9fem

mNeonGreen - Directionality of Optical Properties of Fluorescent Proteins

Method: X-RAY DIFFRACTION Dmax: 55.8 Å Quality: REASONABLE

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

mNeonGreen

Branchiostoma lanceolatum

UniProt A0A1S4NYF2

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 25–260 Non-standard monomer:Yes (specific site not provided by mmCIF) SO4 SULFATE ION × 1 X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, HANGING DROP;pH 7.5;291 K;100 mM sodium HEPES 20% PEG 8000 Resolution 2.32 Å R-free 0.294

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.

8 other PDB entries and 8 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name A0A1S4NYF2_BRALA
Isoform
PDB entities 1
Chains and sequence ranges Author chain A; PDBConstruct 1–234; UniProt 25–260

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 9fem

P(r) Distance Distribution P(r) Distribution

P(r) distribution for 9fem
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2. Structure Basics 2. Structure Basics

Entry ID entry_id9fem
Deposition date deposition_date2024-05-21
最后修订 last_revision2025-06-04
Structure title titlemNeonGreen - Directionality of Optical Properties of Fluorescent Proteins
Keywords keywordsFLUORESCENT PROTEIN; FLUORESCENT PROTEIN
Experimental Method methodX-RAY DIFFRACTION

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

Radius of gyration Rg (Guinier) rg_guinier17.72
Radius of gyration Rg (electron density) rg_electron16.51
Forward intensity I(0) i010951900.00
Molecular weight molecular_weight24402.0 kDa
Excluded volume excluded_volume30341 ų
Envelope volume envelope_volume33567 ų
Hydration-shell volume shell_volume16871 ų
Envelope diameter envelope_diameter55.9
Shell Rg shell_rg22.76
Envelope Rg envelope_rg16.83
Shape Rg shape_rg16.47
Total Rg total_rg17.60
Total atoms total_atoms1723
Residues n_residues214
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 dmax55.8
Rg (real space) rg_real17.61
Rg uncertainty (real space) rg_real_error0.26
I(0) (real space) i0_real1.0950e+07
I(0) uncertainty (real space) i0_real_error1.3030e+05
Rg (reciprocal space) rg_reciprocal17.63
I(0) (reciprocal space) i0_reciprocal10950000.0000
Solution quality estimate total_estimate0.7282
Solution quality rating solution_quality REASONABLE a REASONABLE solution
P(r) peaks n_peaks2
Primary peak position r_peak_primary23.1
Skewness Skewness skewness0.197
Kurtosis Kurtosis kurtosis-0.357
Angular range angular_range— – 0.4500 −1
Current regularization parameter α current_alpha0.0000
Highest regularization parameter α highest_alpha2996000.0000
Real-space data points n_real_points76
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.872; Stabil: 1.000; Sysdev: 0.291; Positv: 1.000; Valcen: 0.997; Smooth: 0.977

5. Crystallography and Experiment 5. Crystallography & Experiment

6. Entities and Polymers Entities & Polymers (3)

8. Citations (2)

9. Files and Curves (10)