SAXSdb — 4bog

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

Acetylcholine receptor beta subunit

OrganismNot specified

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 × 30 PDB declaration: 30-meric（30） Consistent with protein copy count	Chain 0； UniProt 1–493 Chain B； UniProt 1–493 Chain G； UniProt 1–493 Chain L； UniProt 1–493 Chain Q； UniProt 1–493 Chain V； UniProt 1–493	Not recorded	Acetylcholine receptor delta subunit × 6 （Q6S3H8） Acetylcholine receptor subunit alpha × 12 （P02711） Acetylcholine receptor gamma subunit × 6 （Q6S3H9）	ELECTRON MICROSCOPY cryo-EM buffer：400 MM NACL, 20 MM PHOSPHATE BUFFER, LEUPEPTIN 0.3 MG/L, PEPSTATIN 1 MG/L；pH 7.4；400 MM NACL, 20 MM PHOSPHATE BUFFER, LEUPEPTIN 0.3 MG/L, PEPSTATIN 1 MG/L cryo-EM vitrification conditions：Cryogen ETHANE；ETHANE	Resolution 50.00 Å

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 4BOG	Assembly / Oligomeric State	Construct	Mutations and Modifications	Ligands, Ions and Non-polymers	Method and Experimental Conditions	Structure Quality
1OED STRUCTURE OF ACETYLCHOLINE RECEPTOR PORE FROM ELECTRON IMAGES Deposited 2003-03-24	Different construct Different mutation/modification Different oligomeric state Different experimental conditions Different structure-quality metrics	Assembly 1 Protein heterocomplex Heteromer；Protein × 5 PDB declaration: pentameric	Chain B 241–490（250 aa） Fragment：MEMBRANE-SPANNING DOMAIN, RESIDUES 241-490	Not recorded	No recorded non-water small molecule	ELECTRON MICROSCOPY cryo-EM buffer SODIUM CACODYLATE；pH 6.8 cryo-EM vitrification conditions LIQUID ETHANE	Resolution 4.00 Å
2BG9 REFINED STRUCTURE OF THE NICOTINIC ACETYLCHOLINE RECEPTOR AT 4A RESOLUTION. Deposited 2004-12-17	Different construct Different mutation/modification Different oligomeric state Different experimental conditions Different structure-quality metrics	Assembly 1 Protein heterocomplex Heteromer；Protein × 5 PDB declaration: pentameric	Chain B 25–188（164 aa） Chain B 198–336（139 aa） Chain B 427–493（67 aa）	Not recorded	No recorded non-water small molecule	ELECTRON MICROSCOPY cryo-EM buffer 100MM SODIUM CACODYLATE；pH 6.8；100MM SODIUM CACODYLATE cryo-EM vitrification conditions LIQUID ETHANE	Resolution 4.00 Å
4AQ5 Gating movement in acetylcholine receptor analysed by time-resolved electron cryo-microscopy (closed class) Deposited 2012-04-12	Different construct Different mutation/modification Different oligomeric state Different experimental conditions Different structure-quality metrics	Assembly 1 Protein heterocomplex Heteromer；Protein × 5 PDB declaration: pentameric	Chain B 1–493（493 aa）	Not recorded	No recorded non-water small molecule	ELECTRON MICROSCOPY cryo-EM buffer 100MM SODIUM CACODYLATE, 1MM CALCIUM CHLORIDE；pH 7；100MM SODIUM CACODYLATE, 1MM CALCIUM CHLORIDE cryo-EM vitrification conditions Cryogen ETHANE；VITRIFICATION 1 -- CRYOGEN- ETHANE, HUMIDITY- 85 TEMPERATURE- 120 INSTRUMENT- HOMEMADE PLUNGER METHOD- BLOT UNTIL APPLIED DROPLET LOSES CONTACT WITH FILTER PAPER (INDICATED BY LOSS OF TRANSPARENCY TYPICALLY 6S) TIMERESOLVEDSTATE- VITRIFIED WITHIN 10MS OF EXPOSURE TO ACETYLCHOLINE (APPLIED AS THE GRID IS BEING PLUNGED USING A FINE FOCUSSED SPRAY POSITIONED ABOUT 1CM ABOVE THE ETHANE SURFACE) DETAILS- VITRIFICATION CARRIED OUT AT AN AMBIENT TEMPERATURE OF 8 DEGREES	Resolution 6.20 Å
4AQ9 Gating movement in acetylcholine receptor analysed by time- resolved electron cryo-microscopy (open class) Deposited 2012-04-13	Different construct Different mutation/modification Different oligomeric state Different experimental conditions Different structure-quality metrics	Assembly 1 Protein heterocomplex Heteromer；Protein × 5 PDB declaration: pentameric	Chain B 1–493（493 aa）	Not recorded	No recorded non-water small molecule	ELECTRON MICROSCOPY cryo-EM buffer 100MM SODIUM CACODYLATE, 1MM CALCIUM CHLORIDE；pH 7；100MM SODIUM CACODYLATE, 1MM CALCIUM CHLORIDE cryo-EM vitrification conditions Cryogen ETHANE；VITRIFICATION 1 -- CRYOGEN- ETHANE, HUMIDITY- 85 TEMPERATURE- 120 INSTRUMENT- HOMEMADE PLUNGER METHOD- BLOT UNTIL APPLIED DROPLET LOSES CONTACT WITH FILTER PAPER (INDICATED BY LOSS OF TRANSPARENCY TYPICALLY 6S) TIMERESOLVEDSTATE- VITRIFIED WITHIN 10MS OF EXPOSURE TO ACETYLCHOLINE (APPLIED AS THE GRID IS BEING PLUNGED USING A FINE FOCUSSED SPRAY POSITIONED ABOUT 1CM ABOVE THE ETHANE SURFACE) DETAILS- VITRIFICATION CARRIED OUT AT AN AMBIENT TEMPERATURE OF 8 DEGREES	Resolution 6.20 Å
4BOI The structure and super-organization of acetylcholine receptor-rapsyn complexes class A Deposited 2013-05-20	Different construct Different mutation/modification Different oligomeric state Different experimental conditions Different structure-quality metrics	Assembly 1 Protein heterocomplex Heteromer；Protein × 5 PDB declaration: pentameric	Chain B 1–493（493 aa）	Not recorded	No recorded non-water small molecule	ELECTRON MICROSCOPY cryo-EM buffer 400 MM NACL, 20 MM PHOSPHATE BUFFER, LEUPEPTIN 0.3 MG/L, PEPSTATIN 1 MG/L；pH 7.4；400 MM NACL, 20 MM PHOSPHATE BUFFER, LEUPEPTIN 0.3 MG/L, PEPSTATIN 1 MG/L cryo-EM vitrification conditions Cryogen ETHANE；VITRIFICATION 1 -- CRYOGEN- ETHANE, HUMIDITY- 90, TEMPERATURE- 78, INSTRUMENT- HOMEMADE PLUNGER, METHOD- BLOT FROM THE CARBON SIDE	Resolution 41.00 Å
4BON The structure and super-organization of acetylcholine receptor-rapsyn complexes class B Deposited 2013-05-21	Different construct Different mutation/modification Different oligomeric state Different experimental conditions Different structure-quality metrics	Assembly 1 Protein heterocomplex Heteromer；Protein × 5 PDB declaration: pentameric	Chain B 1–493（493 aa）	Not recorded	No recorded non-water small molecule	ELECTRON MICROSCOPY cryo-EM buffer pH 7.4 cryo-EM vitrification conditions Cryogen ETHANE	Resolution 40.00 Å
4BOO The structure and super-organization of acetylcholine receptor-rapsyn complexes class C Deposited 2013-05-21	Different construct Different mutation/modification Different oligomeric state Different experimental conditions Different structure-quality metrics	Assembly 1 Protein heterocomplex Heteromer；Protein × 5 PDB declaration: pentameric	Chain B 1–493（493 aa）	Not recorded	No recorded non-water small molecule	ELECTRON MICROSCOPY cryo-EM buffer 400 MM NACL, 20 MM PHOSPHATE BUFFER, LEUPEPTIN 0.3 MG/L, PEPSTATIN 1 MG/L；pH 7.4；400 MM NACL, 20 MM PHOSPHATE BUFFER, LEUPEPTIN 0.3 MG/L, PEPSTATIN 1 MG/L cryo-EM vitrification conditions Cryogen ETHANE；CRYOGEN- ETHANE, HUMIDITY- 90, TEMPERATURE- 78, INSTRUMENT- HOMEMADE PLUNGER, METHOD- BLOT FROM THE CARBON SIDE	Resolution 42.00 Å
4BOR The structure and super-organization of acetylcholine receptor-rapsyn complexes class D Deposited 2013-05-22	Different construct Different mutation/modification Different oligomeric state Different experimental conditions Different structure-quality metrics	Assembly 1 Protein heterocomplex Heteromer；Protein × 5 PDB declaration: pentameric	Chain B 1–493（493 aa）	Not recorded	No recorded non-water small molecule	ELECTRON MICROSCOPY cryo-EM buffer pH 7.4 cryo-EM vitrification conditions Cryogen ETHANE	Resolution 42.00 Å
4BOT The structure and super-organization of acetylcholine receptor- rapsyn complexes class E Deposited 2013-05-22	Different construct Different mutation/modification Different oligomeric state Different experimental conditions Different structure-quality metrics	Assembly 1 Protein heterocomplex Heteromer；Protein × 5 PDB declaration: pentameric	Chain B 1–493（493 aa）	Not recorded	No recorded non-water small molecule	ELECTRON MICROSCOPY cryo-EM buffer 400 MM NACL, 20 MM PHOSPHATE BUFFER, LEUPEPTIN 0.3 MG/L, PEPSTATIN 1 MG/L；pH 7.4；400 MM NACL, 20 MM PHOSPHATE BUFFER, LEUPEPTIN 0.3 MG/L, PEPSTATIN 1 MG/L cryo-EM vitrification conditions Cryogen ETHANE；VITRIFICATION 1 -- CRYOGEN- ETHANE, HUMIDITY- 90, TEMPERATURE- 78, INSTRUMENT- HOMEMADE PLUNGER, METHOD- BLOT FROM THE CARBON SIDE,	Resolution 42.00 Å

9 other PDB entries and 9 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence

UniProt name	Q6S3I0_TORMA
Isoform	—
PDB entities	1
Chains and sequence ranges	Author chain 0； PDBConstruct 1–493； UniProt 1–493 Author chain B； PDBConstruct 1–493； UniProt 1–493 Author chain G； PDBConstruct 1–493； UniProt 1–493 Author chain L； PDBConstruct 1–493； UniProt 1–493 Author chain Q； PDBConstruct 1–493； UniProt 1–493 Author chain V； PDBConstruct 1–493； UniProt 1–493

Acetylcholine receptor delta subunit

OrganismNot specified

UniProt Q6S3H8

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 × 30 PDB declaration: 30-meric（30） Consistent with protein copy count	Chain 1； UniProt 1–522 Chain C； UniProt 1–522 Chain H； UniProt 1–522 Chain M； UniProt 1–522 Chain R； UniProt 1–522 Chain W； UniProt 1–522	Not recorded	Acetylcholine receptor beta subunit × 6 （Q6S3I0） Acetylcholine receptor subunit alpha × 12 （P02711） Acetylcholine receptor gamma subunit × 6 （Q6S3H9）	ELECTRON MICROSCOPY cryo-EM buffer：400 MM NACL, 20 MM PHOSPHATE BUFFER, LEUPEPTIN 0.3 MG/L, PEPSTATIN 1 MG/L；pH 7.4；400 MM NACL, 20 MM PHOSPHATE BUFFER, LEUPEPTIN 0.3 MG/L, PEPSTATIN 1 MG/L cryo-EM vitrification conditions：Cryogen ETHANE；ETHANE	Resolution 50.00 Å

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 4BOG	Assembly / Oligomeric State	Construct	Mutations and Modifications	Ligands, Ions and Non-polymers	Method and Experimental Conditions	Structure Quality
1OED STRUCTURE OF ACETYLCHOLINE RECEPTOR PORE FROM ELECTRON IMAGES Deposited 2003-03-24	Different construct Different mutation/modification Different oligomeric state Different experimental conditions Different structure-quality metrics	Assembly 1 Protein heterocomplex Heteromer；Protein × 5 PDB declaration: pentameric	Chain C 246–505（260 aa） Fragment：MEMBRANE-SPANNING DOMAIN, RESIDUES 246-505	Not recorded	No recorded non-water small molecule	ELECTRON MICROSCOPY cryo-EM buffer SODIUM CACODYLATE；pH 6.8 cryo-EM vitrification conditions LIQUID ETHANE	Resolution 4.00 Å
2BG9 REFINED STRUCTURE OF THE NICOTINIC ACETYLCHOLINE RECEPTOR AT 4A RESOLUTION. Deposited 2004-12-17	Different construct Different mutation/modification Different oligomeric state Different experimental conditions Different structure-quality metrics	Assembly 1 Protein heterocomplex Heteromer；Protein × 5 PDB declaration: pentameric	Chain C 22–183（162 aa） Chain C 199–341（143 aa） Chain C 442–505（64 aa）	Not recorded	No recorded non-water small molecule	ELECTRON MICROSCOPY cryo-EM buffer 100MM SODIUM CACODYLATE；pH 6.8；100MM SODIUM CACODYLATE cryo-EM vitrification conditions LIQUID ETHANE	Resolution 4.00 Å
4AQ5 Gating movement in acetylcholine receptor analysed by time-resolved electron cryo-microscopy (closed class) Deposited 2012-04-12	Different construct Different mutation/modification Different oligomeric state Different experimental conditions Different structure-quality metrics	Assembly 1 Protein heterocomplex Heteromer；Protein × 5 PDB declaration: pentameric	Chain C 1–522（522 aa）	Not recorded	No recorded non-water small molecule	ELECTRON MICROSCOPY cryo-EM buffer 100MM SODIUM CACODYLATE, 1MM CALCIUM CHLORIDE；pH 7；100MM SODIUM CACODYLATE, 1MM CALCIUM CHLORIDE cryo-EM vitrification conditions Cryogen ETHANE；VITRIFICATION 1 -- CRYOGEN- ETHANE, HUMIDITY- 85 TEMPERATURE- 120 INSTRUMENT- HOMEMADE PLUNGER METHOD- BLOT UNTIL APPLIED DROPLET LOSES CONTACT WITH FILTER PAPER (INDICATED BY LOSS OF TRANSPARENCY TYPICALLY 6S) TIMERESOLVEDSTATE- VITRIFIED WITHIN 10MS OF EXPOSURE TO ACETYLCHOLINE (APPLIED AS THE GRID IS BEING PLUNGED USING A FINE FOCUSSED SPRAY POSITIONED ABOUT 1CM ABOVE THE ETHANE SURFACE) DETAILS- VITRIFICATION CARRIED OUT AT AN AMBIENT TEMPERATURE OF 8 DEGREES	Resolution 6.20 Å
4AQ9 Gating movement in acetylcholine receptor analysed by time- resolved electron cryo-microscopy (open class) Deposited 2012-04-13	Different construct Different mutation/modification Different oligomeric state Different experimental conditions Different structure-quality metrics	Assembly 1 Protein heterocomplex Heteromer；Protein × 5 PDB declaration: pentameric	Chain C 1–522（522 aa）	Not recorded	No recorded non-water small molecule	ELECTRON MICROSCOPY cryo-EM buffer 100MM SODIUM CACODYLATE, 1MM CALCIUM CHLORIDE；pH 7；100MM SODIUM CACODYLATE, 1MM CALCIUM CHLORIDE cryo-EM vitrification conditions Cryogen ETHANE；VITRIFICATION 1 -- CRYOGEN- ETHANE, HUMIDITY- 85 TEMPERATURE- 120 INSTRUMENT- HOMEMADE PLUNGER METHOD- BLOT UNTIL APPLIED DROPLET LOSES CONTACT WITH FILTER PAPER (INDICATED BY LOSS OF TRANSPARENCY TYPICALLY 6S) TIMERESOLVEDSTATE- VITRIFIED WITHIN 10MS OF EXPOSURE TO ACETYLCHOLINE (APPLIED AS THE GRID IS BEING PLUNGED USING A FINE FOCUSSED SPRAY POSITIONED ABOUT 1CM ABOVE THE ETHANE SURFACE) DETAILS- VITRIFICATION CARRIED OUT AT AN AMBIENT TEMPERATURE OF 8 DEGREES	Resolution 6.20 Å
4BOI The structure and super-organization of acetylcholine receptor-rapsyn complexes class A Deposited 2013-05-20	Different construct Different mutation/modification Different oligomeric state Different experimental conditions Different structure-quality metrics	Assembly 1 Protein heterocomplex Heteromer；Protein × 5 PDB declaration: pentameric	Chain C 1–522（522 aa）	Not recorded	No recorded non-water small molecule	ELECTRON MICROSCOPY cryo-EM buffer 400 MM NACL, 20 MM PHOSPHATE BUFFER, LEUPEPTIN 0.3 MG/L, PEPSTATIN 1 MG/L；pH 7.4；400 MM NACL, 20 MM PHOSPHATE BUFFER, LEUPEPTIN 0.3 MG/L, PEPSTATIN 1 MG/L cryo-EM vitrification conditions Cryogen ETHANE；VITRIFICATION 1 -- CRYOGEN- ETHANE, HUMIDITY- 90, TEMPERATURE- 78, INSTRUMENT- HOMEMADE PLUNGER, METHOD- BLOT FROM THE CARBON SIDE	Resolution 41.00 Å
4BON The structure and super-organization of acetylcholine receptor-rapsyn complexes class B Deposited 2013-05-21	Different construct Different mutation/modification Different oligomeric state Different experimental conditions Different structure-quality metrics	Assembly 1 Protein heterocomplex Heteromer；Protein × 5 PDB declaration: pentameric	Chain C 1–522（522 aa）	Not recorded	No recorded non-water small molecule	ELECTRON MICROSCOPY cryo-EM buffer pH 7.4 cryo-EM vitrification conditions Cryogen ETHANE	Resolution 40.00 Å
4BOO The structure and super-organization of acetylcholine receptor-rapsyn complexes class C Deposited 2013-05-21	Different construct Different mutation/modification Different oligomeric state Different experimental conditions Different structure-quality metrics	Assembly 1 Protein heterocomplex Heteromer；Protein × 5 PDB declaration: pentameric	Chain C 1–522（522 aa）	Not recorded	No recorded non-water small molecule	ELECTRON MICROSCOPY cryo-EM buffer 400 MM NACL, 20 MM PHOSPHATE BUFFER, LEUPEPTIN 0.3 MG/L, PEPSTATIN 1 MG/L；pH 7.4；400 MM NACL, 20 MM PHOSPHATE BUFFER, LEUPEPTIN 0.3 MG/L, PEPSTATIN 1 MG/L cryo-EM vitrification conditions Cryogen ETHANE；CRYOGEN- ETHANE, HUMIDITY- 90, TEMPERATURE- 78, INSTRUMENT- HOMEMADE PLUNGER, METHOD- BLOT FROM THE CARBON SIDE	Resolution 42.00 Å
4BOR The structure and super-organization of acetylcholine receptor-rapsyn complexes class D Deposited 2013-05-22	Different construct Different mutation/modification Different oligomeric state Different experimental conditions Different structure-quality metrics	Assembly 1 Protein heterocomplex Heteromer；Protein × 5 PDB declaration: pentameric	Chain C 1–522（522 aa）	Not recorded	No recorded non-water small molecule	ELECTRON MICROSCOPY cryo-EM buffer pH 7.4 cryo-EM vitrification conditions Cryogen ETHANE	Resolution 42.00 Å
4BOT The structure and super-organization of acetylcholine receptor- rapsyn complexes class E Deposited 2013-05-22	Different construct Different mutation/modification Different oligomeric state Different experimental conditions Different structure-quality metrics	Assembly 1 Protein heterocomplex Heteromer；Protein × 5 PDB declaration: pentameric	Chain C 1–522（522 aa）	Not recorded	No recorded non-water small molecule	ELECTRON MICROSCOPY cryo-EM buffer 400 MM NACL, 20 MM PHOSPHATE BUFFER, LEUPEPTIN 0.3 MG/L, PEPSTATIN 1 MG/L；pH 7.4；400 MM NACL, 20 MM PHOSPHATE BUFFER, LEUPEPTIN 0.3 MG/L, PEPSTATIN 1 MG/L cryo-EM vitrification conditions Cryogen ETHANE；VITRIFICATION 1 -- CRYOGEN- ETHANE, HUMIDITY- 90, TEMPERATURE- 78, INSTRUMENT- HOMEMADE PLUNGER, METHOD- BLOT FROM THE CARBON SIDE,	Resolution 42.00 Å

9 other PDB entries and 9 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence

UniProt name	Q6S3H8_TORMA
Isoform	—
PDB entities	2
Chains and sequence ranges	Author chain 1； PDBConstruct 1–522； UniProt 1–522 Author chain C； PDBConstruct 1–522； UniProt 1–522 Author chain H； PDBConstruct 1–522； UniProt 1–522 Author chain M； PDBConstruct 1–522； UniProt 1–522 Author chain R； PDBConstruct 1–522； UniProt 1–522 Author chain W； PDBConstruct 1–522； UniProt 1–522

Acetylcholine receptor subunit alpha

OrganismNot specified

UniProt P02711

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 × 30 PDB declaration: 30-meric（30） Consistent with protein copy count	Chain 2； UniProt 1–461 Chain A； UniProt 1–461 Chain D； UniProt 1–461 Chain F； UniProt 1–461 Chain I； UniProt 1–461 Chain K； UniProt 1–461 Chain N； UniProt 1–461 Chain P； UniProt 1–461 Chain S； UniProt 1–461 Chain U； UniProt 1–461 Chain X； UniProt 1–461 Chain Z； UniProt 1–461	Not recorded	Acetylcholine receptor beta subunit × 6 （Q6S3I0） Acetylcholine receptor delta subunit × 6 （Q6S3H8） Acetylcholine receptor gamma subunit × 6 （Q6S3H9）	ELECTRON MICROSCOPY cryo-EM buffer：400 MM NACL, 20 MM PHOSPHATE BUFFER, LEUPEPTIN 0.3 MG/L, PEPSTATIN 1 MG/L；pH 7.4；400 MM NACL, 20 MM PHOSPHATE BUFFER, LEUPEPTIN 0.3 MG/L, PEPSTATIN 1 MG/L cryo-EM vitrification conditions：Cryogen ETHANE；ETHANE	Resolution 50.00 Å

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 4BOG	Assembly / Oligomeric State	Construct	Mutations and Modifications	Ligands, Ions and Non-polymers	Method and Experimental Conditions	Structure Quality
1L4W NMR structure of an AChR-peptide (Torpedo Californica, alpha-subunit residues 182-202) in complex with alpha-Bungarotoxin Deposited 2002-03-06	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 B 206–226（21 aa） Fragment：Acetylcholine receptor peptide (residues 206-226)	Not recorded	No recorded non-water small molecule	SOLUTION NMR NMR measurement conditions pH 4；303 K；Ionic strength (raw mmCIF value) 50 mM Ac；Pressure ambient NMR sample composition 1.8 mM alpha-Bungarotoxin/AChR-peptide, buffer,pH 4 \| 90% H2O/10% D2O NMR sample composition 1.8 mM alpha-Bungarotoxin/AChR-peptide, buffer,pH 4 \| 100% D2O	Resolution not provided
1LJZ NMR structure of an AChR-peptide (Torpedo Californica, alpha-subunit residues 182-202) in complex with alpha-Bungarotoxin Deposited 2002-04-23	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 206–226（21 aa） Fragment：Acetylcholine receptor peptide (residues 182-202)	Not recorded	No recorded non-water small molecule	SOLUTION NMR NMR measurement conditions pH 4；298 K；Ionic strength (raw mmCIF value) 50 mM NH4Ac；Pressure ambient NMR measurement conditions pH 4；298 K；Ionic strength (raw mmCIF value) 50 mM NH4Ac；Pressure ambient NMR sample composition acetylcholine receptor peptide/alpha-bungarotoxin \| 90% H2O/10% D2O NMR sample composition acetylcholine receptor peptide/alpha-bungarotoxin \| 100% D2O	Resolution not provided
1OED STRUCTURE OF ACETYLCHOLINE RECEPTOR PORE FROM ELECTRON IMAGES Deposited 2003-03-24	Different construct Different mutation/modification Different oligomeric state Different experimental conditions Different structure-quality metrics	Assembly 1 Protein heterocomplex Heteromer；Protein × 5 PDB declaration: pentameric	Chain A 235–461（227 aa） Fragment：MEMBRANE-SPANNING DOMAIN, RESIDUES 235-461 Chain D 235–461（227 aa） Fragment：MEMBRANE-SPANNING DOMAIN, RESIDUES 235-461	Not recorded	No recorded non-water small molecule	ELECTRON MICROSCOPY cryo-EM buffer SODIUM CACODYLATE；pH 6.8 cryo-EM vitrification conditions LIQUID ETHANE	Resolution 4.00 Å
2BG9 REFINED STRUCTURE OF THE NICOTINIC ACETYLCHOLINE RECEPTOR AT 4A RESOLUTION. Deposited 2004-12-17	Different construct Different mutation/modification Different oligomeric state Different experimental conditions Different structure-quality metrics	Assembly 1 Protein heterocomplex Heteromer；Protein × 5 PDB declaration: pentameric	Chain A 25–330（306 aa） Chain A 398–461（64 aa） Chain D 25–330（306 aa） Chain D 398–461（64 aa）	Not recorded	No recorded non-water small molecule	ELECTRON MICROSCOPY cryo-EM buffer 100MM SODIUM CACODYLATE；pH 6.8；100MM SODIUM CACODYLATE cryo-EM vitrification conditions LIQUID ETHANE	Resolution 4.00 Å
4AQ5 Gating movement in acetylcholine receptor analysed by time-resolved electron cryo-microscopy (closed class) Deposited 2012-04-12	Different construct Different mutation/modification Different oligomeric state Different experimental conditions Different structure-quality metrics	Assembly 1 Protein heterocomplex Heteromer；Protein × 5 PDB declaration: pentameric	Chain A 1–461（461 aa） Chain D 1–461（461 aa）	Not recorded	No recorded non-water small molecule	ELECTRON MICROSCOPY cryo-EM buffer 100MM SODIUM CACODYLATE, 1MM CALCIUM CHLORIDE；pH 7；100MM SODIUM CACODYLATE, 1MM CALCIUM CHLORIDE cryo-EM vitrification conditions Cryogen ETHANE；VITRIFICATION 1 -- CRYOGEN- ETHANE, HUMIDITY- 85 TEMPERATURE- 120 INSTRUMENT- HOMEMADE PLUNGER METHOD- BLOT UNTIL APPLIED DROPLET LOSES CONTACT WITH FILTER PAPER (INDICATED BY LOSS OF TRANSPARENCY TYPICALLY 6S) TIMERESOLVEDSTATE- VITRIFIED WITHIN 10MS OF EXPOSURE TO ACETYLCHOLINE (APPLIED AS THE GRID IS BEING PLUNGED USING A FINE FOCUSSED SPRAY POSITIONED ABOUT 1CM ABOVE THE ETHANE SURFACE) DETAILS- VITRIFICATION CARRIED OUT AT AN AMBIENT TEMPERATURE OF 8 DEGREES	Resolution 6.20 Å
4AQ9 Gating movement in acetylcholine receptor analysed by time- resolved electron cryo-microscopy (open class) Deposited 2012-04-13	Different construct Different mutation/modification Different oligomeric state Different experimental conditions Different structure-quality metrics	Assembly 1 Protein heterocomplex Heteromer；Protein × 5 PDB declaration: pentameric	Chain A 1–461（461 aa） Chain D 1–461（461 aa）	Not recorded	No recorded non-water small molecule	ELECTRON MICROSCOPY cryo-EM buffer 100MM SODIUM CACODYLATE, 1MM CALCIUM CHLORIDE；pH 7；100MM SODIUM CACODYLATE, 1MM CALCIUM CHLORIDE cryo-EM vitrification conditions Cryogen ETHANE；VITRIFICATION 1 -- CRYOGEN- ETHANE, HUMIDITY- 85 TEMPERATURE- 120 INSTRUMENT- HOMEMADE PLUNGER METHOD- BLOT UNTIL APPLIED DROPLET LOSES CONTACT WITH FILTER PAPER (INDICATED BY LOSS OF TRANSPARENCY TYPICALLY 6S) TIMERESOLVEDSTATE- VITRIFIED WITHIN 10MS OF EXPOSURE TO ACETYLCHOLINE (APPLIED AS THE GRID IS BEING PLUNGED USING A FINE FOCUSSED SPRAY POSITIONED ABOUT 1CM ABOVE THE ETHANE SURFACE) DETAILS- VITRIFICATION CARRIED OUT AT AN AMBIENT TEMPERATURE OF 8 DEGREES	Resolution 6.20 Å
4BOI The structure and super-organization of acetylcholine receptor-rapsyn complexes class A Deposited 2013-05-20	Different construct Different mutation/modification Different oligomeric state Different experimental conditions Different structure-quality metrics	Assembly 1 Protein heterocomplex Heteromer；Protein × 5 PDB declaration: pentameric	Chain A 1–461（461 aa） Chain D 1–461（461 aa）	Not recorded	No recorded non-water small molecule	ELECTRON MICROSCOPY cryo-EM buffer 400 MM NACL, 20 MM PHOSPHATE BUFFER, LEUPEPTIN 0.3 MG/L, PEPSTATIN 1 MG/L；pH 7.4；400 MM NACL, 20 MM PHOSPHATE BUFFER, LEUPEPTIN 0.3 MG/L, PEPSTATIN 1 MG/L cryo-EM vitrification conditions Cryogen ETHANE；VITRIFICATION 1 -- CRYOGEN- ETHANE, HUMIDITY- 90, TEMPERATURE- 78, INSTRUMENT- HOMEMADE PLUNGER, METHOD- BLOT FROM THE CARBON SIDE	Resolution 41.00 Å
4BON The structure and super-organization of acetylcholine receptor-rapsyn complexes class B Deposited 2013-05-21	Different construct Different mutation/modification Different oligomeric state Different experimental conditions Different structure-quality metrics	Assembly 1 Protein heterocomplex Heteromer；Protein × 5 PDB declaration: pentameric	Chain A 1–461（461 aa） Chain D 1–461（461 aa）	Not recorded	No recorded non-water small molecule	ELECTRON MICROSCOPY cryo-EM buffer pH 7.4 cryo-EM vitrification conditions Cryogen ETHANE	Resolution 40.00 Å
4BOO The structure and super-organization of acetylcholine receptor-rapsyn complexes class C Deposited 2013-05-21	Different construct Different mutation/modification Different oligomeric state Different experimental conditions Different structure-quality metrics	Assembly 1 Protein heterocomplex Heteromer；Protein × 5 PDB declaration: pentameric	Chain A 1–461（461 aa） Chain D 1–461（461 aa）	Not recorded	No recorded non-water small molecule	ELECTRON MICROSCOPY cryo-EM buffer 400 MM NACL, 20 MM PHOSPHATE BUFFER, LEUPEPTIN 0.3 MG/L, PEPSTATIN 1 MG/L；pH 7.4；400 MM NACL, 20 MM PHOSPHATE BUFFER, LEUPEPTIN 0.3 MG/L, PEPSTATIN 1 MG/L cryo-EM vitrification conditions Cryogen ETHANE；CRYOGEN- ETHANE, HUMIDITY- 90, TEMPERATURE- 78, INSTRUMENT- HOMEMADE PLUNGER, METHOD- BLOT FROM THE CARBON SIDE	Resolution 42.00 Å
4BOR The structure and super-organization of acetylcholine receptor-rapsyn complexes class D Deposited 2013-05-22	Different construct Different mutation/modification Different oligomeric state Different experimental conditions Different structure-quality metrics	Assembly 1 Protein heterocomplex Heteromer；Protein × 5 PDB declaration: pentameric	Chain A 1–461（461 aa） Chain D 1–461（461 aa）	Not recorded	No recorded non-water small molecule	ELECTRON MICROSCOPY cryo-EM buffer pH 7.4 cryo-EM vitrification conditions Cryogen ETHANE	Resolution 42.00 Å
4BOT The structure and super-organization of acetylcholine receptor- rapsyn complexes class E Deposited 2013-05-22	Different construct Different mutation/modification Different oligomeric state Different experimental conditions Different structure-quality metrics	Assembly 1 Protein heterocomplex Heteromer；Protein × 5 PDB declaration: pentameric	Chain A 1–461（461 aa） Chain D 1–461（461 aa）	Not recorded	No recorded non-water small molecule	ELECTRON MICROSCOPY cryo-EM buffer 400 MM NACL, 20 MM PHOSPHATE BUFFER, LEUPEPTIN 0.3 MG/L, PEPSTATIN 1 MG/L；pH 7.4；400 MM NACL, 20 MM PHOSPHATE BUFFER, LEUPEPTIN 0.3 MG/L, PEPSTATIN 1 MG/L cryo-EM vitrification conditions Cryogen ETHANE；VITRIFICATION 1 -- CRYOGEN- ETHANE, HUMIDITY- 90, TEMPERATURE- 78, INSTRUMENT- HOMEMADE PLUNGER, METHOD- BLOT FROM THE CARBON SIDE,	Resolution 42.00 Å

11 other PDB entries and 11 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence

UniProt name	ACHA_TORMA
Isoform	—
PDB entities	3
Chains and sequence ranges	Author chain 2； PDBConstruct 1–461； UniProt 1–461 Author chain A； PDBConstruct 1–461； UniProt 1–461 Author chain D； PDBConstruct 1–461； UniProt 1–461 Author chain F； PDBConstruct 1–461； UniProt 1–461 Author chain I； PDBConstruct 1–461； UniProt 1–461 Author chain K； PDBConstruct 1–461； UniProt 1–461 Author chain N； PDBConstruct 1–461； UniProt 1–461 Author chain P； PDBConstruct 1–461； UniProt 1–461 Author chain S； PDBConstruct 1–461； UniProt 1–461 Author chain U； PDBConstruct 1–461； UniProt 1–461 Author chain X； PDBConstruct 1–461； UniProt 1–461 Author chain Z； PDBConstruct 1–461； UniProt 1–461

Acetylcholine receptor gamma subunit

OrganismNot specified

UniProt Q6S3H9

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 × 30 PDB declaration: 30-meric（30） Consistent with protein copy count	Chain 3； UniProt 1–505 Chain E； UniProt 1–505 Chain J； UniProt 1–505 Chain O； UniProt 1–505 Chain T； UniProt 1–505 Chain Y； UniProt 1–505	Not recorded	Acetylcholine receptor beta subunit × 6 （Q6S3I0） Acetylcholine receptor delta subunit × 6 （Q6S3H8） Acetylcholine receptor subunit alpha × 12 （P02711）	ELECTRON MICROSCOPY cryo-EM buffer：400 MM NACL, 20 MM PHOSPHATE BUFFER, LEUPEPTIN 0.3 MG/L, PEPSTATIN 1 MG/L；pH 7.4；400 MM NACL, 20 MM PHOSPHATE BUFFER, LEUPEPTIN 0.3 MG/L, PEPSTATIN 1 MG/L cryo-EM vitrification conditions：Cryogen ETHANE；ETHANE	Resolution 50.00 Å

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 4BOG	Assembly / Oligomeric State	Construct	Mutations and Modifications	Ligands, Ions and Non-polymers	Method and Experimental Conditions	Structure Quality
1OED STRUCTURE OF ACETYLCHOLINE RECEPTOR PORE FROM ELECTRON IMAGES Deposited 2003-03-24	Different construct Different mutation/modification Different oligomeric state Different experimental conditions Different structure-quality metrics	Assembly 1 Protein heterocomplex Heteromer；Protein × 5 PDB declaration: pentameric	Chain E 235–494（260 aa） Fragment：MEMBRANE-SPANNING DOMAIN, RESIDUES 236-495	Not recorded	No recorded non-water small molecule	ELECTRON MICROSCOPY cryo-EM buffer SODIUM CACODYLATE；pH 6.8 cryo-EM vitrification conditions LIQUID ETHANE	Resolution 4.00 Å
2BG9 REFINED STRUCTURE OF THE NICOTINIC ACETYLCHOLINE RECEPTOR AT 4A RESOLUTION. Deposited 2004-12-17	Different construct Different mutation/modification Different oligomeric state Different experimental conditions Different structure-quality metrics	Assembly 1 Protein heterocomplex Heteromer；Protein × 5 PDB declaration: pentameric	Chain E 18–181（164 aa） Chain E 189–332（144 aa） Chain E 432–493（62 aa）	Not recorded	No recorded non-water small molecule	ELECTRON MICROSCOPY cryo-EM buffer 100MM SODIUM CACODYLATE；pH 6.8；100MM SODIUM CACODYLATE cryo-EM vitrification conditions LIQUID ETHANE	Resolution 4.00 Å
4AQ5 Gating movement in acetylcholine receptor analysed by time-resolved electron cryo-microscopy (closed class) Deposited 2012-04-12	Different construct Different mutation/modification Different oligomeric state Different experimental conditions Different structure-quality metrics	Assembly 1 Protein heterocomplex Heteromer；Protein × 5 PDB declaration: pentameric	Chain E 18–505（488 aa）	Not recorded	No recorded non-water small molecule	ELECTRON MICROSCOPY cryo-EM buffer 100MM SODIUM CACODYLATE, 1MM CALCIUM CHLORIDE；pH 7；100MM SODIUM CACODYLATE, 1MM CALCIUM CHLORIDE cryo-EM vitrification conditions Cryogen ETHANE；VITRIFICATION 1 -- CRYOGEN- ETHANE, HUMIDITY- 85 TEMPERATURE- 120 INSTRUMENT- HOMEMADE PLUNGER METHOD- BLOT UNTIL APPLIED DROPLET LOSES CONTACT WITH FILTER PAPER (INDICATED BY LOSS OF TRANSPARENCY TYPICALLY 6S) TIMERESOLVEDSTATE- VITRIFIED WITHIN 10MS OF EXPOSURE TO ACETYLCHOLINE (APPLIED AS THE GRID IS BEING PLUNGED USING A FINE FOCUSSED SPRAY POSITIONED ABOUT 1CM ABOVE THE ETHANE SURFACE) DETAILS- VITRIFICATION CARRIED OUT AT AN AMBIENT TEMPERATURE OF 8 DEGREES	Resolution 6.20 Å
4AQ9 Gating movement in acetylcholine receptor analysed by time- resolved electron cryo-microscopy (open class) Deposited 2012-04-13	Different construct Different mutation/modification Different oligomeric state Different experimental conditions Different structure-quality metrics	Assembly 1 Protein heterocomplex Heteromer；Protein × 5 PDB declaration: pentameric	Chain E 18–505（488 aa）	Not recorded	No recorded non-water small molecule	ELECTRON MICROSCOPY cryo-EM buffer 100MM SODIUM CACODYLATE, 1MM CALCIUM CHLORIDE；pH 7；100MM SODIUM CACODYLATE, 1MM CALCIUM CHLORIDE cryo-EM vitrification conditions Cryogen ETHANE；VITRIFICATION 1 -- CRYOGEN- ETHANE, HUMIDITY- 85 TEMPERATURE- 120 INSTRUMENT- HOMEMADE PLUNGER METHOD- BLOT UNTIL APPLIED DROPLET LOSES CONTACT WITH FILTER PAPER (INDICATED BY LOSS OF TRANSPARENCY TYPICALLY 6S) TIMERESOLVEDSTATE- VITRIFIED WITHIN 10MS OF EXPOSURE TO ACETYLCHOLINE (APPLIED AS THE GRID IS BEING PLUNGED USING A FINE FOCUSSED SPRAY POSITIONED ABOUT 1CM ABOVE THE ETHANE SURFACE) DETAILS- VITRIFICATION CARRIED OUT AT AN AMBIENT TEMPERATURE OF 8 DEGREES	Resolution 6.20 Å
4BOI The structure and super-organization of acetylcholine receptor-rapsyn complexes class A Deposited 2013-05-20	Different construct Different mutation/modification Different oligomeric state Different experimental conditions Different structure-quality metrics	Assembly 1 Protein heterocomplex Heteromer；Protein × 5 PDB declaration: pentameric	Chain E 1–505（505 aa）	Not recorded	No recorded non-water small molecule	ELECTRON MICROSCOPY cryo-EM buffer 400 MM NACL, 20 MM PHOSPHATE BUFFER, LEUPEPTIN 0.3 MG/L, PEPSTATIN 1 MG/L；pH 7.4；400 MM NACL, 20 MM PHOSPHATE BUFFER, LEUPEPTIN 0.3 MG/L, PEPSTATIN 1 MG/L cryo-EM vitrification conditions Cryogen ETHANE；VITRIFICATION 1 -- CRYOGEN- ETHANE, HUMIDITY- 90, TEMPERATURE- 78, INSTRUMENT- HOMEMADE PLUNGER, METHOD- BLOT FROM THE CARBON SIDE	Resolution 41.00 Å
4BON The structure and super-organization of acetylcholine receptor-rapsyn complexes class B Deposited 2013-05-21	Different construct Different mutation/modification Different oligomeric state Different experimental conditions Different structure-quality metrics	Assembly 1 Protein heterocomplex Heteromer；Protein × 5 PDB declaration: pentameric	Chain E 1–505（505 aa）	Not recorded	No recorded non-water small molecule	ELECTRON MICROSCOPY cryo-EM buffer pH 7.4 cryo-EM vitrification conditions Cryogen ETHANE	Resolution 40.00 Å
4BOO The structure and super-organization of acetylcholine receptor-rapsyn complexes class C Deposited 2013-05-21	Different construct Different mutation/modification Different oligomeric state Different experimental conditions Different structure-quality metrics	Assembly 1 Protein heterocomplex Heteromer；Protein × 5 PDB declaration: pentameric	Chain E 1–505（505 aa）	Not recorded	No recorded non-water small molecule	ELECTRON MICROSCOPY cryo-EM buffer 400 MM NACL, 20 MM PHOSPHATE BUFFER, LEUPEPTIN 0.3 MG/L, PEPSTATIN 1 MG/L；pH 7.4；400 MM NACL, 20 MM PHOSPHATE BUFFER, LEUPEPTIN 0.3 MG/L, PEPSTATIN 1 MG/L cryo-EM vitrification conditions Cryogen ETHANE；CRYOGEN- ETHANE, HUMIDITY- 90, TEMPERATURE- 78, INSTRUMENT- HOMEMADE PLUNGER, METHOD- BLOT FROM THE CARBON SIDE	Resolution 42.00 Å
4BOR The structure and super-organization of acetylcholine receptor-rapsyn complexes class D Deposited 2013-05-22	Different construct Different mutation/modification Different oligomeric state Different experimental conditions Different structure-quality metrics	Assembly 1 Protein heterocomplex Heteromer；Protein × 5 PDB declaration: pentameric	Chain E 1–505（505 aa）	Not recorded	No recorded non-water small molecule	ELECTRON MICROSCOPY cryo-EM buffer pH 7.4 cryo-EM vitrification conditions Cryogen ETHANE	Resolution 42.00 Å
4BOT The structure and super-organization of acetylcholine receptor- rapsyn complexes class E Deposited 2013-05-22	Different construct Different mutation/modification Different oligomeric state Different experimental conditions Different structure-quality metrics	Assembly 1 Protein heterocomplex Heteromer；Protein × 5 PDB declaration: pentameric	Chain E 1–505（505 aa）	Not recorded	No recorded non-water small molecule	ELECTRON MICROSCOPY cryo-EM buffer 400 MM NACL, 20 MM PHOSPHATE BUFFER, LEUPEPTIN 0.3 MG/L, PEPSTATIN 1 MG/L；pH 7.4；400 MM NACL, 20 MM PHOSPHATE BUFFER, LEUPEPTIN 0.3 MG/L, PEPSTATIN 1 MG/L cryo-EM vitrification conditions Cryogen ETHANE；VITRIFICATION 1 -- CRYOGEN- ETHANE, HUMIDITY- 90, TEMPERATURE- 78, INSTRUMENT- HOMEMADE PLUNGER, METHOD- BLOT FROM THE CARBON SIDE,	Resolution 42.00 Å

9 other PDB entries and 9 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence

UniProt name	Q6S3H9_TORMA
Isoform	—
PDB entities	4
Chains and sequence ranges	Author chain 3； PDBConstruct 1–505； UniProt 1–505 Author chain E； PDBConstruct 1–505； UniProt 1–505 Author chain J； PDBConstruct 1–505； UniProt 1–505 Author chain O； PDBConstruct 1–505； UniProt 1–505 Author chain T； PDBConstruct 1–505； UniProt 1–505 Author chain Y； PDBConstruct 1–505； UniProt 1–505

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	4bog
Deposition date deposition_date	2013-05-20
Structure title title	The structure and super-organization of acetylcholine receptor-rapsyn complexes
Keywords keywords	TRANSPORT PROTEIN, CLUSTERING, SYNAPSE, NEUROMUSCULAR JUNCTION, NICOTINIC, RAPSYN, 43K, ELECTRIC ORGAN; TRANSPORT PROTEIN
Experimental Method method	ELECTRON MICROSCOPY

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

Radius of gyration Rg (Guinier) rg_guinier	— Å
Radius of gyration Rg (electron density) rg_electron	100.40 Å
Forward intensity I(0) i0	19372700000.00
Molecular weight molecular_weight	1269000.0 kDa
Excluded volume excluded_volume	1618800 Å³
Envelope volume envelope_volume	3210200 Å³
Hydration-shell volume shell_volume	271520 Å³
Envelope diameter envelope_diameter	289.5 Å
Shell Rg shell_rg	89.70 Å
Envelope Rg envelope_rg	93.64 Å
Shape Rg shape_rg	100.40 Å
Total Rg total_rg	100.20 Å
Total atoms total_atoms	89544
Residues n_residues	11106
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	243.3 Å
Rg (real space) rg_real	98.35 Å
Rg uncertainty (real space) rg_real_error	0.47 Å
I(0) (real space) i0_real	1.8640e+10
I(0) uncertainty (real space) i0_real_error	3.8060e+08
Rg (reciprocal space) rg_reciprocal	102.80 Å
I(0) (reciprocal space) i0_reciprocal	19470000000.0000
Solution quality estimate total_estimate	0.8988
Solution quality rating solution_quality	GOOD a GOOD solution
P(r) peaks n_peaks	1
Primary peak position r_peak_primary	129.8 Å
Skewness Skewness skewness	-0.004
Kurtosis Kurtosis kurtosis	-0.683
Angular range angular_range	— – 0.0750 Å⁻¹
Current regularization parameter α current_alpha	0.6348
Highest regularization parameter α highest_alpha	431400000.0000
Real-space data points n_real_points	16
GNOM version gnom_version	4.1.3
Quality Criteria quality_criteria	AN1: 0.000; Oscil: 0.968; Stabil: 0.957; Sysdev: 1.000; Positv: 1.000; Valcen: 0.984; Smooth: 0.000

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5. Crystallography and Experiment 5. Crystallography & Experiment

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6. Entities and Polymers Entities & Polymers (4)

Entity 1 Entity 1 polymer

Description description	Acetylcholine receptor beta subunit
Molecular weight formula_weight	56123.6 kDa
Source method src_method	nat
Copy count entity_count	6

Polymer Polymer

Polymer type type	polypeptide(L)
Chain IDs strand_id	0,B,G,L,Q,V
Atom count atom_count	89544

MEDVRRMALGLVVMMALALSGVGASVMEDTLLSVLFENYNPKVRPSQTVGDKVTVRVGLTLTSLLILNEKNEEMTTSVFLNLAWTDYRLQWDPAAYEGIKDLSIPSDDVWQPDIVLMNNNDGSFEITLHVNVLVQHTGAVSWHPSAIYRSSCTIKVMYFPFDWQNCTMVFKSYTYDTSEVILQHALDAKGEREVKEIMINQDAFTENGQWSIEHKPSRKNWRSDDPSYEDVTFYLIIQRKPLFYIVYTIVPCILISILAILVFYLPPDAGEKMSLSISALLALTVFLLLLADKVPETSLSVPIIISYLMFIMILVAFSVILSVVVLNLHHRSPNTHTMPNWIRQIFIETLPPFLWIQRPVTTPSPDSKPTIISRANDEYFIRKPAGDFVCPVDNARVAVQPERLFSEMKWHLNGLTQPVTLPQDLKEAVEAIKYIAEQLESASEFDDLKKDWQYVAMVADRLFLYIFITMCSIGTFSIFLDASHNVPPDNPFA

Entity 2 Entity 2 polymer

Description description	Acetylcholine receptor delta subunit
Molecular weight formula_weight	60017.7 kDa
Source method src_method	nat
Copy count entity_count	6

Polymer Polymer

Polymer type type	polypeptide(L)
Chain IDs strand_id	1,C,H,M,R,W

MGNIHFVYLLISCLYYSGCSGVNEEERLINDLLIVNKYNKHVRPVKHNNEVVNIALSLTLSNLISLKETDETLTTNVWMDHAWYDHRLTWNASEYSDISILRLRPELIWIPDIVLQNNNDGQYNVAYFCNVLVRPNGYVTWLPPAIFRSSCPINVLYFPFDWQNCSLKFTALNYNANEISMDLMTDTIDGKDYPIEWIIIDPEAFTENGEWEIIHKPAKKNIYGDKFPNGTNYQDVTFYLIIRRKPLFYVINFITPCVLISFLAALAFYLPAESGEKMSTAICVLLAQAVFLLLTSQRLPETALAVPLIGKYLMFIMSLVTGVVVNCGIVLNFHFRTPSTHVLSTRVKQIFLEKLPRILHMSRVDEIEQPDWQNDLKLRRSSSVGYISKAQEYFNIKSRSELMFEKQSERHGLVPRVTPRIGFGNNNENIAASDQLHDEIKSGIDSTNYIVKQIKEKNAYDEEVGNWNLVGQTIDRLSMFIITPVMVLGTIFIFVMGNFNRPPAKPFEGDPFDYSSDHPRCA

Entity 3 Entity 3 polymer

Description description	Acetylcholine receptor subunit alpha
Molecular weight formula_weight	52845.5 kDa
Source method src_method	nat
Copy count entity_count	12

Polymer Polymer

Polymer type type	polypeptide(L)
Chain IDs strand_id	2,A,D,F,I,K,N,P,S,U,X,Z

MILCSYWHVGLVLLLFSCCGLVLGSEHETRLVANLLENYNKVIRPVEHHTHFVDITVGLQLIQLINVDEVNQIVETNVRLRQQWIDVRLRWNPADYGGIKKIRLPSDDVWLPDLVLYNNADGDFAIVHMTKLLLDYTGKIMWTPPAIFKSYCEIIVTHFPFDQQNCTMKLGIWTYDGTKVSISPESDRPDLSTFMESGEWVMKDYRGWKHWVYYTCCPDTPYLDITYHFIMQRIPLYFVVNVIIPCLLFSFLTVLVFYLPTDSGEKMTLSISVLLSLTVFLLVIVELIPSTSSAVPLIGKYMLFTMIFVISSIIVTVVVINTHHRSPSTHTMPQWVRKIFINTIPNVMFFSTMKRASKEKQENKIFADDIDISDISGKQVTGEVIFQTPLIKNPDVKSAIEGVKYIAEHMKSDEESSNAAEEWKYVAMVIDHILLCVFMLICIIGTVSVFAGRLIELSQEG

Entity 4 Entity 4 polymer

Description description	Acetylcholine receptor gamma subunit
Molecular weight formula_weight	58118.0 kDa
Source method src_method	nat
Copy count entity_count	6

Polymer Polymer

Polymer type type	polypeptide(L)
Chain IDs strand_id	3,E,J,O,T,Y

MVLTLLLIICLALEVRSNEEGRLIEKLLGDYDKRIKPAKTLDHVIDVTLKLTLTNLISLNEKEEALTTNVWIEIQWNDYRLSWNTSEYEGIDLVRIPSELLWLPDVVLENNVDGQFEVAYYANVLVYNDGSMYWLPPAIYRSTCPIAVTYFPFDWQNCSLVFRSQTYNAHEVNLQLSAEEGEVVEWIHIDPEDFTENGEWTIRHRPAKKNYNWQLTKDDIDFQEIIFFLIIQRKPLFYIINIIAPCVLISSLVVLVYFLPAQAGGQKCTLSISVLLAQTIFLFLIAQKVPETSLNVPLIGKYLIFVMFVSLVIVTNCVIVLNVSLRTPNTHSLSEKIKHLFLEFLPKYLGMHLEPSEETPEKPQPRRRSSFGIMIKAEEYILKKPRSELMFEEQKDRHGLKRVNKMTSDIDIGTTVDLYKDLANFAPEIKSCVEACNFIAKSTKEQNDSGSENENWVLIGKVIDKACFWIALLLFSLGTLAIFLTGHLNQVPEFPFPGDPRKYVP

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8. Citations (1)

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Unit-cell length a length_a	1.000 Å
Unit-cell length b length_b	1.000 Å
Unit-cell length c length_c	1.000 Å
Unit-cell angle α angle_alpha	90.00 °
Unit-cell angle β angle_beta	90.00 °
Unit-cell angle γ angle_gamma	90.00 °
Molecules per unit cell Z z_pdb	1

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

Resolution resolution	50.000 Å
Low-resolution limit resolution_low	— Å
R factor r_factor	—
R_work r_work	—
R_free r_free	—

Resolution resolution	50.00 Å
Resolution测定方法 resolution_method	MAXIMUM LIKELIHOOD SUBTOMOGRAM AVERAGING
颗粒数 num_particles	3564

fit	/app/data/saxs_computation/bo/4bog/4bog.fit
pddf	/app/data/pr_computation/bo/4bog/4bog.pr.out
profile	/app/data/saxs_computation/bo/4bog/4bog.dat

The structure and super-organization of acetylcholine receptor-rapsyn complexes

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

Acetylcholine receptor beta subunit

State in the Current Structure

Other States of the Same Protein in the Database

Acetylcholine receptor delta subunit

State in the Current Structure

Other States of the Same Protein in the Database

Acetylcholine receptor subunit alpha

State in the Current Structure

Other States of the Same Protein in the Database

Acetylcholine receptor gamma subunit

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

冷冻电镜 EM 3D

6. Entities and Polymers Entities & Polymers (4)

Entity 1 Entity 1 polymer

Polymer Polymer

Entity 2 Entity 2 polymer

Polymer Polymer

Entity 3 Entity 3 polymer

Polymer Polymer

Entity 4 Entity 4 polymer

Polymer Polymer

8. Citations (1)

9. Files and Curves (10)

Files (7)

Curves (3)