SAXSdb — 1mv0

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

Myc proto-oncogene protein

Homo sapiens

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 × 2 PDB declaration: dimeric（2） Consistent with protein copy count	Chain A； UniProt 55–68	Fragment：residues 55-68	Myc box-dependent-interacting protein 1 × 1 （O00499）	SOLUTION NMR NMR measurement conditions：pH 6.5；298 K；Ionic strength (raw mmCIF value) 300e-3；Pressure ambient NMR sample composition：1.4 mM Bin1(402-482)/c-Myc(55-68) U-15N, 13C, 25 mM sodium phosphate, 150 mM NaCl, 1 mM DTT, 95% H2O, 5% D2O pH=6.5 \| 95% H2O/5% D2O	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 1MV0	Assembly / Oligomeric State	Construct	Mutations and Modifications	Ligands, Ions and Non-polymers	Method and Experimental Conditions	Structure Quality
1A93 NMR SOLUTION STRUCTURE OF THE C-MYC-MAX HETERODIMERIC LEUCINE ZIPPER, NMR, MINIMIZED AVERAGE STRUCTURE Deposited 1998-04-15	Different construct Different mutation/modification Different experimental conditions	Assembly 1 Protein heterocomplex Heteromer；Protein × 2 PDB declaration: dimeric	Chain A 406–434（29 aa） Fragment：HETERODIMERIC LEUCINE ZIPPER	Non-standard monomer：Yes (specific site not provided by mmCIF)	No recorded non-water small molecule	SOLUTION NMR NMR measurement conditions pH 4.8；298 K；Ionic strength (raw mmCIF value) 10mM；Pressure 1 NMR sample composition WATER	Resolution not provided
1EE4 CRYSTAL STRUCTURE OF YEAST KARYOPHERIN (IMPORTIN) ALPHA IN A COMPLEX WITH A C-MYC NLS PEPTIDE Deposited 2000-01-30	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 C 320–328（9 aa） Fragment：NLS (NUCLEAR LOCALIZATION SIGNAL) AT THE LARGER (FUNCTIONAL) BINDING SITE Chain D 320–328（9 aa） Fragment：NLS (NUCLEAR LOCALIZATION SIGNAL) AT THE LARGER (FUNCTIONAL) BINDING SITE	Not recorded	No recorded non-water small molecule	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION, HANGING DROP；pH 8.5；298 K；pH 8.5, VAPOR DIFFUSION, HANGING DROP, temperature 298K	Resolution 2.10 Å R-free 0.277
1EE4 CRYSTAL STRUCTURE OF YEAST KARYOPHERIN (IMPORTIN) ALPHA IN A COMPLEX WITH A C-MYC NLS PEPTIDE Deposited 2000-01-30	Different construct Different mutation/modification Different oligomeric state Different experimental method Different experimental conditions Different structure-quality metrics	Assembly 2 Protein heterocomplex Heteromer；Protein × 3 PDB declaration: trimeric	Chain E 320–328（9 aa） Fragment：NLS (NUCLEAR LOCALIZATION SIGNAL) AT THE LARGER (FUNCTIONAL) BINDING SITE Chain F 320–328（9 aa） Fragment：NLS (NUCLEAR LOCALIZATION SIGNAL) AT THE LARGER (FUNCTIONAL) BINDING SITE	Not recorded	No recorded non-water small molecule	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION, HANGING DROP；pH 8.5；298 K；pH 8.5, VAPOR DIFFUSION, HANGING DROP, temperature 298K	Resolution 2.10 Å R-free 0.277
1NKP Crystal structure of Myc-Max recognizing DNA Deposited 2003-01-03	Different construct Different oligomeric state Different experimental method Different experimental conditions Different structure-quality metrics	Assembly 1 Protein–DNA Heteromer；Protein × 2 PDB declaration: tetrameric	Chain A 353–434（82 aa） Fragment：bHLHZ region	Not recorded	No recorded non-water small molecule	X-RAY DIFFRACTION mmCIF provides none of the parsed conditions	Resolution 1.80 Å R-free 0.263
1NKP Crystal structure of Myc-Max recognizing DNA Deposited 2003-01-03	Different construct Different oligomeric state Different experimental method Different experimental conditions Different structure-quality metrics	Assembly 2 Protein–DNA Heteromer；Protein × 2 PDB declaration: tetrameric	Chain D 353–434（82 aa） Fragment：bHLHZ region	Not recorded	No recorded non-water small molecule	X-RAY DIFFRACTION mmCIF provides none of the parsed conditions	Resolution 1.80 Å R-free 0.263
2A93 NMR SOLUTION STRUCTURE OF THE C-MYC-MAX HETERODIMERIC LEUCINE ZIPPER, 40 STRUCTURES Deposited 1998-06-09	Different construct Different mutation/modification Different experimental conditions	Assembly 1 Protein heterocomplex Heteromer；Protein × 2 PDB declaration: dimeric	Chain A 406–434（29 aa） Fragment：LEUCINE ZIPPER	Non-standard monomer：Yes (specific site not provided by mmCIF)	No recorded non-water small molecule	SOLUTION NMR NMR measurement conditions pH 4.8；298 K；Ionic strength (raw mmCIF value) 100 mM；Pressure 1 NMR sample composition WATER	Resolution not provided
5I4Z Structure of apo OmoMYC Deposited 2016-02-13	Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental method Different experimental conditions Different structure-quality metrics	Assembly 1 Protein homooligomer Homooligomer；Protein × 2 PDB declaration: dimeric	Chain A 348–439（92 aa） Fragment：OmoMYC, UNP Residues 348-439 Chain B 348–439（92 aa） Fragment：OmoMYC, UNP Residues 348-439	Not recorded	GOL GLYCEROL × 3 CL CHLORIDE ION × 3 K POTASSIUM ION × 2	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION, SITTING DROP；pH 6；293.15 K；MES, potassium sodium tartrate	Resolution 1.95 Å R-free 0.194
5I50 Structure of OmoMYC bound to double-stranded DNA Deposited 2016-02-13	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 A 350–439（90 aa） Fragment：OmoMYC, UNP Residues 350-439 Chain B 350–439（90 aa） Fragment：OmoMYC, UNP Residues 350-439	Not recorded	No recorded non-water small molecule	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION, SITTING DROP；pH 5.6；293.15 K；MES, magnesium sulfate, potassium chloride, PEG 400	Resolution 2.70 Å R-free 0.279
6E16 Ternary structure of c-Myc-TBP-TAF1 Deposited 2018-07-09	Different construct Different oligomeric state Different experimental method Different experimental conditions Different structure-quality metrics	Assembly 1 Insufficient information Monomer；Protein × 1 PDB declaration: monomeric	Chain A 96–125（30 aa）	Not recorded	No recorded non-water small molecule	X-RAY DIFFRACTION X-ray crystallization conditions BATCH MODE；291 K；20% (w/w) PEG8000, 0.2M ammonium sulfare, and 0.1M HEPES pH7.5	Resolution 2.40 Å R-free 0.220
6E24 Ternary structure of c-Myc-TBP-TAF1 Deposited 2018-07-10	Different construct Different oligomeric state Different experimental method Different experimental conditions Different structure-quality metrics	Assembly 1 Insufficient information Monomer；Protein × 1 PDB declaration: monomeric	Chain A 96–125（30 aa）	Not recorded	No recorded non-water small molecule	X-RAY DIFFRACTION X-ray crystallization conditions EVAPORATION；293 K；16% W/V PEG3350 0.05M CITRIC ACID 0.05M BIS-TRIS PROPANE pH5.0	Resolution 3.00 Å R-free 0.224
6G6J The crystal structures of Human MYC:MAX bHLHZip complex Deposited 2018-04-01	Different construct 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 351–437（87 aa）	Not recorded	SO4 SULFATE ION × 4	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION, SITTING DROP；pH 7；277 K；20% (w/v) PEG 3350 0.2M sodium sulfate decahydrate, pH 7	Resolution 2.25 Å R-free 0.236
6G6J The crystal structures of Human MYC:MAX bHLHZip complex Deposited 2018-04-01	Different construct Different ligand/ion Different experimental method Different experimental conditions Different structure-quality metrics	Assembly 2 Protein heterocomplex Heteromer；Protein × 2 PDB declaration: dimeric	Chain C 351–437（87 aa）	Not recorded	SO4 SULFATE ION × 2	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION, SITTING DROP；pH 7；277 K；20% (w/v) PEG 3350 0.2M sodium sulfate decahydrate, pH 7	Resolution 2.25 Å R-free 0.236
6G6K The crystal structures of Human MYC:MAX bHLHZip complex Deposited 2018-04-01	Different construct 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 351–437（87 aa）	Not recorded	CL CHLORIDE ION × 1	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION, SITTING DROP；pH 7.5；277 K；10% w/v PEG 8000, 20% v/v ethylene glycol, 0.075 %(w/v) of each Additive, 5 %(v/v) EtOH, 0.1 M MOPS/HEPES-Na, pH 7.5, Additive: 0.75 %(w/v) menthol, 0.75 %(w/v) caffeic acid, 0.75 %(w/v) D-quinic acid, 0.75 %(w/v) shikimic acid, 0.75 %(w/v) gallic acid monohydrate, 0.75 %(w/v) N-vanillylnonanamide.	Resolution 1.35 Å R-free 0.203
6G6K The crystal structures of Human MYC:MAX bHLHZip complex Deposited 2018-04-01	Different construct Different ligand/ion Different experimental method Different experimental conditions Different structure-quality metrics	Assembly 2 Protein heterocomplex Heteromer；Protein × 2 PDB declaration: dimeric	Chain C 351–437（87 aa）	Not recorded	CL CHLORIDE ION × 1	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION, SITTING DROP；pH 7.5；277 K；10% w/v PEG 8000, 20% v/v ethylene glycol, 0.075 %(w/v) of each Additive, 5 %(v/v) EtOH, 0.1 M MOPS/HEPES-Na, pH 7.5, Additive: 0.75 %(w/v) menthol, 0.75 %(w/v) caffeic acid, 0.75 %(w/v) D-quinic acid, 0.75 %(w/v) shikimic acid, 0.75 %(w/v) gallic acid monohydrate, 0.75 %(w/v) N-vanillylnonanamide.	Resolution 1.35 Å R-free 0.203
6G6L The crystal structures of Human MYC:MAX bHLHZip complex Deposited 2018-04-01	Different construct 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 351–437（87 aa）	Not recorded	SO4 SULFATE ION × 4	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION, SITTING DROP；277 K；10% w/v PEG 8000, 20% v/v ethylene glycol, 15% PEG 8000 15, 0.2M ammonium sulfate, pH 7	Resolution 2.20 Å R-free 0.268
6G6L The crystal structures of Human MYC:MAX bHLHZip complex Deposited 2018-04-01	Different construct Different ligand/ion Different experimental method Different experimental conditions Different structure-quality metrics	Assembly 2 Protein heterocomplex Heteromer；Protein × 2 PDB declaration: dimeric	Chain C 351–437（87 aa）	Not recorded	SO4 SULFATE ION × 3	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION, SITTING DROP；277 K；10% w/v PEG 8000, 20% v/v ethylene glycol, 15% PEG 8000 15, 0.2M ammonium sulfate, pH 7	Resolution 2.20 Å R-free 0.268
6G6L The crystal structures of Human MYC:MAX bHLHZip complex Deposited 2018-04-01	Different construct Different ligand/ion Different experimental method Different experimental conditions Different structure-quality metrics	Assembly 3 Protein heterocomplex Heteromer；Protein × 2 PDB declaration: dimeric	Chain E 351–437（87 aa）	Not recorded	SO4 SULFATE ION × 3	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION, SITTING DROP；277 K；10% w/v PEG 8000, 20% v/v ethylene glycol, 15% PEG 8000 15, 0.2M ammonium sulfate, pH 7	Resolution 2.20 Å R-free 0.268
6G6L The crystal structures of Human MYC:MAX bHLHZip complex Deposited 2018-04-01	Different construct Different ligand/ion Different experimental method Different experimental conditions Different structure-quality metrics	Assembly 4 Protein heterocomplex Heteromer；Protein × 2 PDB declaration: dimeric	Chain G 351–437（87 aa）	Not recorded	SO4 SULFATE ION × 4	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION, SITTING DROP；277 K；10% w/v PEG 8000, 20% v/v ethylene glycol, 15% PEG 8000 15, 0.2M ammonium sulfate, pH 7	Resolution 2.20 Å R-free 0.268
8J2Q Crystal structure of Cypovirus Polyhedra mutant fused with c-Myc fragment Deposited 2023-04-15	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 417–427（11 aa）	Not recorded	No recorded non-water small molecule	X-RAY DIFFRACTION X-ray crystallization conditions SMALL TUBES；293 K；cell-free crystallization	Resolution 1.92 Å R-free 0.245
8OTS OCT4 and MYC-MAX co-bound to a nucleosome Deposited 2023-04-21	Different construct Different oligomeric state Different ligand/ion Different experimental method Different experimental conditions Different structure-quality metrics	Assembly 1 Insufficient information Heteromer；Protein × 11 PDB declaration: tridecameric	Chain M 351–437（87 aa）	Not recorded	PTD PENTANEDIAL × 8	ELECTRON MICROSCOPY cryo-EM buffer pH 7.2 cryo-EM vitrification conditions Cryogen ETHANE	Resolution 3.30 Å
8OTT MYC-MAX bound to a nucleosome at SHL+5.8 Deposited 2023-04-21	Different construct Different oligomeric state Different ligand/ion Different experimental method Different experimental conditions Different structure-quality metrics	Assembly 1 Protein–DNA Heteromer；Protein × 10 PDB declaration: dodecameric	Chain M 368–420（53 aa）	Not recorded	PTD PENTANEDIAL × 8	ELECTRON MICROSCOPY cryo-EM buffer pH 7.2 cryo-EM vitrification conditions Cryogen ETHANE	Resolution 3.30 Å
8WLG Crystal structure of Cypovirus Polyhedra mutant fused with c-Myc fragment Deposited 2023-09-29	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 417–426（10 aa）	Not recorded	No recorded non-water small molecule	X-RAY DIFFRACTION X-ray crystallization conditions SMALL TUBES；293 K；cell-free crystallization	Resolution 2.55 Å R-free 0.270
8X8S Crystal structure of Cypovirus Polyhedra mutant fused with c-Myc fragment Deposited 2023-11-28	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 417–427（11 aa）	Mutation：R151K	No recorded non-water small molecule	X-RAY DIFFRACTION X-ray crystallization conditions SMALL TUBES；293 K；cell-free crystallization	Resolution 2.04 Å R-free 0.265
8X8V Crystal structure of Cypovirus Polyhedra mutant fused with c-Myc fragment Deposited 2023-11-29	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 417–427（11 aa）	Mutation：R151K	No recorded non-water small molecule	X-RAY DIFFRACTION X-ray crystallization conditions SMALL TUBES；293 K；cell-free crystallization	Resolution 2.00 Å R-free 0.251
9QNH Myc pS294 phosphopeptide binding to 14-3-3sigma Deposited 2025-03-25	Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental method Different experimental conditions Different structure-quality metrics	Assembly 1 Protein heterocomplex Heteromer；Protein × 4 PDB declaration: tetrameric	Chain P 290–298（9 aa）	Non-standard monomer：Yes (specific site not provided by mmCIF)	CL CHLORIDE ION × 2 CA CALCIUM ION × 14	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION, SITTING DROP；277 K；0.095 M HEPES pH=7.1-7.7 0.19 M CaCl2 5% glycerol 24-29% PEG400	Resolution 1.30 Å R-free 0.167

18 other PDB entries and 25 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence

UniProt name	MYC_HUMAN
Isoform	—
PDB entities	1
Chains and sequence ranges	Author chain A； PDBConstruct 1–14； UniProt 55–68

Myc box-dependent-interacting protein 1

Homo sapiens

UniProt O00499

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 × 2 PDB declaration: dimeric（2） Consistent with protein copy count	Chain B； UniProt 513–593	Fragment：residues 513-593	Myc proto-oncogene protein × 1 （P01106）	SOLUTION NMR NMR measurement conditions：pH 6.5；298 K；Ionic strength (raw mmCIF value) 300e-3；Pressure ambient NMR sample composition：1.4 mM Bin1(402-482)/c-Myc(55-68) U-15N, 13C, 25 mM sodium phosphate, 150 mM NaCl, 1 mM DTT, 95% H2O, 5% D2O pH=6.5 \| 95% H2O/5% D2O	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 1MV0	Assembly / Oligomeric State	Construct	Mutations and Modifications	Ligands, Ions and Non-polymers	Method and Experimental Conditions	Structure Quality
1MUZ NMR STRUCTURE OF THE TUMOR SUPPRESSOR BIN1: ALTERNATIVE SPLICING IN MELANOMA AND INTERACTION WITH C-MYC Deposited 2002-09-24	Different oligomeric state Different experimental conditions	Assembly 1 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric	Chain A 513–593（81 aa） Fragment：residues 513-593	Not recorded	No recorded non-water small molecule	SOLUTION NMR NMR measurement conditions pH 6.5；298 K；Ionic strength (raw mmCIF value) 300e-3；Pressure ambient NMR sample composition 1.5 mM Bin1(402-482) U-15N, 13C 25 mM sodium phosphate buffer, 150 mM NaCl, 1 mM DTT, 95% H2O, 5% D2O pH=6.5 \| 95% H2O/5% D2O	Resolution not provided
1MV3 NMR STRUCTURE OF THE TUMOR SUPPRESSOR BIN1: ALTERNATIVE SPLICING IN MELANOMA AND INTERACTION WITH C-MYC Deposited 2002-09-24	Different construct Different mutation/modification Different oligomeric state Different experimental conditions	Assembly 1 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric	Chain A 301–377（77 aa） Fragment：isoform BIN1+12A (residues 301-377, 458-594) Chain A 458–593（136 aa） Fragment：isoform BIN1+12A (residues 301-377, 458-594)	Not recorded	No recorded non-water small molecule	SOLUTION NMR NMR measurement conditions pH 6.5；298 K；Ionic strength (raw mmCIF value) 300e-3；Pressure ambient NMR sample composition 1.3 mM Bin1(270-482,+12A) U-15N, 13C, 25 mM sodium phosphate, 150 mM NaCl, 1 mM DTT, 95 % H2O, 5% D2O \| 95% H2O/5% D2O	Resolution not provided
2FIC The crystal structure of the BAR domain from human Bin1/Amphiphysin II and its implications for molecular recognition Deposited 2005-12-29	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 1–241（241 aa） Fragment：BAR domain Chain B 1–241（241 aa） Fragment：BAR domain	Not recorded	XE XENON × 2	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION, HANGING DROP；pH 8；298 K；20% monomethylether-PEG550, 100mM Tris (pH 8), 100mM NaCl, pH 8.0, VAPOR DIFFUSION, HANGING DROP, temperature 298K	Resolution 1.99 Å R-free 0.280
2FIC The crystal structure of the BAR domain from human Bin1/Amphiphysin II and its implications for molecular recognition Deposited 2005-12-29	Different construct Different oligomeric state Different ligand/ion Different experimental method Different experimental conditions Different structure-quality metrics	Assembly 2 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric	Chain A 1–241（241 aa） Fragment：BAR domain	Not recorded	XE XENON × 1	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION, HANGING DROP；pH 8；298 K；20% monomethylether-PEG550, 100mM Tris (pH 8), 100mM NaCl, pH 8.0, VAPOR DIFFUSION, HANGING DROP, temperature 298K	Resolution 1.99 Å R-free 0.280
2FIC The crystal structure of the BAR domain from human Bin1/Amphiphysin II and its implications for molecular recognition Deposited 2005-12-29	Different construct Different oligomeric state Different ligand/ion Different experimental method Different experimental conditions Different structure-quality metrics	Assembly 3 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric	Chain B 1–241（241 aa） Fragment：BAR domain	Not recorded	XE XENON × 1	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION, HANGING DROP；pH 8；298 K；20% monomethylether-PEG550, 100mM Tris (pH 8), 100mM NaCl, pH 8.0, VAPOR DIFFUSION, HANGING DROP, temperature 298K	Resolution 1.99 Å R-free 0.280
2RMY Structure of the N-terminal BARpeptide in SDS micelles Deposited 2007-12-03	Different construct Different oligomeric state Different experimental conditions	Assembly 1 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric	Chain A 1–33（33 aa） Fragment：UNP residues 1-33	Not recorded	No recorded non-water small molecule	SOLUTION NMR NMR measurement conditions pH 7.4；298 K；Ionic strength (raw mmCIF value) 0；Pressure ambient NMR sample composition 1mM [U-100% 15N] protein, 90% H2O/10% D2O \| 90% H2O/10% D2O	Resolution not provided
2RND Structure of the N-terminal BARpeptide in DPC micelles Deposited 2007-12-16	Different construct Different oligomeric state Different experimental conditions	Assembly 1 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric	Chain A 1–33（33 aa） Fragment：BARpeptide, UNP residues 1-33	Not recorded	No recorded non-water small molecule	SOLUTION NMR NMR measurement conditions pH 7.4；298 K；Ionic strength (raw mmCIF value) 0；Pressure ambient NMR sample composition 1mM [U-100% 15N] protein, 90% H2O/10% D2O \| 90% H2O/10% D2O	Resolution not provided
5I22 Amphiphysin SH3 in complex with Chikungunya virus nsP3 peptide Deposited 2016-02-04	Different construct Different experimental conditions	Assembly 1 Protein heterocomplex Heteromer；Protein × 2 PDB declaration: dimeric	Chain A 513–593（81 aa） Fragment：SH3 fragment, UNP residue 513-593	Not recorded	No recorded non-water small molecule	SOLUTION NMR NMR measurement conditions pH 6.5；298.15 K；Pressure 1 NMR sample composition 0.5 mM [U-13C; U-15N] amphiphysin 2 SH3, 0.5 mM [U-13C; U-15N] CHIKV nsP3 peptide, 90% H2O/10% D2O \| 90% H2O/10% D2O	Resolution not provided

6 other PDB entries and 8 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence

UniProt name	BIN1_HUMAN
Isoform	—
PDB entities	2
Chains and sequence ranges	Author chain B； PDBConstruct 1–81； UniProt 513–593

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.

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2. Structure Basics 2. Structure Basics

Entry ID entry_id	1mv0
Deposition date deposition_date	2002-09-24
Structure title title	NMR STRUCTURE OF THE TUMOR SUPPRESSOR BIN1: ALTERNATIVE SPLICING IN MELANOMA AND INTERACTION WITH C-MYC
Keywords keywords	TUMOR SUPPRESSOR/ONCOPROTEIN, ENDOCYTOSIS/EXOCYTOSIS, TRANSCRIPTION COMPLEX, ENDOCYTOSIS-EXOCYTOSIS; ENDOCYTOSIS/EXOCYTOSIS, TRANSCRIPTION
Experimental Method method	SOLUTION NMR

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

Radius of gyration Rg (Guinier) rg_guinier	16.47 Å
Radius of gyration Rg (electron density) rg_electron	16.30 Å
Forward intensity I(0) i0	661829000.00
Molecular weight molecular_weight	215700.0 kDa
Excluded volume excluded_volume	269450 Å³
Envelope volume envelope_volume	67056 Å³
Hydration-shell volume shell_volume	25881 Å³
Envelope diameter envelope_diameter	76.6 Å
Shell Rg shell_rg	28.95 Å
Envelope Rg envelope_rg	21.62 Å
Shape Rg shape_rg	16.25 Å
Total Rg total_rg	16.84 Å
Total atoms total_atoms	30040
Residues n_residues	1900
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

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

Maximum dimension Dmax dmax	43.6 Å
Rg (real space) rg_real	15.60 Å
Rg uncertainty (real space) rg_real_error	0.05 Å
I(0) (real space) i0_real	6.3000e+08
I(0) uncertainty (real space) i0_real_error	4.7060e+06
Rg (reciprocal space) rg_reciprocal	16.50 Å
I(0) (reciprocal space) i0_reciprocal	661800000.0000
Solution quality estimate total_estimate	0.6829
Solution quality rating solution_quality	REASONABLE a REASONABLE solution
P(r) peaks n_peaks	2
Primary peak position r_peak_primary	19.6 Å
Skewness Skewness skewness	0.236
Kurtosis Kurtosis kurtosis	-0.383
Angular range angular_range	— – 0.4850 Å⁻¹
Current regularization parameter α current_alpha	2.6850
Highest regularization parameter α highest_alpha	5491000.0000
Real-space data points n_real_points	79
GNOM version gnom_version	4.1.3
Quality Criteria quality_criteria	AN1: 0.005; Oscil: 0.979; Stabil: 0.985; Sysdev: 0.000; Positv: 1.000; Valcen: 0.993; Smooth: 0.000

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5. Crystallography and Experiment 5. Crystallography & Experiment

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6. Entities and Polymers Entities & Polymers (2)

Entity 1 Entity 1 polymer

Description description	Myc proto-oncogene protein
Molecular weight formula_weight	1479.7 kDa
Source method src_method	man
Copy count entity_count	1

Polymer Polymer

Polymer type type	polypeptide(L)
Chain IDs strand_id	A
Atom count atom_count	30040

LLPTPPLSPSRRSG

来源 Source

来源生物 organism	Homo sapiens
通用名 common_name	human
NCBI Class编号 ncbi_taxonomy_id	9606
宿主生物 host_organism	Escherichia coli

Entity 2 Entity 2 polymer

Description description	Myc box-dependent-interacting protein 1
Molecular weight formula_weight	9356.5 kDa
Source method src_method	man
Copy count entity_count	1

Polymer Polymer

Polymer type type	polypeptide(L)
Chain IDs strand_id	B

GRLDLPPGFMFKVQAQHDYTATDTDELQLKAGDVVLVIPFQNPEEQDEGWLMGVKESDWNQHKKLEKCRGVFPENFTERVP

来源 Source

来源生物 organism	Homo sapiens
通用名 common_name	human
NCBI Class编号 ncbi_taxonomy_id	9606
宿主生物 host_organism	Escherichia coli

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7. Fold Classification (SCOP + CATH) 2 domains

SCOP 2.08 (1 domains)

Domain ID domain_id	d1mv0b_
Class class	b — All beta proteins
Fold Fold fold	b.34 — SH3-like barrel
Superfamily Superfamily superfamily	b.34.2 — SH3-domain
Family Family family	b.34.2.1 — SH3-domain

CATH v4.4 (1 domains)

Domain ID domain_id	1mv0B00
Class class	2 — Mainly Beta
Architecture architecture	30 — Roll
Topology topology	30 — SH3 type barrels.
Homologous superfamily homologous superfamily	40 — SH3 Domains

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8. Citations (1)

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fit	/app/data/saxs_computation/mv/1mv0/1mv0.fit
pddf	/app/data/pr_computation/mv/1mv0/1mv0.pr.out
profile	/app/data/saxs_computation/mv/1mv0/1mv0.dat

NMR STRUCTURE OF THE TUMOR SUPPRESSOR BIN1: ALTERNATIVE SPLICING IN MELANOMA AND INTERACTION WITH C-MYC

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

Myc proto-oncogene protein

State in the Current Structure

Other States of the Same Protein in the Database

Myc box-dependent-interacting protein 1

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

6. Entities and Polymers Entities & Polymers (2)

Entity 1 Entity 1 polymer

Polymer Polymer

来源 Source

Entity 2 Entity 2 polymer

Polymer Polymer

来源 Source

7. Fold Classification (SCOP + CATH) 2 domains

SCOP 2.08 (1 domains)

CATH v4.4 (1 domains)

8. Citations (1)

9. Files and Curves (10)

Files (7)

Curves (3)