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1tor

MOLECULAR DYNAMICS SIMULATION FROM 2D-NMR DATA OF THE FREE ACHR MIR DECAPEPTIDE AND THE ANTIBODY-BOUND [A76]MIR ANALOGUE

Method: SOLUTION NMR
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1. Protein Identity and Related Structures Protein Identity & Related Structures

ACETYLCHOLINE RECEPTOR, MAIN IMMUNOGENIC REGION

OrganismNot specified

UniProt P02710

State in the Current Structure

Assembly Physical composition Protein state Molecular copy count Associated components Data consistency
1 Protein monomer Monomer Protein 1 No other associated polymer Consistent with protein count

Other States of the Same Protein in the Database

Monomer
1dxz 1tor 1tos 3mra

4 assemblies

Homodimer

None

Homotetramer

None

Other homooligomers

None

Heteromeric or nucleic-acid complex
1abt 1idg 1idh 1lxg 1lxh 6uwz 7qko 7ql5 7ql6 7smm 7smq 7smr

25 assemblies; showing the first 12

View Construct and Data Evidence
UniProt name ACHA_TORCA
Isoform —
PDB entities 1
Chains and sequence ranges Author chain A； PDBConstruct 1–10； UniProt 91–100

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_id1tor
Deposition date deposition_date1995-10-11
Structure title titleMOLECULAR DYNAMICS SIMULATION FROM 2D-NMR DATA OF THE FREE ACHR MIR DECAPEPTIDE AND THE ANTIBODY-BOUND [A76]MIR ANALOGUE
Keywords keywordsTRANSMEMBRANE PROTEIN; TRANSMEMBRANE PROTEIN
Experimental Method methodSOLUTION NMR
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3. Official assembly/model SAXS Official SAXS Profiles

This page reads only the latest assembly calculations. Every curve maps to an explicit PDB entry, official biological assembly and coordinate model.

1tor__assembly_1__model_1

Assembly 1 · Model 1 · CRYSOL 4.1.3-1-20251215 (887e7ef)

Download this curve (.dat)

1tor__assembly_1__model_1 | I(q)

10-2 10-1 104 q (1/Angstrom) I(q)
100 plotted points; both axes use logarithmic scales.

1tor__assembly_1__model_1 | P(r) · Pending

The new assembly/model P(r) has not been calculated yet This placeholder does not display legacy data r (Angstrom) P(r)
P(r) will be calculated and displayed separately for the same assembly/model.
Rg（Guinier）6.90 Å
Rg (electron density)5.60 Å
Total Rg7.64 Å
Atom count153
Residues10
Excluded volume1401 ų
Maximum q0.500 Å⁻¹
Assembly Model Structure unit Oligomeric description Status CRYSOL Actions
1 1 1tor__assembly_1__model_1 monomeric （1） Success 4.1.3-1-20251215 (887e7ef) View Download
1 2 1tor__assembly_1__model_2 monomeric （1） Success 4.1.3-1-20251215 (887e7ef) View Download
1 3 1tor__assembly_1__model_3 monomeric （1） Success 4.1.3-1-20251215 (887e7ef) View Download
1 4 1tor__assembly_1__model_4 monomeric （1） Success 4.1.3-1-20251215 (887e7ef) View Download
1 5 1tor__assembly_1__model_5 monomeric （1） Success 4.1.3-1-20251215 (887e7ef) View Download
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4. Crystallography and Experiment 4. Crystallography & Experiment

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5. Entities and Polymers Entities & Polymers (1)

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6. Fold Classification (SCOP + CATH) 1 domains

SCOP 2.08 (1 domains)

Domain ID domain_idd1tora_
Class classj — Peptides
Fold Fold foldj.44 — Acetylcholine receptor fragment (residues alpha 67-76)
Superfamily Superfamily superfamilyj.44.1 — Acetylcholine receptor fragment (residues alpha 67-76)
Family Family familyj.44.1.1 — Acetylcholine receptor fragment (residues alpha 67-76)
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7. Citations (5)