SAXSdb — 1abt

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

ALPHA-BUNGAROTOXIN

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 × 2 PDB declaration: dimeric（2） Consistent with protein copy count	Chain A； UniProt 1–74	Not recorded	NICOTINIC RECEPTOR PEPTIDE × 1 （P02710）	SOLUTION NMR mmCIF provides none of the parsed experimental conditions	Resolution not provided

Other States of the Same Protein in the Database

Each row is a biological assembly of the same UniProt protein in another PDB entry. The “Difference from current entry” column identifies evidence-level differences; no tag means the currently parsed fields agree.

Other PDB	Difference from Current Entry 1ABT	Assembly / Oligomeric State	Construct	Mutations and Modifications	Ligands, Ions and Non-polymers	Method and Experimental Conditions	Structure Quality
1BXP SOLUTION NMR STRUCTURE OF THE COMPLEX OF ALPHA-BUNGAROTOXIN WITH A LIBRARY DERIVED PEPTIDE, 20 STRUCTURES Deposited 1998-08-23	Different experimental conditions	Assembly 1 Protein heterocomplex Heteromer；Protein × 2 PDB declaration: dimeric	Chain A 1–74（74 aa）	Not recorded	No recorded non-water small molecule	SOLUTION NMR NMR measurement conditions pH 5.8；303 K	Resolution not provided
1HC9 alpha-bungarotoxin complexed with high affinity peptide Deposited 2001-05-02	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 B 22–95（74 aa）	Not recorded	IOD IODIDE ION × 1	X-RAY DIFFRACTION X-ray crystallization conditions pH 7.5；40% PEG 3350, 0.1M PIPES BUFFER PH 7.5	Resolution 1.80 Å R-free 0.235
1HOY NMR STRUCTURE OF THE COMPLEX BETWEEN A-BUNGAROTOXIN AND A MIMOTOPE OF THE NICOTINIC ACETYLCHOLINE RECEPTOR Deposited 2000-12-12	Different experimental conditions	Assembly 1 Protein heterocomplex Heteromer；Protein × 2 PDB declaration: dimeric	Chain A 1–74（74 aa）	Not recorded	No recorded non-water small molecule	SOLUTION NMR NMR measurement conditions pH 5.67；303 K；Pressure ambient NMR sample composition 0.5mM a-bungarotoxin;0.5mM peptide; 90% H2O, 10% D2O \| 90% H2O/10% D2O	Resolution not provided
1IDG THE NMR SOLUTION STRUCTURE OF THE COMPLEX FORMED BETWEEN ALPHA-BUNGAROTOXIN AND AN 18MER COGNATE PEPTIDE Deposited 2001-04-04	Different experimental conditions	Assembly 1 Protein heterocomplex Heteromer；Protein × 2 PDB declaration: dimeric	Chain A 1–74（74 aa）	Not recorded	No recorded non-water small molecule	SOLUTION NMR NMR measurement conditions pH 4；308 K；Pressure ambient NMR sample composition 2.1 mM alpha-Bungarotoxin/alpha18mer complex, alpha18mer is 15N labeled, 50 mM perdeuterated potassium acetate buffer (pH 4.0) with 5% D2O and 0.05% sodium azide \| 95% H2O/5% D2O	Resolution not provided
1IDH THE NMR SOLUTION STRUCTURE OF THE COMPLEX FORMED BETWEEN ALPHA-BUNGAROTOXIN AND AN 18MER COGNATE PEPTIDE Deposited 2001-04-04	Different experimental conditions	Assembly 1 Protein heterocomplex Heteromer；Protein × 2 PDB declaration: dimeric	Chain A 1–74（74 aa）	Not recorded	No recorded non-water small molecule	SOLUTION NMR NMR measurement conditions pH 4；308 K；Pressure ambient NMR sample composition 2.1 mM alpha-Bungarotoxin/alpha18mer complex, alpha18mer is 15N labeled, 50 mM perdeuterated potassium acetate buffer (pH 4.0) with 5% D2O and 0.05% sodium azide \| 95% H2O/5% D2O	Resolution not provided
1IDI THE NMR SOLUTION STRUCTURE OF ALPHA-BUNGAROTOXIN Deposited 2001-04-04	Different oligomeric state Different experimental conditions	Assembly 1 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric	Chain A 1–74（74 aa）	Not recorded	No recorded non-water small molecule	SOLUTION NMR NMR measurement conditions pH 4；308 K；Pressure ambient NMR sample composition 2.0 mM free alpha-Bungarotoxin, 50 mM perdeuterated potassium acetate buffer (pH 4.0) with 5% D2O and 0.05% SODIUM azide \| 95% H2O/5% D2O	Resolution not provided
1IDL THE NMR SOLUTION STRUCTURE OF ALPHA-BUNGAROTOXIN Deposited 2001-04-04	Different oligomeric state Different experimental conditions	Assembly 1 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric	Chain A 1–74（74 aa）	Not recorded	No recorded non-water small molecule	SOLUTION NMR NMR measurement conditions pH 4；308 K；Ionic strength (raw mmCIF value) 29 mM；Pressure ambient NMR sample composition 2.0 mM free alpha-Bungarotoxin, 50 mM perdeuterated potassium acetate buffer (pH 4.0) with 5% D2O and 0.05% sodium azide \| 95% H2O/5% D2O	Resolution not provided
1IK8 NMR structure of Alpha-Bungarotoxin Deposited 2001-05-03	Different oligomeric state Different experimental conditions	Assembly 1 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric	Chain A 1–74（74 aa）	Not recorded	No recorded non-water small molecule	SOLUTION NMR NMR measurement conditions pH 5.67；303 K NMR sample composition 0.5mM alpha-bungarotoxin; 90% H2O, 10% D2O \| 90% H2O/10% D2O	Resolution not provided
1IKC NMR Structure of alpha-Bungarotoxin Deposited 2001-05-03	Different oligomeric state Different experimental conditions	Assembly 1 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric	Chain A 1–74（74 aa）	Not recorded	No recorded non-water small molecule	SOLUTION NMR NMR measurement conditions pH 5.67；303 K NMR sample composition 0.5mM alpha-bungarotoxin; 90% H2O, 10% D2O \| 90% H2O/10% D2O	Resolution not provided
1JBD NMR Structure of the Complex Between alpha-bungarotoxin and a Mimotope of the Nicotinic Acetylcholine Receptor Deposited 2001-06-04	Different experimental conditions	Assembly 1 Protein heterocomplex Heteromer；Protein × 2 PDB declaration: dimeric	Chain A 1–74（74 aa）	Not recorded	No recorded non-water small molecule	SOLUTION NMR NMR measurement conditions pH 5.67；300 K；Pressure ambient NMR sample composition 0.5MM ALPHA-BUNGAROTOXIN; 90% H2O, 10% D2O \| 90% H2O/10% D2O	Resolution not provided
1KC4 NMR Structural Analysis of the Complex Formed Between alpha-Bungarotoxin and the Principal alpha-Neurotoxin Binding Sequence on the alpha7 Subunit of a Neuronal Nicotinic Acetylcholine Receptor Deposited 2001-11-07	Different experimental conditions	Assembly 1 Protein heterocomplex Heteromer；Protein × 2 PDB declaration: dimeric	Chain A 1–74（74 aa）	Not recorded	No recorded non-water small molecule	SOLUTION NMR NMR measurement conditions pH 5.5；308 K；Pressure ambient NMR sample composition 1.6 mM alpha-bungarotoxin/[U-15N]-alpha 7 19mer complex 30 mM sodium phosphate, pH 5.5 50 micromolar sodium azide 50 micromolar TMSP \| 95% H2O/5% D2O NMR sample composition 1.6 mM alpha-bungarotoxin/[U-15N]-alpha 7 19mer complex 30 mM sodium phosphate, pH 5.5 50 micromolar sodium azide 50 micromolar TMSP \| 99.9% D2O	Resolution not provided
1KFH Solution Structure of alpha-Bungarotoxin by NMR Spectroscopy Deposited 2001-11-20	Different oligomeric state Different experimental conditions	Assembly 1 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric	Chain A 1–74（74 aa）	Not recorded	No recorded non-water small molecule	SOLUTION NMR NMR measurement conditions pH 5.79；298 K；Ionic strength (raw mmCIF value) no buffers, pH adjusted w/HCl and NaOH；Pressure ambient NMR measurement conditions pH 5.79；308 K；Ionic strength (raw mmCIF value) no buffers, pH adjusted w/DCl and NaOD；Pressure ambient NMR sample composition 4mM alpha-Bungarotoxin pH 5.79 at 288, 298, and 308 degrees K \| 95% H2O/5% D2O NMR sample composition 4mM alpha-Bungarotoxin pH 5.79 \| 99.9% D2O	Resolution not provided
1KL8 NMR STRUCTURAL ANALYSIS OF THE COMPLEX FORMED BETWEEN ALPHA-BUNGAROTOXIN AND THE PRINCIPAL ALPHA-NEUROTOXIN BINDING SEQUENCE ON THE ALPHA7 SUBUNIT OF A NEURONAL NICOTINIC ACETYLCHOLINE RECEPTOR Deposited 2001-12-11	Different experimental conditions	Assembly 1 Protein heterocomplex Heteromer；Protein × 2 PDB declaration: dimeric	Chain A 1–74（74 aa）	Not recorded	No recorded non-water small molecule	SOLUTION NMR NMR measurement conditions pH 5.5；308 K；Pressure AMBIENT NMR sample composition 1.6 MM ALPHA-BUNGAROTOXIN 15N]-ALPHA 7 19MER COMPLEX MM SODIUM PHOSPHATE, PH 5. MICROMOLAR SODIUM AZIDE 50 MICROMOLAR TMSP \| 95% H2O/5% D2O	Resolution not provided
1L4W NMR structure of an AChR-peptide (Torpedo Californica, alpha-subunit residues 182-202) in complex with alpha-Bungarotoxin Deposited 2002-03-06	Different experimental conditions	Assembly 1 Protein heterocomplex Heteromer；Protein × 2 PDB declaration: dimeric	Chain A 1–74（74 aa）	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 experimental conditions	Assembly 1 Protein heterocomplex Heteromer；Protein × 2 PDB declaration: dimeric	Chain A 1–74（74 aa）	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
1RGJ NMR STRUCTURE OF THE COMPLEX BETWEEN ALPHA-BUNGAROTOXIN AND MIMOTOPE OF THE NICOTINIC ACETYLCHOLINE RECEPTOR WITH ENHANCED ACTIVITY Deposited 2003-11-12	Different experimental conditions	Assembly 1 Protein heterocomplex Heteromer；Protein × 2 PDB declaration: dimeric	Chain A 1–74（74 aa）	Not recorded	No recorded non-water small molecule	SOLUTION NMR NMR measurement conditions pH 5.6；303 K；Pressure AMBIENT NMR sample composition 2MM ALPHA-BUNGAROTOXIN, 2MM PEPTIDE \| 90% H2O/10% D2O	Resolution not provided
2ABX THE CRYSTAL STRUCTURE OF ALPHA-BUNGAROTOXIN AT 2.5 ANGSTROMS RESOLUTION. RELATION TO SOLUTION STRUCTURE AND BINDING TO ACETYLCHOLINE RECEPTOR Deposited 1986-02-19	Different construct Different mutation/modification Different oligomeric state Different experimental method Different structure-quality metrics	Assembly 1 Protein homooligomer Homooligomer；Protein × 2 PDB declaration: dimeric	Chain A 1–74（74 aa） Chain B 1–74（74 aa）	Not recorded	No recorded non-water small molecule	X-RAY DIFFRACTION mmCIF provides none of the parsed conditions	Resolution 2.50 Å
2BTX SOLUTION NMR STRUCTURE OF THE COMPLEX OF ALPHA-BUNGAROTOXIN WITH A LIBRARY DERIVED PEPTIDE, NMR, MINIMIZED AVERAGE STRUCTURE Deposited 1998-08-23	Different experimental conditions	Assembly 1 Protein heterocomplex Heteromer；Protein × 2 PDB declaration: dimeric	Chain A 1–74（74 aa）	Not recorded	No recorded non-water small molecule	SOLUTION NMR NMR measurement conditions pH 5.8；303 K	Resolution not provided
6UWZ Cryo-EM structure of Torpedo acetylcholine receptor in complex with alpha-bungarotoxin Deposited 2019-11-06	Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental method Different experimental conditions Different structure-quality metrics	Assembly 1 Other combination Heteromer；Protein × 7 PDB declaration: heptameric	Chain F 22–95（74 aa） Chain G 22–95（74 aa）	Not recorded	POV (2S)-3-(hexadecanoyloxy)-2-[(9Z)-octadec-9-enoyloxy]propyl 2-(trimethylammonio)ethyl phosphate × 5 NAG 2-acetamido-2-deoxy-beta-D-glucopyranose × 3 OCT N-OCTANE × 1	ELECTRON MICROSCOPY cryo-EM buffer pH 7.4 cryo-EM vitrification conditions Cryogen ETHANE	Resolution 2.69 Å
8DA1 Crystal structure of Krait alpha-neurotoxin in complex with Centi-LNX-D09 antibody Deposited 2022-06-12	Different construct Different oligomeric state Different experimental method Different experimental conditions Different structure-quality metrics	Assembly 1 Protein heterocomplex Heteromer；Protein × 3 PDB declaration: trimeric	Chain I 22–95（74 aa）	Not recorded	No recorded non-water small molecule	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION；293 K；40% PEG 400, 5% PEG 3350, 0.1M sodium acetate pH 5.5	Resolution 2.67 Å R-free 0.253
9FYS D11 mAbs bound to alpha-Bungarotoxin Deposited 2024-07-03	Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental method Different experimental conditions Different structure-quality metrics	Assembly 1 Protein heterocomplex Heteromer；Protein × 6 PDB declaration: hexameric	Chain X 1–95（95 aa） Chain Z 1–95（95 aa）	Not recorded	MES 2-(N-MORPHOLINO)-ETHANESULFONIC ACID × 1	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION, SITTING DROP；pH 6.5；293 K；0.1 M MES: NaOH, 12 % PEG 20000, pH 6.5	Resolution 1.32 Å R-free 0.192
9GU0 Human adult muscle nAChR in resting state in detergent with alpha-bungarotoxin Deposited 2024-09-18	Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental method Different experimental conditions Different structure-quality metrics	Assembly 1 Insufficient information Heteromer；Protein × 11 PDB declaration: 11-meric	Chain I 22–95（74 aa） Chain J 22–95（74 aa）	Not recorded	NAG 2-acetamido-2-deoxy-beta-D-glucopyranose × 1	ELECTRON MICROSCOPY cryo-EM buffer pH 7.5；20 mM HEPES pH 7.5, 150 mM NaCl, 0.013% DDM, 0.0013% CHS cryo-EM vitrification conditions Cryogen ETHANE；blot time 2s, blot force -10	Resolution 2.96 Å
9GU1 Human adult muscle nAChR in resting state in nanodisc with alpha-bungarotoxin Deposited 2024-09-18	Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental method Different experimental conditions Different structure-quality metrics	Assembly 1 Insufficient information Heteromer；Protein × 11 PDB declaration: 11-meric	Chain I 22–95（74 aa） Chain J 22–95（74 aa）	Not recorded	NAG 2-acetamido-2-deoxy-beta-D-glucopyranose × 1 CU COPPER (II) ION × 1	ELECTRON MICROSCOPY cryo-EM buffer pH 7.5；20 mM HEPES pH 7.5, 150 mM NaCl cryo-EM vitrification conditions Cryogen ETHANE；2.5 uL of sample was frozen; blot time 4.5 s, blot force -10	Resolution 2.48 Å
9HUB D11 mAbs bound to alpha-Bungarotoxin at pH 7.5 Deposited 2024-12-21	Different construct Different oligomeric state Different ligand/ion Different experimental method Different experimental conditions Different structure-quality metrics	Assembly 1 Protein heterocomplex Heteromer；Protein × 3 PDB declaration: trimeric	Chain X 1–95（95 aa）	Not recorded	EDO 1,2-ETHANEDIOL × 5	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION；pH 7.5；293 K；0.1 M HEPES pH 7.5, 70% (v/v) MPD)	Resolution 1.33 Å R-free 0.195
9HUB D11 mAbs bound to alpha-Bungarotoxin at pH 7.5 Deposited 2024-12-21	Different construct Different oligomeric state Different ligand/ion Different experimental method Different experimental conditions Different structure-quality metrics	Assembly 2 Protein heterocomplex Heteromer；Protein × 3 PDB declaration: trimeric	Chain Z 1–95（95 aa）	Not recorded	EDO 1,2-ETHANEDIOL × 2	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION；pH 7.5；293 K；0.1 M HEPES pH 7.5, 70% (v/v) MPD)	Resolution 1.33 Å R-free 0.195

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

View Construct and Data Evidence

UniProt name	NXL1A_BUNMU
Isoform	—
PDB entities	1
Chains and sequence ranges	Author chain A； PDBConstruct 1–74； UniProt 1–74

NICOTINIC RECEPTOR PEPTIDE

OrganismNot specified

UniProt P02710

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 209–220	Not recorded	ALPHA-BUNGAROTOXIN × 1 （P60615）	SOLUTION NMR mmCIF provides none of the parsed experimental conditions	Resolution not provided

Other States of the Same Protein in the Database

Each row is a biological assembly of the same UniProt protein in another PDB entry. The “Difference from current entry” column identifies evidence-level differences; no tag means the currently parsed fields agree.

Other PDB	Difference from Current Entry 1ABT	Assembly / Oligomeric State	Construct	Mutations and Modifications	Ligands, Ions and Non-polymers	Method and Experimental Conditions	Structure Quality
1DXZ M2 TRANSMEMBRANE SEGMENT OF ALPHA-SUBUNIT OF NICOTINIC ACETYLCHOLINE RECEPTOR FROM TORPEDO CALIFORNICA, NMR, 20 STRUCTURES Deposited 2000-01-20	Different construct Different mutation/modification Different oligomeric state Different experimental conditions	Assembly 1 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric	Chain A 260–291（32 aa） Fragment：M2 TRANSMEMBRANE SEGMENT	Non-standard monomer：Yes (specific site not provided by mmCIF)	No recorded non-water small molecule	SOLUTION NMR NMR measurement conditions pH 4；303 K；Ionic strength (raw mmCIF value) 0.1 M LICLO4；Pressure 1 NMR sample composition CDCL3/CD3OH=1/1 WITH 0.1 M LICLO4	Resolution not provided
1IDG THE NMR SOLUTION STRUCTURE OF THE COMPLEX FORMED BETWEEN ALPHA-BUNGAROTOXIN AND AN 18MER COGNATE PEPTIDE Deposited 2001-04-04	Different construct Different mutation/modification Different experimental conditions	Assembly 1 Protein heterocomplex Heteromer；Protein × 2 PDB declaration: dimeric	Chain B 205–222（18 aa）	Non-standard monomer：Yes (specific site not provided by mmCIF)	No recorded non-water small molecule	SOLUTION NMR NMR measurement conditions pH 4；308 K；Pressure ambient NMR sample composition 2.1 mM alpha-Bungarotoxin/alpha18mer complex, alpha18mer is 15N labeled, 50 mM perdeuterated potassium acetate buffer (pH 4.0) with 5% D2O and 0.05% sodium azide \| 95% H2O/5% D2O	Resolution not provided
1IDH THE NMR SOLUTION STRUCTURE OF THE COMPLEX FORMED BETWEEN ALPHA-BUNGAROTOXIN AND AN 18MER COGNATE PEPTIDE Deposited 2001-04-04	Different construct Different mutation/modification Different experimental conditions	Assembly 1 Protein heterocomplex Heteromer；Protein × 2 PDB declaration: dimeric	Chain B 205–222（18 aa）	Non-standard monomer：Yes (specific site not provided by mmCIF)	No recorded non-water small molecule	SOLUTION NMR NMR measurement conditions pH 4；308 K；Pressure ambient NMR sample composition 2.1 mM alpha-Bungarotoxin/alpha18mer complex, alpha18mer is 15N labeled, 50 mM perdeuterated potassium acetate buffer (pH 4.0) with 5% D2O and 0.05% sodium azide \| 95% H2O/5% D2O	Resolution not provided
1LXG Solution structure of alpha-cobratoxin complexed with a cognate peptide (structure ensemble) Deposited 2002-06-05	Different construct Different mutation/modification Different experimental conditions	Assembly 1 Protein heterocomplex Heteromer；Protein × 2 PDB declaration: dimeric	Chain B 205–222（18 aa）	Non-standard monomer：Yes (specific site not provided by mmCIF)	No recorded non-water small molecule	SOLUTION NMR NMR measurement conditions pH 4；308 K；Pressure AMBIENT NMR sample composition 1.6 mM alpha-cobratoxin/alpha18-mer complex, alpha18-mer is U-15N, 50 mM perdeuterated potassium acetate buffer (pH 4.0) with 5% D2O and 0.05% sodium azide \| 95% H2O/5% D2O	Resolution not provided
1LXH Solution structure of alpha-cobratoxin complexed with a cognate peptide (minimized average structure) Deposited 2002-06-05	Different construct Different mutation/modification Different experimental conditions	Assembly 1 Protein heterocomplex Heteromer；Protein × 2 PDB declaration: dimeric	Chain B 205–222（18 aa）	Non-standard monomer：Yes (specific site not provided by mmCIF)	No recorded non-water small molecule	SOLUTION NMR NMR measurement conditions pH 4；308 K；Ionic strength (raw mmCIF value) NULL；Pressure AMBIENT NMR sample composition 1.6 mM alpha-cobratoxin/alpha18-mer complex, alpha18-mer is U-15N, 50 mM perdeuterated potassium acetate buffer (pH 4.0) with 5% D2O and 0.05% sodium azide \| 95% H2O/5% D2O	Resolution not provided
1TOR MOLECULAR DYNAMICS SIMULATION FROM 2D-NMR DATA OF THE FREE ACHR MIR DECAPEPTIDE AND THE ANTIBODY-BOUND [A76]MIR ANALOGUE Deposited 1995-10-11	Different construct Different oligomeric state	Assembly 1 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric	Chain A 91–100（10 aa）	Not recorded	No recorded non-water small molecule	SOLUTION NMR mmCIF provides none of the parsed conditions	Resolution not provided
1TOS TORPEDO CALIFORNICA ACHR RECEPTOR [ALA76] ANALOGUE COMPLEXED WITH THE ANTI-ACETYLCHOLINE MAB6 MONOCLONAL ANTIBODY Deposited 1995-10-11	Different construct Different oligomeric state	Assembly 1 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric	Chain A 91–99（9 aa） Fragment：ALPHA 67-76 DOMAIN OF THE ACETYLCHOLINE RECEPTOR	Not recorded	No recorded non-water small molecule	SOLUTION NMR mmCIF provides none of the parsed conditions	Resolution not provided
3MRA M3 TRANSMEMBRANE SEGMENT OF ALPHA-SUBUNIT OF NICOTINIC ACETYLCHOLINE RECEPTOR FROM TORPEDO CALIFORNICA, NMR, 15 STRUCTURES Deposited 1997-07-15	Different construct Different oligomeric state Different experimental conditions	Assembly 1 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric	Chain A 301–325（25 aa） Fragment：M3 TRANSMEMBRANE SEGMENT	Not recorded	No recorded non-water small molecule	SOLUTION NMR NMR measurement conditions pH 3.5；303 K	Resolution not provided
6UWZ Cryo-EM structure of Torpedo acetylcholine receptor in complex with alpha-bungarotoxin Deposited 2019-11-06	Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental method Different experimental conditions Different structure-quality metrics	Assembly 1 Other combination Heteromer；Protein × 7 PDB declaration: heptameric	Chain A 25–461（437 aa） Chain D 25–461（437 aa）	Not recorded	POV (2S)-3-(hexadecanoyloxy)-2-[(9Z)-octadec-9-enoyloxy]propyl 2-(trimethylammonio)ethyl phosphate × 5 NAG 2-acetamido-2-deoxy-beta-D-glucopyranose × 3 OCT N-OCTANE × 1	ELECTRON MICROSCOPY cryo-EM buffer pH 7.4 cryo-EM vitrification conditions Cryogen ETHANE	Resolution 2.69 Å
7QKO Torpedo muscle-type nicotinic acetylcholine receptor - Resting conformation Deposited 2021-12-18	Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental method Different experimental conditions Different structure-quality metrics	Assembly 1 Other combination Heteromer；Protein × 5 PDB declaration: pentameric	Chain A 25–461（437 aa） Chain D 25–461（437 aa）	Not recorded	POV (2S)-3-(hexadecanoyloxy)-2-[(9Z)-octadec-9-enoyloxy]propyl 2-(trimethylammonio)ethyl phosphate × 9	ELECTRON MICROSCOPY cryo-EM buffer pH 7.4 cryo-EM vitrification conditions Cryogen ETHANE	Resolution 2.90 Å
7QL5 Torpedo muscle-type nicotinic acetylcholine receptor - nicotine-bound conformation Deposited 2021-12-19	Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental method Different experimental conditions Different structure-quality metrics	Assembly 1 Other combination Heteromer；Protein × 5 PDB declaration: pentameric	Chain A 25–461（437 aa） Chain D 25–461（437 aa）	Not recorded	NCT (S)-3-(1-METHYLPYRROLIDIN-2-YL)PYRIDINE × 2 POV (2S)-3-(hexadecanoyloxy)-2-[(9Z)-octadec-9-enoyloxy]propyl 2-(trimethylammonio)ethyl phosphate × 11 NAG 2-acetamido-2-deoxy-beta-D-glucopyranose × 1	ELECTRON MICROSCOPY cryo-EM buffer pH 7.4 cryo-EM vitrification conditions Cryogen ETHANE	Resolution 2.50 Å
7QL6 Torpedo muscle-type nicotinic acetylcholine receptor - carbamylcholine-bound conformation Deposited 2021-12-19	Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental method Different experimental conditions Different structure-quality metrics	Assembly 1 Other combination Heteromer；Protein × 5 PDB declaration: pentameric	Chain A 25–461（437 aa） Chain D 25–461（437 aa）	Not recorded	CCE 2-[(AMINOCARBONYL)OXY]-N,N,N-TRIMETHYLETHANAMINIUM × 2 NAG 2-acetamido-2-deoxy-beta-D-glucopyranose × 1	ELECTRON MICROSCOPY cryo-EM buffer pH 7.4 cryo-EM vitrification conditions Cryogen ETHANE	Resolution 3.23 Å
7SMM Cryo-EM structure of Torpedo acetylcholine receptor in apo form Deposited 2021-10-26	Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental method Different experimental conditions Different structure-quality metrics	Assembly 1 Other combination Heteromer；Protein × 5 PDB declaration: pentameric	Chain A 25–461（437 aa） Chain D 25–461（437 aa）	Not recorded	POV (2S)-3-(hexadecanoyloxy)-2-[(9Z)-octadec-9-enoyloxy]propyl 2-(trimethylammonio)ethyl phosphate × 8 CLR CHOLESTEROL × 3 NAG 2-acetamido-2-deoxy-beta-D-glucopyranose × 3 DD9 nonane × 1	ELECTRON MICROSCOPY cryo-EM buffer pH 7.4 cryo-EM vitrification conditions Cryogen ETHANE	Resolution 2.50 Å
7SMQ Cryo-EM structure of Torpedo acetylcholine receptor in apo form with added cholesterol Deposited 2021-10-26	Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental method Different experimental conditions Different structure-quality metrics	Assembly 1 Other combination Heteromer；Protein × 5 PDB declaration: pentameric	Chain A 25–461（437 aa） Chain D 25–461（437 aa）	Not recorded	POV (2S)-3-(hexadecanoyloxy)-2-[(9Z)-octadec-9-enoyloxy]propyl 2-(trimethylammonio)ethyl phosphate × 8 CLR CHOLESTEROL × 11 NAG 2-acetamido-2-deoxy-beta-D-glucopyranose × 3 DD9 nonane × 1	ELECTRON MICROSCOPY cryo-EM buffer pH 7.4 cryo-EM vitrification conditions Cryogen ETHANE	Resolution 2.74 Å
7SMR Cryo-EM structure of Torpedo acetylcholine receptor in complex with carbachol, desensitized state Deposited 2021-10-26	Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental method Different experimental conditions Different structure-quality metrics	Assembly 1 Other combination Heteromer；Protein × 5 PDB declaration: pentameric	Chain A 25–461（437 aa） Chain D 25–461（437 aa）	Not recorded	CCE 2-[(AMINOCARBONYL)OXY]-N,N,N-TRIMETHYLETHANAMINIUM × 2 CLR CHOLESTEROL × 3 POV (2S)-3-(hexadecanoyloxy)-2-[(9Z)-octadec-9-enoyloxy]propyl 2-(trimethylammonio)ethyl phosphate × 6 NAG 2-acetamido-2-deoxy-beta-D-glucopyranose × 2 DD9 nonane × 1	ELECTRON MICROSCOPY cryo-EM buffer pH 7.4 cryo-EM vitrification conditions Cryogen ETHANE	Resolution 2.77 Å
7SMS Cryo-EM structure of Torpedo acetylcholine receptor in complex with d-tubocurarine Deposited 2021-10-26	Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental method Different experimental conditions Different structure-quality metrics	Assembly 1 Other combination Heteromer；Protein × 5 PDB declaration: pentameric	Chain A 25–461（437 aa） Chain D 25–461（437 aa）	Not recorded	CLR CHOLESTEROL × 3 TC9 D-TUBOCURARINE × 4 POV (2S)-3-(hexadecanoyloxy)-2-[(9Z)-octadec-9-enoyloxy]propyl 2-(trimethylammonio)ethyl phosphate × 5	ELECTRON MICROSCOPY cryo-EM buffer pH 7.4 cryo-EM vitrification conditions Cryogen ETHANE	Resolution 3.18 Å
7SMT Cryo-EM structure of Torpedo acetylcholine receptor in complex with d-tubocurarine and carbachol Deposited 2021-10-26	Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental method Different experimental conditions Different structure-quality metrics	Assembly 1 Other combination Heteromer；Protein × 5 PDB declaration: pentameric	Chain A 25–461（437 aa） Chain D 25–461（437 aa）	Not recorded	CCE 2-[(AMINOCARBONYL)OXY]-N,N,N-TRIMETHYLETHANAMINIUM × 1 CLR CHOLESTEROL × 3 POV (2S)-3-(hexadecanoyloxy)-2-[(9Z)-octadec-9-enoyloxy]propyl 2-(trimethylammonio)ethyl phosphate × 5 NAG 2-acetamido-2-deoxy-beta-D-glucopyranose × 2 DD9 nonane × 1 TC9 D-TUBOCURARINE × 1	ELECTRON MICROSCOPY cryo-EM buffer pH 7.4 cryo-EM vitrification conditions Cryogen ETHANE	Resolution 2.56 Å
7Z14 Cryo-EM structure of Torpedo nicotinic acetylcholine receptor in complex with a short-chain neurotoxin. Deposited 2022-02-24	Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental method Different experimental conditions Different structure-quality metrics	Assembly 1 Other combination Heteromer；Protein × 7 PDB declaration: heptameric	Chain A 25–461（437 aa） Chain D 25–461（437 aa）	Not recorded	NAG 2-acetamido-2-deoxy-beta-D-glucopyranose × 1	ELECTRON MICROSCOPY cryo-EM buffer pH 7.5 cryo-EM vitrification conditions Cryogen ETHANE	Resolution 3.15 Å
8ESK Cryo-EM structure of Torpedo nicotinic acetylcholine receptor in complex with rocuronium, resting-like state Deposited 2022-10-14	Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental method Different experimental conditions Different structure-quality metrics	Assembly 1 Other combination Heteromer；Protein × 5 PDB declaration: pentameric	Chain A 25–461（437 aa） Chain D 25–461（437 aa）	Not recorded	RBR rocuronium × 2 POV (2S)-3-(hexadecanoyloxy)-2-[(9Z)-octadec-9-enoyloxy]propyl 2-(trimethylammonio)ethyl phosphate × 8 CLR CHOLESTEROL × 3 NAG 2-acetamido-2-deoxy-beta-D-glucopyranose × 3	ELECTRON MICROSCOPY cryo-EM buffer pH 7.4 cryo-EM vitrification conditions Cryogen ETHANE	Resolution 2.90 Å
8F2S Cryo-EM structure of Torpedo nicotinic acetylcholine receptor in complex with rocuronium, pore-blocked state Deposited 2022-11-08	Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental method Different experimental conditions Different structure-quality metrics	Assembly 1 Other combination Heteromer；Protein × 5 PDB declaration: pentameric	Chain A 25–457（433 aa） Chain D 25–457（433 aa）	Not recorded	RBR rocuronium × 3 POV (2S)-3-(hexadecanoyloxy)-2-[(9Z)-octadec-9-enoyloxy]propyl 2-(trimethylammonio)ethyl phosphate × 6 CLR CHOLESTEROL × 3 NAG 2-acetamido-2-deoxy-beta-D-glucopyranose × 3 DD9 nonane × 1	ELECTRON MICROSCOPY cryo-EM buffer pH 7.4 cryo-EM vitrification conditions Cryogen ETHANE	Resolution 2.90 Å
8F6Y Cryo-EM structure of Torpedo nicotinic acetylcholine receptor in complex with etomidate, desensitized-like state Deposited 2022-11-17	Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental method Different experimental conditions Different structure-quality metrics	Assembly 1 Other combination Heteromer；Protein × 5 PDB declaration: pentameric	Chain A 25–457（433 aa） Chain D 25–457（433 aa）	Not recorded	V8D Etomidate × 2 CHT CHOLINE ION × 2 CLR CHOLESTEROL × 3 NAG 2-acetamido-2-deoxy-beta-D-glucopyranose × 2 POV (2S)-3-(hexadecanoyloxy)-2-[(9Z)-octadec-9-enoyloxy]propyl 2-(trimethylammonio)ethyl phosphate × 6 DD9 nonane × 1	ELECTRON MICROSCOPY cryo-EM buffer pH 7.4 cryo-EM vitrification conditions Cryogen ETHANE	Resolution 2.79 Å
8F6Z Cryo-EM structure of Torpedo nicotinic acetylcholine receptor in complex with succinylcholine, desensitized-like state Deposited 2022-11-17	Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental method Different experimental conditions Different structure-quality metrics	Assembly 1 Other combination Heteromer；Protein × 5 PDB declaration: pentameric	Chain A 25–457（433 aa） Chain D 25–457（433 aa）	Not recorded	SCK 2,2'-[(1,4-DIOXOBUTANE-1,4-DIYL)BIS(OXY)]BIS(N,N,N-TRIMETHYLETHANAMINIUM) × 2 CLR CHOLESTEROL × 3 NAG 2-acetamido-2-deoxy-beta-D-glucopyranose × 2 POV (2S)-3-(hexadecanoyloxy)-2-[(9Z)-octadec-9-enoyloxy]propyl 2-(trimethylammonio)ethyl phosphate × 5 DD9 nonane × 1	ELECTRON MICROSCOPY cryo-EM buffer pH 7.4 cryo-EM vitrification conditions Cryogen ETHANE	Resolution 2.70 Å
8QQM nicotinic acetylcholine receptor in intact synaptic membrane Deposited 2023-10-05	Different construct Different mutation/modification Different oligomeric state Different experimental method Different experimental conditions Different structure-quality metrics	Assembly 1 Protein heterocomplex Heteromer；Protein × 5 PDB declaration: pentameric	Chain A 25–461（437 aa） Chain D 25–461（437 aa）	Not recorded	No recorded non-water small molecule	ELECTRON MICROSCOPY cryo-EM buffer pH 7 cryo-EM vitrification conditions Cryogen ETHANE	Resolution 4.70 Å
8YQN Torpedo acetylcholine receptor in complex with Erabutoxin A Deposited 2024-03-19	Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental method Different experimental conditions Different structure-quality metrics	Assembly 1 Other combination Heteromer；Protein × 7 PDB declaration: heptameric	Chain A 25–461（437 aa） Chain D 25–461（437 aa）	Not recorded	POV (2S)-3-(hexadecanoyloxy)-2-[(9Z)-octadec-9-enoyloxy]propyl 2-(trimethylammonio)ethyl phosphate × 4 NAG 2-acetamido-2-deoxy-beta-D-glucopyranose × 3 OCT N-OCTANE × 1 PLM PALMITIC ACID × 1	ELECTRON MICROSCOPY cryo-EM buffer pH 7.4 cryo-EM vitrification conditions Cryogen ETHANE	Resolution 2.27 Å
9E3E Torpedo muscle-type nicotinic acetylcholine receptor - Diliganded State Deposited 2024-10-23	Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental method Different experimental conditions Different structure-quality metrics	Assembly 1 Other combination Heteromer；Protein × 5 PDB declaration: pentameric	Chain A 25–461（437 aa） Chain D 25–461（437 aa）	Not recorded	ACH ACETYLCHOLINE × 2	ELECTRON MICROSCOPY cryo-EM buffer pH 7.4 cryo-EM vitrification conditions Cryogen ETHANE	Resolution 2.80 Å
9E3F Torpedo muscle-type nicotinic acetylcholine receptor - Unliganded State Deposited 2024-10-23	Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental method Different experimental conditions Different structure-quality metrics	Assembly 1 Other combination Heteromer；Protein × 5 PDB declaration: pentameric	Chain A 25–461（437 aa） Chain D 25–461（437 aa）	Not recorded	POV (2S)-3-(hexadecanoyloxy)-2-[(9Z)-octadec-9-enoyloxy]propyl 2-(trimethylammonio)ethyl phosphate × 8	ELECTRON MICROSCOPY cryo-EM buffer pH 7.4 cryo-EM vitrification conditions Cryogen ETHANE	Resolution 3.20 Å
9E3G Torpedo muscle-type nicotinic acetylcholine receptor - Monoliganded State Deposited 2024-10-23	Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental method Different experimental conditions Different structure-quality metrics	Assembly 1 Other combination Heteromer；Protein × 5 PDB declaration: pentameric	Chain A 25–461（437 aa） Chain D 25–461（437 aa）	Not recorded	ACH ACETYLCHOLINE × 1 POV (2S)-3-(hexadecanoyloxy)-2-[(9Z)-octadec-9-enoyloxy]propyl 2-(trimethylammonio)ethyl phosphate × 5	ELECTRON MICROSCOPY cryo-EM buffer pH 7.4；This map comes from particles from five datasets recorded in the presence of five sub-saturating concentrations of acetylcholine: 20, 50, 100, 250, and 500 nM. cryo-EM vitrification conditions Cryogen ETHANE	Resolution 3.13 Å
9NX2 Muscle-type nicotinic acetylcholine receptor bound to conotoxin ImII 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 Other combination Heteromer；Protein × 7 PDB declaration: heptameric	Chain A 25–458（434 aa） Chain D 25–458（434 aa）	Not recorded	CCE 2-[(AMINOCARBONYL)OXY]-N,N,N-TRIMETHYLETHANAMINIUM × 2 NAG 2-acetamido-2-deoxy-beta-D-glucopyranose × 2	ELECTRON MICROSCOPY cryo-EM buffer pH 7.4 cryo-EM vitrification conditions Cryogen ETHANE	Resolution 2.96 Å

28 other PDB entries and 28 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence

UniProt name	ACHA_TORCA
Isoform	—
PDB entities	2
Chains and sequence ranges	Author chain B； PDBConstruct 1–12； UniProt 209–220

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	1abt
Deposition date deposition_date	1993-11-17
Structure title title	NMR SOLUTION STRUCTURE OF AN ALPHA-BUNGAROTOXIN(SLASH)NICOTINIC RECEPTOR PEPTIDE COMPLEX
Keywords keywords	TOXIN; TOXIN
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	12.40 Å
Radius of gyration Rg (electron density) rg_electron	12.11 Å
Forward intensity I(0) i0	21764600.00
Molecular weight molecular_weight	35437.0 kDa
Excluded volume excluded_volume	43625 Å³
Envelope volume envelope_volume	18548 Å³
Hydration-shell volume shell_volume	11685 Å³
Envelope diameter envelope_diameter	43.4 Å
Shell Rg shell_rg	19.34 Å
Envelope Rg envelope_rg	13.88 Å
Shape Rg shape_rg	12.09 Å
Total Rg total_rg	12.85 Å
Total atoms total_atoms	4820
Residues n_residues	320
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	43.5 Å
Rg (real space) rg_real	12.38 Å
Rg uncertainty (real space) rg_real_error	0.43 Å
I(0) (real space) i0_real	2.1760e+07
I(0) uncertainty (real space) i0_real_error	2.3520e+05
Rg (reciprocal space) rg_reciprocal	12.39 Å
I(0) (reciprocal space) i0_reciprocal	21760000.0000
Solution quality estimate total_estimate	0.7867
Solution quality rating solution_quality	GOOD a GOOD solution
P(r) peaks n_peaks	3
Primary peak position r_peak_primary	14.3 Å
Skewness Skewness skewness	0.304
Kurtosis Kurtosis kurtosis	-0.303
Angular range angular_range	— – 0.5000 Å⁻¹
Current regularization parameter α current_alpha	0.0000
Highest regularization parameter α highest_alpha	259000.0000
Real-space data points n_real_points	80
GNOM version gnom_version	4.1.3
Quality Criteria quality_criteria	AN1: 0.000; Oscil: 0.768; Stabil: 0.998; Sysdev: 1.000; Positv: 1.000; Valcen: 0.926; 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)

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7. Fold Classification (SCOP + CATH) 2 domains

SCOP 2.08 (1 domains)

Domain ID domain_id	d1abta_
Class class	g — Small proteins
Fold Fold fold	g.7 — Snake toxin-like
Superfamily Superfamily superfamily	g.7.1 — Snake toxin-like
Family Family family	g.7.1.1 — Snake venom toxins

CATH v4.4 (1 domains)

Domain ID domain_id	1abtA00
Class class	2 — Mainly Beta
Architecture architecture	10 — Ribbon
Topology topology	60 — CD59
Homologous superfamily homologous superfamily	10 — CD59

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8. Citations (3)

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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	—

Description description	ALPHA-BUNGAROTOXIN
Molecular weight formula_weight	8005.3 kDa
Source method src_method	man
Copy count entity_count	1

Polymer type type	polypeptide(L)
Chain IDs strand_id	A
Atom count atom_count	4820

Description description	NICOTINIC RECEPTOR PEPTIDE
Molecular weight formula_weight	1517.7 kDa
Source method src_method	man
Copy count entity_count	1

NMR SOLUTION STRUCTURE OF AN ALPHA-BUNGAROTOXIN(SLASH)NICOTINIC RECEPTOR PEPTIDE COMPLEX

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

ALPHA-BUNGAROTOXIN

State in the Current Structure

Other States of the Same Protein in the Database

NICOTINIC RECEPTOR PEPTIDE

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

6. Entities and Polymers Entities & Polymers (2)

Entity 1 Entity 1 polymer

Polymer Polymer

Entity 2 Entity 2 polymer

Polymer Polymer

7. Fold Classification (SCOP + CATH) 2 domains

SCOP 2.08 (1 domains)

CATH v4.4 (1 domains)

8. Citations (3)

9. Files and Curves (10)

Files (7)

Curves (3)

fit	/app/data/saxs_computation/ab/1abt/1abt.fit
pddf	/app/data/pr_computation/ab/1abt/1abt.pr.out
profile	/app/data/saxs_computation/ab/1abt/1abt.dat