1ejl

MOUSE IMPORTIN ALPHA-SV40 LARGE T ANTIGEN NLS PEPTIDE COMPLEX

Method: X-RAY DIFFRACTION Dmax: 98.5 Å Quality: GOOD

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

SV40 LARGE T ANTIGEN NLS PEPTIDE

OrganismNot specified

UniProt P03070

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 × 3 PDB declaration: trimeric(3) Consistent with protein copy count Chain A; UniProt 126–132 Chain B; UniProt 126–132 Fragment:NLS (NUCLEAR LOCALIZATION SIGNAL) MONOPARTITE PEPTIDE, RESIDUES 126-132 IMPORTIN ALPHA × 1 (P52293) X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, HANGING DROP;pH 6.5;293 K;sodium citrate, Hepes, DTT, pH 6.5, VAPOR DIFFUSION, HANGING DROP, temperature 293K Resolution 2.80 Å R-free 0.254

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.

44 other PDB entries and 44 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name TALA_SV40
Isoform
PDB entities 1
Chains and sequence ranges Author chain A; PDBConstruct 1–7; UniProt 126–132 Author chain B; PDBConstruct 1–7; UniProt 126–132

IMPORTIN ALPHA

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 × 3 PDB declaration: trimeric(3) Consistent with protein copy count Chain I; UniProt 70–529 Fragment:NLS-BINDING DOMAIN, RESIDUES 70-529 SV40 LARGE T ANTIGEN NLS PEPTIDE × 2 (P03070) X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, HANGING DROP;pH 6.5;293 K;sodium citrate, Hepes, DTT, pH 6.5, VAPOR DIFFUSION, HANGING DROP, temperature 293K Resolution 2.80 Å R-free 0.254

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 IMA2_MOUSE
Isoform
PDB entities 2
Chains and sequence ranges Author chain I; PDBConstruct 1–460; UniProt 70–529

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 1ejl

P(r) Distance Distribution P(r) Distribution

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

Entry ID entry_id1ejl
Deposition date deposition_date2000-03-03
Structure title titleMOUSE IMPORTIN ALPHA-SV40 LARGE T ANTIGEN NLS PEPTIDE COMPLEX
Keywords keywords;importin alpha/karyopherin alpha; nuclear localization sequence (NLS) recognition; simian virus (SV40) large T-antigen, PROTEIN BINDING ;; PROTEIN BINDING
Experimental Method methodX-RAY DIFFRACTION

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

Radius of gyration Rg (Guinier) rg_guinier28.25
Radius of gyration Rg (electron density) rg_electron27.94
Forward intensity I(0) i034942800.00
Molecular weight molecular_weight47852.0 kDa
Excluded volume excluded_volume60717 ų
Envelope volume envelope_volume72938 ų
Hydration-shell volume shell_volume23272 ų
Envelope diameter envelope_diameter102.2
Shell Rg shell_rg33.12
Envelope Rg envelope_rg28.09
Shape Rg shape_rg27.95
Total Rg total_rg28.45
Total atoms total_atoms3368
Residues n_residues440
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 dmax98.5
Rg (real space) rg_real28.61
Rg uncertainty (real space) rg_real_error1.03
I(0) (real space) i0_real3.4940e+07
I(0) uncertainty (real space) i0_real_error4.8950e+05
Rg (reciprocal space) rg_reciprocal28.50
I(0) (reciprocal space) i0_reciprocal34940000.0000
Solution quality estimate total_estimate0.7933
Solution quality rating solution_quality GOOD a GOOD solution
P(r) peaks n_peaks2
Primary peak position r_peak_primary22.9
Skewness Skewness skewness0.536
Kurtosis Kurtosis kurtosis-0.398
Angular range angular_range— – 0.2800 −1
Current regularization parameter α current_alpha0.0000
Highest regularization parameter α highest_alpha12330000.0000
Real-space data points n_real_points57
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.638; Stabil: 0.994; Sysdev: 1.000; Positv: 1.000; Valcen: 0.510; Smooth: 0.903

5. Crystallography and Experiment 5. Crystallography & Experiment

6. Entities and Polymers Entities & Polymers (2)

7. Fold Classification (SCOP + CATH) 2 domains

SCOP 2.08 (1 domains)

Domain ID domain_idd1ejli_
Class classa — All alpha proteins
Fold Fold folda.118 — alpha-alpha superhelix
Superfamily Superfamily superfamilya.118.1 — ARM repeat
Family Family familya.118.1.1 — Armadillo repeat

CATH v4.4 (1 domains)

Domain ID domain_id1ejlI00
Class class1 — Mainly Alpha
Architecture architecture25 — Alpha Horseshoe
Topology topology10 — Leucine-rich Repeat Variant
Homologous superfamily homologous superfamily10 — Leucine-rich Repeat Variant

8. Citations (2)

9. Files and Curves (10)