4d2m

Vaccinia Virus F1L bound to Bim BH3

Method: X-RAY DIFFRACTION Dmax: 70.9 Å Quality: REASONABLE

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

PROTEIN F1

VACCINIA VIRUS ANKARA

UniProt O57173

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 × 8 PDB declaration: octameric(8) Consistent with protein copy count Chain A; UniProt 18–186 Chain C; UniProt 18–186 Fragment:RESIDUES 18-186 Mutation:YES Non-standard monomer:Yes (specific site not provided by mmCIF) BCL-2-LIKE PROTEIN 11 × 4 (O43521) MRD (4R)-2-METHYLPENTANE-2,4-DIOL × 2 CL CHLORIDE ION × 8 X-RAY DIFFRACTION X-ray crystallization conditions:pH 6.2;0.2M KCL, 15 % PEG400, 1.44 % MPD AND 0.1M AMMONIUM CITRATE PH 6.2. Resolution 2.10 Å R-free 0.255

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.

2 other PDB entries and 2 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name F1_VACCA
Isoform
PDB entities 1
Chains and sequence ranges Author chain A; PDBConstruct 14–182; UniProt 18–186 Author chain C; PDBConstruct 14–182; UniProt 18–186

BCL-2-LIKE PROTEIN 11

HOMO SAPIENS

UniProt O43521

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 × 8 PDB declaration: octameric(8) Consistent with protein copy count Chain B; UniProt 141–166 Chain D; UniProt 141–166 Fragment:RESIDUES 141-166 PROTEIN F1 × 4 (O57173) MRD (4R)-2-METHYLPENTANE-2,4-DIOL × 2 CL CHLORIDE ION × 8 X-RAY DIFFRACTION X-ray crystallization conditions:pH 6.2;0.2M KCL, 15 % PEG400, 1.44 % MPD AND 0.1M AMMONIUM CITRATE PH 6.2. Resolution 2.10 Å R-free 0.255

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.

38 other PDB entries and 49 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name B2L11_HUMAN
Isoform
PDB entities 2
Chains and sequence ranges Author chain B; PDBConstruct 1–26; UniProt 141–166 Author chain D; PDBConstruct 1–26; UniProt 141–166

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 4d2m

P(r) Distance Distribution P(r) Distribution

P(r) distribution for 4d2m
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2. Structure Basics 2. Structure Basics

Entry ID entry_id4d2m
Deposition date deposition_date2014-05-12
Structure title titleVaccinia Virus F1L bound to Bim BH3
Keywords keywordsAPOPTOSIS; APOPTOSIS
Experimental Method methodX-RAY DIFFRACTION

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

Radius of gyration Rg (Guinier) rg_guinier22.40
Radius of gyration Rg (electron density) rg_electron21.49
Forward intensity I(0) i024807300.00
Molecular weight molecular_weight37766.0 kDa
Excluded volume excluded_volume47108 ų
Envelope volume envelope_volume54908 ų
Hydration-shell volume shell_volume21750 ų
Envelope diameter envelope_diameter72.1
Shell Rg shell_rg27.82
Envelope Rg envelope_rg21.64
Shape Rg shape_rg21.56
Total Rg total_rg22.09
Total atoms total_atoms5224
Residues n_residues313
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 dmax70.9
Rg (real space) rg_real22.83
Rg uncertainty (real space) rg_real_error0.14
I(0) (real space) i0_real2.4420e+07
I(0) uncertainty (real space) i0_real_error2.5930e+05
Rg (reciprocal space) rg_reciprocal22.42
I(0) (reciprocal space) i0_reciprocal24810000.0000
Solution quality estimate total_estimate0.6843
Solution quality rating solution_quality REASONABLE a REASONABLE solution
P(r) peaks n_peaks1
Primary peak position r_peak_primary23.6
Skewness Skewness skewness0.403
Kurtosis Kurtosis kurtosis-0.395
Angular range angular_range— – 0.3550 −1
Current regularization parameter α current_alpha7.4180
Highest regularization parameter α highest_alpha10750000.0000
Real-space data points n_real_points67
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.917; Stabil: 0.921; Sysdev: 0.000; Positv: 1.000; Valcen: 0.990; Smooth: 0.416

5. Crystallography and Experiment 5. Crystallography & Experiment

6. Entities and Polymers Entities & Polymers (5)

7. Fold Classification (SCOP + CATH) 2 domains

CATH v4.4 (2 domains)

Domain ID domain_id4d2mA00
Class class1 — Mainly Alpha
Architecture architecture10 — Orthogonal Bundle
Topology topology437 — Apoptosis Regulator Bcl-x
Homologous superfamily homologous superfamily10 — Blc2-like
Domain ID domain_id4d2mC00
Class class1 — Mainly Alpha
Architecture architecture10 — Orthogonal Bundle
Topology topology437 — Apoptosis Regulator Bcl-x
Homologous superfamily homologous superfamily10 — Blc2-like

8. Citations (1)

9. Files and Curves (10)