← Back to search
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

Method: SOLUTION NMR Dmax: 32.8 Å Quality: REASONABLE
▼

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

APOLIPOPROTEIN C-I PRECURSOR

Homo sapiens

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 33–50 Not recorded No other associated polymer SOLUTION NMR mmCIF provides none of the parsed experimental conditions 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 1ALE Assembly / Oligomeric State Construct Mutations and Modifications Ligands, Ions and Non-polymers Method and Experimental Conditions Structure Quality
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 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
1IOJ HUMAN APOLIPOPROTEIN C-I, NMR, 18 STRUCTURES Deposited 1998-05-12 Different construct Different experimental conditions Assembly 1 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric
Chain A 27–83（57 aa）
Not recorded No recorded non-water small molecule 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
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 1–18； UniProt 33–50

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 1ale

P(r) Distance Distribution P(r) Distribution

P(r) distribution for 1ale
Download Download
▼

2. Structure Basics 2. Structure Basics

Entry ID entry_id1ale
Deposition date deposition_date1995-02-20
Structure title titleCONFORMATION 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
Keywords keywordsAPOLIPOPROTEIN; APOLIPOPROTEIN
Experimental Method methodSOLUTION NMR
▼

3. SAXS Parameters (CRYSOL theoretical calculation) 3. SAXS Parameters (CRYSOL)

Radius of gyration Rg (Guinier) rg_guinier8.57 Å
Radius of gyration Rg (electron density) rg_electron9.13 Å
Forward intensity I(0) i01944650.00
Molecular weight molecular_weight10382.0 kDa
Excluded volume excluded_volume12937 ų
Envelope volume envelope_volume4275 ų
Hydration-shell volume shell_volume4433 ų
Envelope diameter envelope_diameter34.5 Å
Shell Rg shell_rg13.61 Å
Envelope Rg envelope_rg10.16 Å
Shape Rg shape_rg9.05 Å
Total Rg total_rg9.99 Å
Total atoms total_atoms1470
Residues n_residues90
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
▼

4. P(r) Distance Distribution (GNOM inversion) 4. P(r) Analysis (GNOM)

Maximum dimension Dmax dmax32.8 Å
Rg (real space) rg_real8.77 Å
Rg uncertainty (real space) rg_real_error0.33 Å
I(0) (real space) i0_real1.9450e+06
I(0) uncertainty (real space) i0_real_error1.8050e+04
Rg (reciprocal space) rg_reciprocal8.77 Å
I(0) (reciprocal space) i0_reciprocal1945000.0000
Solution quality estimate total_estimate0.7341
Solution quality rating solution_quality REASONABLE a REASONABLE solution
P(r) peaks n_peaks1
Primary peak position r_peak_primary31.9 Å
Skewness Skewness skewness0.623
Kurtosis Kurtosis kurtosis-0.231
Angular range angular_range— – 0.5000 Å−1
Current regularization parameter α current_alpha0.0000
Highest regularization parameter α highest_alpha2122.0000
Real-space data points n_real_points80
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.525; Stabil: 1.000; Sysdev: 1.000; Positv: 1.000; Valcen: 0.087; Smooth: 0.877
▶

5. Crystallography and Experiment 5. Crystallography & Experiment

▶

6. Entities and Polymers Entities & Polymers (1)

▼

7. Fold Classification (SCOP + CATH) 1 domains

SCOP 2.08 (1 domains)

Domain ID domain_idd1alea_
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
▶

8. Citations (1)

▶

9. Files and Curves (10)