1i3p

THE 3.1 ANGSTROM RESOLUTION CRYSTAL STRUCTURE OF A MUTATED BACULOVIRUS P35 AFTER CASPASE CLEAVAGE

Method: X-RAY DIFFRACTION Dmax: 68.0 Å Quality: GOOD

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

EARLY 35 KDA PROTEIN

Autographa californica nucleopolyhedrovirus

UniProt P08160

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 2–299 Mutation:V71P No other associated polymer X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, HANGING DROP;pH 6;9-13% PEG 20,000, 100-400 mM NaCl, 100 mM MES, pH 6.0, VAPOR DIFFUSION, HANGING DROP Resolution 3.10 Å R-free 0.291

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.

4 other PDB entries and 9 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name VP35_NPVAC
Isoform
PDB entities 1
Chains and sequence ranges Author chain A; PDBConstruct 1–298; UniProt 2–299

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 1i3p

P(r) Distance Distribution P(r) Distribution

P(r) distribution for 1i3p
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2. Structure Basics 2. Structure Basics

Entry ID entry_id1i3p
Deposition date deposition_date2001-02-15
Structure title titleTHE 3.1 ANGSTROM RESOLUTION CRYSTAL STRUCTURE OF A MUTATED BACULOVIRUS P35 AFTER CASPASE CLEAVAGE
Keywords keywordshelix-turn-helix, reactive site loop, hairpin loop, APOPTOSIS; APOPTOSIS
Experimental Method methodX-RAY DIFFRACTION

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

Radius of gyration Rg (Guinier) rg_guinier20.15
Radius of gyration Rg (electron density) rg_electron19.00
Forward intensity I(0) i014607900.00
Molecular weight molecular_weight29384.0 kDa
Excluded volume excluded_volume36964 ų
Envelope volume envelope_volume43229 ų
Hydration-shell volume shell_volume19181 ų
Envelope diameter envelope_diameter69.9
Shell Rg shell_rg25.25
Envelope Rg envelope_rg19.34
Shape Rg shape_rg19.02
Total Rg total_rg19.86
Total atoms total_atoms2077
Residues n_residues274
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 dmax68.0
Rg (real space) rg_real20.09
Rg uncertainty (real space) rg_real_error0.38
I(0) (real space) i0_real1.4610e+07
I(0) uncertainty (real space) i0_real_error1.8400e+05
Rg (reciprocal space) rg_reciprocal20.10
I(0) (reciprocal space) i0_reciprocal14610000.0000
Solution quality estimate total_estimate0.7987
Solution quality rating solution_quality GOOD a GOOD solution
P(r) peaks n_peaks2
Primary peak position r_peak_primary25.3
Skewness Skewness skewness0.292
Kurtosis Kurtosis kurtosis-0.248
Angular range angular_range— – 0.3950 −1
Current regularization parameter α current_alpha0.0000
Highest regularization parameter α highest_alpha3098000.0000
Real-space data points n_real_points71
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.793; Stabil: 1.000; Sysdev: 1.000; Positv: 1.000; Valcen: 1.000; Smooth: 0.000

5. Crystallography and Experiment 5. Crystallography & Experiment

6. Entities and Polymers Entities & Polymers (1)

7. Fold Classification (SCOP + CATH) 2 domains

SCOP 2.08 (1 domains)

Domain ID domain_idd1i3pa_
Class classb — All beta proteins
Fold Fold foldb.28 — Baculovirus p35 protein
Superfamily Superfamily superfamilyb.28.1 — Baculovirus p35 protein
Family Family familyb.28.1.1 — Baculovirus p35 protein

CATH v4.4 (1 domains)

Domain ID domain_id1i3pA00
Class class2 — Mainly Beta
Architecture architecture60 — Sandwich
Topology topology250 — Baculovirus p35
Homologous superfamily homologous superfamily10 — Baculovirus p35

8. Citations (2)

9. Files and Curves (10)