8sfs

High Affinity nanobodies against GFP

Method: X-RAY DIFFRACTION Dmax: 106.3 Å Quality: GOOD

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

Green fluorescent protein

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 heterocomplex Heteromer Protein × 2 PDB declaration: dimeric(2) Consistent with protein copy count Chain A; UniProt 1–238 Non-standard monomer:Yes (specific site not provided by mmCIF) LaG16 × 1 NH4 AMMONIUM ION × 6 GOL GLYCEROL × 6 CL CHLORIDE ION × 1 SO4 SULFATE ION × 3 X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, SITTING DROP;294 K;0.1 M HEPES pH 7.5, 1.26 M ammonium sulphate Resolution 2.37 Å R-free 0.218
2 Protein heterocomplex Heteromer Protein × 2 PDB declaration: dimeric(2) Consistent with protein copy count Chain B; UniProt 1–238 Non-standard monomer:Yes (specific site not provided by mmCIF) LaG16 × 1 NH4 AMMONIUM ION × 5 GOL GLYCEROL × 4 CL CHLORIDE ION × 3 SO4 SULFATE ION × 4 NA SODIUM ION × 3 X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, SITTING DROP;294 K;0.1 M HEPES pH 7.5, 1.26 M ammonium sulphate Resolution 2.37 Å R-free 0.218

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 743 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 1–237; UniProt 1–238 Author chain B; PDBConstruct 1–237; UniProt 1–238

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 8sfs

P(r) Distance Distribution P(r) Distribution

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

Entry ID entry_id8sfs
Deposition date deposition_date2023-04-11
Structure title titleHigh Affinity nanobodies against GFP
Keywords keywords;Nanobody, nanobodies, GFP, green fluorescent protein, high-affinity antibody variant, antibody variant, single-domain antibody, IMMUNE SYSTEM ;; IMMUNE SYSTEM
Experimental Method methodX-RAY DIFFRACTION

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

Radius of gyration Rg (Guinier) rg_guinier31.61
Radius of gyration Rg (electron density) rg_electron30.85
Forward intensity I(0) i0111530000.00
Molecular weight molecular_weight81437.0 kDa
Excluded volume excluded_volume100870 ų
Envelope volume envelope_volume126730 ų
Hydration-shell volume shell_volume35997 ų
Envelope diameter envelope_diameter112.0
Shell Rg shell_rg36.14
Envelope Rg envelope_rg31.01
Shape Rg shape_rg30.78
Total Rg total_rg31.51
Total atoms total_atoms5838
Residues n_residues708
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 dmax106.3
Rg (real space) rg_real31.70
Rg uncertainty (real space) rg_real_error0.94
I(0) (real space) i0_real1.1150e+08
I(0) uncertainty (real space) i0_real_error1.7240e+06
Rg (reciprocal space) rg_reciprocal31.67
I(0) (reciprocal space) i0_reciprocal111500000.0000
Solution quality estimate total_estimate0.8784
Solution quality rating solution_quality GOOD a GOOD solution
P(r) peaks n_peaks2
Primary peak position r_peak_primary36.1
Skewness Skewness skewness0.398
Kurtosis Kurtosis kurtosis-0.319
Angular range angular_range— – 0.2500 −1
Current regularization parameter α current_alpha0.0000
Highest regularization parameter α highest_alpha21930000.0000
Real-space data points n_real_points51
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.873; Stabil: 1.000; Sysdev: 1.000; Positv: 1.000; Valcen: 0.967; Smooth: 0.829

5. Crystallography and Experiment 5. Crystallography & Experiment

6. Entities and Polymers Entities & Polymers (8)

8. Citations (1)

9. Files and Curves (10)