1bjb

SOLUTION NMR STRUCTURE OF AMYLOID BETA[E16], RESIDUES 1-28, 14 STRUCTURES

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

AMYLOID BETA-PEPTIDE

Homo sapiens

UniProt P05067

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

View Construct and Data Evidence
UniProt name A4_HUMAN
Isoform —
PDB entities 1
Chains and sequence ranges Author chain A; PDBConstruct 1–28; UniProt 672–699

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_id1bjb
Deposition date deposition_date1998-06-23
Structure title titleSOLUTION NMR STRUCTURE OF AMYLOID BETA[E16], RESIDUES 1-28, 14 STRUCTURES
Keywords keywords;GLYCOPROTEIN, AMYLOID BETA-PEPTIDE, ALZHEIMER'S DISEASE ;; GLYCOPROTEIN
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.

1bjb__assembly_1__model_5

Assembly 1 · Model 5 · CRYSOL 4.1.3-1-20251215 (887e7ef)

Download this curve (.dat)

1bjb__assembly_1__model_5 | I(q)

10-2 10-1 104 105 q (1/Angstrom) I(q)
100 plotted points; both axes use logarithmic scales.

1bjb__assembly_1__model_5 | 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)12.74 Å
Rg (electron density)12.32 Å
Total Rg13.18 Å
Atom count431
Residues28
Excluded volume3935 ų
Maximum q0.500 Å⁻¹
Assembly Model Structure unit Oligomeric description Status CRYSOL Actions
1 1 1bjb__assembly_1__model_1 monomeric (1) Success 4.1.3-1-20251215 (887e7ef) View Download
1 2 1bjb__assembly_1__model_2 monomeric (1) Success 4.1.3-1-20251215 (887e7ef) View Download
1 3 1bjb__assembly_1__model_3 monomeric (1) Success 4.1.3-1-20251215 (887e7ef) View Download
1 4 1bjb__assembly_1__model_4 monomeric (1) Success 4.1.3-1-20251215 (887e7ef) View Download
1 5 1bjb__assembly_1__model_5 monomeric (1) Success 4.1.3-1-20251215 (887e7ef) View Download
1 6 1bjb__assembly_1__model_6 monomeric (1) Success 4.1.3-1-20251215 (887e7ef) View Download
1 7 1bjb__assembly_1__model_7 monomeric (1) Success 4.1.3-1-20251215 (887e7ef) View Download
1 8 1bjb__assembly_1__model_8 monomeric (1) Success 4.1.3-1-20251215 (887e7ef) View Download
1 9 1bjb__assembly_1__model_9 monomeric (1) Success 4.1.3-1-20251215 (887e7ef) View Download
1 10 1bjb__assembly_1__model_10 monomeric (1) Success 4.1.3-1-20251215 (887e7ef) View Download
1 11 1bjb__assembly_1__model_11 monomeric (1) Success 4.1.3-1-20251215 (887e7ef) View Download
1 12 1bjb__assembly_1__model_12 monomeric (1) Success 4.1.3-1-20251215 (887e7ef) View Download
1 13 1bjb__assembly_1__model_13 monomeric (1) Success 4.1.3-1-20251215 (887e7ef) View Download
1 14 1bjb__assembly_1__model_14 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_idd1bjba_
Class classj — Peptides
Fold Fold foldj.42 — Amyloid peptides
Superfamily Superfamily superfamilyj.42.1 — Amyloid peptides
Family Family familyj.42.1.1 — Amyloid peptides
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7. Citations (1)