5svz

HIV-1 Tat NLS in complex with importin alpha

Method: X-RAY DIFFRACTION Dmax: 98.2 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 Not recorded Tat × 1 X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, HANGING DROP;296 K;1.25 M sodium citrate pH 7 and 10 mM DTT Resolution 2.00 Å R-free 0.192

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

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 5svz

P(r) Distance Distribution P(r) Distribution

P(r) distribution for 5svz
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2. Structure Basics 2. Structure Basics

Entry ID entry_id5svz
Deposition date deposition_date2016-08-08
Structure title titleHIV-1 Tat NLS in complex with importin alpha
Keywords keywordsHIV-1, Tat, Importin alpha, Virus, Complex, Transport Protein-Viral Protein complex; Transport Protein/Viral Protein
Experimental Method methodX-RAY DIFFRACTION

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

Radius of gyration Rg (Guinier) rg_guinier28.33
Radius of gyration Rg (electron density) rg_electron28.07
Forward intensity I(0) i034586800.00
Molecular weight molecular_weight47148.0 kDa
Excluded volume excluded_volume59645 ų
Envelope volume envelope_volume73001 ų
Hydration-shell volume shell_volume23236 ų
Envelope diameter envelope_diameter101.6
Shell Rg shell_rg33.11
Envelope Rg envelope_rg27.99
Shape Rg shape_rg28.07
Total Rg total_rg28.58
Total atoms total_atoms6727
Residues n_residues434
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 dmax98.2
Rg (real space) rg_real28.68
Rg uncertainty (real space) rg_real_error0.88
I(0) (real space) i0_real3.4590e+07
I(0) uncertainty (real space) i0_real_error5.3540e+05
Rg (reciprocal space) rg_reciprocal28.58
I(0) (reciprocal space) i0_reciprocal34580000.0000
Solution quality estimate total_estimate0.8051
Solution quality rating solution_quality GOOD a GOOD solution
P(r) peaks n_peaks2
Primary peak position r_peak_primary22.8
Skewness Skewness skewness0.522
Kurtosis Kurtosis kurtosis-0.420
Angular range angular_range— – 0.2800 −1
Current regularization parameter α current_alpha0.0000
Highest regularization parameter α highest_alpha11100000.0000
Real-space data points n_real_points57
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.681; Stabil: 1.000; Sysdev: 1.000; Positv: 1.000; Valcen: 0.539; Smooth: 0.881

5. Crystallography and Experiment 5. Crystallography & Experiment

6. Entities and Polymers Entities & Polymers (3)

7. Fold Classification (SCOP + CATH) 2 domains

SCOP 2.08 (1 domains)

Domain ID domain_idd5svza_
Class classa — All alpha proteins
Fold Fold folda.118 — alpha-alpha superhelix
Superfamily Superfamily superfamilya.118.1 — ARM repeat
Family Family familya.118.1.0 — automated matches

CATH v4.4 (1 domains)

Domain ID domain_id5svzA00
Class class1 — Mainly Alpha
Architecture architecture25 — Alpha Horseshoe
Topology topology10 — Leucine-rich Repeat Variant
Homologous superfamily homologous superfamily10 — Leucine-rich Repeat Variant

8. Citations (1)

9. Files and Curves (10)