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1ioj

HUMAN APOLIPOPROTEIN C-I, NMR, 18 STRUCTURES

Method: SOLUTION NMR Dmax: 50.5 Å Quality: REASONABLE
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1. Protein Identity and Related Structures Protein Identity & Related Structures

APOC-I

OrganismNot specified

UniProt P02654

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 27–83 Not recorded No other associated polymer SOLUTION NMR NMR measurement conditions：pH 4.8；323 K NMR sample composition：5.8 mM native apoC-I, 90%H2O/10%D2O, 232 mM SDS-D25 | 90% H2O/10% D2O NMR sample composition：5 mM selectively 15N-labeled synthetic apoC-I, 90%H2O/10%D2O, 200 mM SDS-D25 | 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 1IOJ Assembly / Oligomeric State Construct Mutations and Modifications Ligands, Ions and Non-polymers Method and Experimental Conditions Structure Quality
1ALE CONFORMATION OF TWO PEPTIDES CORRESPONDING TO HUMAN APOLIPOPROTEIN C-I RESIDUES 7-24 AND 35-53 IN THE PRESENCE OF SODIUM DODECYLSULFATE BY CD AND NMR SPECTROSCOPY Deposited 1995-02-20 Different construct Different experimental conditions Assembly 1 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric
Chain A 33–50（18 aa）
Not recorded No recorded non-water small molecule SOLUTION NMR mmCIF provides none of the parsed conditions Resolution not provided
1ALF CONFORMATION OF TWO PEPTIDES CORRESPONDING TO HUMAN APOLIPOPROTEIN C-I RESIDUES 7-24 AND 35-53 IN THE PRESENCE OF SODIUM DODECYLSULFATE BY CD AND NMR SPECTROSCOPY Deposited 1995-02-20 Different construct Different experimental conditions Assembly 1 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric
Chain A 61–79（19 aa）
Not recorded No recorded non-water small molecule SOLUTION NMR mmCIF provides none of the parsed conditions Resolution not provided
1OPP PEPTIDE OF HUMAN APOLIPOPROTEIN C-I RESIDUES 1-38, NMR, 28 STRUCTURES Deposited 1997-05-08 Different construct Different experimental conditions Assembly 1 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric
Chain A 27–64（38 aa） Fragment：RESIDUES 1 - 38
Not recorded No recorded non-water small molecule SOLUTION NMR
NMR measurement conditions pH 4.8；310 K
NMR sample composition 5 mM apoC, 300 mM SDS-d2s | 90% H2O/10% D2O
NMR sample composition 5 mM apoC, 300 mM SDS-d2s | 99.9% D2O
NMR sample composition 5 mM apoC, 50 mM potassium chloride, 20 mM potassium phosphate | 50% (v/v) TFE-d, 10% D2O
Resolution not provided
6DVU Structure of the Monoclinic-1 (Monocl-1) Crystal Form of Human Apolipoprotein C1 Deposited 2018-06-25 Different construct Different mutation/modification Different oligomeric state Different experimental method Different experimental conditions Different structure-quality metrics Assembly 1 Protein homooligomer Homooligomer；Protein × 2 PDB declaration: dimeric
Chain A 1–83（83 aa）
Chain B 1–83（83 aa）
Not recorded No recorded non-water small molecule X-RAY DIFFRACTION
X-ray crystallization conditions VAPOR DIFFUSION, SITTING DROP；pH 8；298 K；Crystallized in Cryschem sitting drop plates with reservoirs of 16%-18% 2-methyl-2,4-pentanediol (MPD), 0.1 M sodium acetate and 0.25% octyl-beta-s-1-thioglucopyanoside. The drops were composed of equal amounts of 8 mg/ml protein in 0.02 ammonium bicarbonate and reservoir.
Resolution 1.80 Å R-free 0.276
6DXR Structure of the Monoclinic-2 (Monocl-2) Crystal Form of Human Apolipoprotein C1 Deposited 2018-06-29 Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental method Different experimental conditions Different structure-quality metrics Assembly 1 Protein homooligomer Homooligomer；Protein × 2 PDB declaration: dimeric
Chain A 1–83（83 aa）
Chain B 1–83（83 aa）
Not recorded MPD (4S)-2-METHYL-2,4-PENTANEDIOL × 2 X-RAY DIFFRACTION
X-ray crystallization conditions VAPOR DIFFUSION, SITTING DROP；pH 6；298 K；20% PEG
Resolution 2.00 Å R-free 0.287
6DZ6 Structure of the Orthorhombic (Orthrhmb) Crystal Form of Human Apolipoprotein C1 Deposited 2018-07-03 Different construct Different mutation/modification Different oligomeric state Different experimental method Different experimental conditions Different structure-quality metrics Assembly 1 Protein homooligomer Homooligomer；Protein × 2 PDB declaration: dimeric
Chain A 1–83（83 aa）
Chain B 1–83（83 aa）
Not recorded No recorded non-water small molecule X-RAY DIFFRACTION
X-ray crystallization conditions VAPOR DIFFUSION；pH 6；298 K；16% MPD - 18% MPD
Resolution 3.00 Å R-free 0.283
6NF3 Structure of the Monoclinic-3 (Monocln-3) Crystal Form of Human Apolipoprotein C1 Deposited 2018-12-18 Different construct Different mutation/modification Different oligomeric state Different experimental method Different experimental conditions Different structure-quality metrics Assembly 1 Protein homooligomer Homooligomer；Protein × 2 PDB declaration: dimeric
Chain A 1–83（83 aa）
Chain B 1–83（83 aa）
Not recorded No recorded non-water small molecule X-RAY DIFFRACTION
X-ray crystallization conditions VAPOR DIFFUSION；pH 6.5；298 K；The crystals were grown by sitting drop vapor diffusion in Cryschem plates using 0.6 ml reservoirs of 16% to 18% 2-methyl-2,4-pentanediol (MPD) containing o.1 M sodium acetate and 0.25% octyl-beta-s-1-thioglucopyanoside. The drops were equal volumes, generally 6 ul each, of the reservoir and an 8 mg/ml solution of protein dissolved in .02 M ammonium bicarbonate.
Resolution 2.33 Å R-free 0.318

7 other PDB entries and 7 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name APOC1_HUMAN
Isoform —
PDB entities 1
Chains and sequence ranges Author chain A； PDBConstruct 1–57； UniProt 27–83

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 1ioj

P(r) Distance Distribution P(r) Distribution

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

Entry ID entry_id1ioj
Deposition date deposition_date1998-05-12
Structure title titleHUMAN APOLIPOPROTEIN C-I, NMR, 18 STRUCTURES
Keywords keywordsAPOLIPOPROTEIN, AMPHIPATHIC HELIX, LIPID ASSOCIATION, LCAT ACTIVATION; APOLIPOPROTEIN
Experimental Method methodSOLUTION NMR
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3. SAXS Parameters (CRYSOL theoretical calculation) 3. SAXS Parameters (CRYSOL)

Radius of gyration Rg (Guinier) rg_guinier19.08 Å
Radius of gyration Rg (electron density) rg_electron19.36 Å
Forward intensity I(0) i0198672000.00
Molecular weight molecular_weight119370.0 kDa
Excluded volume excluded_volume150560 ų
Envelope volume envelope_volume39035 ų
Hydration-shell volume shell_volume16072 ų
Envelope diameter envelope_diameter88.6 Å
Shell Rg shell_rg27.11 Å
Envelope Rg envelope_rg23.08 Å
Shape Rg shape_rg19.34 Å
Total Rg total_rg19.73 Å
Total atoms total_atoms17064
Residues n_residues1026
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 dmax50.5 Å
Rg (real space) rg_real17.77 Å
Rg uncertainty (real space) rg_real_error0.10 Å
I(0) (real space) i0_real1.8930e+08
I(0) uncertainty (real space) i0_real_error1.8760e+06
Rg (reciprocal space) rg_reciprocal19.43 Å
I(0) (reciprocal space) i0_reciprocal198700000.0000
Solution quality estimate total_estimate0.6342
Solution quality rating solution_quality REASONABLE a REASONABLE solution
P(r) peaks n_peaks1
Primary peak position r_peak_primary12.6 Å
Skewness Skewness skewness0.327
Kurtosis Kurtosis kurtosis-0.856
Angular range angular_range— – 0.4150 Å−1
Current regularization parameter α current_alpha3.5080
Highest regularization parameter α highest_alpha116700.0000
Real-space data points n_real_points73
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.002; Oscil: 0.945; Stabil: 0.983; Sysdev: 0.000; Positv: 1.000; Valcen: 0.485; 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_idd1ioja_
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_id1iojA00
Class class4 — Few Secondary Structures
Architecture architecture10 — Irregular
Topology topology260 — G Protein Gi Gamma 2
Homologous superfamily homologous superfamily30 — Apolipoprotein C-I
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8. Citations (1)

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9. Files and Curves (10)