SAXSdb — 6dmx

▼

1. Protein Identity and Related Structures Protein Identity & Related Structures

BZIP factor

Human T-lymphotropic virus 1

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 heterocomplex Heteromer Protein × 5 PDB declaration: pentameric（5） Consistent with protein copy count	Chain E； UniProt 3–56	Fragment：residues 3-56 Mutation：C9A, C14A	Transcriptional activator Myb × 2 （P06876） CREB-binding protein × 2 （P45481）	X-RAY DIFFRACTION X-ray crystallization conditions：VAPOR DIFFUSION, SITTING DROP；293 K；PEG 3350, ammonium iodide	Resolution 2.80 Å R-free 0.301
2	Protein heterocomplex Heteromer Protein × 5 PDB declaration: pentameric（5） Consistent with protein copy count	Chain J； UniProt 3–56	Fragment：residues 3-56 Mutation：C9A, C14A	Transcriptional activator Myb × 2 （P06876） CREB-binding protein × 2 （P45481）	X-RAY DIFFRACTION X-ray crystallization conditions：VAPOR DIFFUSION, SITTING DROP；293 K；PEG 3350, ammonium iodide	Resolution 2.80 Å R-free 0.301

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 6DMX	Assembly / Oligomeric State	Construct	Mutations and Modifications	Ligands, Ions and Non-polymers	Method and Experimental Conditions	Structure Quality
6DNQ HBZ77 in complex with KIX and c-Myb Deposited 2018-06-07	Different construct Different mutation/modification Different ligand/ion Different experimental conditions Different structure-quality metrics	Assembly 1 Protein heterocomplex Heteromer；Protein × 5 PDB declaration: pentameric	Chain E 3–77（75 aa） Fragment：residues 3-77	Not recorded	EDO 1,2-ETHANEDIOL × 1	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION, SITTING DROP；293 K；PEG 3350, calcium chloride	Resolution 2.35 Å R-free 0.229

1 other PDB entries and 1 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence

UniProt name	Q2Q067_9DELA
Isoform	—
PDB entities	1
Chains and sequence ranges	Author chain E； PDBConstruct 5–58； UniProt 3–56 Author chain J； PDBConstruct 5–58； UniProt 3–56

Transcriptional activator Myb

Mus musculus

UniProt P06876

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 heterocomplex Heteromer Protein × 5 PDB declaration: pentameric（5） Consistent with protein copy count	Chain A； UniProt 284–315 Chain C； UniProt 284–315	Fragment：residues 284-315	BZIP factor × 1 （Q2Q067） CREB-binding protein × 2 （P45481）	X-RAY DIFFRACTION X-ray crystallization conditions：VAPOR DIFFUSION, SITTING DROP；293 K；PEG 3350, ammonium iodide	Resolution 2.80 Å R-free 0.301
2	Protein heterocomplex Heteromer Protein × 5 PDB declaration: pentameric（5） Consistent with protein copy count	Chain F； UniProt 284–315 Chain H； UniProt 284–315	Fragment：residues 284-315	BZIP factor × 1 （Q2Q067） CREB-binding protein × 2 （P45481）	X-RAY DIFFRACTION X-ray crystallization conditions：VAPOR DIFFUSION, SITTING DROP；293 K；PEG 3350, ammonium iodide	Resolution 2.80 Å R-free 0.301

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 6DMX	Assembly / Oligomeric State	Construct	Mutations and Modifications	Ligands, Ions and Non-polymers	Method and Experimental Conditions	Structure Quality
1GUU CRYSTAL STRUCTURE OF C-MYB R1 Deposited 2002-01-30	Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental conditions Different structure-quality metrics	Assembly 1 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric	Chain A 38–89（52 aa） Fragment：R1, RESIDUES 38-89	Not recorded	NA SODIUM ION × 1	X-RAY DIFFRACTION X-ray crystallization conditions pH 6.8；1.6-1.7 M SODIUM CITRATE PH 6.8, PROTEIN CONCENTRATION 15 MG/ML, CRYSTAL WAS TRANSFORMED TO LOW HUMIDITY FORM AND FLASH COOLED, 1-2% V/V OF GLYCEROL WAS ADDED TO PREVENT THE CRYSTAL CRACKING DURING THE FLASH COOLING	Resolution 1.60 Å R-free 0.223
1GV2 CRYSTAL STRUCTURE OF C-MYB R2R3 Deposited 2002-02-05	Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental conditions Different structure-quality metrics	Assembly 1 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric	Chain A 89–193（105 aa） Fragment：R2R3, RESIDUES 89-193	Not recorded	NA SODIUM ION × 2	X-RAY DIFFRACTION X-ray crystallization conditions pH 6.8；1.6-1.7 M SODIUM CITRATE PH 6.8, PROTEIN CONCENTRATION 15 MG/ML, CRYSTAL WAS GROWN BY REPEATED MACROSEEDING, TRANSFORMED TO LOW HUMIDITY FORM AND FLASH COOLED, 1-2% V/V OF GLYCEROL WAS ADDED TO SODIUM CITRATE TO PREVENT THE CRYSTAL CRACKING DURING THE FLASH COOLING	Resolution 1.68 Å R-free 0.210
1GV5 CRYSTAL STRUCTURE OF C-MYB R2 Deposited 2002-02-06	Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental conditions Different structure-quality metrics	Assembly 1 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric	Chain A 90–141（52 aa） Fragment：R2, RESIDUES 90-141	Not recorded	NA SODIUM ION × 1	X-RAY DIFFRACTION X-ray crystallization conditions pH 6.8；297 K；1.65 M SODIUM CITRATE PH 6.8, PROTEIN CONCENTRATION 10 MG/ML PLUS 10 MM DTT, TEMPERATURE 297 K	Resolution 1.58 Å R-free 0.190
1GVD CRYSTAL STRUCTURE OF C-MYB R2 V103L MUTANT Deposited 2002-02-08	Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental conditions Different structure-quality metrics	Assembly 1 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric	Chain A 90–141（52 aa） Fragment：R2, RESIDUES 90-141	Mutation：YES	NH4 AMMONIUM ION × 1 SO4 SULFATE ION × 2	X-RAY DIFFRACTION X-ray crystallization conditions pH 6.8；297 K；3.15 M AMMONIUM SULFATE IN 0.05 M MES BUFFER AT PH 6.8, PROTEIN CONCENTRATION 10 MG/ML PLUS 10 MM DTT, TEMPERATURE 297 K	Resolution 1.45 Å R-free 0.195
1H88 CRYSTAL STRUCTURE OF TERNARY PROTEIN-DNA COMPLEX1 Deposited 2001-01-29	Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental conditions Different structure-quality metrics	Assembly 1 Protein–DNA Heteromer；Protein × 3 PDB declaration: pentameric	Chain C 35–193（159 aa） Fragment：RESIDUES 35-193	Mutation：YES	NH4 AMMONIUM ION × 1	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION, SITTING DROP；pH 7.5；297 K；0.05 M AMMONIUM ACETATE, 0.01 M MAGNESIUM CHLORIDE, 10% V/V MPD, 6% V/V GLYCEROL, 0.05 M TRIS HCL BUFFER PH 7.5 AT 24 DEGREES C	Resolution 2.80 Å R-free 0.277
1IDY STRUCTURE OF MYB TRANSFORMING PROTEIN, NMR, MINIMIZED AVERAGE STRUCTURE Deposited 1996-08-15	Different construct Different mutation/modification Different oligomeric state Different experimental method Different experimental conditions Different structure-quality metrics	Assembly 1 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric	Chain A 141–193（53 aa）	Mutation：P140M, I155L	No recorded non-water small molecule	SOLUTION NMR NMR measurement conditions pH 5；283 K	Resolution not provided
1IDZ STRUCTURE OF MYB TRANSFORMING PROTEIN, NMR, 20 STRUCTURES Deposited 1996-08-15	Different construct Different mutation/modification Different oligomeric state Different experimental method Different experimental conditions Different structure-quality metrics	Assembly 1 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric	Chain A 141–193（53 aa）	Mutation：P140M, I155L	No recorded non-water small molecule	SOLUTION NMR NMR measurement conditions pH 5；283 K	Resolution not provided
1MBE MOUSE C-MYB DNA-BINDING DOMAIN REPEAT 1 Deposited 1995-05-19	Different construct Different mutation/modification Different oligomeric state Different experimental method Different experimental conditions Different structure-quality metrics	Assembly 1 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric	Chain A 38–89（52 aa）	Non-standard monomer：Yes (specific site not provided by mmCIF)	No recorded non-water small molecule	SOLUTION NMR NMR measurement conditions pH 6.8；290 K NMR measurement conditions pH 6.8；300 K	Resolution not provided
1MBF MOUSE C-MYB DNA-BINDING DOMAIN REPEAT 1 Deposited 1995-05-19	Different construct Different mutation/modification Different oligomeric state Different experimental method Different experimental conditions Different structure-quality metrics	Assembly 1 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric	Chain A 38–89（52 aa）	Non-standard monomer：Yes (specific site not provided by mmCIF)	No recorded non-water small molecule	SOLUTION NMR NMR measurement conditions pH 6.8；290 K NMR measurement conditions pH 6.8；300 K	Resolution not provided
1MBG MOUSE C-MYB DNA-BINDING DOMAIN REPEAT 2 Deposited 1995-05-19	Different construct Different mutation/modification Different oligomeric state Different experimental method Different experimental conditions Different structure-quality metrics	Assembly 1 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric	Chain A 90–141（52 aa）	Non-standard monomer：Yes (specific site not provided by mmCIF)	No recorded non-water small molecule	SOLUTION NMR NMR measurement conditions pH 6.8；290 K	Resolution not provided
1MBH MOUSE C-MYB DNA-BINDING DOMAIN REPEAT 2 Deposited 1995-05-19	Different construct Different mutation/modification Different oligomeric state Different experimental method Different experimental conditions Different structure-quality metrics	Assembly 1 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric	Chain A 90–141（52 aa）	Non-standard monomer：Yes (specific site not provided by mmCIF)	No recorded non-water small molecule	SOLUTION NMR NMR measurement conditions pH 6.8；290 K	Resolution not provided
1MBJ MOUSE C-MYB DNA-BINDING DOMAIN REPEAT 3 Deposited 1995-05-19	Different construct Different mutation/modification Different oligomeric state Different experimental method Different experimental conditions Different structure-quality metrics	Assembly 1 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric	Chain A 142–193（52 aa）	Non-standard monomer：Yes (specific site not provided by mmCIF)	No recorded non-water small molecule	SOLUTION NMR NMR measurement conditions pH 6.8；290 K NMR measurement conditions pH 6.8；300 K	Resolution not provided
1MBK MOUSE C-MYB DNA-BINDING DOMAIN REPEAT 3 Deposited 1995-05-19	Different construct Different mutation/modification Different oligomeric state Different experimental method Different experimental conditions Different structure-quality metrics	Assembly 1 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric	Chain A 142–193（52 aa）	Non-standard monomer：Yes (specific site not provided by mmCIF)	No recorded non-water small molecule	SOLUTION NMR NMR measurement conditions pH 6.8；290 K NMR measurement conditions pH 6.8；300 K	Resolution not provided
1MSE SOLUTION STRUCTURE OF A SPECIFIC DNA COMPLEX OF THE MYB DNA-BINDING DOMAIN WITH COOPERATIVE RECOGNITION HELICES Deposited 1995-01-24	Different construct Different mutation/modification Different oligomeric state Different experimental method Different experimental conditions Different structure-quality metrics	Assembly 1 Protein–DNA Monomer；Protein × 1 PDB declaration: trimeric	Chain C 90–193（104 aa）	Not recorded	No recorded non-water small molecule	SOLUTION NMR NMR measurement conditions pH 6.8；310 K	Resolution not provided
1MSF SOLUTION STRUCTURE OF A SPECIFIC DNA COMPLEX OF THE MYB DNA-BINDING DOMAIN WITH COOPERATIVE RECOGNITION HELICES Deposited 1995-01-24	Different construct Different mutation/modification Different oligomeric state Different experimental method Different experimental conditions Different structure-quality metrics	Assembly 1 Protein–DNA Monomer；Protein × 1 PDB declaration: trimeric	Chain C 90–193（104 aa）	Not recorded	No recorded non-water small molecule	SOLUTION NMR mmCIF provides none of the parsed conditions	Resolution not provided
1SB0 Solution structure of the KIX domain of CBP bound to the transactivation domain of c-Myb Deposited 2004-02-09	Different construct Different mutation/modification Different oligomeric state Different experimental method Different experimental conditions Different structure-quality metrics	Assembly 1 Protein heterocomplex Heteromer；Protein × 2 PDB declaration: dimeric	Chain B 291–315（25 aa） Fragment：transcriptional activation domain	Not recorded	No recorded non-water small molecule	SOLUTION NMR NMR measurement conditions pH 5.5；27 K；Ionic strength (raw mmCIF value) 50 mM；Pressure ambient NMR sample composition 20 mM Tris d11 acetate d4; 50 mM NaCl; 2 mM NaN3; pH 5.5 \| 90% H20; 10% D2O	Resolution not provided
2AGH Structural basis for cooperative transcription factor binding to the CBP coactivator Deposited 2005-07-26	Different construct Different mutation/modification Different oligomeric state Different experimental method Different experimental conditions Different structure-quality metrics	Assembly 1 Protein heterocomplex Heteromer；Protein × 3 PDB declaration: trimeric	Chain A 291–315（25 aa）	Not recorded	No recorded non-water small molecule	SOLUTION NMR NMR measurement conditions pH 5.5；298 K；Pressure 1 NMR sample composition 0.5-0.8 mM 15N,13C-labeled protein (e.g. CBP) + 3 fold excess of unlabeled binding partners (MYB + MLL), 20 mM Tris-d3-acetate, 50 mM NaCl, 0.2% sodium azide, 10% D2O \| 20 mM Tris-d3-acetate, 50 mM NaCl, 0.2% sodium azide, 10% D2O NMR sample composition 13C,15N-MYB + UNLABELED CBP & MYB, 20 mM Tris-d3-acetate, 50 mM NaCl, 0.2% sodium azide, 10% D2O \| 20 mM Tris-d3-acetate, 50 mM NaCl, 0.2% sodium azide, 10% D2O NMR sample composition 13C,15N-MLL + UNLABELED CBP & MLL, 20 mM Tris-d3-acetate, 50 mM NaCl, 0.2% sodium azide, 10% D2O \| 20 mM Tris-d3-acetate, 50 mM NaCl, 0.2% sodium azide, 10% D2O	Resolution not provided
6DNQ HBZ77 in complex with KIX and c-Myb Deposited 2018-06-07	Different ligand/ion Different experimental conditions Different structure-quality metrics	Assembly 1 Protein heterocomplex Heteromer；Protein × 5 PDB declaration: pentameric	Chain A 284–315（32 aa） Fragment：residues 284-315 Chain C 284–315（32 aa） Fragment：residues 284-315	Not recorded	EDO 1,2-ETHANEDIOL × 1	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION, SITTING DROP；293 K；PEG 3350, calcium chloride	Resolution 2.35 Å R-free 0.229

18 other PDB entries and 18 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence

UniProt name	MYB_MOUSE
Isoform	—
PDB entities	2
Chains and sequence ranges	Author chain A； PDBConstruct 1–32； UniProt 284–315 Author chain C； PDBConstruct 1–32； UniProt 284–315 Author chain F； PDBConstruct 1–32； UniProt 284–315 Author chain H； PDBConstruct 1–32； UniProt 284–315

CREB-binding protein

Mus musculus

UniProt P45481

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 heterocomplex Heteromer Protein × 5 PDB declaration: pentameric（5） Consistent with protein copy count	Chain B； UniProt 586–672 Chain D； UniProt 586–672	Fragment：residues 284-315	BZIP factor × 1 （Q2Q067） Transcriptional activator Myb × 2 （P06876）	X-RAY DIFFRACTION X-ray crystallization conditions：VAPOR DIFFUSION, SITTING DROP；293 K；PEG 3350, ammonium iodide	Resolution 2.80 Å R-free 0.301
2	Protein heterocomplex Heteromer Protein × 5 PDB declaration: pentameric（5） Consistent with protein copy count	Chain G； UniProt 586–672 Chain I； UniProt 586–672	Fragment：residues 284-315	BZIP factor × 1 （Q2Q067） Transcriptional activator Myb × 2 （P06876）	X-RAY DIFFRACTION X-ray crystallization conditions：VAPOR DIFFUSION, SITTING DROP；293 K；PEG 3350, ammonium iodide	Resolution 2.80 Å R-free 0.301

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 6DMX	Assembly / Oligomeric State	Construct	Mutations and Modifications	Ligands, Ions and Non-polymers	Method and Experimental Conditions	Structure Quality
1F81 SOLUTION STRUCTURE OF THE TAZ2 DOMAIN OF THE TRANSCRIPTIONAL ADAPTOR PROTEIN CBP Deposited 2000-06-28	Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental method Different experimental conditions Different structure-quality metrics	Assembly 1 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric	Chain A 1764–1850（87 aa） Fragment：TAZ2 DOMAIN (1764-1850)	Not recorded	ZN ZINC ION × 3	SOLUTION NMR NMR measurement conditions pH 5.9；298 K；Ionic strength (raw mmCIF value) 25 mM；Pressure 1 NMR sample composition 1.5 mM Taz2 \| 25 mM deuterated acetate 0.1 mM ZnCl2 0.1 mM DTT pH 5.9	Resolution not provided
1JJS NMR Structure of IBiD, A Domain of CBP/p300 Deposited 2001-07-09	Different construct Different mutation/modification Different oligomeric state Different experimental method Different experimental conditions Different structure-quality metrics	Assembly 1 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric	Chain A 2067–2112（46 aa）	Not recorded	No recorded non-water small molecule	SOLUTION NMR NMR measurement conditions pH 6.5；298 K	Resolution not provided
1KBH Mutual Synergistic Folding in the Interaction Between Nuclear Receptor Coactivators CBP and ACTR Deposited 2001-11-06	Different construct Different mutation/modification Different oligomeric state Different experimental method Different experimental conditions Different structure-quality metrics	Assembly 1 Protein heterocomplex Heteromer；Protein × 2 PDB declaration: dimeric	Chain B 2059–2117（59 aa）	Not recorded	No recorded non-water small molecule	SOLUTION NMR NMR measurement conditions pH 6.6；31 K；Ionic strength (raw mmCIF value) 60 mM；Pressure ambient NMR measurement conditions pH 6.6；31 K；Ionic strength (raw mmCIF value) 60 mM；Pressure ambient NMR measurement conditions pH 6.6；31 K；Ionic strength (raw mmCIF value) 60 mM；Pressure ambient NMR measurement conditions pH 6.6；31 K；Ionic strength (raw mmCIF value) 60 mM；Pressure ambient NMR measurement conditions pH 6.6；31 K；Ionic strength (raw mmCIF value) 60 mM；Pressure ambient NMR measurement conditions pH 6.6；31 K；Ionic strength (raw mmCIF value) 60 mM；Pressure ambient NMR sample composition 3mM U-15N,13C-CBP:2059-2117 6mM 14N,12C-ACTR:1018-1088 \| 10 mM Tris, 50 mM NaCl 95%H2O,5%D2O NMR sample composition 3mM U-15N,12C-CBP:2059-2117 6mM 14N,12C-ACTR:1018-1088 \| 10 mM Tris, 50 mM NaCl 95%H2O,5%D2O NMR sample composition 3mM U-15N,13C-CBP:2059-2117 6mM 14N,12C-ACTR:1018-1088 \| 10 mM Tris, 50 mM NaCl 100%D2O NMR sample composition 2mM U-15N,13C-ACTR:1018-1088 4mM 14N,12C-CBP:2059-2117 \| 10 mM Tris, 50 mM NaCl 95%H2O,5%D2O NMR sample composition 2mM U-15N,12C-ACTR:1018-1088 4mM 14N,12C-CBP:2059-2117 \| 10 mM Tris, 50 mM NaCl 95%H2O,5%D2O NMR sample composition 2mM U-15N,13C-ACTR:1018-1088 4mM 14N,12C-CBP:2059-2117 \| 10 mM Tris, 50 mM NaCl 100%D2O	Resolution not provided
1KDX KIX DOMAIN OF MOUSE CBP (CREB BINDING PROTEIN) IN COMPLEX WITH PHOSPHORYLATED KINASE INDUCIBLE DOMAIN (PKID) OF RAT CREB (CYCLIC AMP RESPONSE ELEMENT BINDING PROTEIN), NMR 17 STRUCTURES Deposited 1997-09-16	Different construct Different mutation/modification Different oligomeric state Different experimental method Different experimental conditions Different structure-quality metrics	Assembly 1 Protein heterocomplex Heteromer；Protein × 2 PDB declaration: dimeric	Chain A 586–666（81 aa） Fragment：KIX, RESIDUES 586-666	Not recorded	No recorded non-water small molecule	SOLUTION NMR NMR measurement conditions pH 5.5；315 K；Ionic strength (raw mmCIF value) 0.07；Pressure 1 NMR sample composition H2O OR D2O	Resolution not provided
1L8C STRUCTURAL BASIS FOR HIF-1ALPHA/CBP RECOGNITION IN THE CELLULAR HYPOXIC RESPONSE Deposited 2002-03-19	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 × 2 PDB declaration: dimeric	Chain A 345–439（95 aa） Fragment：TAZ1 (Transcription activation zinc finger) domain, Residues 345-439	Not recorded	ZN ZINC ION × 3	SOLUTION NMR NMR measurement conditions pH 6.1；298 K；Ionic strength (raw mmCIF value) 2.0 Millimolar；Pressure Ambient NMR sample composition 1MM 13C, 15N-TAZ1, 2MM HIF-1a NMR sample composition 1MM 13C, 15N-HIF-1a, 2MM TAZ1 NMR sample composition 10MM D-TRIS, 10MM D-DTT, 0.02% NAN3, 0.5MM ZnSO4	Resolution not provided
1SB0 Solution structure of the KIX domain of CBP bound to the transactivation domain of c-Myb Deposited 2004-02-09	Different construct Different mutation/modification Different oligomeric state Different experimental method Different experimental conditions Different structure-quality metrics	Assembly 1 Protein heterocomplex Heteromer；Protein × 2 PDB declaration: dimeric	Chain A 580–666（87 aa） Fragment：KIX domain	Not recorded	No recorded non-water small molecule	SOLUTION NMR NMR measurement conditions pH 5.5；27 K；Ionic strength (raw mmCIF value) 50 mM；Pressure ambient NMR sample composition 20 mM Tris d11 acetate d4; 50 mM NaCl; 2 mM NaN3; pH 5.5 \| 90% H20; 10% D2O	Resolution not provided
1TOT ZZ Domain of CBP- a Novel Fold for a Protein Interaction Module Deposited 2004-06-15	Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental method Different experimental conditions Different structure-quality metrics	Assembly 1 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric	Chain A 1700–1751（52 aa） Fragment：ZZ domain of murine CBP (residues 1700-1751)	Not recorded	ZN ZINC ION × 2	SOLUTION NMR NMR measurement conditions pH 6.8；298 K；Ionic strength (raw mmCIF value) 10 mM；Pressure ambient NMR sample composition 2.3 mM solutions in degassed 10 mM Tris-d11 pH 6.8, 200 M ZnCl2, 10 mM DTT-d10, 0.05% w/v sodium azide, 94 % H2O, 6 % D2O \| 94 % H2O, 6 % D2O	Resolution not provided
1U2N Structure CBP TAZ1 Domain Deposited 2004-07-19	Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental method Different experimental conditions Different structure-quality metrics	Assembly 1 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric	Chain A 340–439（100 aa） Fragment：CBP TAZ1 Domain	Not recorded	ZN ZINC ION × 3	SOLUTION NMR NMR measurement conditions pH 6.9；298 K；Ionic strength (raw mmCIF value) 50mM；Pressure ambient NMR sample composition 1mM N15 TAZ1; 10mM Tris-d11 pH 6.9; 50mM NaCl; 2mM DTT \| 90% H2O, 10% 2H2O NMR sample composition 1mM C13,N15 TAZ1; 10mM Tris-d11 pH 6.9; 50mM NaCl; 2mM DTT \| 100% 2H2O NMR sample composition 1mM C13,N15 TAZ1; 10mM Tris-d11 pH 6.9; 50mM NaCl; 2mM DTT \| 90% H2O, 10% 2H2O	Resolution not provided
2AGH Structural basis for cooperative transcription factor binding to the CBP coactivator Deposited 2005-07-26	Different construct Different mutation/modification Different oligomeric state Different experimental method Different experimental conditions Different structure-quality metrics	Assembly 1 Protein heterocomplex Heteromer；Protein × 3 PDB declaration: trimeric	Chain B 586–672（87 aa）	Not recorded	No recorded non-water small molecule	SOLUTION NMR NMR measurement conditions pH 5.5；298 K；Pressure 1 NMR sample composition 0.5-0.8 mM 15N,13C-labeled protein (e.g. CBP) + 3 fold excess of unlabeled binding partners (MYB + MLL), 20 mM Tris-d3-acetate, 50 mM NaCl, 0.2% sodium azide, 10% D2O \| 20 mM Tris-d3-acetate, 50 mM NaCl, 0.2% sodium azide, 10% D2O NMR sample composition 13C,15N-MYB + UNLABELED CBP & MYB, 20 mM Tris-d3-acetate, 50 mM NaCl, 0.2% sodium azide, 10% D2O \| 20 mM Tris-d3-acetate, 50 mM NaCl, 0.2% sodium azide, 10% D2O NMR sample composition 13C,15N-MLL + UNLABELED CBP & MLL, 20 mM Tris-d3-acetate, 50 mM NaCl, 0.2% sodium azide, 10% D2O \| 20 mM Tris-d3-acetate, 50 mM NaCl, 0.2% sodium azide, 10% D2O	Resolution not provided
2C52 Structural diversity in CBP p160 complexes Deposited 2005-10-25	Different construct Different mutation/modification Different oligomeric state Different experimental method Different experimental conditions Different structure-quality metrics	Assembly 1 Protein heterocomplex Heteromer；Protein × 2 PDB declaration: dimeric	Chain A 2059–2117（59 aa） Fragment：SID, RESIDUES 2059-2117	Not recorded	No recorded non-water small molecule	SOLUTION NMR NMR measurement conditions pH 7；298 K；Ionic strength (raw mmCIF value) 100 NMR measurement conditions pH 7；298 K；Ionic strength (raw mmCIF value) 100 NMR measurement conditions pH 7；298 K；Ionic strength (raw mmCIF value) 100 NMR measurement conditions pH 7；298 K；Ionic strength (raw mmCIF value) 100 NMR sample composition 90% WATER/10% D2O NMR sample composition 90% WATER/10% D2O NMR sample composition 100% D2O NMR sample composition 100% D2O	Resolution not provided
2KA6 NMR structure of the CBP-TAZ2/STAT1-TAD complex Deposited 2008-10-30	Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental method Different experimental conditions Different structure-quality metrics	Assembly 1 Protein heterocomplex Heteromer；Protein × 2 PDB declaration: dimeric	Chain A 1764–1855（92 aa） Fragment：UNP residues 1764 to 1855	Not recorded	ZN ZINC ION × 3	SOLUTION NMR NMR measurement conditions pH 6.8；290 K；Ionic strength (raw mmCIF value) 0.05；Pressure ambient NMR sample composition 1 mM [U-100% 15N] TAZ2, 90% H2O/10% D2O \| 90% H2O/10% D2O	Resolution not provided
2KKJ Solution structure of the Nuclear coactivator binding domain of CBP Deposited 2009-06-24	Different construct Different mutation/modification Different oligomeric state Different experimental method Different experimental conditions Different structure-quality metrics	Assembly 1 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric	Chain A 2059–2117（59 aa） Fragment：Nuclear coactivator binding domain, UNP residues 2059-2441	Not recorded	No recorded non-water small molecule	SOLUTION NMR NMR measurement conditions pH 6.5；31 K；Ionic strength (raw mmCIF value) 0.1；Pressure ambient NMR sample composition 10 % D2O-1, 20 mM sodium chloride-2, 20 mM sodium phosphate-3, 2 mM [U-100% 13C; U-100% 15N] protein-4, 90% H2O/10% D2O \| 90% H2O/10% D2O	Resolution not provided
2L14 Structure of CBP nuclear coactivator binding domain in complex with p53 TAD Deposited 2010-07-22	Different construct Different mutation/modification Different oligomeric state Different experimental method Different experimental conditions Different structure-quality metrics	Assembly 1 Protein heterocomplex Heteromer；Protein × 2 PDB declaration: dimeric	Chain A 2059–2117（59 aa） Fragment：CBP nuclear coactivator binding domain	Not recorded	No recorded non-water small molecule	SOLUTION NMR NMR measurement conditions pH 6.5；298 K；Ionic strength (raw mmCIF value) 0.05；Pressure ambient NMR sample composition 0.5 mM [U-99% 15N] CBP nuclear coactivator binding domain, 0.5 mM [U-99% 15N] p53 TAD, 0.5 mM [U-99% 13C; U-99% 15N] CBP nuclear coactivator binding domain, 0.5 mM [U-99% 13C; U-99% 15N] p53 TAD, 90% H2O/10% D2O \| 90% H2O/10% D2O	Resolution not provided
2LQH NMR structure of FOXO3a transactivation domains (CR2C-CR3) in complex with CBP KIX domain (2b3l conformation) Deposited 2012-03-06	Different construct Different mutation/modification Different oligomeric state Different experimental method Different experimental conditions Different structure-quality metrics	Assembly 1 Protein heterocomplex Heteromer；Protein × 2 PDB declaration: dimeric	Chain A 586–672（87 aa） Fragment：KIX domain	Not recorded	No recorded non-water small molecule	SOLUTION NMR NMR measurement conditions pH 6；303 K；Ionic strength (raw mmCIF value) 0.05；Pressure ambient NMR sample composition 0.6 mM [U-100% 13C; U-100% 15N] KIX, 0.6 mM CR2C-CR3, 20 mM MES, 50 mM sodium chloride, 1 mM DTT, 90% H2O/10% D2O \| 90% H2O/10% D2O NMR sample composition 0.6 mM [U-100% 13C; U-100% 15N] KIX, 0.6 mM CR2C-CR3, 20 mM MES, 50 mM sodium chloride, 1 mM DTT, 100% D2O \| 100% D2O NMR sample composition 0.6 mM [U-100% 13C; U-100% 15N] CR2C-CR3, 0.6 mM KIX, 20 mM MES, 50 mM sodium chloride, 1 mM DTT, 90% H2O/10% D2O \| 90% H2O/10% D2O NMR sample composition 0.6 mM [U-100% 13C; U-100% 15N] CR2C-CR3, 0.6 mM KIX, 20 mM MES, 50 mM sodium chloride, 1 mM DTT, 100% D2O \| 100% D2O	Resolution not provided
2LQI NMR structure of FOXO3a transactivation domains (CR2C-CR3) in complex with CBP KIX domain (2l3b conformation) Deposited 2012-03-06	Different construct Different mutation/modification Different oligomeric state Different experimental method Different experimental conditions Different structure-quality metrics	Assembly 1 Protein heterocomplex Heteromer；Protein × 2 PDB declaration: dimeric	Chain A 586–672（87 aa） Fragment：KIX DOMAIN	Not recorded	No recorded non-water small molecule	SOLUTION NMR NMR measurement conditions pH 6；303 K；Ionic strength (raw mmCIF value) 0.05；Pressure ambient NMR sample composition 0.6 mM [U-100% 13C; U-100% 15N] KIX, 0.6 mM CR2C-CR3, 20 mM MES, 50 mM sodium chloride, 1 mM DTT, 90% H2O/10% D2O \| 90% H2O/10% D2O NMR sample composition 0.6 mM [U-100% 13C; U-100% 15N] KIX, 0.6 mM CR2C-CR3, 20 mM MES, 50 mM sodium chloride, 1 mM DTT, 100% D2O \| 100% D2O NMR sample composition 0.6 mM [U-100% 13C; U-100% 15N] CR2C-CR3, 0.6 mM KIX, 20 mM MES, 50 mM sodium chloride, 1 mM DTT, 90% H2O/10% D2O \| 90% H2O/10% D2O NMR sample composition 0.6 mM [U-100% 13C; U-100% 15N] CR2C-CR3, 0.6 mM KIX, 20 mM MES, 50 mM sodium chloride, 1 mM DTT, 100% D2O \| 100% D2O	Resolution not provided
2LWW NMR structure of RelA-TAD/CBP-TAZ1 complex Deposited 2012-08-07	Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental method Different experimental conditions Different structure-quality metrics	Assembly 1 Protein heterocomplex Heteromer；Protein × 2 PDB declaration: dimeric	Chain A 340–439（100 aa） Fragment：TAZ-type 1 zinc finger residues 340-439	Not recorded	ZN ZINC ION × 3	SOLUTION NMR NMR measurement conditions pH 6.5；298 K；Ionic strength (raw mmCIF value) 40；Pressure ambient NMR sample composition 0.8-1.1 mM [U-13C; U-15N] TAZ1, 1.2-1.5 mM RelA-TA2, 2 mM DTT, 20 mM TRIS, 40 mM sodium chloride, 5 % [U-2H] D2O, 95% H2O/5% D2O \| 95% H2O/5% D2O NMR sample composition 0.8-1.1 mM [U-13C] TAZ1, 1.2-1.5 mM RelA-TA2, 2 mM [U-2H] DTT, 20 mM [U-2H] TRIS, 40 mM sodium chloride, 99.8 % [U-2H] D2O, 100% D2O \| 100% D2O NMR sample composition 0.7-0.9 mM [U-13C] RelA-TA2, 1.5-1.8 mM TAZ1, 2 mM [U-2H] DTT, 20 mM [U-2H] TRIS, 40 mM sodium chloride, 99.8 % [U-2H] D2O, 100% D2O \| 100% D2O NMR sample composition 0.7-0.9 mM [U-13C; U-15N] RelA-TA2, 1.5-1.8 mM TAZ1, 2 mM DTT, 20 mM TRIS, 40 mM sodium chloride, 5 % [U-2H] D2O, 95% H2O/5% D2O \| 95% H2O/5% D2O NMR sample composition 0.8-1.1 mM [U-15N] TAZ1, 1.2-1.5 mM RelA-TA2, 2 mM DTT, 20 mM TRIS, 40 mM sodium chloride, 5 % [U-2H] D2O, 95% H2O/5% D2O \| 95% H2O/5% D2O NMR sample composition 0.7-0.9 mM [U-15N] RelA-TA2, 1.5-1.8 mM TAZ1, 2 mM DTT, 20 mM TRIS, 40 mM sodium chloride, 5 % [U-2H] D2O, 95% H2O/5% D2O \| 95% H2O/5% D2O	Resolution not provided
4I9O Crystal Structure of GACKIX L664C Tethered to 1-10 Deposited 2012-12-05	Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental conditions Different structure-quality metrics	Assembly 1 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric	Chain A 586–672（87 aa） Fragment：UNP residues 562-672, GACKIX domain	Mutation：L664C Non-standard monomer：Yes (specific site not provided by mmCIF)	KI1 1-{4-[4-chloro-3-(trifluoromethyl)phenyl]-4-hydroxypiperidin-1-yl}-3-sulfanylpropan-1-one × 1 EDO 1,2-ETHANEDIOL × 2	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION, HANGING DROP；pH 7；293 K；1.8 M (NH4)2SO4, 0.1 M Tris-HCl, pH 7.0, VAPOR DIFFUSION, HANGING DROP, temperature 293K	Resolution 2.00 Å R-free 0.233
4I9O Crystal Structure of GACKIX L664C Tethered to 1-10 Deposited 2012-12-05	Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental conditions Different structure-quality metrics	Assembly 2 Protein homooligomer Homooligomer；Protein × 2 PDB declaration: dimeric	Chain A 586–672（87 aa） Fragment：UNP residues 562-672, GACKIX domain	Mutation：L664C Non-standard monomer：Yes (specific site not provided by mmCIF)	KI1 1-{4-[4-chloro-3-(trifluoromethyl)phenyl]-4-hydroxypiperidin-1-yl}-3-sulfanylpropan-1-one × 2 EDO 1,2-ETHANEDIOL × 4	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION, HANGING DROP；pH 7；293 K；1.8 M (NH4)2SO4, 0.1 M Tris-HCl, pH 7.0, VAPOR DIFFUSION, HANGING DROP, temperature 293K	Resolution 2.00 Å R-free 0.233
5HOU Solution Structure of p53TAD-TAZ1 Deposited 2016-01-19	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 Monomer；Protein × 1 PDB declaration: monomeric	Chain A 340–439（100 aa） Fragment：p53TAD, TAZ1 domain of CBP	Not recorded	ZN ZINC ION × 3	SOLUTION NMR NMR measurement conditions pH 6.8；308 K；Ionic strength (raw mmCIF value) 50；Pressure 1 NMR measurement conditions pH 6.4；308 K；Ionic strength (raw mmCIF value) 50；Pressure 1 NMR sample composition 1.0 mM [U-15N] p53TAD - [NA] TAZ1 p53TAD-TAZ1 fusion protein, 20 mM TRIS, 50 mM sodium chloride, 2 mM DTT, 5 % [U-2H] D2O, 95% H2O, 5% D2O \| 95% H2O/5% D2O NMR sample composition 1.0 mM [U-15N][U-13C] p53TAD - [NA] TAZ1 p53TAD-TAZ1 fusion protein, 20 mM [U-2H] TRIS, 50 mM sodium chloride, 2 mM [U-2H] DTT, 99 % [U-2H] D2O, 99% D2O, 1% H2O \| 99% D2O, 1% H2O NMR sample composition 1.0 mM [NA] p53TAD - [U-15N] TAZ1 p53TAD-TAZ1 fusion protein, 20 mM TRIS, 50 mM sodium chloride, 2 mM DTT, 5 % [U-2H] D2O, 95% H2O/5% D2O \| 95% H2O/5% D2O NMR sample composition 1.0 mM [NA] p53TAD - [U-15N][U-13C] TAZ1 p53TAD-TAZ1 fusion protein, 20 mM [U-2H] TRIS, 50 mM sodium chloride, 2 mM [U-2H] DTT, 99 % [U-2H] D2O, 99% D2O, 1% H2O \| 99% D2O, 1% H2O NMR sample composition 1.0 mM [U-15N][U-13C] p53TAD - [NA] TAZ1 p53TAD-TAZ1 fusion protein, 20 mM TRIS, 50 mM sodium chloride, 2 mM DTT, 5 % [U-2H] D2O, 95% H2O/5% D2O \| 95% H2O/5% D2O NMR sample composition 1 mM [NA] p53TAD - [U-15N][U-13C] TAZ1 p53TAD-TAZ1 fusion protein, 20 mM TRIS, 50 mM sodium chloride, 2 mM DTT, 5 % [U-2H] D2O, 95% H2O/5% D2O \| 95% H2O/5% D2O	Resolution not provided
5HP0 Solution Structure of TAZ2-p53AD2 Deposited 2016-01-19	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 Monomer；Protein × 1 PDB declaration: monomeric	Chain A 1764–1855（92 aa） Fragment：p53AD2, TAZ2 domain of CBP	Not recorded	ZN ZINC ION × 3	SOLUTION NMR NMR measurement conditions pH 6.8；305 K；Ionic strength (raw mmCIF value) 50；Pressure 1 NMR measurement conditions pH 6.4；305 K；Ionic strength (raw mmCIF value) 50；Pressure 1 NMR sample composition 1 mM [U-13C; U-15N] TAZ2-p53AD2, 20 mM TRIS, 50 mM sodium chloride, 2 mM DTT, 10 % [U-2H] D2O, 90% H2O/10% D2O \| 90% H2O/10% D2O NMR sample composition 1 mM [U-13C; U-15N] TAZ2-p53AD2, 20 mM [U-2H] TRIS, 50 mM sodium chloride, 2 mM [U-2H] DTT, 99 % [U-2H] D2O, 99% D2O, 1% H2O \| 99% D2O, 1% H2O NMR sample composition 1 mM [U-13C; U-15N] TAZ2-p53AD2, 20 mM TRIS, 50 mM sodium chloride, 2 mM DTT, 5 % [U-2H] D2O, 90% H2O/10% D2O \| 90% H2O/10% D2O NMR sample composition 1 mM [U-13C] TAZ2, 1 mM p53AD2(38-61), 20 mM [U-2H] TRIS, 50 mM sodium chloride, 2 mM [U-2H] DTT, 5 % [U-2H] D2O, 99% D2O, 1% H2O \| 99% D2O, 1% H2O NMR sample composition 1 mM [U-13C] p53AD2, 1 mM TAZ2, 20 mM [U-2H] TRIS, 50 mM sodium chloride, 2 mM [U-2H] DTT, 99 % [U-2H] D2O, 99% D2O, 1% H2O \| 99% D2O, 1% H2O	Resolution not provided
5HPD Solution Structure of TAZ2-p53TAD Deposited 2016-01-20	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 Monomer；Protein × 1 PDB declaration: monomeric	Chain A 1764–1855（92 aa） Fragment：p53TAD, TAZ2 domain of CBP	Not recorded	ZN ZINC ION × 3	SOLUTION NMR NMR measurement conditions pH 6.8；305 K；Ionic strength (raw mmCIF value) 50；Pressure 1 NMR measurement conditions pH 6.4；305 K；Ionic strength (raw mmCIF value) 50；Pressure 1 NMR sample composition 1.75 mM [U-13C; U-15N] TAZ2-p53TAD, 20 mM TRIS, 50 mM sodium chloride, 1 mM DTT, 10 % [U-2H] D2O, 90% H2O/10% D2O \| 90% H2O/10% D2O NMR sample composition 1.75 mM [U-13C; U-15N] TAZ2-p53TAD, 20 mM [U-2H] TRIS, 50 mM sodium chloride, 1 mM [U-2H] DTT, 99 % [U-2H] D2O, 99% D2O, 1% H2O \| 99% D2O, 1% H2O NMR sample composition 1 mM [U-13C] TAZ2, 1 mM p53(13-37, 1 mM p53(38-61), 50 mM sodium chloride, 2 mM [U-2H] DTT, 99 % [U-2H] D2O, 20 mM [U-2H] TRIS, 99% D2O, 1% H2O \| 99% D2O, 1% H2O NMR sample composition 1 mM TAZ2, 1 mM [U-13C] p53(13-37), 1 mM [U-13C] p53(38-61), 20 mM [U-2H] TRIS, 50 mM sodium chloride, 2 mM [U-2H] DTT, 99 % [U-2H] D2O, 99% D2O, 1% H2O \| 99% D2O, 1% H2O NMR sample composition 1 mM TAZ2, 1 mM [U-15N] p53(13-61), 20 mM TRIS, 50 mM sodium chloride, 2 mM DTT, 10 % [U-2H] D2O, 90% H2O/10% D2O \| 90% H2O/10% D2O NMR sample composition 1 mM [U-15N] TAZ2, 1 mM p53(13-61), 20 mM TRIS, 50 mM sodium chloride, 2 mM DTT, 10 % [U-2H] D2O, 90% H2O/10% D2O \| 90% H2O/10% D2O NMR sample composition 1 mM TAZ2, 1 mM [U-13C] p53(13-61), 20 mM [U-2H] TRIS, 50 mM sodium chloride, 2 mM [U-2H] DTT, 99 % [U-2H] D2O, 99% D2O, 1% H2O \| 99% D2O, 1% H2O NMR sample composition 1 mM [U-13C] TAZ2, 1 mM p53(13-61), 20 mM [U-2H] TRIS, 50 mM sodium chloride, 2 mM [U-2H] DTT, 99 % [U-2H] D2O, 99% D2O, 1% H2O \| 99% D2O, 1% H2O	Resolution not provided
5W0I CREBBP Bromodomain in complex with Cpd8 (1-(3-(7-(difluoromethyl)-6-(1-methyl-1H-pyrazol-4-yl)-3,4-dihydroquinolin-1(2H)-yl)-1-(tetrahydrofuran-3-yl)-1,4,6,7-tetrahydro-5H-pyrazolo[4,3-c]pyridin-5-yl)ethan-1-one) Deposited 2017-05-30	Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental conditions Different structure-quality metrics	Assembly 1 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric	Chain A 1083–1198（116 aa） Fragment：Bromodomain, UNP residues 1083-1198	Not recorded	9UA 1-{3-[7-(difluoromethyl)-6-(1-methyl-1H-pyrazol-4-yl)-3,4-dihydroquinolin-1(2H)-yl]-1-[(3S)-oxolan-3-yl]-1,4,6,7-tetrahydro-5H-pyrazolo[4,3-c]pyridin-5-yl}ethan-1-one × 1 DMS DIMETHYL SULFOXIDE × 2 GOL GLYCEROL × 1	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION；pH 6.5；277 K；0.2 M Li2SO4, 0.1M Bis-Tris pH 6.5, 23% PEG33500	Resolution 1.43 Å R-free 0.192
6DNQ HBZ77 in complex with KIX and c-Myb Deposited 2018-06-07	Different construct Different ligand/ion Different experimental conditions Different structure-quality metrics	Assembly 1 Protein heterocomplex Heteromer；Protein × 5 PDB declaration: pentameric	Chain B 586–672（87 aa） Fragment：residues 586-672 Chain D 586–672（87 aa） Fragment：residues 586-672	Not recorded	EDO 1,2-ETHANEDIOL × 1	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION, SITTING DROP；293 K；PEG 3350, calcium chloride	Resolution 2.35 Å R-free 0.229
7LVS The CBP TAZ1 Domain in Complex with a CITED2-HIF-1-Alpha Fusion Peptide Deposited 2021-02-26	Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental conditions Different structure-quality metrics	Assembly 1 Insufficient information Heteromer；Protein × 2 PDB declaration: dimeric	Chain B 340–439（100 aa）	Not recorded	ZN ZINC ION × 3	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION, SITTING DROP；293 K；0.1 M HEPES pH 6.87, 28% PEG 4000	Resolution 2.02 Å R-free 0.241

23 other PDB entries and 24 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence

UniProt name	CBP_MOUSE
Isoform	—
PDB entities	3
Chains and sequence ranges	Author chain B； PDBConstruct 2–88； UniProt 586–672 Author chain D； PDBConstruct 2–88； UniProt 586–672 Author chain G； PDBConstruct 2–88； UniProt 586–672 Author chain I； PDBConstruct 2–88； UniProt 586–672

The page prioritizes protein identity, the current assembly, associated components, oligomeric state and cross-PDB links. Chain mapping and sequence ranges are retained as data evidence. Internal IDs, import timestamps and assembly operation expressions are maintenance fields and are not shown here.

▼

2. Structure Basics 2. Structure Basics

Entry ID entry_id	6dmx
Deposition date deposition_date	2018-06-05
Structure title title	HBZ56 in complex with KIX and c-Myb
Keywords keywords	transcription coactivator, transcription factor, viral, eukaryotic, complex, TRANSCRIPTION; TRANSCRIPTION
Experimental Method method	X-RAY DIFFRACTION

▼

3. SAXS Parameters (CRYSOL theoretical calculation) 3. SAXS Parameters (CRYSOL)

Radius of gyration Rg (Guinier) rg_guinier	31.12 Å
Radius of gyration Rg (electron density) rg_electron	30.58 Å
Forward intensity I(0) i0	58500300.00
Molecular weight molecular_weight	59490.0 kDa
Excluded volume excluded_volume	74425 Å³
Envelope volume envelope_volume	102500 Å³
Hydration-shell volume shell_volume	29833 Å³
Envelope diameter envelope_diameter	117.6 Å
Shell Rg shell_rg	35.13 Å
Envelope Rg envelope_rg	30.45 Å
Shape Rg shape_rg	30.60 Å
Total Rg total_rg	30.94 Å
Total atoms total_atoms	4187
Residues n_residues	506
Spherical-harmonic order n_harmonics	20
q range q_range	— – 0.5000 Å⁻¹
Data points n_points	101
Shell type shell_type	directional
Solvent electron density solvent_density	0.3340 e/Å³
Shell contrast contrast_shell	0.0300 e/Å³
CRYSOL version crysol_version	4.1.3

▼

4. P(r) Distance Distribution (GNOM inversion) 4. P(r) Analysis (GNOM)

Maximum dimension Dmax dmax	110.2 Å
Rg (real space) rg_real	31.24 Å
Rg uncertainty (real space) rg_real_error	1.04 Å
I(0) (real space) i0_real	5.8500e+07
I(0) uncertainty (real space) i0_real_error	8.6920e+05
Rg (reciprocal space) rg_reciprocal	31.19 Å
I(0) (reciprocal space) i0_reciprocal	58500000.0000
Solution quality estimate total_estimate	0.6586
Solution quality rating solution_quality	REASONABLE a REASONABLE solution
P(r) peaks n_peaks	2
Primary peak position r_peak_primary	34.6 Å
Skewness Skewness skewness	0.428
Kurtosis Kurtosis kurtosis	-0.160
Angular range angular_range	— – 0.2550 Å⁻¹
Current regularization parameter α current_alpha	0.0000
Highest regularization parameter α highest_alpha	7298000.0000
Real-space data points n_real_points	52
GNOM version gnom_version	4.1.3
Quality Criteria quality_criteria	AN1: 0.000; Oscil: 0.804; Stabil: 1.000; Sysdev: 0.115; Positv: 1.000; Valcen: 0.829; Smooth: 0.971

▶

5. Crystallography and Experiment 5. Crystallography & Experiment

▶

6. Entities and Polymers Entities & Polymers (3)

Entity 1 Entity 1 polymer

Description description	BZIP factor
Molecular weight formula_weight	6300.0 kDa
Mutation mutation	C9A, C14A
Source method src_method	man
Copy count entity_count	2

Polymer Polymer

Polymer type type	polypeptide(L)
Chain IDs strand_id	E,J
Atom count atom_count	4187

GSHMASGLFRALPVSAPEDLLVEELVDGLLSLEEELKDKEEEKAVLDGLLSLEEESRG

来源 Source

来源生物 organism	Human T-lymphotropic virus 1
NCBI Class编号 ncbi_taxonomy_id	11908
宿主生物 host_organism	Escherichia coli

Entity 2 Entity 2 polymer

Description description	Transcriptional activator Myb
Molecular weight formula_weight	3810.3 kDa
Source method src_method	man
Copy count entity_count	4

Polymer Polymer

Polymer type type	polypeptide(L)
Chain IDs strand_id	C,A,H,F

YNDEDPEKEKRIKELELLLMSTENELKGQQAL

来源 Source

来源生物 organism	Mus musculus
通用名 common_name	Mouse
NCBI Class编号 ncbi_taxonomy_id	10090
宿主生物 host_organism	Escherichia coli

Entity 3 Entity 3 polymer

Description description	CREB-binding protein
Molecular weight formula_weight	10485.1 kDa
EC 编号 ec_number	2.3.1.48
Source method src_method	man
Copy count entity_count	4

Polymer Polymer

Polymer type type	polypeptide(L)
Chain IDs strand_id	D,B,I,G

MGVRKGWHEHVTQDLRSHLVHKLVQAIFPTPDPAALKDRRMENLVAYAKKVEGDMYESANSRDEYYHLLAEKIYKIQKELEEKRRSRL

来源 Source

来源生物 organism	Mus musculus
通用名 common_name	Mouse
NCBI Class编号 ncbi_taxonomy_id	10090
宿主生物 host_organism	Escherichia coli

▼

7. Fold Classification (SCOP + CATH) 8 domains

SCOP 2.08 (4 domains)

Domain ID domain_id	d6dmxb_
Class class	a — All alpha proteins
Fold Fold fold	a.12 — Kix domain of CBP (creb binding protein)
Superfamily Superfamily superfamily	a.12.1 — Kix domain of CBP (creb binding protein)
Family Family family	a.12.1.1 — Kix domain of CBP (creb binding protein)

Domain ID domain_id	d6dmxd_
Class class	a — All alpha proteins
Fold Fold fold	a.12 — Kix domain of CBP (creb binding protein)
Superfamily Superfamily superfamily	a.12.1 — Kix domain of CBP (creb binding protein)
Family Family family	a.12.1.1 — Kix domain of CBP (creb binding protein)

Domain ID domain_id	d6dmxg_
Class class	a — All alpha proteins
Fold Fold fold	a.12 — Kix domain of CBP (creb binding protein)
Superfamily Superfamily superfamily	a.12.1 — Kix domain of CBP (creb binding protein)
Family Family family	a.12.1.1 — Kix domain of CBP (creb binding protein)

Domain ID domain_id	d6dmxi_
Class class	a — All alpha proteins
Fold Fold fold	a.12 — Kix domain of CBP (creb binding protein)
Superfamily Superfamily superfamily	a.12.1 — Kix domain of CBP (creb binding protein)
Family Family family	a.12.1.1 — Kix domain of CBP (creb binding protein)

CATH v4.4 (4 domains)

Domain ID domain_id	6dmxB00
Class class	1 — Mainly Alpha
Architecture architecture	10 — Orthogonal Bundle
Topology topology	246 — Serum Albumin; Chain A, Domain 1
Homologous superfamily homologous superfamily	20 — Coactivator CBP, KIX domain

Domain ID domain_id	6dmxD00
Class class	1 — Mainly Alpha
Architecture architecture	10 — Orthogonal Bundle
Topology topology	246 — Serum Albumin; Chain A, Domain 1
Homologous superfamily homologous superfamily	20 — Coactivator CBP, KIX domain

Domain ID domain_id	6dmxG00
Class class	1 — Mainly Alpha
Architecture architecture	10 — Orthogonal Bundle
Topology topology	246 — Serum Albumin; Chain A, Domain 1
Homologous superfamily homologous superfamily	20 — Coactivator CBP, KIX domain

Domain ID domain_id	6dmxI00
Class class	1 — Mainly Alpha
Architecture architecture	10 — Orthogonal Bundle
Topology topology	246 — Serum Albumin; Chain A, Domain 1
Homologous superfamily homologous superfamily	20 — Coactivator CBP, KIX domain

▶

8. Citations (1)

▶

Unit-cell length a length_a	54.997 Å
Unit-cell length b length_b	80.311 Å
Unit-cell length c length_c	64.641 Å
Unit-cell angle α angle_alpha	90.00 °
Unit-cell angle β angle_beta	92.60 °
Unit-cell angle γ angle_gamma	90.00 °
Molecules per unit cell Z z_pdb	8

Space group space_group	P 1 21 1
Space-group number int_tables_number	4
Crystal system crystal_system	—

Resolution resolution	2.800 Å
Low-resolution limit resolution_low	40.970 Å
R factor r_factor	0.2420
R_work r_work	0.2387
R_free r_free	0.3008

fit	/app/data/saxs_computation/dm/6dmx/6dmx.fit
pddf	/app/data/pr_computation/dm/6dmx/6dmx.pr.out
profile	/app/data/saxs_computation/dm/6dmx/6dmx.dat

HBZ56 in complex with KIX and c-Myb

1. Protein Identity and Related Structures Protein Identity & Related Structures

BZIP factor

State in the Current Structure

Other States of the Same Protein in the Database

Transcriptional activator Myb

State in the Current Structure

Other States of the Same Protein in the Database

CREB-binding protein

State in the Current Structure

Other States of the Same Protein in the Database

SAXS scattering curve SAXS Profile

P(r) Distance Distribution P(r) Distribution

2. Structure Basics 2. Structure Basics

3. SAXS Parameters (CRYSOL theoretical calculation) 3. SAXS Parameters (CRYSOL)

4. P(r) Distance Distribution (GNOM inversion) 4. P(r) Analysis (GNOM)

5. Crystallography and Experiment 5. Crystallography & Experiment

Unit cell Unit Cell

Symmetry Symmetry

Refinement Refinement

Diffraction experiment Diffraction

6. Entities and Polymers Entities & Polymers (3)

Entity 1 Entity 1 polymer

Polymer Polymer

来源 Source

Entity 2 Entity 2 polymer

Polymer Polymer

来源 Source

Entity 3 Entity 3 polymer

Polymer Polymer

来源 Source

7. Fold Classification (SCOP + CATH) 8 domains

SCOP 2.08 (4 domains)

CATH v4.4 (4 domains)

8. Citations (1)

9. Files and Curves (10)

Files (7)

Curves (3)