7o7h

Crystal structure of rsEGFP2 mutant V151L in the non-fluorescent off-state determined by synchrotron radiation at 100K

Method: X-RAY DIFFRACTION Dmax: 63.5 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 monomer Monomer Protein × 1 PDB declaration: monomeric(1) Consistent with protein copy count Chain A; UniProt 1–238 Mutation:M1_S2insV, F64L, S65T, H231L, A206K, Q69L, V163S, T65A, V150L 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 8.2;293 K;1.8 M ammonium sulfate, 100 mM HEPES pH 8.2 Resolution 1.70 Å R-free 0.197

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 744 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 14–250; 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 7o7h

P(r) Distance Distribution P(r) Distribution

P(r) distribution for 7o7h
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2. Structure Basics 2. Structure Basics

Entry ID entry_id7o7h
Deposition date deposition_date2021-04-13
Structure title titleCrystal structure of rsEGFP2 mutant V151L in the non-fluorescent off-state determined by synchrotron radiation at 100K
Keywords keywordsReversibly photoswitchable fluorescent protein, 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_guinier18.82
Radius of gyration Rg (electron density) rg_electron17.51
Forward intensity I(0) i013028600.00
Molecular weight molecular_weight26937.0 kDa
Excluded volume excluded_volume33690 ų
Envelope volume envelope_volume38383 ų
Hydration-shell volume shell_volume18207 ų
Envelope diameter envelope_diameter63.9
Shell Rg shell_rg23.92
Envelope Rg envelope_rg17.94
Shape Rg shape_rg17.50
Total Rg total_rg18.54
Total atoms total_atoms1902
Residues n_residues236
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 dmax63.5
Rg (real space) rg_real18.75
Rg uncertainty (real space) rg_real_error0.39
I(0) (real space) i0_real1.3030e+07
I(0) uncertainty (real space) i0_real_error1.7370e+05
Rg (reciprocal space) rg_reciprocal18.76
I(0) (reciprocal space) i0_reciprocal13030000.0000
Solution quality estimate total_estimate0.7918
Solution quality rating solution_quality GOOD a GOOD solution
P(r) peaks n_peaks2
Primary peak position r_peak_primary23.5
Skewness Skewness skewness0.275
Kurtosis Kurtosis kurtosis-0.277
Angular range angular_range— – 0.4250 −1
Current regularization parameter α current_alpha0.0000
Highest regularization parameter α highest_alpha4203000.0000
Real-space data points n_real_points74
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.764; Stabil: 1.000; Sysdev: 1.000; Positv: 1.000; Valcen: 0.999; Smooth: 0.000

5. Crystallography and Experiment 5. Crystallography & Experiment

6. Entities and Polymers Entities & Polymers (2)

8. Citations (1)

9. Files and Curves (10)