leucine zipper
Chain B
251–281（31 aa）
Fragment：GCN4 leucine zipper
Chain C
251–281（31 aa）
Fragment：GCN4 leucine zipper
Chain D
251–281（31 aa）
Fragment：GCN4 leucine zipper
|
Mutation：E254A, E268A, K275A Mutation：E254A, E268A, K275A Mutation：E254A, E268A, K275A Mutation：E254A, E268A, K275A | PO4 PHOSPHATE ION × 4 |
X-RAY DIFFRACTION
X-ray crystallization conditions
VAPOR DIFFUSION, HANGING DROP；pH 5.4；295 K；0.1M sodium citrate, 1M ammonium dihydrophosphate, pH 5.4, VAPOR DIFFUSION, HANGING DROP, temperature 295.0K
|
Resolution 1.40 Å R-free 0.219 |
| 2O7H Crystal structure of trimeric coiled coil GCN4 leucine zipper Deposited 2006-12-11 | Different construct Different mutation/modification Different oligomeric state Different experimental method Different experimental conditions Different structure-quality metrics | Assembly 1 Protein homooligomer Homooligomer；Protein × 3 PDB declaration: trimeric |
Chain A
249–281（33 aa）
Fragment：LEUCINE ZIPPER
Chain B
249–281（33 aa）
Fragment：LEUCINE ZIPPER
Chain C
249–281（33 aa）
Fragment：LEUCINE ZIPPER
|
Mutation：E22R, K27E Mutation：E22R, K27E Mutation：E22R, K27E | No recorded non-water small molecule |
X-RAY DIFFRACTION
X-ray crystallization conditions
VAPOR DIFFUSION, SITTING DROP；pH 6；293 K；30% 2-Proponal, 0.2M Sodium Citrate, 0.1M Sodium cacodylate, pH 6.0, VAPOR DIFFUSION, SITTING DROP, temperature 293K
|
Resolution 1.86 Å R-free 0.231 |
| 2O7H Crystal structure of trimeric coiled coil GCN4 leucine zipper Deposited 2006-12-11 | Different construct Different mutation/modification Different oligomeric state Different experimental method Different experimental conditions Different structure-quality metrics | Assembly 2 Protein homooligomer Homooligomer；Protein × 3 PDB declaration: trimeric |
Chain D
249–281（33 aa）
Fragment：LEUCINE ZIPPER
Chain E
249–281（33 aa）
Fragment：LEUCINE ZIPPER
Chain F
249–281（33 aa）
Fragment：LEUCINE ZIPPER
|
Mutation：E22R, K27E Mutation：E22R, K27E Mutation：E22R, K27E | No recorded non-water small molecule |
X-RAY DIFFRACTION
X-ray crystallization conditions
VAPOR DIFFUSION, SITTING DROP；pH 6；293 K；30% 2-Proponal, 0.2M Sodium Citrate, 0.1M Sodium cacodylate, pH 6.0, VAPOR DIFFUSION, SITTING DROP, temperature 293K
|
Resolution 1.86 Å R-free 0.231 |
| 2OVN NMR structure of the GCN4 trigger peptide Deposited 2007-02-14 | Different construct | Assembly 1 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric |
Chain A
264–280（17 aa）
|
Not recorded | No recorded non-water small molecule | SOLUTION NMR mmCIF provides none of the parsed conditions | Resolution not provided |
| 2WG5 Proteasome-Activating Nucleotidase (PAN) N-domain (57-134) from Archaeoglobus fulgidus fused to GCN4 Deposited 2009-04-15 | Different construct Different mutation/modification Different oligomeric state Different experimental method Different experimental conditions Different structure-quality metrics | Assembly 1 Insufficient information Homooligomer；Protein × 6 PDB declaration: hexameric |
Chain A
249–272（24 aa）
Fragment：N-DOMAIN (57-134) FUSED TO GCN4, RESIDUES 33-56,57-134
Chain B
249–272（24 aa）
Fragment：N-DOMAIN (57-134) FUSED TO GCN4, RESIDUES 33-56,57-134
Chain C
249–272（24 aa）
Fragment：N-DOMAIN (57-134) FUSED TO GCN4, RESIDUES 33-56,57-134
Chain D
249–272（24 aa）
Fragment：N-DOMAIN (57-134) FUSED TO GCN4, RESIDUES 33-56,57-134
Chain E
249–272（24 aa）
Fragment：N-DOMAIN (57-134) FUSED TO GCN4, RESIDUES 33-56,57-134
Chain F
249–272（24 aa）
Fragment：N-DOMAIN (57-134) FUSED TO GCN4, RESIDUES 33-56,57-134
|
Not recorded | No recorded non-water small molecule |
X-RAY DIFFRACTION
X-ray crystallization conditions
100 MM TRIS PH 9.0, 1 M NH4H2PO4, 25% ETHYLENE GLYCOL
|
Resolution 2.10 Å R-free 0.227 |
| 2WG5 Proteasome-Activating Nucleotidase (PAN) N-domain (57-134) from Archaeoglobus fulgidus fused to GCN4 Deposited 2009-04-15 | Different construct Different mutation/modification Different oligomeric state Different experimental method Different experimental conditions Different structure-quality metrics | Assembly 2 Insufficient information Homooligomer；Protein × 6 PDB declaration: hexameric |
Chain G
249–272（24 aa）
Fragment：N-DOMAIN (57-134) FUSED TO GCN4, RESIDUES 33-56,57-134
Chain H
249–272（24 aa）
Fragment：N-DOMAIN (57-134) FUSED TO GCN4, RESIDUES 33-56,57-134
Chain I
249–272（24 aa）
Fragment：N-DOMAIN (57-134) FUSED TO GCN4, RESIDUES 33-56,57-134
Chain J
249–272（24 aa）
Fragment：N-DOMAIN (57-134) FUSED TO GCN4, RESIDUES 33-56,57-134
Chain K
249–272（24 aa）
Fragment：N-DOMAIN (57-134) FUSED TO GCN4, RESIDUES 33-56,57-134
Chain L
249–272（24 aa）
Fragment：N-DOMAIN (57-134) FUSED TO GCN4, RESIDUES 33-56,57-134
|
Not recorded | No recorded non-water small molecule |
X-RAY DIFFRACTION
X-ray crystallization conditions
100 MM TRIS PH 9.0, 1 M NH4H2PO4, 25% ETHYLENE GLYCOL
|
Resolution 2.10 Å R-free 0.227 |
| 2WG6 Proteasome-Activating Nucleotidase (PAN) N-domain (57-134) from Archaeoglobus fulgidus fused to GCN4, P61A Mutant Deposited 2009-04-15 | Different construct Different mutation/modification Different oligomeric state Different experimental method Different experimental conditions Different structure-quality metrics | Assembly 1 Insufficient information Homooligomer；Protein × 6 PDB declaration: hexameric |
Chain A
249–272（24 aa）
Fragment：N-DOMAIN (57-134) FUSED TO GCN4,RESIDUES 33-56,57-134
Chain B
249–272（24 aa）
Fragment：N-DOMAIN (57-134) FUSED TO GCN4,RESIDUES 33-56,57-134
Chain C
249–272（24 aa）
Fragment：N-DOMAIN (57-134) FUSED TO GCN4,RESIDUES 33-56,57-134
Chain D
249–272（24 aa）
Fragment：N-DOMAIN (57-134) FUSED TO GCN4,RESIDUES 33-56,57-134
Chain E
249–272（24 aa）
Fragment：N-DOMAIN (57-134) FUSED TO GCN4,RESIDUES 33-56,57-134
Chain F
249–272（24 aa）
Fragment：N-DOMAIN (57-134) FUSED TO GCN4,RESIDUES 33-56,57-134
|
Mutation：YES Mutation：YES Mutation：YES Mutation：YES Mutation：YES Mutation：YES | No recorded non-water small molecule |
X-RAY DIFFRACTION
X-ray crystallization conditions
100 MM TRIS PH 8.6, 1 M NH4H2PO4, 25% PEG 200
|
Resolution 2.50 Å R-free 0.222 |
| 2WG6 Proteasome-Activating Nucleotidase (PAN) N-domain (57-134) from Archaeoglobus fulgidus fused to GCN4, P61A Mutant Deposited 2009-04-15 | Different construct Different mutation/modification Different oligomeric state Different experimental method Different experimental conditions Different structure-quality metrics | Assembly 2 Insufficient information Homooligomer；Protein × 6 PDB declaration: hexameric |
Chain G
249–272（24 aa）
Fragment：N-DOMAIN (57-134) FUSED TO GCN4,RESIDUES 33-56,57-134
Chain H
249–272（24 aa）
Fragment：N-DOMAIN (57-134) FUSED TO GCN4,RESIDUES 33-56,57-134
Chain I
249–272（24 aa）
Fragment：N-DOMAIN (57-134) FUSED TO GCN4,RESIDUES 33-56,57-134
Chain J
249–272（24 aa）
Fragment：N-DOMAIN (57-134) FUSED TO GCN4,RESIDUES 33-56,57-134
Chain K
249–272（24 aa）
Fragment：N-DOMAIN (57-134) FUSED TO GCN4,RESIDUES 33-56,57-134
Chain L
249–272（24 aa）
Fragment：N-DOMAIN (57-134) FUSED TO GCN4,RESIDUES 33-56,57-134
|
Mutation：YES Mutation：YES Mutation：YES Mutation：YES Mutation：YES Mutation：YES | No recorded non-water small molecule |
X-RAY DIFFRACTION
X-ray crystallization conditions
100 MM TRIS PH 8.6, 1 M NH4H2PO4, 25% PEG 200
|
Resolution 2.50 Å R-free 0.222 |
| 2WPY GCN4 leucine zipper mutant with one VxxNxxx motif coordinating chloride Deposited 2009-08-12 | Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental method Different experimental conditions Different structure-quality metrics | Assembly 1 Protein homooligomer Homooligomer；Protein × 3 PDB declaration: trimeric |
Chain A
249–281（33 aa）
Fragment：COILED-COIL DOMAIN, RESIDUES 249-281
|
Mutation：YES Non-standard monomer：Yes (specific site not provided by mmCIF) | CL CHLORIDE ION × 6 |
X-RAY DIFFRACTION
X-ray crystallization conditions
3.2 M NACL, 100 MM NA-ACETATE, PH 4.6
|
Resolution 1.75 Å R-free 0.252 |
| 2WPZ GCN4 leucine zipper mutant with two VxxNxxx motifs coordinating chloride Deposited 2009-08-12 | Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental method Different experimental conditions Different structure-quality metrics | Assembly 1 Protein homooligomer Homooligomer；Protein × 3 PDB declaration: trimeric |
Chain A
249–281（33 aa）
Fragment：COILED-COIL DOMAIN, RESIDUES 249-281
Chain B
249–281（33 aa）
Fragment：COILED-COIL DOMAIN, RESIDUES 249-281
Chain C
249–281（33 aa）
Fragment：COILED-COIL DOMAIN, RESIDUES 249-281
|
Mutation：YES Non-standard monomer：Yes (specific site not provided by mmCIF) Mutation：YES Non-standard monomer：Yes (specific site not provided by mmCIF) Mutation：YES Non-standard monomer：Yes (specific site not provided by mmCIF) | CL CHLORIDE ION × 2 |
X-RAY DIFFRACTION
X-ray crystallization conditions
30% PEG 4000, 200 MM NA-ACETATE, 0.1 M TRIS, PH 8.5
|
Resolution 1.25 Å R-free 0.223 |
| 2WQ0 GCN4 leucine zipper mutant with three IxxNTxx motifs coordinating chloride Deposited 2009-08-12 | Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental method Different experimental conditions Different structure-quality metrics | Assembly 1 Protein homooligomer Homooligomer；Protein × 3 PDB declaration: trimeric |
Chain A
249–281（33 aa）
Fragment：COILED-COIL DOMAIN, RESIDUES 249-281
|
Mutation：YES | CL CHLORIDE ION × 9 |
X-RAY DIFFRACTION
X-ray crystallization conditions
2.4 M (NH4)2HPO4, 100 MM TRIS PH 8.5
|
Resolution 1.12 Å R-free 0.197 |
| 2WQ1 GCN4 leucine zipper mutant with three IxxNTxx motifs coordinating bromide Deposited 2009-08-12 | Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental method Different experimental conditions Different structure-quality metrics | Assembly 1 Protein homooligomer Homooligomer；Protein × 3 PDB declaration: trimeric |
Chain A
249–281（33 aa）
Fragment：COILED-COIL DOMAIN, RESIDUES 249-281
|
Mutation：YES | BR BROMIDE ION × 9 |
X-RAY DIFFRACTION
X-ray crystallization conditions
20% (W/V) PEG 3350, 200 MM NABR, 100 MM BIS-TRIS PROPANE PH 8.5
|
Resolution 1.08 Å R-free 0.167 |
| 2WQ2 GCN4 leucine zipper mutant with three IxxNTxx motifs coordinating iodide Deposited 2009-08-12 | Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental method Different experimental conditions Different structure-quality metrics | Assembly 1 Protein homooligomer Homooligomer；Protein × 3 PDB declaration: trimeric |
Chain A
249–281（33 aa）
Fragment：COILED-COIL DOMAIN, RESIDUES 249-281
|
Mutation：YES | IOD IODIDE ION × 9 |
X-RAY DIFFRACTION
X-ray crystallization conditions
2.4 M (NH4)2HPO4, 100 MM TRIS PH 8.5
|
Resolution 1.36 Å R-free 0.184 |
| 2WQ3 GCN4 leucine zipper mutant with three IxxNTxx motifs coordinating chloride and nitrate Deposited 2009-08-12 | Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental method Different experimental conditions Different structure-quality metrics | Assembly 1 Protein homooligomer Homooligomer；Protein × 3 PDB declaration: trimeric |
Chain A
249–281（33 aa）
Fragment：COILED-COIL DOMAIN, RESIDUES 249-281
|
Mutation：YES | CL CHLORIDE ION × 6 NO3 NITRATE ION × 3 |
X-RAY DIFFRACTION
X-ray crystallization conditions
25,5% (W/V) PEG 4000, 15% (V/V) GLYCEROL, 170MM NA-ACETATE, 90MM TRIS PH 8.5
|
Resolution 1.22 Å R-free 0.200 |
| 2YNY Salmonella enterica SadA 255-302 fused to GCN4 adaptors (SadAK1) Deposited 2012-10-20 | Different construct Different mutation/modification Different oligomeric state Different experimental method Different experimental conditions Different structure-quality metrics | Assembly 1 Insufficient information Homooligomer；Protein × 3 PDB declaration: trimeric |
Chain A
250–278（29 aa）
Fragment：GCN4 AT EITHER END, RESIDUES 250-278. ADHESIN, RESIDUES 255-302
Chain B
250–278（29 aa）
Fragment：GCN4 AT EITHER END, RESIDUES 250-278. ADHESIN, RESIDUES 255-302
Chain C
250–278（29 aa）
Fragment：GCN4 AT EITHER END, RESIDUES 250-278. ADHESIN, RESIDUES 255-302
|
Mutation：YES Mutation：YES Mutation：YES | No recorded non-water small molecule |
X-RAY DIFFRACTION
X-ray crystallization conditions
16% (W/V) PEG 4000, 80 MM SODIUM ACETATE, 100 MM HEPES PH 7.5
|
Resolution 1.35 Å R-free 0.198 |
| 2YNZ Salmonella enterica SadA 823-947 fused to a GCN4 adaptor (SadAK5) Deposited 2012-10-20 | Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental method Different experimental conditions Different structure-quality metrics | Assembly 1 Insufficient information Homooligomer；Protein × 3 PDB declaration: trimeric |
Chain A
250–278（29 aa）
Fragment：GCN ADAPTOR RESIDUES, 250-278, ADHESIN RESIDUES 823-947
Chain B
250–278（29 aa）
Fragment：GCN ADAPTOR RESIDUES, 250-278, ADHESIN RESIDUES 823-947
Chain C
250–278（29 aa）
Fragment：GCN ADAPTOR RESIDUES, 250-278, ADHESIN RESIDUES 823-947
|
Mutation：YES Mutation：YES Mutation：YES | NO3 NITRATE ION × 4 |
X-RAY DIFFRACTION
X-ray crystallization conditions
10% (W/V) PEG 10000, 200 MM MAGNESIUM NITRATE
|
Resolution 1.40 Å R-free 0.232 |
| 2YO0 Salmonella enterica SadA 1049-1304 fused to GCN4 adaptors (SadAK9-cfI) Deposited 2012-10-20 | Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental method Different experimental conditions Different structure-quality metrics | Assembly 1 Insufficient information Homooligomer；Protein × 3 PDB declaration: trimeric |
Chain A
250–278（29 aa）
Fragment：GCN4 ADAPTOR, RESIDUES 250-278, ADHESIN, RESIDUES 1049-1304
|
Mutation：YES | CL CHLORIDE ION × 3 |
X-RAY DIFFRACTION
X-ray crystallization conditions
20% (V/V) BUTANEDIOL, 100 MM SODIUM ACETATE PH 4.5
|
Resolution 2.80 Å R-free 0.297 |
| 2YO1 Salmonella enterica SadA 1049-1304 fused to GCN4 adaptors (SadAK9- cfII) Deposited 2012-10-20 | Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental method Different experimental conditions Different structure-quality metrics | Assembly 1 Insufficient information Homooligomer；Protein × 3 PDB declaration: trimeric |
Chain A
250–278（29 aa）
Fragment：RESIDUES 1049-1304 FUSED TO GCN4 ADAPTORS, RESIDUES 250-278
Chain B
250–278（29 aa）
Fragment：RESIDUES 1049-1304 FUSED TO GCN4 ADAPTORS, RESIDUES 250-278
Chain C
250–278（29 aa）
Fragment：RESIDUES 1049-1304 FUSED TO GCN4 ADAPTORS, RESIDUES 250-278
|
Mutation：YES Mutation：YES Mutation：YES | CL CHLORIDE ION × 1 |
X-RAY DIFFRACTION
X-ray crystallization conditions
15 % (V/V) BUTANEDIOL, 100 MM SODIUM ACETATE PH 4.2
|
Resolution 3.10 Å R-free 0.320 |
| 2YO2 Salmonella enterica SadA 255-358 fused to GCN4 adaptors (SadAK12) Deposited 2012-10-20 | Different construct Different mutation/modification Different oligomeric state Different experimental method Different experimental conditions Different structure-quality metrics | Assembly 1 Insufficient information Homooligomer；Protein × 3 PDB declaration: trimeric |
Chain A
250–278（29 aa）
Fragment：RESIDUES 255-358 FUSED TO GCN4 ADAPTORS AT EITHER END, RESIDUES 250-278
|
Mutation：YES | No recorded non-water small molecule |
X-RAY DIFFRACTION
X-ray crystallization conditions
500 MM AMMONIUM TARTRATE, 100 MM SODIUM ACETATE PH 5.0
|
Resolution 2.00 Å R-free 0.284 |
| 2YO3 Salmonella enterica SadA 1185-1386 fused to GCN4 adaptors (SadAK14) Deposited 2012-10-20 | Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental method Different experimental conditions Different structure-quality metrics | Assembly 1 Insufficient information Homooligomer；Protein × 3 PDB declaration: trimeric |
Chain A
250–278（29 aa）
Fragment：GCN4 ADAPTOR RESIDUES 250-278, ADHESIN RESIDUES 1185-1386, GCN4 ADAPTOR RESIDUES 250-278
Chain B
250–278（29 aa）
Fragment：GCN4 ADAPTOR RESIDUES 250-278, ADHESIN RESIDUES 1185-1386, GCN4 ADAPTOR RESIDUES 250-278
Chain C
250–278（29 aa）
Fragment：GCN4 ADAPTOR RESIDUES 250-278, ADHESIN RESIDUES 1185-1386, GCN4 ADAPTOR RESIDUES 250-278
|
Mutation：YES Mutation：YES Mutation：YES | CL CHLORIDE ION × 1 |
X-RAY DIFFRACTION
X-ray crystallization conditions
12% (W/V) PEG 8000, 100 MM MAGNESIUM ACETATE, 100 MM TRIS PH 8.5
|
Resolution 2.00 Å R-free 0.253 |
| 2Z5H Crystal structure of the head-to-tail junction of tropomyosin complexed with a fragment of TnT Deposited 2007-07-12 | Different construct Different mutation/modification Different oligomeric state Different experimental method Different experimental conditions Different structure-quality metrics | Assembly 1 Insufficient information Heteromer；Protein × 4 PDB declaration: tetrameric |
Chain A
259–278（20 aa）
Fragment：C terminal domain of GCN4 and Tropomyosin alpha-1 chain
Chain B
259–278（20 aa）
Fragment：C terminal domain of GCN4 and Tropomyosin alpha-1 chain
Chain I
267–278（12 aa）
Fragment：N terminal domain of Tropomyosin alpha-1 chain and C terminal domain of GCN4
|
Not recorded | No recorded non-water small molecule |
X-RAY DIFFRACTION
X-ray crystallization conditions
VAPOR DIFFUSION, HANGING DROP；pH 6.5；293 K；pH 6.5, VAPOR DIFFUSION, HANGING DROP, temperature 293K
|
Resolution 2.89 Å R-free 0.247 |
| 2Z5H Crystal structure of the head-to-tail junction of tropomyosin complexed with a fragment of TnT Deposited 2007-07-12 | Different construct Different mutation/modification Different oligomeric state Different experimental method Different experimental conditions Different structure-quality metrics | Assembly 2 Insufficient information Homooligomer；Protein × 2 PDB declaration: dimeric |
Chain C
259–278（20 aa）
Fragment：C terminal domain of GCN4 and Tropomyosin alpha-1 chain
Chain D
259–278（20 aa）
Fragment：C terminal domain of GCN4 and Tropomyosin alpha-1 chain
|
Not recorded | No recorded non-water small molecule |
X-RAY DIFFRACTION
X-ray crystallization conditions
VAPOR DIFFUSION, HANGING DROP；pH 6.5；293 K；pH 6.5, VAPOR DIFFUSION, HANGING DROP, temperature 293K
|
Resolution 2.89 Å R-free 0.247 |
| 2Z5H Crystal structure of the head-to-tail junction of tropomyosin complexed with a fragment of TnT Deposited 2007-07-12 | Different construct Different mutation/modification Different oligomeric state Different experimental method Different experimental conditions Different structure-quality metrics | Assembly 3 Insufficient information Homooligomer；Protein × 2 PDB declaration: dimeric |
Chain E
259–278（20 aa）
Fragment：C terminal domain of GCN4 and Tropomyosin alpha-1 chain
Chain F
259–278（20 aa）
Fragment：C terminal domain of GCN4 and Tropomyosin alpha-1 chain
|
Not recorded | No recorded non-water small molecule |
X-RAY DIFFRACTION
X-ray crystallization conditions
VAPOR DIFFUSION, HANGING DROP；pH 6.5；293 K；pH 6.5, VAPOR DIFFUSION, HANGING DROP, temperature 293K
|
Resolution 2.89 Å R-free 0.247 |
| 2Z5H Crystal structure of the head-to-tail junction of tropomyosin complexed with a fragment of TnT Deposited 2007-07-12 | Different construct Different mutation/modification Different oligomeric state Different experimental method Different experimental conditions Different structure-quality metrics | Assembly 4 Insufficient information Homooligomer；Protein × 2 PDB declaration: dimeric |
Chain G
259–278（20 aa）
Fragment：C terminal domain of GCN4 and Tropomyosin alpha-1 chain
Chain H
259–278（20 aa）
Fragment：C terminal domain of GCN4 and Tropomyosin alpha-1 chain
|
Not recorded | No recorded non-water small molecule |
X-RAY DIFFRACTION
X-ray crystallization conditions
VAPOR DIFFUSION, HANGING DROP；pH 6.5；293 K；pH 6.5, VAPOR DIFFUSION, HANGING DROP, temperature 293K
|
Resolution 2.89 Å R-free 0.247 |
| 2Z5I Crystal structure of the head-to-tail junction of tropomyosin Deposited 2007-07-12 | Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental method Different experimental conditions Different structure-quality metrics | Assembly 1 Insufficient information Homooligomer；Protein × 2 PDB declaration: dimeric |
Chain A
259–278（20 aa）
Fragment：C terminal domain of GCN4 and Tropomyosin alpha-1 chain
Chain B
259–278（20 aa）
Fragment：C terminal domain of GCN4 and Tropomyosin alpha-1 chain
|
Not recorded | MG MAGNESIUM ION × 1 |
X-RAY DIFFRACTION
X-ray crystallization conditions
VAPOR DIFFUSION, HANGING DROP；pH 6.5；293 K；pH 6.5, VAPOR DIFFUSION, HANGING DROP, temperature 293K
|
Resolution 2.10 Å R-free 0.246 |
| 2Z5I Crystal structure of the head-to-tail junction of tropomyosin Deposited 2007-07-12 | Different construct Different mutation/modification Different oligomeric state Different experimental method Different experimental conditions Different structure-quality metrics | Assembly 2 Insufficient information Homooligomer；Protein × 2 PDB declaration: dimeric |
Chain C
259–278（20 aa）
Fragment：C terminal domain of GCN4 and Tropomyosin alpha-1 chain
Chain D
259–278（20 aa）
Fragment：C terminal domain of GCN4 and Tropomyosin alpha-1 chain
|
Not recorded | No recorded non-water small molecule |
X-RAY DIFFRACTION
X-ray crystallization conditions
VAPOR DIFFUSION, HANGING DROP；pH 6.5；293 K；pH 6.5, VAPOR DIFFUSION, HANGING DROP, temperature 293K
|
Resolution 2.10 Å R-free 0.246 |
| 2Z5I Crystal structure of the head-to-tail junction of tropomyosin Deposited 2007-07-12 | Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental method Different experimental conditions Different structure-quality metrics | Assembly 3 Insufficient information Homooligomer；Protein × 2 PDB declaration: dimeric |
Chain E
259–278（20 aa）
Fragment：C terminal domain of GCN4 and Tropomyosin alpha-1 chain
Chain F
259–278（20 aa）
Fragment：C terminal domain of GCN4 and Tropomyosin alpha-1 chain
|
Not recorded | MG MAGNESIUM ION × 1 |
X-RAY DIFFRACTION
X-ray crystallization conditions
VAPOR DIFFUSION, HANGING DROP；pH 6.5；293 K；pH 6.5, VAPOR DIFFUSION, HANGING DROP, temperature 293K
|
Resolution 2.10 Å R-free 0.246 |
| 2Z5I Crystal structure of the head-to-tail junction of tropomyosin Deposited 2007-07-12 | Different construct Different mutation/modification Different oligomeric state Different experimental method Different experimental conditions Different structure-quality metrics | Assembly 4 Insufficient information Homooligomer；Protein × 2 PDB declaration: dimeric |
Chain G
259–278（20 aa）
Fragment：C terminal domain of GCN4 and Tropomyosin alpha-1 chain
Chain H
259–278（20 aa）
Fragment：C terminal domain of GCN4 and Tropomyosin alpha-1 chain
|
Not recorded | No recorded non-water small molecule |
X-RAY DIFFRACTION
X-ray crystallization conditions
VAPOR DIFFUSION, HANGING DROP；pH 6.5；293 K；pH 6.5, VAPOR DIFFUSION, HANGING DROP, temperature 293K
|
Resolution 2.10 Å R-free 0.246 |
| 2Z5I Crystal structure of the head-to-tail junction of tropomyosin Deposited 2007-07-12 | Different construct Different mutation/modification Different oligomeric state Different experimental method Different experimental conditions Different structure-quality metrics | Assembly 5 Insufficient information Homooligomer；Protein × 2 PDB declaration: dimeric |
Chain I
267–278（12 aa）
Fragment：N terminal domain of Tropomyosin alpha-1 chain and C terminal domain of GCN4
Chain J
267–278（12 aa）
Fragment：N terminal domain of Tropomyosin alpha-1 chain and C terminal domain of GCN4
|
Not recorded | No recorded non-water small molecule |
X-RAY DIFFRACTION
X-ray crystallization conditions
VAPOR DIFFUSION, HANGING DROP；pH 6.5；293 K；pH 6.5, VAPOR DIFFUSION, HANGING DROP, temperature 293K
|
Resolution 2.10 Å R-free 0.246 |
| 2Z5I Crystal structure of the head-to-tail junction of tropomyosin Deposited 2007-07-12 | Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental method Different experimental conditions Different structure-quality metrics | Assembly 6 Insufficient information Homooligomer；Protein × 10 PDB declaration: decameric |
Chain A
259–278（20 aa）
Fragment：C terminal domain of GCN4 and Tropomyosin alpha-1 chain
Chain B
259–278（20 aa）
Fragment：C terminal domain of GCN4 and Tropomyosin alpha-1 chain
Chain C
259–278（20 aa）
Fragment：C terminal domain of GCN4 and Tropomyosin alpha-1 chain
Chain D
259–278（20 aa）
Fragment：C terminal domain of GCN4 and Tropomyosin alpha-1 chain
Chain E
259–278（20 aa）
Fragment：C terminal domain of GCN4 and Tropomyosin alpha-1 chain
Chain F
259–278（20 aa）
Fragment：C terminal domain of GCN4 and Tropomyosin alpha-1 chain
Chain G
259–278（20 aa）
Fragment：C terminal domain of GCN4 and Tropomyosin alpha-1 chain
Chain H
259–278（20 aa）
Fragment：C terminal domain of GCN4 and Tropomyosin alpha-1 chain
Chain I
267–278（12 aa）
Fragment：N terminal domain of Tropomyosin alpha-1 chain and C terminal domain of GCN4
Chain J
267–278（12 aa）
Fragment：N terminal domain of Tropomyosin alpha-1 chain and C terminal domain of GCN4
|
Not recorded | MG MAGNESIUM ION × 2 |
X-RAY DIFFRACTION
X-ray crystallization conditions
VAPOR DIFFUSION, HANGING DROP；pH 6.5；293 K；pH 6.5, VAPOR DIFFUSION, HANGING DROP, temperature 293K
|
Resolution 2.10 Å R-free 0.246 |
| 2ZTA X-RAY STRUCTURE OF THE GCN4 LEUCINE ZIPPER, A TWO-STRANDED, PARALLEL COILED COIL Deposited 1991-07-05 | Different construct Different mutation/modification Different oligomeric state Different experimental method Different structure-quality metrics | Assembly 1 Protein homooligomer Homooligomer；Protein × 2 PDB declaration: dimeric |
Chain A
249–281（33 aa）
Chain B
249–281（33 aa）
|
Non-standard monomer：Yes (specific site not provided by mmCIF) Non-standard monomer：Yes (specific site not provided by mmCIF) | No recorded non-water small molecule | X-RAY DIFFRACTION mmCIF provides none of the parsed conditions | Resolution 1.80 Å |
| 3AZD Crystal structure of tropomyosin N-terminal fragment at 0.98A resolution Deposited 2011-05-23 | Different construct Different mutation/modification Different oligomeric state Different experimental method Different experimental conditions Different structure-quality metrics | Assembly 1 Insufficient information Homooligomer；Protein × 2 PDB declaration: dimeric |
Chain A
264–281（18 aa）
Chain B
264–281（18 aa）
|
Not recorded | No recorded non-water small molecule |
X-RAY DIFFRACTION
X-ray crystallization conditions
VAPOR DIFFUSION, HANGING DROP；pH 7；293 K；0.17M ammonium sulfate, 10% PEG 4000, pH 7.0, VAPOR DIFFUSION, HANGING DROP, temperature 293K
|
Resolution 0.98 Å R-free 0.171 |
| 3BAS Crystal structure of the N-terminal region of the scallop myosin rod, monoclinic (C2) form Deposited 2007-11-08 | Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental method Different experimental conditions Different structure-quality metrics | Assembly 1 Insufficient information Homooligomer；Protein × 2 PDB declaration: dimeric |
Chain A
250–281（32 aa）
Fragment：Bay Scallop Myosin (Residues 835-885)/Yeast GCN4 Transcription Factor (Residues 250-281)
Chain B
250–281（32 aa）
Fragment：Bay Scallop Myosin (Residues 835-885)/Yeast GCN4 Transcription Factor (Residues 250-281)
|
Not recorded | IOD IODIDE ION × 1 |
X-RAY DIFFRACTION
X-ray crystallization conditions
VAPOR DIFFUSION, HANGING DROP；pH 7.2；277 K；1.5 microliter of protein solution (4 mg/ml protein in 30 mM MOPS buffer pH 7.2, 40 mM NaCl, 2 mM NaN3) mixed with 3 microliters of (16.6% PEG 3350, 4.6% MPD, 13 mM NaCl, 2 mM NaN3, 10 mM MOPS pH 7.2) and equilibrated against (15% PEG 3350, 4.2% MPD, 18 mM MOPS, 24 mM NaCl), VAPOR DIFFUSION, HANGING DROP, temperature 277K
|
Resolution 2.30 Å R-free 0.287 |
| 3BAT Crystal structure of the N-terminal region of the scallop myosin rod, monoclinic (P21) form Deposited 2007-11-08 | Different construct Different mutation/modification Different oligomeric state Different experimental method Different experimental conditions Different structure-quality metrics | Assembly 1 Insufficient information Homooligomer；Protein × 2 PDB declaration: dimeric |
Chain A
250–281（32 aa）
Fragment：Bay Scallop Myosin (Residues 835-885)/Yeast GCN4 Transcription Factor (Residues 250-281)
Chain B
250–281（32 aa）
Fragment：Bay Scallop Myosin (Residues 835-885)/Yeast GCN4 Transcription Factor (Residues 250-281)
|
Not recorded | No recorded non-water small molecule |
X-RAY DIFFRACTION
X-ray crystallization conditions
VAPOR DIFFUSION, HANGING DROP；pH 6.2；277 K；2 microliters of protein solution (4 mg/ml protein in 30 mM MOPS buffer pH 7.2, 40 mM NaCl, 2 mM NaN3) mixed with 2 microliters of (25% PEG 3350, 50 mM NH4I) and equilibrated against 1 ml of (17.5% PEG 3350, 35 mM NH4I, 28 mM NaCl, 2 mM NaN3, 20 mM MOPS pH 6.2). Harvested crystals were cryoprotected in 25.5% PEG 3350 and 15% glycerol, VAPOR DIFFUSION, HANGING DROP, temperature 277K
|
Resolution 2.30 Å R-free 0.299 |
| 3BAT Crystal structure of the N-terminal region of the scallop myosin rod, monoclinic (P21) form Deposited 2007-11-08 | Different construct Different mutation/modification Different oligomeric state Different experimental method Different experimental conditions Different structure-quality metrics | Assembly 2 Insufficient information Homooligomer；Protein × 2 PDB declaration: dimeric |
Chain C
250–281（32 aa）
Fragment：Bay Scallop Myosin (Residues 835-885)/Yeast GCN4 Transcription Factor (Residues 250-281)
Chain D
250–281（32 aa）
Fragment：Bay Scallop Myosin (Residues 835-885)/Yeast GCN4 Transcription Factor (Residues 250-281)
|
Not recorded | No recorded non-water small molecule |
X-RAY DIFFRACTION
X-ray crystallization conditions
VAPOR DIFFUSION, HANGING DROP；pH 6.2；277 K；2 microliters of protein solution (4 mg/ml protein in 30 mM MOPS buffer pH 7.2, 40 mM NaCl, 2 mM NaN3) mixed with 2 microliters of (25% PEG 3350, 50 mM NH4I) and equilibrated against 1 ml of (17.5% PEG 3350, 35 mM NH4I, 28 mM NaCl, 2 mM NaN3, 20 mM MOPS pH 6.2). Harvested crystals were cryoprotected in 25.5% PEG 3350 and 15% glycerol, VAPOR DIFFUSION, HANGING DROP, temperature 277K
|
Resolution 2.30 Å R-free 0.299 |
| 3CK4 A heterospecific leucine zipper tetramer Deposited 2008-03-14 | Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental method Different experimental conditions Different structure-quality metrics | Assembly 1 Protein homooligomer Homooligomer；Protein × 4 PDB declaration: tetrameric |
Chain A
251–281（31 aa）
Fragment：UNP residues 251-281
Chain B
251–281（31 aa）
Fragment：UNP residues 251-281
Chain C
251–281（31 aa）
Fragment：UNP residues 251-281
Chain D
251–281（31 aa）
Fragment：UNP residues 251-281
|
Not recorded | MG MAGNESIUM ION × 1 |
X-RAY DIFFRACTION
X-ray crystallization conditions
VAPOR DIFFUSION, HANGING DROP；pH 8.5；295 K；0.1M Tris-HCl, 0.2M magnesium chloride, 30% PEG 4000, pH 8.5, VAPOR DIFFUSION, HANGING DROP, temperature 295K
|
Resolution 1.70 Å R-free 0.221 |
| 3CK4 A heterospecific leucine zipper tetramer Deposited 2008-03-14 | Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental method Different experimental conditions Different structure-quality metrics | Assembly 2 Protein homooligomer Homooligomer；Protein × 4 PDB declaration: tetrameric |
Chain E
251–281（31 aa）
Fragment：UNP residues 251-281
Chain F
251–281（31 aa）
Fragment：UNP residues 251-281
Chain G
251–281（31 aa）
Fragment：UNP residues 251-281
Chain H
251–281（31 aa）
Fragment：UNP residues 251-281
|
Not recorded | MG MAGNESIUM ION × 1 |
X-RAY DIFFRACTION
X-ray crystallization conditions
VAPOR DIFFUSION, HANGING DROP；pH 8.5；295 K；0.1M Tris-HCl, 0.2M magnesium chloride, 30% PEG 4000, pH 8.5, VAPOR DIFFUSION, HANGING DROP, temperature 295K
|
Resolution 1.70 Å R-free 0.221 |
| 3CK4 A heterospecific leucine zipper tetramer Deposited 2008-03-14 | Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental method Different experimental conditions Different structure-quality metrics | Assembly 3 Protein homooligomer Homooligomer；Protein × 4 PDB declaration: tetrameric |
Chain I
251–281（31 aa）
Fragment：UNP residues 251-281
Chain J
251–281（31 aa）
Fragment：UNP residues 251-281
Chain K
251–281（31 aa）
Fragment：UNP residues 251-281
Chain L
251–281（31 aa）
Fragment：UNP residues 251-281
|
Not recorded | MG MAGNESIUM ION × 2 |
X-RAY DIFFRACTION
X-ray crystallization conditions
VAPOR DIFFUSION, HANGING DROP；pH 8.5；295 K；0.1M Tris-HCl, 0.2M magnesium chloride, 30% PEG 4000, pH 8.5, VAPOR DIFFUSION, HANGING DROP, temperature 295K
|
Resolution 1.70 Å R-free 0.221 |
| 3CRP A heterospecific leucine zipper tetramer Deposited 2008-04-07 | Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental method Different experimental conditions Different structure-quality metrics | Assembly 1 Protein homooligomer Homooligomer；Protein × 4 PDB declaration: tetrameric |
Chain A
251–281（31 aa）
Fragment：UNP residues 251-281
Chain B
251–281（31 aa）
Fragment：UNP residues 251-281
Chain C
251–281（31 aa）
Fragment：UNP residues 251-281
Chain D
251–281（31 aa）
Fragment：UNP residues 251-281
|
Not recorded | NA SODIUM ION × 1 |
X-RAY DIFFRACTION
X-ray crystallization conditions
VAPOR DIFFUSION, HANGING DROP；pH 9.8；295 K；0.1M Tris-HCl, 0.05M magnesium chloride, 13% PEG 4000, pH 9.8, VAPOR DIFFUSION, HANGING DROP, temperature 295.0K
|
Resolution 1.70 Å R-free 0.230 |
| 3CRP A heterospecific leucine zipper tetramer Deposited 2008-04-07 | Different construct Different oligomeric state Different experimental method Different experimental conditions Different structure-quality metrics | Assembly 2 Protein homooligomer Homooligomer；Protein × 4 PDB declaration: tetrameric |
Chain E
251–281（31 aa）
Fragment：UNP residues 251-281
|
Not recorded | No recorded non-water small molecule |
X-RAY DIFFRACTION
X-ray crystallization conditions
VAPOR DIFFUSION, HANGING DROP；pH 9.8；295 K；0.1M Tris-HCl, 0.05M magnesium chloride, 13% PEG 4000, pH 9.8, VAPOR DIFFUSION, HANGING DROP, temperature 295.0K
|
Resolution 1.70 Å R-free 0.230 |
| 3G9R Structure of the HIV-1 gp41 Membrane-Proximal Ectodomain Region in a Putative Prefusion Conformation Deposited 2009-02-13 | Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental method Different experimental conditions Different structure-quality metrics | Assembly 1 Insufficient information Homooligomer；Protein × 3 PDB declaration: trimeric |
Chain A
258–276（19 aa）
Fragment：C-terminal MPER of HIV-1 GP41, Leucine-zipper domain of GCN4
Chain B
258–276（19 aa）
Fragment：C-terminal MPER of HIV-1 GP41, Leucine-zipper domain of GCN4
Chain C
258–276（19 aa）
Fragment：C-terminal MPER of HIV-1 GP41, Leucine-zipper domain of GCN4
|
Mutation：L27K, N30I, Y31K, H32R, L33I, V37I, A38K, L40I Mutation：L27K, N30I, Y31K, H32R, L33I, V37I, A38K, L40I Mutation：L27K, N30I, Y31K, H32R, L33I, V37I, A38K, L40I | PO4 PHOSPHATE ION × 4 MPD (4S)-2-METHYL-2,4-PENTANEDIOL × 6 |
X-RAY DIFFRACTION
X-ray crystallization conditions
VAPOR DIFFUSION, HANGING DROP；pH 7.6；298 K；0.1M sodium HEPES, 0.1M ammonium dihydrogenphosphate, 50% MPD, pH 7.6, VAPOR DIFFUSION, HANGING DROP, temperature 298.0K
|
Resolution 2.00 Å R-free 0.269 |
| 3G9R Structure of the HIV-1 gp41 Membrane-Proximal Ectodomain Region in a Putative Prefusion Conformation Deposited 2009-02-13 | Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental method Different experimental conditions Different structure-quality metrics | Assembly 2 Insufficient information Homooligomer；Protein × 3 PDB declaration: trimeric |
Chain D
258–276（19 aa）
Fragment：C-terminal MPER of HIV-1 GP41, Leucine-zipper domain of GCN4
Chain E
258–276（19 aa）
Fragment：C-terminal MPER of HIV-1 GP41, Leucine-zipper domain of GCN4
Chain F
258–276（19 aa）
Fragment：C-terminal MPER of HIV-1 GP41, Leucine-zipper domain of GCN4
|
Mutation：L27K, N30I, Y31K, H32R, L33I, V37I, A38K, L40I Mutation：L27K, N30I, Y31K, H32R, L33I, V37I, A38K, L40I Mutation：L27K, N30I, Y31K, H32R, L33I, V37I, A38K, L40I | PO4 PHOSPHATE ION × 1 MPD (4S)-2-METHYL-2,4-PENTANEDIOL × 2 |
X-RAY DIFFRACTION
X-ray crystallization conditions
VAPOR DIFFUSION, HANGING DROP；pH 7.6；298 K；0.1M sodium HEPES, 0.1M ammonium dihydrogenphosphate, 50% MPD, pH 7.6, VAPOR DIFFUSION, HANGING DROP, temperature 298.0K
|
Resolution 2.00 Å R-free 0.269 |
| 3GJP Crystal structure of mutant coiled coil GCN4 leucine zipper Deposited 2009-03-09 | Different construct Different mutation/modification Different oligomeric state Different experimental method Different structure-quality metrics | Assembly 1 Protein homooligomer Homooligomer；Protein × 3 PDB declaration: trimeric |
Chain A
249–281（33 aa）
Fragment：Leucine zipper
Chain B
249–281（33 aa）
Fragment：Leucine zipper
Chain C
249–281（33 aa）
Fragment：Leucine zipper
|
Mutation：V271I,L274I Mutation：V271I,L274I Mutation：V271I,L274I | No recorded non-water small molecule | X-RAY DIFFRACTION mmCIF provides none of the parsed conditions | Resolution 2.00 Å R-free 0.269 |
| 3I1G Crystal structure of a GCN4 leucine zipper mutant at 1.6 A resolution Deposited 2009-06-26 | Different construct Different mutation/modification Different oligomeric state Different experimental method Different experimental conditions Different structure-quality metrics | Assembly 1 Protein homooligomer Homooligomer；Protein × 2 PDB declaration: dimeric |
Chain A
249–281（33 aa）
Fragment：Leucine zipper domain: UNP residues 249-281
|
Mutation：K251A, D255A, Y265W, H266N | No recorded non-water small molecule |
X-RAY DIFFRACTION
X-ray crystallization conditions
VAPOR DIFFUSION, HANGING DROP；pH 4.5；298 K；Protein solution: 8 mg/mL Leucine zipper peptide, 0.1 M Sodium acetate pH 4.5. Reservoir solution: 0.2 M CaCl2, 0.1 M Sodium acetate pH 4.5, 20 % v/v Isopropanol, VAPOR DIFFUSION, HANGING DROP, temperature 298.0K
|
Resolution 1.60 Å R-free 0.287 |
| 3I5C Crystal structure of a fusion protein containing the leucine zipper of GCN4 and the GGDEF domain of WspR from Pseudomonas aeruginosa Deposited 2009-07-03 | Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental method Different experimental conditions Different structure-quality metrics | Assembly 1 Insufficient information Homooligomer；Protein × 2 PDB declaration: dimeric |
Chain A
249–278（30 aa）
Fragment：GCN4 leucine zipper fused with GGDEF domain
Chain B
249–278（30 aa）
Fragment：GCN4 leucine zipper fused with GGDEF domain
|
Not recorded | MG MAGNESIUM ION × 1 C2E 9,9'-[(2R,3R,3aS,5S,7aR,9R,10R,10aS,12S,14aR)-3,5,10,12-tetrahydroxy-5,12-dioxidooctahydro-2H,7H-difuro[3,2-d:3',2'-j][1,3,7,9,2,8]tetraoxadiphosphacyclododecine-2,9-diyl]bis(2-amino-1,9-dihydro-6H-purin-6-one) × 4 |
X-RAY DIFFRACTION
X-ray crystallization conditions
VAPOR DIFFUSION, HANGING DROP；pH 7.5；298 K；Magnesium formate dihydrate, pH 7.5, VAPOR DIFFUSION, HANGING DROP, temperature 298.0K
|
Resolution 1.94 Å R-free 0.259 |
| 3K7Z GCN4-Leucine zipper core mutant as N16A trigonal automatic solution Deposited 2009-10-13 | Different construct Different mutation/modification Different oligomeric state Different experimental method Different experimental conditions Different structure-quality metrics | Assembly 1 Protein homooligomer Homooligomer；Protein × 3 PDB declaration: trimeric |
Chain A
249–281（33 aa）
Fragment：LEUCINE-ZIPPER (RESIDUES 249-281)
Chain B
249–281（33 aa）
Fragment：LEUCINE-ZIPPER (RESIDUES 249-281)
Chain C
249–281（33 aa）
Fragment：LEUCINE-ZIPPER (RESIDUES 249-281)
|
Mutation：N16A Mutation：N16A Mutation：N16A | No recorded non-water small molecule |
X-RAY DIFFRACTION
X-ray crystallization conditions
VAPOR DIFFUSION, SITTING DROP；pH 7.3；298 K；100MM BIS-TRIS buffer only, pH 7.3, VAPOR DIFFUSION, SITTING DROP, temperature 298K
|
Resolution 1.90 Å R-free 0.259 |
| 3M48 GCN4 Leucine Zipper Peptide Mutant Deposited 2010-03-10 | Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental method Different experimental conditions Different structure-quality metrics | Assembly 1 Protein homooligomer Homooligomer；Protein × 2 PDB declaration: dimeric |
Chain A
249–281（33 aa）
Fragment：Leucine Zipper domain (UNP residues 249-281)
|
Mutation：K251A, D255A, Y265W, H266N | NA SODIUM ION × 4 |
X-RAY DIFFRACTION
X-ray crystallization conditions
VAPOR DIFFUSION；pH 4.6；298 K；8 mg/ml leucine zipper peptide, 0.1M sodium acetate, 0.2M calcium chloride, 20% v/v 2-propanol, pH 4.6, VAPOR DIFFUSION, temperature 298K
|
Resolution 1.45 Å R-free 0.225 |
| 3P8M Human dynein light chain (DYNLL2) in complex with an in vitro evolved peptide dimerized by leucine zipper Deposited 2010-10-14 | Different construct Different mutation/modification Different oligomeric state Different experimental method Different experimental conditions Different structure-quality metrics | Assembly 1 Protein heterocomplex Heteromer；Protein × 4 PDB declaration: tetrameric |
Chain C
250–281（32 aa）
Chain D
250–281（32 aa）
|
Not recorded | No recorded non-water small molecule |
X-RAY DIFFRACTION
X-ray crystallization conditions
pH 7；293 K；20% PEG8000, 0.2 M MgCl2, 0.1 M TRIS, pH 7.0, VAPOR DIFFUSION, HANGING DROP, temperature 293K
|
Resolution 2.90 Å R-free 0.295 |
| 3ZMF Salmonella enterica SadA 303-358 fused to GCN4 adaptors (SadAK2) Deposited 2013-02-08 | Different construct Different mutation/modification Different oligomeric state Different experimental method Different experimental conditions Different structure-quality metrics | Assembly 1 Insufficient information Homooligomer；Protein × 3 PDB declaration: trimeric |
Chain C
250–277（28 aa）
Fragment：GCN4 ADAPTOR RESIDUES 250-278, ADHESIN RESIDUES 303-358, GCN4 ADAPTOR RESIDUES 250-278
Chain C
250–278（29 aa）
Fragment：GCN4 ADAPTOR RESIDUES 250-278, ADHESIN RESIDUES 303-358, GCN4 ADAPTOR RESIDUES 250-278
|
Mutation：YES Mutation：YES | No recorded non-water small molecule |
X-RAY DIFFRACTION
X-ray crystallization conditions
50% PEG 200, 0.1 M NA-CITRATE PH 5.5
|
Resolution 1.85 Å R-free 0.221 |
| 3ZMF Salmonella enterica SadA 303-358 fused to GCN4 adaptors (SadAK2) Deposited 2013-02-08 | Different construct Different mutation/modification Different oligomeric state Different experimental method Different experimental conditions Different structure-quality metrics | Assembly 2 Insufficient information Homooligomer；Protein × 3 PDB declaration: trimeric |
Chain B
250–277（28 aa）
Fragment：GCN4 ADAPTOR RESIDUES 250-278, ADHESIN RESIDUES 303-358, GCN4 ADAPTOR RESIDUES 250-278
Chain B
250–278（29 aa）
Fragment：GCN4 ADAPTOR RESIDUES 250-278, ADHESIN RESIDUES 303-358, GCN4 ADAPTOR RESIDUES 250-278
|
Mutation：YES Mutation：YES | No recorded non-water small molecule |
X-RAY DIFFRACTION
X-ray crystallization conditions
50% PEG 200, 0.1 M NA-CITRATE PH 5.5
|
Resolution 1.85 Å R-free 0.221 |
| 3ZMF Salmonella enterica SadA 303-358 fused to GCN4 adaptors (SadAK2) Deposited 2013-02-08 | Different construct Different mutation/modification Different oligomeric state Different experimental method Different experimental conditions Different structure-quality metrics | Assembly 3 Insufficient information Homooligomer；Protein × 3 PDB declaration: trimeric |
Chain A
250–277（28 aa）
Fragment：GCN4 ADAPTOR RESIDUES 250-278, ADHESIN RESIDUES 303-358, GCN4 ADAPTOR RESIDUES 250-278
Chain A
250–278（29 aa）
Fragment：GCN4 ADAPTOR RESIDUES 250-278, ADHESIN RESIDUES 303-358, GCN4 ADAPTOR RESIDUES 250-278
|
Mutation：YES Mutation：YES | No recorded non-water small molecule |
X-RAY DIFFRACTION
X-ray crystallization conditions
50% PEG 200, 0.1 M NA-CITRATE PH 5.5
|
Resolution 1.85 Å R-free 0.221 |
| 4C46 ANDREI-N-LVPAS fused to GCN4 adaptors Deposited 2013-08-30 | Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental method Different experimental conditions Different structure-quality metrics | Assembly 1 Protein homooligomer Homooligomer；Protein × 3 PDB declaration: trimeric |
Chain A
250–278（29 aa）
Fragment：RESIDUES 250-278,250-278
Chain B
250–278（29 aa）
Fragment：RESIDUES 250-278,250-278
Chain C
250–278（29 aa）
Fragment：RESIDUES 250-278,250-278
|
Mutation：YES Mutation：YES Mutation：YES | BR BROMIDE ION × 1 |
X-RAY DIFFRACTION
X-ray crystallization conditions
VAPOR DIFFUSION, SITTING DROP；pH 4；SITTING DROP, PROTEIN SOLUTION 50 MM NACL AND 50 MM SODIUM ACETATE PH 4.0, RESERVOUR SOLUTION 0.1 M HEPES PH 7.5 1.75 M SODIUM BROMIDE
|
Resolution 1.95 Å R-free 0.275 |
| 4G2K Crystal structure of the Marburg Virus GP2 ectodomain in its post-fusion conformation Deposited 2012-07-12 | Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental method Different experimental conditions Different structure-quality metrics | Assembly 1 Insufficient information Homooligomer；Protein × 3 PDB declaration: trimeric |
Chain A
250–279（30 aa）
Fragment：SEE REMARK 999
Chain B
250–279（30 aa）
Fragment：SEE REMARK 999
Chain C
250–279（30 aa）
Fragment：SEE REMARK 999
|
Not recorded | GOL GLYCEROL × 2 CL CHLORIDE ION × 1 |
X-RAY DIFFRACTION
X-ray crystallization conditions
VAPOR DIFFUSION, SITTING DROP；pH 8.5；298 K；0.17 M sodium acetate, 0.085 M Tris-HCl, pH 8.5, 25.5% PEG3350, 15% glycerol, VAPOR DIFFUSION, SITTING DROP, temperature 298K
|
Resolution 1.90 Å R-free 0.244 |
| 4HU5 Oxime side-chain cross-links in the GCN4-p1 dimeric coiled coil: Linear precursor Deposited 2012-11-02 | Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental method Different experimental conditions Different structure-quality metrics | Assembly 1 Protein homooligomer Homooligomer；Protein × 2 PDB declaration: dimeric |
Chain A
249–281（33 aa）
Chain B
249–281（33 aa）
|
Non-standard monomer：Yes (specific site not provided by mmCIF) Non-standard monomer：Yes (specific site not provided by mmCIF) | GOL GLYCEROL × 1 ACT ACETATE ION × 3 |
X-RAY DIFFRACTION
X-ray crystallization conditions
VAPOR DIFFUSION, HANGING DROP；pH 4.6；298 K；0.1 M sodium acetate pH 4.6, 1.6 M sodium chloride, 5% w/v PEG 1500, VAPOR DIFFUSION, HANGING DROP, temperature 298K
|
Resolution 2.30 Å R-free 0.268 |
| 4HU6 Oxime side-chain cross-links in the GCN4-p1 dimeric coiled coil: Cyclic product Deposited 2012-11-02 | Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental method Different experimental conditions Different structure-quality metrics | Assembly 1 Protein homooligomer Homooligomer；Protein × 2 PDB declaration: dimeric |
Chain A
249–281（33 aa）
Chain B
249–281（33 aa）
|
Non-standard monomer：Yes (specific site not provided by mmCIF) Non-standard monomer：Yes (specific site not provided by mmCIF) | ACT ACETATE ION × 2 GOL GLYCEROL × 1 |
X-RAY DIFFRACTION
X-ray crystallization conditions
VAPOR DIFFUSION, HANGING DROP；pH 4.6；298 K；0.1 M sodium acetate pH 4.6, 1.6 M sodium chloride, 5% w/v PEG 1500; crystal was treated with 1 equiv. sodium periodate relative to protein and allowed to incubate for 2 days prior to harvesting, VAPOR DIFFUSION, HANGING DROP, temperature 298K
|
Resolution 2.30 Å R-free 0.292 |
| 4HU6 Oxime side-chain cross-links in the GCN4-p1 dimeric coiled coil: Cyclic product Deposited 2012-11-02 | Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental method Different experimental conditions Different structure-quality metrics | Assembly 2 Protein homooligomer Homooligomer；Protein × 2 PDB declaration: dimeric |
Chain C
249–281（33 aa）
Chain D
249–281（33 aa）
|
Non-standard monomer：Yes (specific site not provided by mmCIF) Non-standard monomer：Yes (specific site not provided by mmCIF) | GOL GLYCEROL × 2 |
X-RAY DIFFRACTION
X-ray crystallization conditions
VAPOR DIFFUSION, HANGING DROP；pH 4.6；298 K；0.1 M sodium acetate pH 4.6, 1.6 M sodium chloride, 5% w/v PEG 1500; crystal was treated with 1 equiv. sodium periodate relative to protein and allowed to incubate for 2 days prior to harvesting, VAPOR DIFFUSION, HANGING DROP, temperature 298K
|
Resolution 2.30 Å R-free 0.292 |
| 4NIZ GCN4-p1 single Val9 to aminobutyric acid mutant Deposited 2013-11-08 | Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental method Different experimental conditions Different structure-quality metrics | Assembly 1 Protein homooligomer Homooligomer；Protein × 2 PDB declaration: dimeric |
Chain A
249–281（33 aa）
Fragment：unp residues 249-281
Chain B
249–281（33 aa）
Fragment：unp residues 249-281
|
Mutation：V9(ABA) Non-standard monomer：Yes (specific site not provided by mmCIF) Mutation：V9(ABA) Non-standard monomer：Yes (specific site not provided by mmCIF) | GOL GLYCEROL × 1 |
X-RAY DIFFRACTION
X-ray crystallization conditions
VAPOR DIFFUSION, HANGING DROP；pH 5.6；298 K；0.05 M sodium acetate, 0.1 M sodium citrate tribasic dihydrate, 20% w/v PEG 4000, pH 5.6, VAPOR DIFFUSION, HANGING DROP, temperature 298K
|
Resolution 2.00 Å R-free 0.243 |
| 4NJ0 GCN4-p1 single Val9 to Ile mutant Deposited 2013-11-08 | Different construct Different mutation/modification Different oligomeric state Different experimental method Different experimental conditions Different structure-quality metrics | Assembly 1 Protein homooligomer Homooligomer；Protein × 2 PDB declaration: dimeric |
Chain A
249–281（33 aa）
Fragment：unp residues 249-281
Chain B
249–281（33 aa）
Fragment：unp residues 249-281
|
Mutation：V9I Non-standard monomer：Yes (specific site not provided by mmCIF) Mutation：V9I Non-standard monomer：Yes (specific site not provided by mmCIF) | No recorded non-water small molecule |
X-RAY DIFFRACTION
X-ray crystallization conditions
VAPOR DIFFUSION, HANGING DROP；pH 5.6；298 K；0.2 M sodium acetate, 0.1 M sodium citrate tribasic dihydrate, 25% w/v PEG 4000, pH 5.6, VAPOR DIFFUSION, HANGING DROP, temperature 298K
|
Resolution 1.90 Å R-free 0.283 |
| 4NJ1 GCN4-p1 double Val9, 23 to Ile mutant Deposited 2013-11-08 | Different construct Different mutation/modification Different oligomeric state Different experimental method Different experimental conditions Different structure-quality metrics | Assembly 1 Protein homooligomer Homooligomer；Protein × 2 PDB declaration: dimeric |
Chain A
249–281（33 aa）
Fragment：unp residues 249-281
Chain B
249–281（33 aa）
Fragment：unp residues 249-281
|
Mutation：V9I, V23I Non-standard monomer：Yes (specific site not provided by mmCIF) Mutation：V9I, V23I Non-standard monomer：Yes (specific site not provided by mmCIF) | No recorded non-water small molecule |
X-RAY DIFFRACTION
X-ray crystallization conditions
VAPOR DIFFUSION, HANGING DROP；pH 5.6；298 K；0.1 M soduim aceteate, 0.1 M sodium citrate tribasic dihyrdrate, 20% w/v PEG 4000, pH 5.6, VAPOR DIFFUSION, HANGING DROP, temperature 298K
|
Resolution 2.00 Å R-free 0.255 |
| 4NJ2 GCN4-p1 triple Val9, 23,30 to Ile mutant Deposited 2013-11-08 | Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental method Different experimental conditions Different structure-quality metrics | Assembly 1 Protein homooligomer Homooligomer；Protein × 2 PDB declaration: dimeric |
Chain A
249–281（33 aa）
Fragment：unp residues 249-281
Chain B
249–281（33 aa）
Fragment：unp residues 249-281
|
Mutation：V29I, V30I, V31I Non-standard monomer：Yes (specific site not provided by mmCIF) Mutation：V29I, V30I, V31I Non-standard monomer：Yes (specific site not provided by mmCIF) | GOL GLYCEROL × 1 |
X-RAY DIFFRACTION
X-ray crystallization conditions
VAPOR DIFFUSION, HANGING DROP；pH 5.6；298 K；0.15M sodium citrate tribasic dihydrate, 20% v/v 2-propanol, 15% w/v PEG 4000, pH 5.6, VAPOR DIFFUSION, HANGING DROP, temperature 298K
|
Resolution 2.20 Å R-free 0.313 |
| 4TL1 GCN4-p1 with mutation to 1-Aminocyclohexanecarboxylic acid at residue 10 Deposited 2014-05-28 | Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental method Different experimental conditions Different structure-quality metrics | Assembly 1 Protein homooligomer Homooligomer；Protein × 2 PDB declaration: dimeric |
Chain A
249–281（33 aa）
Fragment：UNP residues 249-281
Chain B
249–281（33 aa）
Fragment：UNP residues 249-281
|
Non-standard monomer：Yes (specific site not provided by mmCIF) Non-standard monomer：Yes (specific site not provided by mmCIF) | IPA ISOPROPYL ALCOHOL × 1 |
X-RAY DIFFRACTION
X-ray crystallization conditions
VAPOR DIFFUSION, HANGING DROP；298 K；0.2 M sodium citrate tribasic, 0.1 M sodium cacodylate pH 6.5, 30% v/v isopropanol
|
Resolution 1.80 Å R-free 0.228 |
| 5APP Actinobacillus actinomycetemcomitans OMP100 residues 133-198 fused to GCN4 adaptors Deposited 2015-09-17 | Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental method Different experimental conditions Different structure-quality metrics | Assembly 1 Protein homooligomer Homooligomer；Protein × 3 PDB declaration: trimeric |
Chain A
250–277（28 aa）
Fragment：;UNP RESIDUES P03069 250-277, G4B386 133-199, P03069 250-277,UNP RESIDUES P03069 250-277, G4B386 133-199, P03069 250-277,UNP RESIDUES P03069 250-277, G4B386 133-199, P03069 250-277
;
Chain B
250–277（28 aa）
Fragment：;UNP RESIDUES P03069 250-277, G4B386 133-199, P03069 250-277,UNP RESIDUES P03069 250-277, G4B386 133-199, P03069 250-277,UNP RESIDUES P03069 250-277, G4B386 133-199, P03069 250-277
;
Chain C
250–277（28 aa）
Fragment：;UNP RESIDUES P03069 250-277, G4B386 133-199, P03069 250-277,UNP RESIDUES P03069 250-277, G4B386 133-199, P03069 250-277,UNP RESIDUES P03069 250-277, G4B386 133-199, P03069 250-277
;
|
Mutation：YES,YES,YES Mutation：YES,YES,YES Mutation：YES,YES,YES | CL CHLORIDE ION × 5 |
X-RAY DIFFRACTION
X-ray crystallization conditions
0.1 M TRI-SODIUM CITRATE PH 5.5, 2 %(V/V) DIOXANE 15 %(W/V) PEG 10,000
|
Resolution 2.30 Å R-free 0.254 |
| 5APQ Sequence IENKAD inserted between GCN4 adaptors - Structure A6 Deposited 2015-09-17 | Different construct Different mutation/modification Different oligomeric state Different experimental method Different experimental conditions Different structure-quality metrics | Assembly 1 Protein homooligomer Homooligomer；Protein × 3 PDB declaration: trimeric |
Chain A
250–277（28 aa）
Chain A
250–281（32 aa）
Chain B
250–277（28 aa）
Chain B
250–281（32 aa）
Chain C
250–277（28 aa）
Chain C
250–281（32 aa）
|
Mutation：YES Mutation：YES Mutation：YES Mutation：YES Mutation：YES Mutation：YES | No recorded non-water small molecule |
X-RAY DIFFRACTION
X-ray crystallization conditions
95 MM TRI-SODIUM CITRATE PH 5.6, 19 %(V/V) ISOPROPANOL, 19 %(W/V) PEG 4000, 5 %(V/V) GLYCEROL
|
Resolution 2.10 Å R-free 0.251 |
| 5APS Sequence IENKKAD inserted between GCN4 adaptors - Structure A7 Deposited 2015-09-17 | Different construct Different mutation/modification Different oligomeric state Different experimental method Different experimental conditions Different structure-quality metrics | Assembly 1 Protein homooligomer Homooligomer；Protein × 3 PDB declaration: trimeric |
Chain A
250–277（28 aa）
Chain A
250–281（32 aa）
|
Mutation：YES Mutation：YES | No recorded non-water small molecule |
X-RAY DIFFRACTION
X-ray crystallization conditions
0.1 M CITRIC ACID PH 3.5, 3 M NACL
|
Resolution 1.37 Å R-free 0.238 |
| 5APT Sequence IENKADKAD inserted between GCN4 adaptors - Structure A9 Deposited 2015-09-17 | Different construct Different mutation/modification Different oligomeric state Different experimental method Different experimental conditions Different structure-quality metrics | Assembly 1 Protein homooligomer Homooligomer；Protein × 3 PDB declaration: trimeric |
Chain A
250–277（28 aa）
Chain A
250–281（32 aa）
Chain B
250–277（28 aa）
Chain B
250–281（32 aa）
Chain C
250–277（28 aa）
Chain C
250–281（32 aa）
|
Mutation：YES Mutation：YES Mutation：YES Mutation：YES Mutation：YES Mutation：YES | No recorded non-water small molecule |
X-RAY DIFFRACTION
X-ray crystallization conditions
1.6 M TRI-SODIUM CITRATE PH 6.5
|
Resolution 1.80 Å R-free 0.256 |
| 5APU Sequence IANKEDKAD inserted between GCN4 adaptors - Structure A9b black Deposited 2015-09-17 | Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental method Different experimental conditions Different structure-quality metrics | Assembly 1 Protein homooligomer Homooligomer；Protein × 3 PDB declaration: trimeric |
Chain A
250–277（28 aa）
Chain A
250–281（32 aa）
Chain B
250–277（28 aa）
Chain B
250–281（32 aa）
Chain C
250–277（28 aa）
Chain C
250–281（32 aa）
|
Mutation：YES Mutation：YES Mutation：YES Mutation：YES Mutation：YES Mutation：YES | URE UREA × 1 |
X-RAY DIFFRACTION
X-ray crystallization conditions
2.4 M SODIUM MALONATE PH 5.0
|
Resolution 1.35 Å R-free 0.199 |
| 5APV Sequence IANKEDKAD inserted between GCN4 adaptors - Structure A9b grey Deposited 2015-09-17 | Different construct Different mutation/modification Different oligomeric state Different experimental method Different experimental conditions Different structure-quality metrics | Assembly 1 Protein homooligomer Homooligomer；Protein × 3 PDB declaration: trimeric |
Chain D
250–277（28 aa）
Fragment：UNP RESIDUES 250-277,250-281
Chain D
250–281（32 aa）
Fragment：UNP RESIDUES 250-277,250-281
Chain E
250–277（28 aa）
Fragment：UNP RESIDUES 250-277,250-281
Chain E
250–281（32 aa）
Fragment：UNP RESIDUES 250-277,250-281
Chain F
250–277（28 aa）
Fragment：UNP RESIDUES 250-277,250-281
Chain F
250–281（32 aa）
Fragment：UNP RESIDUES 250-277,250-281
|
Mutation：YES Mutation：YES Mutation：YES Mutation：YES Mutation：YES Mutation：YES | No recorded non-water small molecule |
X-RAY DIFFRACTION
X-ray crystallization conditions
0.2 M SODIUM CITRATE, 0.1 M BIS TRIS PROPANE PH 6.5, 20%(W/V) PEG 3350
|
Resolution 2.00 Å R-free 0.253 |
| 5APV Sequence IANKEDKAD inserted between GCN4 adaptors - Structure A9b grey Deposited 2015-09-17 | Different construct Different mutation/modification Different oligomeric state Different experimental method Different experimental conditions Different structure-quality metrics | Assembly 2 Protein homooligomer Homooligomer；Protein × 3 PDB declaration: trimeric |
Chain A
250–277（28 aa）
Fragment：UNP RESIDUES 250-277,250-281
Chain A
250–281（32 aa）
Fragment：UNP RESIDUES 250-277,250-281
Chain B
250–277（28 aa）
Fragment：UNP RESIDUES 250-277,250-281
Chain B
250–281（32 aa）
Fragment：UNP RESIDUES 250-277,250-281
Chain C
250–277（28 aa）
Fragment：UNP RESIDUES 250-277,250-281
Chain C
250–281（32 aa）
Fragment：UNP RESIDUES 250-277,250-281
|
Mutation：YES Mutation：YES Mutation：YES Mutation：YES Mutation：YES Mutation：YES | No recorded non-water small molecule |
X-RAY DIFFRACTION
X-ray crystallization conditions
0.2 M SODIUM CITRATE, 0.1 M BIS TRIS PROPANE PH 6.5, 20%(W/V) PEG 3350
|
Resolution 2.00 Å R-free 0.253 |
| 5APW Sequence MATKDD inserted between GCN4 adaptors - Structure T6 Deposited 2015-09-17 | Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental method Different experimental conditions Different structure-quality metrics | Assembly 1 Protein homooligomer Homooligomer；Protein × 3 PDB declaration: trimeric |
Chain A
250–277（28 aa）
Fragment：UNP RESIDUES 250-277,250-281
Chain A
250–281（32 aa）
Fragment：UNP RESIDUES 250-277,250-281
Chain B
250–277（28 aa）
Fragment：UNP RESIDUES 250-277,250-281
Chain B
250–281（32 aa）
Fragment：UNP RESIDUES 250-277,250-281
Chain C
250–277（28 aa）
Fragment：UNP RESIDUES 250-277,250-281
Chain C
250–281（32 aa）
Fragment：UNP RESIDUES 250-277,250-281
|
Mutation：YES Mutation：YES Mutation：YES Mutation：YES Mutation：YES Mutation：YES | URE UREA × 1 CL CHLORIDE ION × 1 CA CALCIUM ION × 1 |
X-RAY DIFFRACTION
X-ray crystallization conditions
0.2 M CACL, 0.1 M HEPES PH 7.5, 30 %(W/V) PEG 4000
|
Resolution 1.60 Å R-free 0.205 |
| 5APX Sequence MATKDDIAN inserted between GCN4 adaptors - Structure T9(6) Deposited 2015-09-17 | Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental method Different experimental conditions Different structure-quality metrics | Assembly 1 Protein homooligomer Homooligomer；Protein × 3 PDB declaration: trimeric |
Chain A
250–277（28 aa）
Fragment：UNP RESIDUES 250-277,250-281
Chain A
250–281（32 aa）
Fragment：UNP RESIDUES 250-277,250-281
Chain B
250–277（28 aa）
Fragment：UNP RESIDUES 250-277,250-281
Chain B
250–281（32 aa）
Fragment：UNP RESIDUES 250-277,250-281
Chain C
250–277（28 aa）
Fragment：UNP RESIDUES 250-277,250-281
Chain C
250–281（32 aa）
Fragment：UNP RESIDUES 250-277,250-281
|
Mutation：YES Mutation：YES Mutation：YES Mutation：YES Mutation：YES Mutation：YES | PO4 PHOSPHATE ION × 1 |
X-RAY DIFFRACTION
X-ray crystallization conditions
0.2 M AMMONIUM PHOSPHATE, 0.1 M TRIS PH 8.5, 50 %(V/V) MPD
|
Resolution 1.80 Å R-free 0.226 |
| 5APY Sequence MATKDDIAN inserted between GCN4 adaptors - Structure T9(9) Deposited 2015-09-17 | Different construct Different mutation/modification Different oligomeric state Different experimental method Different experimental conditions Different structure-quality metrics | Assembly 1 Protein homooligomer Homooligomer；Protein × 3 PDB declaration: trimeric |
Chain A
250–277（28 aa）
Fragment：250-277,250-281
Chain A
250–281（32 aa）
Fragment：250-277,250-281
Chain B
250–277（28 aa）
Fragment：250-277,250-281
Chain B
250–281（32 aa）
Fragment：250-277,250-281
Chain C
250–277（28 aa）
Fragment：250-277,250-281
Chain C
250–281（32 aa）
Fragment：250-277,250-281
|
Mutation：YES Mutation：YES Mutation：YES Mutation：YES Mutation：YES Mutation：YES | No recorded non-water small molecule |
X-RAY DIFFRACTION
X-ray crystallization conditions
0.1 M CITRIC ACID PH 5.0, 20 %(V/V) ISOPROPANOL
|
Resolution 2.00 Å R-free 0.255 |
| 5APZ Thermosinus carboxydivorans Nor1 Tcar0761 residues 68-101 and 191-211 fused to GCN4 adaptors Deposited 2015-09-17 | Different construct Different oligomeric state Different experimental method Different experimental conditions Different structure-quality metrics | Assembly 1 Insufficient information Homooligomer；Protein × 3 PDB declaration: trimeric |
Chain A
250–279（30 aa）
Fragment：RESIDUES 250-279,68-101,191-211,250-279
|
Not recorded | No recorded non-water small molecule |
X-RAY DIFFRACTION
X-ray crystallization conditions
0.1 M TRI-SODIUM CITRATE PH 4.0, 30 %(V/V) MPD
|
Resolution 1.60 Å R-free 0.213 |
| 5IEW NMR Structures Show Unwinding of the GCN4p Coiled Coil Superhelix Accompanying Disruption of Ion Pairs at Acidic pH Deposited 2016-02-25 | Different construct Different mutation/modification Different oligomeric state Different experimental conditions | Assembly 1 Protein homooligomer Homooligomer；Protein × 2 PDB declaration: dimeric |
Chain A
250–280（31 aa）
Fragment：UNP residues 250-280
Chain B
250–280（31 aa）
Fragment：UNP residues 250-280
|
Not recorded | No recorded non-water small molecule |
SOLUTION NMR
NMR measurement conditions
pH 6.6；298 K；Ionic strength (raw mmCIF value) 20；Pressure 1
NMR measurement conditions
pH 6.6；298 K；Ionic strength (raw mmCIF value) 20；Pressure 1
NMR sample composition
1.5 mM [U-99% 13C; U-99% 15N] GCN4p, 90% H2O/10% D2O | 90% H2O/10% D2O
NMR sample composition
1.5 mM 66%-13C 33%-12C GCN4p, 100% D2O | 100% D2O
|
Resolution not provided |
| 5IIR NMR Structures Show Unwinding of the GCN4p Coiled Coil Superhelix Accompanying Disruption of Ion Pairs at Acidic pH Deposited 2016-03-01 | Different construct Different mutation/modification Different oligomeric state Different experimental conditions | Assembly 1 Protein homooligomer Homooligomer；Protein × 2 PDB declaration: dimeric |
Chain A
250–280（31 aa）
Fragment：UNP residues 250-280
Chain B
250–280（31 aa）
Fragment：UNP residues 250-280
|
Not recorded | No recorded non-water small molecule |
SOLUTION NMR
NMR measurement conditions
pH 4.4；298 K；Ionic strength (raw mmCIF value) 20；Pressure 1
NMR measurement conditions
pH 4.6；283 K；Ionic strength (raw mmCIF value) 20；Pressure 1
NMR measurement conditions
pH 4.4；298 K；Ionic strength (raw mmCIF value) 20；Pressure 1
NMR sample composition
1.5 mM [U-99% 13C; U-99% 15N] GCN4p, 90% H2O/10% D2O | 90% H2O/10% D2O
NMR sample composition
1.5 mM [U-99% 13C; U-99% 15N] GCN4p, 100% D2O | 100% D2O
NMR sample composition
1.5 mM 66% - 13C 33% - 12C GCN4p, 100% D2O | 100% D2O
|
Resolution not provided |
| 5IIV GCN4p pH 1.5 Deposited 2016-03-01 | Different construct Different mutation/modification Different oligomeric state Different experimental conditions | Assembly 1 Protein homooligomer Homooligomer；Protein × 2 PDB declaration: dimeric |
Chain A
250–280（31 aa）
Fragment：UNP residues 250-280
Chain B
250–280（31 aa）
Fragment：UNP residues 250-280
|
Not recorded | No recorded non-water small molecule |
SOLUTION NMR
NMR measurement conditions
pH 1.5；298 K；Ionic strength (raw mmCIF value) 20；Pressure 1
NMR measurement conditions
pH 1.5；298 K；Ionic strength (raw mmCIF value) 20；Pressure 1
NMR sample composition
1.5 mM [U-99% 13C; U-99% 15N] GCN4p, 100% D2O | 100% D2O
NMR sample composition
1.5 mM 66% - 13C 33%- 12C GCN4p, 100% D2O | 100% D2O
NMR sample composition
1.5 mM [U-99% 13C; U-99% 15N] GCN4p, 90% H2O/10% D2O | 90% H2O/10% D2O
|
Resolution not provided |
| 5KHT Crystal structure of the N-terminal fragment of tropomyosin isoform Tpm1.1 at 1.5 A resolution Deposited 2016-06-15 | Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental method Different experimental conditions Different structure-quality metrics | Assembly 1 Insufficient information Homooligomer；Protein × 2 PDB declaration: dimeric |
Chain A
264–281（18 aa）
Chain C
264–281（18 aa）
|
Not recorded | PEG DI(HYDROXYETHYL)ETHER × 2 |
X-RAY DIFFRACTION
X-ray crystallization conditions
VAPOR DIFFUSION, SITTING DROP；pH 7.5；293 K；PEG 8000, Hepes/sodium hydroxide
|
Resolution 1.50 Å R-free 0.249 |
| 5KHT Crystal structure of the N-terminal fragment of tropomyosin isoform Tpm1.1 at 1.5 A resolution Deposited 2016-06-15 | Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental method Different experimental conditions Different structure-quality metrics | Assembly 2 Insufficient information Homooligomer；Protein × 2 PDB declaration: dimeric |
Chain B
264–281（18 aa）
Chain D
264–281（18 aa）
|
Not recorded | PEG DI(HYDROXYETHYL)ETHER × 2 |
X-RAY DIFFRACTION
X-ray crystallization conditions
VAPOR DIFFUSION, SITTING DROP；pH 7.5；293 K；PEG 8000, Hepes/sodium hydroxide
|
Resolution 1.50 Å R-free 0.249 |
| 6E52 Chimeric structure of Saccharomyces cerevisiae GCN4 leucine zipper fused to Staphylococcus aureus AgrC cytoplasmic histidine kinase module (dataset anisotropically truncated by STARANISO) Deposited 2018-07-19 | Different construct Different mutation/modification Different oligomeric state Different experimental method Different experimental conditions Different structure-quality metrics | Assembly 1 Insufficient information Homooligomer；Protein × 2 PDB declaration: dimeric |
Chain A
250–274（25 aa）
Chain B
250–274（25 aa）
|
Not recorded | No recorded non-water small molecule |
X-RAY DIFFRACTION
X-ray crystallization conditions
VAPOR DIFFUSION, HANGING DROP；pH 8；295 K；0.1 M Tris pH 8.0 and 2.8 M NaCl
|
Resolution 1.93 Å R-free 0.268 |
| 6E52 Chimeric structure of Saccharomyces cerevisiae GCN4 leucine zipper fused to Staphylococcus aureus AgrC cytoplasmic histidine kinase module (dataset anisotropically truncated by STARANISO) Deposited 2018-07-19 | Different construct Different mutation/modification Different oligomeric state Different experimental method Different experimental conditions Different structure-quality metrics | Assembly 2 Insufficient information Homooligomer；Protein × 4 PDB declaration: tetrameric |
Chain A
250–274（25 aa）
Chain B
250–274（25 aa）
|
Not recorded | No recorded non-water small molecule |
X-RAY DIFFRACTION
X-ray crystallization conditions
VAPOR DIFFUSION, HANGING DROP；pH 8；295 K；0.1 M Tris pH 8.0 and 2.8 M NaCl
|
Resolution 1.93 Å R-free 0.268 |
| 6E95 Chimeric structure of Saccharomyces cerevisiae GCN4 leucine zipper fused to Staphylococcus aureus AgrC cytoplasmic histidine kinase module (dataset isotropically truncated by HKL2000) Deposited 2018-07-31 | Different construct Different mutation/modification Different oligomeric state Different experimental method Different experimental conditions Different structure-quality metrics | Assembly 1 Insufficient information Homooligomer；Protein × 2 PDB declaration: dimeric |
Chain A
250–274（25 aa）
Chain B
250–274（25 aa）
|
Not recorded | No recorded non-water small molecule |
X-RAY DIFFRACTION
X-ray crystallization conditions
VAPOR DIFFUSION, HANGING DROP；pH 8；295 K；0.1 M Tris pH 8.0 and 2.8 M NaCl
|
Resolution 2.25 Å R-free 0.275 |
| 6E95 Chimeric structure of Saccharomyces cerevisiae GCN4 leucine zipper fused to Staphylococcus aureus AgrC cytoplasmic histidine kinase module (dataset isotropically truncated by HKL2000) Deposited 2018-07-31 | Different construct Different mutation/modification Different oligomeric state Different experimental method Different experimental conditions Different structure-quality metrics | Assembly 2 Insufficient information Homooligomer；Protein × 4 PDB declaration: tetrameric |
Chain A
250–274（25 aa）
Chain B
250–274（25 aa）
|
Not recorded | No recorded non-water small molecule |
X-RAY DIFFRACTION
X-ray crystallization conditions
VAPOR DIFFUSION, HANGING DROP；pH 8；295 K；0.1 M Tris pH 8.0 and 2.8 M NaCl
|
Resolution 2.25 Å R-free 0.275 |
| 6H9M Coiled-coil domain-containing protein 90B residues 43-125 from Homo sapiens fused to a GCN4 adaptor Deposited 2018-08-04 | Different construct Different mutation/modification Different oligomeric state Different experimental method Different experimental conditions Different structure-quality metrics | Assembly 1 Insufficient information Homooligomer；Protein × 3 PDB declaration: trimeric |
Chain A
251–281（31 aa）
Chain B
251–281（31 aa）
Chain C
251–281（31 aa）
|
Not recorded | No recorded non-water small molecule |
X-RAY DIFFRACTION
X-ray crystallization conditions
VAPOR DIFFUSION, SITTING DROP；294 K；Molecular Dimensions Morpheus Screen, Well F2
|
Resolution 2.10 Å R-free 0.257 |
| 6HN4 Leucine-zippered human insulin receptor ectodomain with single bound insulin - "lower" membrane-proximal part Deposited 2018-09-14 | Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental method Different experimental conditions Different structure-quality metrics | Assembly 1 Insufficient information Homooligomer；Protein × 2 PDB declaration: dimeric |
Chain E
249–281（33 aa）
Chain F
249–281（33 aa）
|
Not recorded | NAG 2-acetamido-2-deoxy-beta-D-glucopyranose × 6 |
ELECTRON MICROSCOPY
cryo-EM buffer
pH 7.5
cryo-EM vitrification conditions
Cryogen ETHANE
|
Resolution 4.20 Å |
| 6HN5 Leucine-zippered human insulin receptor ectodomain with single bound insulin - "upper" membrane-distal part Deposited 2018-09-14 | Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental method Different experimental conditions Different structure-quality metrics | Assembly 1 Insufficient information Heteromer；Protein × 4 PDB declaration: tetrameric |
Chain E
249–281（33 aa）
Chain F
249–281（33 aa）
|
Not recorded | NAG 2-acetamido-2-deoxy-beta-D-glucopyranose × 9 |
ELECTRON MICROSCOPY
cryo-EM buffer
pH 7.5
cryo-EM vitrification conditions
Cryogen ETHANE
|
Resolution 3.20 Å |
| 6O2E GCN4 with asparagine at position 18 Deposited 2019-02-22 | Different construct Different mutation/modification Different oligomeric state Different experimental method Different experimental conditions Different structure-quality metrics | Assembly 1 Protein homooligomer Homooligomer；Protein × 2 PDB declaration: dimeric |
Chain A
249–279（31 aa）
|
Mutation：H266N Non-standard monomer：Yes (specific site not provided by mmCIF) | No recorded non-water small molecule |
X-RAY DIFFRACTION
X-ray crystallization conditions
VAPOR DIFFUSION, SITTING DROP；293 K；Pact premier C1
|
Resolution 1.90 Å R-free 0.247 |
| 6O2F GCN4 with NPEG4 at position 18 Deposited 2019-02-22 | Different construct Different mutation/modification Different oligomeric state Different experimental method Different experimental conditions Different structure-quality metrics | Assembly 1 Protein homooligomer Homooligomer；Protein × 2 PDB declaration: dimeric |
Chain A
249–279（31 aa）
|
Mutation：H266N Non-standard monomer：Yes (specific site not provided by mmCIF) | No recorded non-water small molecule |
X-RAY DIFFRACTION
X-ray crystallization conditions
VAPOR DIFFUSION, SITTING DROP；293 K；Pact Premier B1
|
Resolution 1.80 Å R-free 0.235 |
| 6PSA PIE12 D-PEPTIDE AGAINST HIV ENTRY (IN COMPLEX WITH IQN17 Q577R RESISTANCE MUTANT) Deposited 2019-07-12 | Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental method Different experimental conditions Different structure-quality metrics | Assembly 1 Insufficient information Heteromer；Protein × 6 PDB declaration: hexameric |
Chain A
249–276（28 aa）
Fragment：GP41 HYDROPHOBIC POCKET, RESIDUES 565-581, GCN4, RESIDUES 249-276
|
Mutation：Q577R Non-standard monomer：Yes (specific site not provided by mmCIF) | CL CHLORIDE ION × 6 |
X-RAY DIFFRACTION
X-ray crystallization conditions
VAPOR DIFFUSION, SITTING DROP；pH 4.6；294 K；HAMPTON RESEARCH SALT RX SCREEN, CONDITION B4 - 1.8M AMMONIUM CITRATE DIBASIC, 0.1 M SODIUM ACETATE TRIHYDRATE, PH 4.6
|
Resolution 1.30 Å R-free 0.217 |
| 6VWG Head region of the open conformation of the human type 1 insulin-like growth factor receptor ectodomain in complex with human insulin-like growth factor II. Deposited 2020-02-19 | Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental method Different experimental conditions Different structure-quality metrics | Assembly 1 Insufficient information Heteromer；Protein × 3 PDB declaration: trimeric |
Chain A
249–281（33 aa）
Chain B
249–281（33 aa）
|
Not recorded | NAG 2-acetamido-2-deoxy-beta-D-glucopyranose × 4 |
ELECTRON MICROSCOPY
cryo-EM buffer
pH 7.5
cryo-EM vitrification conditions
Cryogen ETHANE
|
Resolution 3.21 Å |
| 6VWH Leg region of the open conformation of the human type 1 insulin-like growth factor receptor ectodomain in complex with human insulin-like growth factor II. Deposited 2020-02-19 | Different construct Different mutation/modification Different oligomeric state Different experimental method Different experimental conditions Different structure-quality metrics | Assembly 1 Insufficient information Homooligomer；Protein × 2 PDB declaration: dimeric |
Chain A
249–281（33 aa）
Chain B
249–281（33 aa）
|
Not recorded | No recorded non-water small molecule |
ELECTRON MICROSCOPY
cryo-EM buffer
pH 7.5
cryo-EM vitrification conditions
Cryogen ETHANE
|
Resolution 4.26 Å |
| 6VWI Head region of the closed conformation of the human type 1 insulin-like growth factor receptor ectodomain in complex with human insulin-like growth factor II. Deposited 2020-02-19 | Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental method Different experimental conditions Different structure-quality metrics | Assembly 1 Insufficient information Heteromer；Protein × 3 PDB declaration: trimeric |
Chain A
249–281（33 aa）
Chain B
249–281（33 aa）
|
Not recorded | NAG 2-acetamido-2-deoxy-beta-D-glucopyranose × 4 |
ELECTRON MICROSCOPY
cryo-EM buffer
pH 7.5
cryo-EM vitrification conditions
Cryogen ETHANE
|
Resolution 3.70 Å |
| 6VWJ Leg region of the closed conformation of the human type 1 insulin-like growth factor receptor ectodomain in complex with human insulin-like growth factor II Deposited 2020-02-19 | Different construct Different mutation/modification Different oligomeric state Different experimental method Different experimental conditions Different structure-quality metrics | Assembly 1 Insufficient information Homooligomer；Protein × 2 PDB declaration: dimeric |
Chain A
249–281（33 aa）
Chain B
249–281（33 aa）
|
Not recorded | No recorded non-water small molecule |
ELECTRON MICROSCOPY
cryo-EM buffer
pH 7.5
cryo-EM vitrification conditions
Cryogen ETHANE
|
Resolution 4.21 Å |
| 6XNE GCN4-p1 Peptide Trimer with p-methylphenylalanine residue at position 16 (me-F16) Deposited 2020-07-02 | Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental method Different experimental conditions Different structure-quality metrics | Assembly 1 Protein homooligomer Homooligomer；Protein × 3 PDB declaration: trimeric |
Chain A
249–278（30 aa）
Chain B
249–278（30 aa）
Chain C
249–278（30 aa）
|
Mutation：me-F16 Non-standard monomer：Yes (specific site not provided by mmCIF) Mutation：N16A Mutation：N16A | NA SODIUM ION × 6 MG MAGNESIUM ION × 1 |
X-RAY DIFFRACTION
X-ray crystallization conditions
VAPOR DIFFUSION, HANGING DROP；pH 7；298 K；Crystallization drops were prepared by mixing 2 uL of stock peptide solution with 2 uL of mother liquor and allowed to equilibrate at 298 K over a well containing 500 uL of mother liquor. The stock peptide solution (total concentration 1.5 mM) was prepared by mixing 2:1 ratios of the A16 peptide with me-F16 in 10 mM potassium phosphate, 100 mM potassium chloride pH 7.0.
|
Resolution 1.96 Å R-free 0.309 |
| 6XNF GCN4-p1 Peptide Trimer with Tetrafluoroiodophenylalanine residue at position 16 (TFI-F16) Deposited 2020-07-02 | Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental method Different experimental conditions Different structure-quality metrics | Assembly 1 Protein homooligomer Homooligomer；Protein × 3 PDB declaration: trimeric |
Chain A
249–278（30 aa）
Chain B
249–278（30 aa）
Chain C
249–278（30 aa）
|
Mutation：TFI-F16 Non-standard monomer：Yes (specific site not provided by mmCIF) Mutation：TFI-F16 Mutation：TFI-F16 | NA SODIUM ION × 4 |
X-RAY DIFFRACTION
X-ray crystallization conditions
VAPOR DIFFUSION, HANGING DROP；pH 7；298 K；Crystallization drops were prepared by mixing 2 uL of stock peptide solution with 2 uL of mother liquor and allowed to equilibrate at 298 K over a well containing 500 uL of mother liquor. The stock peptide solution (total concentration 1.5 mM) was prepared by mixing 2:1 ratios of the A16 peptide with TFI-F16 in 10 mM potassium phosphate, 100 mM potassium chloride pH 7.0.
|
Resolution 2.00 Å R-free 0.254 |
| 6XNL GCN4-p1 Peptide Trimer with iodo-phenylalanine residue at position 16 (IPF-F16) Deposited 2020-07-03 | Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental method Different experimental conditions Different structure-quality metrics | Assembly 1 Protein homooligomer Homooligomer；Protein × 3 PDB declaration: trimeric |
Chain A
249–278（30 aa）
Chain B
249–278（30 aa）
Chain C
249–278（30 aa）
|
Mutation：IPF-F16 Non-standard monomer：Yes (specific site not provided by mmCIF) Mutation：N16A Mutation：N16A | NA SODIUM ION × 2 |
X-RAY DIFFRACTION
X-ray crystallization conditions
VAPOR DIFFUSION, HANGING DROP；pH 7；298 K；Crystallization drops were prepared by mixing 2 uL of stock peptide solution with 2 uL of mother liquor and allowed to equilibrate at 298 K over a well containing 500 uL of mother liquor. The stock peptide solution (total concentration 1.5 mM) was prepared by mixing 2:1 ratios of the A16 peptide with IPF-F16 in 10 mM potassium phosphate, 100 mM potassium chloride pH 7.0.
|
Resolution 2.20 Å R-free 0.321 |
| 6XNM GCN4-p1 Peptide Trimer with tyrosine residue at position 16 Deposited 2020-07-03 | Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental method Different experimental conditions Different structure-quality metrics | Assembly 1 Protein homooligomer Homooligomer；Protein × 3 PDB declaration: trimeric |
Chain A
249–278（30 aa）
Chain B
249–278（30 aa）
Chain C
249–278（30 aa）
|
Mutation：N16A Mutation：N16Y Mutation：N16A | NA SODIUM ION × 7 |
X-RAY DIFFRACTION
X-ray crystallization conditions
VAPOR DIFFUSION, HANGING DROP；pH 7；298 K；Crystallization drops were prepared by mixing 2 uL of stock peptide solution with 2 uL of mother liquor and allowed to equilibrate at 298 K over a well containing 500 uL of mother liquor. The stock peptide solution (total concentration 1.5 mM) was prepared by mixing 2:1 ratios of the A16 peptide with me-F16 in 10 mM potassium phosphate, 100 mM potassium chloride pH 7.0.
|
Resolution 2.25 Å R-free 0.358 |
| 7O9V hypothetical protein OMM_04225 residues 244-274 from Candidatus Magnetoglobus multicellularis fused to GCN4 adaptors Deposited 2021-04-17 | Different construct Different mutation/modification Different oligomeric state Different experimental method Different experimental conditions Different structure-quality metrics | Assembly 1 Insufficient information Homooligomer；Protein × 3 PDB declaration: trimeric |
Chain A
250–277（28 aa）
Chain B
250–277（28 aa）
Chain C
250–277（28 aa）
|
Not recorded | No recorded non-water small molecule |
X-RAY DIFFRACTION
X-ray crystallization conditions
VAPOR DIFFUSION, SITTING DROP；294 K；0.2M KSCN, 0.1M bis tris propane pH 8.5, 20% (w/v) PEG 3350
|
Resolution 1.99 Å R-free 0.315 |
| 7OAA conserved hypothetical protein residues 311-335 from Candidatus Magnetomorum sp. HK-1 fused to GCN4 adaptors Deposited 2021-04-19 | Different construct Different oligomeric state Different experimental method Different experimental conditions Different structure-quality metrics | Assembly 1 Insufficient information Homooligomer；Protein × 3 PDB declaration: trimeric |
Chain A
250–277（28 aa）
|
Not recorded | No recorded non-water small molecule |
X-RAY DIFFRACTION
X-ray crystallization conditions
VAPOR DIFFUSION, SITTING DROP；294 K；0.1M HEPES pH 7.5, 30% (w/v) PEG 300
|
Resolution 1.40 Å R-free 0.269 |
| 7OAC conserved hypothetical protein residues 311-335 from Candidatus Magnetomorum sp. HK-1 fused to GCN4 adaptors, mutant beta1/A, crystal form I Deposited 2021-04-19 | Different construct Different mutation/modification Different oligomeric state Different experimental method Different experimental conditions Different structure-quality metrics | Assembly 1 Insufficient information Homooligomer；Protein × 3 PDB declaration: trimeric |
Chain A
250–277（28 aa）
Chain B
250–277（28 aa）
Chain C
250–277（28 aa）
|
Not recorded | No recorded non-water small molecule |
X-RAY DIFFRACTION
X-ray crystallization conditions
VAPOR DIFFUSION, SITTING DROP；294 K；0.1M tri-sodium citrate pH 4.5, 7.1 % (w/v) PEG 10000
|
Resolution 2.15 Å R-free 0.258 |
| 7OAD conserved hypothetical protein residues 311-335 from Candidatus Magnetomorum sp. HK-1 fused to GCN4 adaptors, mutant beta1/A, crystal form II Deposited 2021-04-19 | Different construct Different mutation/modification Different oligomeric state Different experimental method Different experimental conditions Different structure-quality metrics | Assembly 1 Insufficient information Homooligomer；Protein × 3 PDB declaration: trimeric |
Chain A
250–277（28 aa）
Chain B
250–277（28 aa）
Chain C
250–277（28 aa）
|
Not recorded | No recorded non-water small molecule |
X-RAY DIFFRACTION
X-ray crystallization conditions
VAPOR DIFFUSION, SITTING DROP；294 K；0.1M tri-sodium citrate pH 4.5, 7.1% PEG 10000
|
Resolution 2.00 Å R-free 0.294 |
| 7OAF conserved hypothetical protein residues 311-335 from Candidatus Magnetomorum sp. HK-1 fused to GCN4 adaptors, mutant beta1/A, crystal form III Deposited 2021-04-19 | Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental method Different experimental conditions Different structure-quality metrics | Assembly 1 Insufficient information Homooligomer；Protein × 3 PDB declaration: trimeric |
Chain A
250–277（28 aa）
Chain B
250–277（28 aa）
Chain C
250–277（28 aa）
|
Not recorded | 1PE PENTAETHYLENE GLYCOL × 1 |
X-RAY DIFFRACTION
X-ray crystallization conditions
VAPOR DIFFUSION, SITTING DROP；294 K；0.1M tri-sodium citrate pH 4.5, 9.3% PEG 6000
|
Resolution 1.45 Å R-free 0.215 |
| 7OAH conserved hypothetical protein residues 311-335 from Candidatus Magnetomorum sp. HK-1 fused to GCN4 adaptors, mutant beta2/A Deposited 2021-04-19 | Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental method Different experimental conditions Different structure-quality metrics | Assembly 1 Insufficient information Homooligomer；Protein × 3 PDB declaration: trimeric |
Chain A
250–277（28 aa）
Chain B
250–277（28 aa）
Chain C
250–277（28 aa）
|
Not recorded | PG4 TETRAETHYLENE GLYCOL × 1 |
X-RAY DIFFRACTION
X-ray crystallization conditions
VAPOR DIFFUSION, SITTING DROP；294 K；0.1 M tri-sodium citrate pH 5.5, 20% (w/v) PEG 3000
|
Resolution 1.69 Å R-free 0.268 |
| 7SAF Fragment of streptococcal M87 protein fused to GCN4 adaptor Deposited 2021-09-22 | Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental method Different experimental conditions Different structure-quality metrics | Assembly 1 Insufficient information Homooligomer；Protein × 2 PDB declaration: dimeric |
Chain A
250–278（29 aa）
Chain B
250–278（29 aa）
|
Not recorded | PO4 PHOSPHATE ION × 2 |
X-RAY DIFFRACTION
X-ray crystallization conditions
VAPOR DIFFUSION, HANGING DROP；293 K；0.6 M monobasic ammonium phosphate, 0.1 M Tris-HCl, pH 8.0
|
Resolution 2.45 Å R-free 0.272 |
| 7SAY Fragment of streptococcal M87 protein fused to GCN4 adaptor in complex with human cathelicidin Deposited 2021-09-23 | Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental method Different experimental conditions Different structure-quality metrics | Assembly 1 Insufficient information Heteromer；Protein × 3 PDB declaration: trimeric |
Chain A
250–278（29 aa）
Chain B
250–278（29 aa）
|
Not recorded | EDO 1,2-ETHANEDIOL × 3 |
X-RAY DIFFRACTION
X-ray crystallization conditions
VAPOR DIFFUSION, HANGING DROP；293 K；10% (v/v) acetonitrile, 0.1 M MES-NaOH, pH 6.5
|
Resolution 2.10 Å R-free 0.271 |
| 7SAY Fragment of streptococcal M87 protein fused to GCN4 adaptor in complex with human cathelicidin Deposited 2021-09-23 | Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental method Different experimental conditions Different structure-quality metrics | Assembly 2 Insufficient information Heteromer；Protein × 3 PDB declaration: trimeric |
Chain C
250–278（29 aa）
Chain D
250–278（29 aa）
|
Not recorded | EDO 1,2-ETHANEDIOL × 1 |
X-RAY DIFFRACTION
X-ray crystallization conditions
VAPOR DIFFUSION, HANGING DROP；293 K；10% (v/v) acetonitrile, 0.1 M MES-NaOH, pH 6.5
|
Resolution 2.10 Å R-free 0.271 |
| 8OPM Human Coronavirus HKU1 spike glycoprotein in complex with an alpha2,8-linked 9-O-acetylated disialoside (closed state) Deposited 2023-04-07 | Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental method Different experimental conditions Different structure-quality metrics | Assembly 1 Insufficient information Homooligomer；Protein × 3 PDB declaration: trimeric |
Chain A
249–278（30 aa）
Chain B
249–278（30 aa）
Chain C
249–278（30 aa）
|
Not recorded | NAG 2-acetamido-2-deoxy-beta-D-glucopyranose × 30 |
ELECTRON MICROSCOPY
cryo-EM buffer
pH 8
cryo-EM vitrification conditions
Cryogen ETHANE
|
Resolution 3.70 Å |
| 8OPN Human Coronavirus HKU1 spike glycoprotein in complex with an alpha2,8-linked 9-O-acetylated disialoside (1-up state) Deposited 2023-04-07 | Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental method Different experimental conditions Different structure-quality metrics | Assembly 1 Insufficient information Homooligomer；Protein × 3 PDB declaration: trimeric |
Chain A
249–278（30 aa）
Chain B
249–278（30 aa）
Chain C
249–278（30 aa）
|
Not recorded | NAG 2-acetamido-2-deoxy-beta-D-glucopyranose × 26 |
ELECTRON MICROSCOPY
cryo-EM buffer
pH 8
cryo-EM vitrification conditions
Cryogen ETHANE
|
Resolution 4.70 Å |
| 8OPO Human Coronavirus HKU1 spike glycoprotein in complex with an alpha2,8-linked 9-O-acetylated disialoside (3-up state) Deposited 2023-04-07 | Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental method Different experimental conditions Different structure-quality metrics | Assembly 1 Insufficient information Homooligomer；Protein × 3 PDB declaration: trimeric |
Chain A
249–278（30 aa）
Chain B
249–278（30 aa）
Chain C
249–278（30 aa）
|
Not recorded | NAG 2-acetamido-2-deoxy-beta-D-glucopyranose × 33 |
ELECTRON MICROSCOPY
cryo-EM buffer
pH 8
cryo-EM vitrification conditions
Cryogen ETHANE
|
Resolution 3.60 Å |
| 9YOP Cryo-EM structure of human beta-cardiac myosin in the interacting-heads motif and S2-FH docked state Deposited 2025-10-13 | Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental method Different experimental conditions Different structure-quality metrics | Assembly 1 Insufficient information Heteromer；Protein × 6 PDB declaration: hexameric |
Chain A
250–281（32 aa）
Chain B
250–281（32 aa）
|
Not recorded | ADP ADENOSINE-5'-DIPHOSPHATE × 2 PO4 PHOSPHATE ION × 2 |
ELECTRON MICROSCOPY
cryo-EM buffer
pH 7.4
cryo-EM vitrification conditions
Cryogen ETHANE
|
Resolution 3.50 Å |
| 9YP4 Cryo-EM structure of human beta-cardiac myosin bound to omecamtiv mecarbil in the interacting-heads motif and S2-FH docked state Deposited 2025-10-13 | Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental method Different experimental conditions Different structure-quality metrics | Assembly 1 Insufficient information Heteromer；Protein × 6 PDB declaration: hexameric |
Chain A
250–281（32 aa）
Chain B
250–281（32 aa）
|
Not recorded | 2OW methyl 4-(2-fluoro-3-{[(6-methylpyridin-3-yl)carbamoyl]amino}benzyl)piperazine-1-carboxylate × 2 ADP ADENOSINE-5'-DIPHOSPHATE × 2 PO4 PHOSPHATE ION × 2 |
ELECTRON MICROSCOPY
cryo-EM buffer
pH 7.4
cryo-EM vitrification conditions
Cryogen ETHANE
|
Resolution 4.50 Å |
| 9YP9 Cryo-EM structure of human beta-cardiac myosin bound to mavacamten in the interacting-heads motif and S2-FH docked state Deposited 2025-10-13 | Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental method Different experimental conditions Different structure-quality metrics | Assembly 1 Insufficient information Heteromer；Protein × 6 PDB declaration: hexameric |
Chain A
250–281（32 aa）
Chain B
250–281（32 aa）
|
Not recorded | PO4 PHOSPHATE ION × 2 XB2 Mavacamten × 2 ADP ADENOSINE-5'-DIPHOSPHATE × 2 |
ELECTRON MICROSCOPY
cryo-EM buffer
pH 7.4
cryo-EM vitrification conditions
Cryogen ETHANE
|
Resolution 3.00 Å |
| 9YR7 Cryo-EM structure of human beta-cardiac myosin bound to mavacamten in the interacting-heads motif and S2-FH undocked state Deposited 2025-10-16 | Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental method Different experimental conditions Different structure-quality metrics | Assembly 1 Insufficient information Heteromer；Protein × 6 PDB declaration: hexameric |
Chain A
250–281（32 aa）
Chain B
250–281（32 aa）
|
Not recorded | XB2 Mavacamten × 2 ADP ADENOSINE-5'-DIPHOSPHATE × 2 PO4 PHOSPHATE ION × 2 |
ELECTRON MICROSCOPY
cryo-EM buffer
pH 7.4
cryo-EM vitrification conditions
Cryogen ETHANE
|
Resolution 3.00 Å |
| 9YRG Cryo-EM structure of human beta-cardiac myosin in the interacting-heads motif and S2-FH undocked state Deposited 2025-10-16 | Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental method Different experimental conditions Different structure-quality metrics | Assembly 1 Insufficient information Heteromer；Protein × 6 PDB declaration: hexameric |
Chain A
250–281（32 aa）
Chain B
250–281（32 aa）
|
Not recorded | ADP ADENOSINE-5'-DIPHOSPHATE × 2 PO4 PHOSPHATE ION × 2 |
ELECTRON MICROSCOPY
cryo-EM buffer
pH 7.4
cryo-EM vitrification conditions
Cryogen ETHANE
|
Resolution 3.20 Å |
| 9YRH Cryo-EM structure of human beta-cardiac myosin bound to omecamtiv mecarbil in the interacting-heads motif and S2-FH undocked state Deposited 2025-10-16 | Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental method Different experimental conditions Different structure-quality metrics | Assembly 1 Insufficient information Heteromer；Protein × 6 PDB declaration: hexameric |
Chain A
250–281（32 aa）
Chain B
250–281（32 aa）
|
Not recorded | 2OW methyl 4-(2-fluoro-3-{[(6-methylpyridin-3-yl)carbamoyl]amino}benzyl)piperazine-1-carboxylate × 2 ADP ADENOSINE-5'-DIPHOSPHATE × 2 PO4 PHOSPHATE ION × 2 |
ELECTRON MICROSCOPY
cryo-EM buffer
pH 7.4
cryo-EM vitrification conditions
Cryogen ETHANE
|
Resolution 3.80 Å |
| 9YZU Isoreticular co-crystal 1 with asymmetrical expanded duplex (31mer) containing insert sequence ATGAGTCATA and loaded with mutated Bzip region of GCN4 transcription factor Deposited 2025-10-30 | Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental method Different experimental conditions Different structure-quality metrics | Assembly 1 Protein–DNA Heteromer；Protein × 4 PDB declaration: hexameric |
Chain D
226–251（26 aa）
Chain E
226–251（26 aa）
Chain F
226–251（26 aa）
|
Not recorded | MG MAGNESIUM ION × 2 |
X-RAY DIFFRACTION
X-ray crystallization conditions
VAPOR DIFFUSION, SITTING DROP；pH 6.5；298 K；50mM magnesium acetate, 1.8M lithium sulfate, 50mM MES pH 6.5. The crystal was crosslinked with 50mg/mL EDC overnight, and then looped into a solution of 50mM potassium chloride, 4mM calcium chloride, 10% glycerol, and 10mM Tris hydrochloride for 1 hour. The drop was then supplemented with 33 micromolar bZip
|
Resolution 3.05 Å R-free 0.246 |
| 9Z1P Backbone Modification in the GCN4 Leucine Zipper: Prototype Deposited 2025-11-04 | Different construct Different mutation/modification Different oligomeric state Different experimental method Different experimental conditions Different structure-quality metrics | Assembly 1 Protein homooligomer Homooligomer；Protein × 2 PDB declaration: dimeric |
Chain A
249–281（33 aa）
Fragment：leucine zipper domain
Chain B
249–281（33 aa）
Fragment：leucine zipper domain
|
Non-standard monomer：Yes (specific site not provided by mmCIF) Non-standard monomer：Yes (specific site not provided by mmCIF) | No recorded non-water small molecule |
X-RAY DIFFRACTION
X-ray crystallization conditions
VAPOR DIFFUSION, HANGING DROP；298 K；0.2 M sodium acetate pH 4.5, 0.1 M sodium citrate pH 5.6, 10% w/v PEG 3350
|
Resolution 1.60 Å R-free 0.230 |
| 9Z1Q Backbone Modification in the GCN4 Leucine Zipper: Calpha-methyl-Glu at position 11 Deposited 2025-11-04 | Different construct Different mutation/modification Different oligomeric state Different experimental method Different experimental conditions Different structure-quality metrics | Assembly 1 Protein homooligomer Homooligomer；Protein × 2 PDB declaration: dimeric |
Chain A
249–281（33 aa）
Fragment：leucine zipper domain
Chain B
249–281（33 aa）
Fragment：leucine zipper domain
|
Non-standard monomer：Yes (specific site not provided by mmCIF) Non-standard monomer：Yes (specific site not provided by mmCIF) | No recorded non-water small molecule |
X-RAY DIFFRACTION
X-ray crystallization conditions
VAPOR DIFFUSION, HANGING DROP；pH 4.6；298 K；0.3 M sodium acetate pH 4.6, 0.1 M sodium citrate pH 4.6, 5% w/v PEG 3350
|
Resolution 1.80 Å R-free 0.196 |
| 9Z1R Backbone Modification in the GCN4 Leucine Zipper: beta3-Glu at position 20 Deposited 2025-11-04 | Different construct Different mutation/modification Different oligomeric state Different experimental method Different experimental conditions Different structure-quality metrics | Assembly 1 Protein homooligomer Homooligomer；Protein × 2 PDB declaration: dimeric |
Chain A
249–281（33 aa）
Fragment：leucine zipper domain
Chain B
249–281（33 aa）
Fragment：leucine zipper domain
|
Non-standard monomer：Yes (specific site not provided by mmCIF) Non-standard monomer：Yes (specific site not provided by mmCIF) | No recorded non-water small molecule |
X-RAY DIFFRACTION
X-ray crystallization conditions
VAPOR DIFFUSION, HANGING DROP；pH 4.6；298 K；0.3 M sodium acetate pH 4.6, 0.1 M sodium citrate pH 4.6, 5% w/v PEG 3350
|
Resolution 1.90 Å R-free 0.214 |
| 9Z1R Backbone Modification in the GCN4 Leucine Zipper: beta3-Glu at position 20 Deposited 2025-11-04 | Different construct Different mutation/modification Different oligomeric state Different experimental method Different experimental conditions Different structure-quality metrics | Assembly 2 Protein homooligomer Homooligomer；Protein × 2 PDB declaration: dimeric |
Chain C
249–281（33 aa）
Fragment：leucine zipper domain
Chain D
249–281（33 aa）
Fragment：leucine zipper domain
|
Non-standard monomer：Yes (specific site not provided by mmCIF) Non-standard monomer：Yes (specific site not provided by mmCIF) | No recorded non-water small molecule |
X-RAY DIFFRACTION
X-ray crystallization conditions
VAPOR DIFFUSION, HANGING DROP；pH 4.6；298 K；0.3 M sodium acetate pH 4.6, 0.1 M sodium citrate pH 4.6, 5% w/v PEG 3350
|
Resolution 1.90 Å R-free 0.214 |
| 9Z1S Backbone Modification in the GCN4 Leucine Zipper: beta3-Ala at position 24 Deposited 2025-11-04 | Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental method Different experimental conditions Different structure-quality metrics | Assembly 1 Protein homooligomer Homooligomer；Protein × 2 PDB declaration: dimeric |
Chain A
249–281（33 aa）
Fragment：leucine zipper domain
Chain B
249–281（33 aa）
Fragment：leucine zipper domain
|
Non-standard monomer：Yes (specific site not provided by mmCIF) Non-standard monomer：Yes (specific site not provided by mmCIF) | GOL GLYCEROL × 1 ACT ACETATE ION × 1 |
X-RAY DIFFRACTION
X-ray crystallization conditions
VAPOR DIFFUSION, HANGING DROP；pH 4.6；298 K；0.2 M sodium acetate pH 4.6, 0.1 M sodium citrate pH 4.6, 10% w/v PEG 3350
|
Resolution 1.75 Å R-free 0.233 |
| 9Z1T Backbone Modification in the GCN4 Leucine Zipper: Aib at position 24 Deposited 2025-11-04 | Different construct Different mutation/modification Different oligomeric state Different experimental method Different experimental conditions Different structure-quality metrics | Assembly 1 Protein homooligomer Homooligomer；Protein × 2 PDB declaration: dimeric |
Chain A
249–281（33 aa）
Fragment：leucine zipper domain
Chain B
249–281（33 aa）
Fragment：leucine zipper domain
|
Non-standard monomer：Yes (specific site not provided by mmCIF) Non-standard monomer：Yes (specific site not provided by mmCIF) | No recorded non-water small molecule |
X-RAY DIFFRACTION
X-ray crystallization conditions
VAPOR DIFFUSION, HANGING DROP；pH 4.6；298 K；0.2 M sodium acetate pH 4.6, 0.1 M sodium citrate pH 4.6, 10% w/v PEG 3350
|
Resolution 1.60 Å R-free 0.216 |
| 9Z1U Backbone Modification in the GCN4 Leucine Zipper: beta3-Lys at position 28 Deposited 2025-11-04 | Different construct Different mutation/modification Different oligomeric state Different experimental method Different experimental conditions Different structure-quality metrics | Assembly 1 Protein homooligomer Homooligomer；Protein × 2 PDB declaration: dimeric |
Chain A
249–281（33 aa）
Fragment：leucine zipper domain
Chain B
249–281（33 aa）
Fragment：leucine zipper domain
|
Non-standard monomer：Yes (specific site not provided by mmCIF) Non-standard monomer：Yes (specific site not provided by mmCIF) | No recorded non-water small molecule |
X-RAY DIFFRACTION
X-ray crystallization conditions
VAPOR DIFFUSION, HANGING DROP；pH 4.6；298 K；0.2 M sodium acetate pH 4.6, 0.1 M sodium citrate pH 4.6, 10% w/v PEG 3350
|
Resolution 1.50 Å R-free 0.206 |
| 9Z1V Backbone Modification in the GCN4 Leucine Zipper: Calpha-methyl-Lys at position 28 Deposited 2025-11-04 | Different construct Different mutation/modification Different oligomeric state Different experimental method Different experimental conditions Different structure-quality metrics | Assembly 1 Protein homooligomer Homooligomer；Protein × 2 PDB declaration: dimeric |
Chain A
249–281（33 aa）
Fragment：leucine zipper domain
Chain B
249–281（33 aa）
Fragment：leucine zipper domain
|
Non-standard monomer：Yes (specific site not provided by mmCIF) Non-standard monomer：Yes (specific site not provided by mmCIF) | No recorded non-water small molecule |
X-RAY DIFFRACTION
X-ray crystallization conditions
VAPOR DIFFUSION, HANGING DROP；pH 4.6；298 K；0.2 M sodium acetate pH 4.6, 0.1 M sodium citrate pH 4.6, 15% w/v PEG 3350
|
Resolution 1.65 Å R-free 0.211 |
| 9Z4E Isoreticular co-crystal 1 with asymmetrical expanded duplex (31mer) containing insert sequence CATGAGTCAT and loaded with mutated Bzip region of GCN4 transcription factor Deposited 2025-11-10 | Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental method Different experimental conditions Different structure-quality metrics | Assembly 1 Protein–DNA Heteromer；Protein × 4 PDB declaration: hexameric |
Chain D
226–253（28 aa）
Fragment：Bzip region
Chain E
226–253（28 aa）
Fragment：Bzip region
Chain F
226–253（28 aa）
Fragment：Bzip region
|
Mutation：residues 251-253 (Uniprot numbering) mutated from KQL to KKQC Mutation：residues 251-253 (Uniprot numbering) mutated from KQL to KKQC Mutation：residues 251-253 (Uniprot numbering) mutated from KQL to KKQC | MG MAGNESIUM ION × 3 |
X-RAY DIFFRACTION
X-ray crystallization conditions
VAPOR DIFFUSION, SITTING DROP；pH 6.5；298 K；50mM magnesium acetate, 1.6M Lithium sulfate, 50mM MES pH 6.5. The crystal was crosslinked with 47.5 mg/mL EDC overnight, and then looped into a solution of 50mM potassium chloride, 4mM calcium chloride, 10% glycerol, and 10mM Tris hydrochloride for 1 hour. The drop was then supplemented with 100 micromolar bZip
|
Resolution 3.63 Å R-free 0.285 |
162 other PDB entries and 200 assemblies. Open the comparison page and filter oligomeric states
View Construct and Data Evidence
| UniProt name | GCN4_YEAST |
| Isoform | — |
| PDB entities | 1 |
| Chains and sequence ranges | Author chain A； PDBConstruct 1–35； UniProt 247–281 |
