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1o8t

Global Structure and Dynamics of Human Apolipoprotein CII in Complex with Micelles: Evidence for increased mobility of the helix involved in the activation of lipoprotein lipase

Method: SOLUTION NMR Dmax: 70.7 Å Quality: REASONABLE
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1. Protein Identity and Related Structures Protein Identity & Related Structures

APOLIPOPROTEIN C-II

HOMO SAPIENS

UniProt P02655

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 monomer Monomer Protein × 1 PDB declaration: monomeric（1） Consistent with protein copy count Chain A； UniProt 23–101 Not recorded No other associated polymer SOLUTION NMR NMR measurement conditions：pH 4.5；313 K；Ionic strength (raw mmCIF value) 10 MM ACETIC ACID 380 MM SDS；Pressure 1 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 1O8T Assembly / Oligomeric State Construct Mutations and Modifications Ligands, Ions and Non-polymers Method and Experimental Conditions Structure Quality
1BY6 Peptide of human apolipoprotein C-II Deposited 1999-12-03 Different construct Different experimental conditions Assembly 1 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric
Chain A 66–101（36 aa） Fragment：RESIDUES 44-79
Not recorded No recorded non-water small molecule SOLUTION NMR
NMR measurement conditions pH 4.1；310 K
NMR sample composition PERDEUTERATED SODIUM DODECYL SULFATE (SDS) IN 160 FOLD MOLAR EXCESS RELATIVE TO PEPTIDE CONCENTRATION | 90% H2O/10% D2O
Resolution not provided
1I5J NMR STRUCTURE OF HUMAN APOLIPOPROTEIN C-II IN THE PRESENCE OF SDS Deposited 2001-02-27 Different construct Different experimental conditions Assembly 1 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric
Chain A 1–79（79 aa）
Not recorded No recorded non-water small molecule SOLUTION NMR
NMR measurement conditions pH 5；313 K；Ionic strength (raw mmCIF value) 20 mM sodium acetate, 220 mM sodium dodecy sulfate；Pressure ambient
NMR sample composition 1.8 mM U-15N ApoC-II; 220 mM SDS; 20 mM sodium acetate, pH5 | 90% H2O/10% D2O
Resolution not provided
1SOH The structure of human apolipoprotein C-II in dodecyl phosphocholine Deposited 2004-03-14 Different experimental conditions Assembly 1 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric
Chain A 23–101（79 aa）
Not recorded No recorded non-water small molecule SOLUTION NMR
NMR measurement conditions pH 5；308 K；Pressure ambient
NMR sample composition 1.8 mM U-15N apoC-II,85 mM DPC, 20 mM sodium acetate, 90% H2O, 10% D2O | 90% H2O/10% D2O
Resolution not provided

3 other PDB entries and 3 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name APC2_HUMAN
Isoform —
PDB entities 1
Chains and sequence ranges Author chain A； PDBConstruct 1–79； UniProt 23–101

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.

SAXS scattering curve SAXS Profile

SAXS profile for 1o8t

P(r) Distance Distribution P(r) Distribution

P(r) distribution for 1o8t
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2. Structure Basics 2. Structure Basics

Entry ID entry_id1o8t
Deposition date deposition_date2002-11-29
Structure title titleGlobal Structure and Dynamics of Human Apolipoprotein CII in Complex with Micelles: Evidence for increased mobility of the helix involved in the activation of lipoprotein lipase
Keywords keywords;APOCII, LPL, ACTIVATION MECHANISM, DOMAIN MOTION, SDS, MICELLE, GLOBAL STRUCTURE, LOCAL STRUCTURE, DYNAMICS, HELIX, LIPID TRANSPORT, LIPID DEGRADATION, CHYLOMICRON ;; LIPID TRANSPORT
Experimental Method methodSOLUTION NMR
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3. SAXS Parameters (CRYSOL theoretical calculation) 3. SAXS Parameters (CRYSOL)

Radius of gyration Rg (Guinier) rg_guinier20.51 Å
Radius of gyration Rg (electron density) rg_electron20.26 Å
Forward intensity I(0) i05015730000.00
Molecular weight molecular_weight605940.0 kDa
Excluded volume excluded_volume757690 ų
Envelope volume envelope_volume70095 ų
Hydration-shell volume shell_volume22525 ų
Envelope diameter envelope_diameter84.6 Å
Shell Rg shell_rg33.07 Å
Envelope Rg envelope_rg26.86 Å
Shape Rg shape_rg20.25 Å
Total Rg total_rg20.43 Å
Total atoms total_atoms84184
Residues n_residues5372
Spherical-harmonic order n_harmonics20
q range q_range— – 0.5000 Å−1
Data points n_points101
Shell type shell_typedirectional
Solvent electron density solvent_density0.3340 e/ų
Shell contrast contrast_shell0.0300 e/ų
CRYSOL version crysol_version4.1.3
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4. P(r) Distance Distribution (GNOM inversion) 4. P(r) Analysis (GNOM)

Maximum dimension Dmax dmax70.7 Å
Rg (real space) rg_real20.52 Å
Rg uncertainty (real space) rg_real_error0.79 Å
I(0) (real space) i0_real5.0160e+09
I(0) uncertainty (real space) i0_real_error7.5420e+07
Rg (reciprocal space) rg_reciprocal20.52 Å
I(0) (reciprocal space) i0_reciprocal5016000000.0000
Solution quality estimate total_estimate0.6401
Solution quality rating solution_quality REASONABLE a REASONABLE solution
P(r) peaks n_peaks4
Primary peak position r_peak_primary28.3 Å
Skewness Skewness skewness0.049
Kurtosis Kurtosis kurtosis-0.345
Angular range angular_range— – 0.3900 Å−1
Current regularization parameter α current_alpha0.0000
Highest regularization parameter α highest_alpha39230.0000
Real-space data points n_real_points71
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.119; Stabil: 0.999; Sysdev: 1.000; Positv: 1.000; Valcen: 0.962; Smooth: 0.000
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5. Crystallography and Experiment 5. Crystallography & Experiment

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6. Entities and Polymers Entities & Polymers (1)

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7. Fold Classification (SCOP + CATH) 2 domains

SCOP 2.08 (1 domains)

Domain ID domain_idd1o8ta_
Class classj — Peptides
Fold Fold foldj.39 — Fragments of apolipoproteins
Superfamily Superfamily superfamilyj.39.1 — Fragments of apolipoproteins
Family Family familyj.39.1.1 — Fragments of apolipoproteins

CATH v4.4 (1 domains)

Domain ID domain_id1o8tA00
Class class1 — Mainly Alpha
Architecture architecture10 — Orthogonal Bundle
Topology topology1440 — Apolipoprotein Cii; Chain: A;
Homologous superfamily homologous superfamily10 — Apolipoprotein C-II
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8. Citations (1)

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9. Files and Curves (10)