4ik3

High resolution structure of GCaMP3 at pH 8.5

Method: X-RAY DIFFRACTION Dmax: 78.8 Å Quality: GOOD

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

RCaMP, Green fluorescent protein

Entacmaea quadricolor

UniProt K4DIE3

State in the Current Structure

Assembly Oligomeric State Construct Mutations and Modifications Ligands, Ions and Associated Components Method and Experimental Conditions Structure Quality
1 Insufficient information Homooligomer Protein × 2 PDB declaration: dimeric(2) Consistent with protein copy count Chain A; UniProt 1–48 Chain A; UniProt 284–432 Mutation:M153K, V163A, S175G, D180Y, T203V, A206K, H231L, F64L, V93I, I354T Non-standard monomer:Yes (specific site not provided by mmCIF) CA CALCIUM ION × 8 X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, HANGING DROP;pH 8.5;289 K;Tris pH 8.5, (NH4)2SO4, 23% PEG 3350, VAPOR DIFFUSION, HANGING DROP, temperature 289K Resolution 2.01 Å R-free 0.214

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 K4DIE3_ENTQU
Isoform
PDB entities 1
Chains and sequence ranges Author chain A; PDBConstruct 11–58; UniProt 1–48 Author chain A; PDBConstruct 300–448; UniProt 284–432

RCaMP, Green fluorescent protein

Entacmaea quadricolor

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 Insufficient information Homooligomer Protein × 2 PDB declaration: dimeric(2) Consistent with protein copy count Chain A; UniProt 149–238 Chain A; UniProt 2–144 Mutation:M153K, V163A, S175G, D180Y, T203V, A206K, H231L, F64L, V93I, I354T Non-standard monomer:Yes (specific site not provided by mmCIF) CA CALCIUM ION × 8 X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, HANGING DROP;pH 8.5;289 K;Tris pH 8.5, (NH4)2SO4, 23% PEG 3350, VAPOR DIFFUSION, HANGING DROP, temperature 289K Resolution 2.01 Å R-free 0.214

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 61–150; UniProt 149–238 Author chain A; PDBConstruct 159–299; UniProt 2–144

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 4ik3

P(r) Distance Distribution P(r) Distribution

P(r) distribution for 4ik3
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2. Structure Basics 2. Structure Basics

Entry ID entry_id4ik3
Deposition date deposition_date2012-12-25
Structure title titleHigh resolution structure of GCaMP3 at pH 8.5
Keywords keywordscalcium indicator, mutants, fluorescent intensity, dimerization, Beta barrel, Calmodulin, 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_guinier25.64
Radius of gyration Rg (electron density) rg_electron24.52
Forward intensity I(0) i035280400.00
Molecular weight molecular_weight44679.0 kDa
Excluded volume excluded_volume55483 ų
Envelope volume envelope_volume72407 ų
Hydration-shell volume shell_volume25419 ų
Envelope diameter envelope_diameter79.6
Shell Rg shell_rg30.76
Envelope Rg envelope_rg24.44
Shape Rg shape_rg24.50
Total Rg total_rg25.34
Total atoms total_atoms3137
Residues n_residues393
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 dmax78.8
Rg (real space) rg_real25.60
Rg uncertainty (real space) rg_real_error0.66
I(0) (real space) i0_real3.5280e+07
I(0) uncertainty (real space) i0_real_error5.2090e+05
Rg (reciprocal space) rg_reciprocal25.62
I(0) (reciprocal space) i0_reciprocal35280000.0000
Solution quality estimate total_estimate0.8384
Solution quality rating solution_quality GOOD a GOOD solution
P(r) peaks n_peaks2
Primary peak position r_peak_primary29.2
Skewness Skewness skewness0.227
Kurtosis Kurtosis kurtosis-0.610
Angular range angular_range— – 0.3100 −1
Current regularization parameter α current_alpha0.0000
Highest regularization parameter α highest_alpha3794000.0000
Real-space data points n_real_points63
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.966; Stabil: 0.999; Sysdev: 1.000; Positv: 1.000; Valcen: 0.998; Smooth: 0.000

5. Crystallography and Experiment 5. Crystallography & Experiment

6. Entities and Polymers Entities & Polymers (3)

7. Fold Classification (SCOP + CATH) 1 domains

CATH v4.4 (1 domains)

Domain ID domain_id4ik3A01
Class class2 — Mainly Beta
Architecture architecture40 — Beta Barrel
Topology topology155 — Green Fluorescent Protein
Homologous superfamily homologous superfamily10 — Green fluorescent protein

8. Citations (1)

9. Files and Curves (10)