9cft

Adeno-associated virus serotype 6 basic regions in complex with importin alpha 2

Method: X-RAY DIFFRACTION Dmax: 99.4 Å Quality: GOOD

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

Importin subunit alpha-1

Mus musculus

UniProt P52293

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 heterocomplex Heteromer Protein × 2 PDB declaration: dimeric(2) Consistent with protein copy count Chain A; UniProt 70–529 Fragment:UNP residues 70-529 Capsid protein VP1 × 1 (O56137) GOL GLYCEROL × 1 X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, HANGING DROP;pH 7;298 K;0.65 M Na citrate, 0.01 M DTT, 0.1 M HEPES, pH 7.0 Resolution 2.30 Å R-free 0.238

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.

150 other PDB entries and 151 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name IMA1_MOUSE
Isoform
PDB entities 1
Chains and sequence ranges Author chain A; PDBConstruct 51–510; UniProt 70–529

Capsid protein VP1

Adeno-associated virus - 6

UniProt O56137

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 heterocomplex Heteromer Protein × 2 PDB declaration: dimeric(2) Consistent with protein copy count Chain B; UniProt 115–174 Not recorded Importin subunit alpha-1 × 1 (P52293) GOL GLYCEROL × 1 X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, HANGING DROP;pH 7;298 K;0.65 M Na citrate, 0.01 M DTT, 0.1 M HEPES, pH 7.0 Resolution 2.30 Å R-free 0.238

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.

3 other PDB entries and 11 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name O56137_9VIRU
Isoform
PDB entities 2
Chains and sequence ranges Author chain B; PDBConstruct 1–60; UniProt 115–174

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 9cft

P(r) Distance Distribution P(r) Distribution

P(r) distribution for 9cft
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2. Structure Basics 2. Structure Basics

Entry ID entry_id9cft
Deposition date deposition_date2024-06-27
Structure title titleAdeno-associated virus serotype 6 basic regions in complex with importin alpha 2
Keywords keywordsimportin alpha, adeno associated, complex, basic regions, transport, nucleus, TRANSPORT PROTEIN; TRANSPORT PROTEIN
Experimental Method methodX-RAY DIFFRACTION

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

Radius of gyration Rg (Guinier) rg_guinier28.29
Radius of gyration Rg (electron density) rg_electron28.06
Forward intensity I(0) i035566900.00
Molecular weight molecular_weight48068.0 kDa
Excluded volume excluded_volume60916 ų
Envelope volume envelope_volume73470 ų
Hydration-shell volume shell_volume23579 ų
Envelope diameter envelope_diameter102.6
Shell Rg shell_rg32.93
Envelope Rg envelope_rg28.22
Shape Rg shape_rg28.05
Total Rg total_rg28.57
Total atoms total_atoms6865
Residues n_residues442
Spherical-harmonic order n_harmonics20
q range q_range— – 0.5000 −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 dmax99.4
Rg (real space) rg_real28.67
Rg uncertainty (real space) rg_real_error0.91
I(0) (real space) i0_real3.5570e+07
I(0) uncertainty (real space) i0_real_error5.1260e+05
Rg (reciprocal space) rg_reciprocal28.56
I(0) (reciprocal space) i0_reciprocal35560000.0000
Solution quality estimate total_estimate0.7881
Solution quality rating solution_quality GOOD a GOOD solution
P(r) peaks n_peaks2
Primary peak position r_peak_primary23.1
Skewness Skewness skewness0.549
Kurtosis Kurtosis kurtosis-0.380
Angular range angular_range— – 0.2800 −1
Current regularization parameter α current_alpha0.0000
Highest regularization parameter α highest_alpha15640000.0000
Real-space data points n_real_points57
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.623; Stabil: 1.000; Sysdev: 1.000; Positv: 1.000; Valcen: 0.480; Smooth: 0.893

5. Crystallography and Experiment 5. Crystallography & Experiment

6. Entities and Polymers Entities & Polymers (4)

8. Citations (1)

9. Files and Curves (10)