8bvg

Bright fluorescent protein BrUSLEE with subnanosecond fluorescence lifetime

Method: X-RAY DIFFRACTION Dmax: 117.9 Å Quality: EXCELLENT

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

BrUSSLEE

Aequorea victoria

UniProt P42212

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 homooligomer Homooligomer Protein × 2 PDB declaration: dimeric(2) Consistent with protein copy count Chain A; UniProt 2–238 Chain C; UniProt 2–238 Non-standard monomer:Yes (specific site not provided by mmCIF) GOL GLYCEROL × 3 X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, HANGING DROP;pH 5;293 K;6.4% Tacsimate pH 5.0, 16% PEG 3350 Resolution 2.38 Å R-free 0.271
2 Protein homooligomer Homooligomer Protein × 2 PDB declaration: dimeric(2) Consistent with protein copy count Chain B; UniProt 2–238 Chain D; UniProt 2–238 Non-standard monomer:Yes (specific site not provided by mmCIF) GOL GLYCEROL × 1 X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, HANGING DROP;pH 5;293 K;6.4% Tacsimate pH 5.0, 16% PEG 3350 Resolution 2.38 Å R-free 0.271
3 Protein homooligomer Homooligomer Protein × 2 PDB declaration: dimeric(2) Consistent with protein copy count Chain E; UniProt 2–238 Chain F; UniProt 2–238 Non-standard monomer:Yes (specific site not provided by mmCIF) No other associated polymer X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, HANGING DROP;pH 5;293 K;6.4% Tacsimate pH 5.0, 16% PEG 3350 Resolution 2.38 Å R-free 0.271

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.

568 other PDB entries and 742 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name GFP_AEQVI
Isoform
PDB entities 1
Chains and sequence ranges Author chain A; PDBConstruct 2–236; UniProt 2–238 Author chain B; PDBConstruct 2–236; UniProt 2–238 Author chain C; PDBConstruct 2–236; UniProt 2–238 Author chain D; PDBConstruct 2–236; UniProt 2–238 Author chain E; PDBConstruct 2–236; UniProt 2–238 Author chain F; PDBConstruct 2–236; UniProt 2–238

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 8bvg

P(r) Distance Distribution P(r) Distribution

P(r) distribution for 8bvg
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2. Structure Basics 2. Structure Basics

Entry ID entry_id8bvg
Deposition date deposition_date2022-12-03
Structure title titleBright fluorescent protein BrUSLEE with subnanosecond fluorescence lifetime
Keywords keywordsBrUSSLEE, GFP-like biomarker, Fluorescent Protein; FLUORESCENT PROTEIN
Experimental Method methodX-RAY DIFFRACTION

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

Radius of gyration Rg (Guinier) rg_guinier38.03
Radius of gyration Rg (electron density) rg_electron37.47
Forward intensity I(0) i0362480000.00
Molecular weight molecular_weight155250.0 kDa
Excluded volume excluded_volume194290 ų
Envelope volume envelope_volume251480 ų
Hydration-shell volume shell_volume55041 ų
Envelope diameter envelope_diameter115.9
Shell Rg shell_rg44.36
Envelope Rg envelope_rg36.75
Shape Rg shape_rg37.45
Total Rg total_rg37.95
Total atoms total_atoms10950
Residues n_residues1365
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 dmax117.9
Rg (real space) rg_real37.85
Rg uncertainty (real space) rg_real_error1.03
I(0) (real space) i0_real3.6250e+08
I(0) uncertainty (real space) i0_real_error5.9870e+06
Rg (reciprocal space) rg_reciprocal37.97
I(0) (reciprocal space) i0_reciprocal362500000.0000
Solution quality estimate total_estimate0.9116
Solution quality rating solution_quality EXCELLENT a EXCELLENT solution
P(r) peaks n_peaks1
Primary peak position r_peak_primary47.7
Skewness Skewness skewness0.097
Kurtosis Kurtosis kurtosis-0.719
Angular range angular_range— – 0.2100 −1
Current regularization parameter α current_alpha0.0000
Highest regularization parameter α highest_alpha76660000.0000
Real-space data points n_real_points43
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.962; Stabil: 1.000; Sysdev: 1.000; Positv: 1.000; Valcen: 0.998; Smooth: 0.962

5. Crystallography and Experiment 5. Crystallography & Experiment

6. Entities and Polymers Entities & Polymers (3)

8. Citations (1)

9. Files and Curves (10)