SAXSdb — 1i5j

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

APOLIPOPROTEIN CII

Homo sapiens

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 1–79	Not recorded	No other associated polymer	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

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 1I5J	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
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 Deposited 2002-11-29	Different construct 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 4.5；313 K；Ionic strength (raw mmCIF value) 10 MM ACETIC ACID 380 MM SDS；Pressure 1	Resolution not provided
1SOH The structure of human apolipoprotein C-II in dodecyl phosphocholine Deposited 2004-03-14	Different construct 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	APOC2_HUMAN
Isoform	—
PDB entities	1
Chains and sequence ranges	Author chain A； PDBConstruct 1–79； UniProt 1–79

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	1i5j
Deposition date deposition_date	2001-02-27
Structure title title	NMR STRUCTURE OF HUMAN APOLIPOPROTEIN C-II IN THE PRESENCE OF SDS
Keywords keywords	PROTEIN-LIPID INTERACTION, AMPHIPATHIC ALPHA HELIX, LIPID TRANSPORT; LIPID TRANSPORT
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	17.70 Å
Radius of gyration Rg (electron density) rg_electron	18.21 Å
Forward intensity I(0) i0	470680000.00
Molecular weight molecular_weight	188210.0 kDa
Excluded volume excluded_volume	237900 Å³
Envelope volume envelope_volume	65112 Å³
Hydration-shell volume shell_volume	25078 Å³
Envelope diameter envelope_diameter	82.4 Å
Shell Rg shell_rg	28.83 Å
Envelope Rg envelope_rg	22.04 Å
Shape Rg shape_rg	18.19 Å
Total Rg total_rg	18.62 Å
Total atoms total_atoms	26375
Residues n_residues	1675
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	45.5 Å
Rg (real space) rg_real	16.78 Å
Rg uncertainty (real space) rg_real_error	0.05 Å
I(0) (real space) i0_real	4.4830e+08
I(0) uncertainty (real space) i0_real_error	3.2950e+06
Rg (reciprocal space) rg_reciprocal	17.75 Å
I(0) (reciprocal space) i0_reciprocal	470700000.0000
Solution quality estimate total_estimate	0.6843
Solution quality rating solution_quality	REASONABLE a REASONABLE solution
P(r) peaks n_peaks	1
Primary peak position r_peak_primary	21.2 Å
Skewness Skewness skewness	0.155
Kurtosis Kurtosis kurtosis	-0.678
Angular range angular_range	— – 0.4500 Å⁻¹
Current regularization parameter α current_alpha	3.9290
Highest regularization parameter α highest_alpha	1574000.0000
Real-space data points n_real_points	76
GNOM version gnom_version	4.1.3
Quality Criteria quality_criteria	AN1: 0.002; Oscil: 0.999; Stabil: 0.972; Sysdev: 0.000; 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 (1)

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7. Fold Classification (SCOP + CATH) 2 domains

SCOP 2.08 (1 domains)

Domain ID domain_id	d1i5ja_
Class class	j — Peptides
Fold Fold fold	j.39 — Fragments of apolipoproteins
Superfamily Superfamily superfamily	j.39.1 — Fragments of apolipoproteins
Family Family family	j.39.1.1 — Fragments of apolipoproteins

CATH v4.4 (1 domains)

Domain ID domain_id	1i5jA00
Class class	1 — Mainly Alpha
Architecture architecture	10 — Orthogonal Bundle
Topology topology	1440 — Apolipoprotein Cii; Chain: A;
Homologous superfamily homologous superfamily	10 — Apolipoprotein C-II

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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	—

Description description	APOLIPOPROTEIN CII
Molecular weight formula_weight	8921.9 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	26375

来源生物 organism	Homo sapiens
通用名 common_name	human
NCBI Class编号 ncbi_taxonomy_id	9606
宿主生物 host_organism	Escherichia coli

NMR STRUCTURE OF HUMAN APOLIPOPROTEIN C-II IN THE PRESENCE OF SDS

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

APOLIPOPROTEIN CII

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 (1)

Entity 1 Entity 1 polymer

Polymer Polymer

来源 Source

7. Fold Classification (SCOP + CATH) 2 domains

SCOP 2.08 (1 domains)

CATH v4.4 (1 domains)

8. Citations (1)

9. Files and Curves (10)

Files (7)

Curves (3)

fit	/app/data/saxs_computation/i5/1i5j/1i5j.fit
pddf	/app/data/pr_computation/i5/1i5j/1i5j.pr.out
profile	/app/data/saxs_computation/i5/1i5j/1i5j.dat