1rmm

Probing the Role of Tryptophans in Aequorea Victoria Green Fluorescent Proteins with an Expanded Genetic Code

Method: X-RAY DIFFRACTION Dmax: 57.0 Å Quality: GOOD

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

SIGF1-GFP fusion 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 290–517 Non-standard monomer:Yes (specific site not provided by mmCIF) No other associated polymer X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, SITTING DROP;pH 7;293 K;14% PEG 1000, pH 7.0, VAPOR DIFFUSION, SITTING DROP, temperature 293K Resolution 1.90 Å R-free 0.233

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 1–224; UniProt 290–517

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 1rmm

P(r) Distance Distribution P(r) Distribution

P(r) distribution for 1rmm
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2. Structure Basics 2. Structure Basics

Entry ID entry_id1rmm
Deposition date deposition_date2003-11-28
Structure title titleProbing the Role of Tryptophans in Aequorea Victoria Green Fluorescent Proteins with an Expanded Genetic Code
Keywords keywordsBeta-barrel; GFP; Noncanonical amino acid, LUMINESCENT PROTEIN; LUMINESCENT PROTEIN
Experimental Method methodX-RAY DIFFRACTION

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

Radius of gyration Rg (Guinier) rg_guinier18.23
Radius of gyration Rg (electron density) rg_electron16.95
Forward intensity I(0) i011974900.00
Molecular weight molecular_weight25688.0 kDa
Excluded volume excluded_volume32071 ų
Envelope volume envelope_volume36228 ų
Hydration-shell volume shell_volume17671 ų
Envelope diameter envelope_diameter57.1
Shell Rg shell_rg23.24
Envelope Rg envelope_rg17.29
Shape Rg shape_rg16.94
Total Rg total_rg17.97
Total atoms total_atoms1809
Residues n_residues224
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 dmax57.0
Rg (real space) rg_real18.13
Rg uncertainty (real space) rg_real_error0.26
I(0) (real space) i0_real1.1970e+07
I(0) uncertainty (real space) i0_real_error1.4340e+05
Rg (reciprocal space) rg_reciprocal18.15
I(0) (reciprocal space) i0_reciprocal11980000.0000
Solution quality estimate total_estimate0.8966
Solution quality rating solution_quality GOOD a GOOD solution
P(r) peaks n_peaks1
Primary peak position r_peak_primary55.4
Skewness Skewness skewness0.186
Kurtosis Kurtosis kurtosis-0.401
Angular range angular_range— – 0.4350 −1
Current regularization parameter α current_alpha0.0000
Highest regularization parameter α highest_alpha3826000.0000
Real-space data points n_real_points75
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.891; Stabil: 1.000; Sysdev: 1.000; Positv: 1.000; Valcen: 0.990; Smooth: 0.990

5. Crystallography and Experiment 5. Crystallography & Experiment

6. Entities and Polymers Entities & Polymers (2)

7. Fold Classification (SCOP + CATH) 2 domains

SCOP 2.08 (1 domains)

Domain ID domain_idd1rmma_
Class classd — Alpha and beta proteins (a+b)
Fold Fold foldd.22 — GFP-like
Superfamily Superfamily superfamilyd.22.1 — GFP-like
Family Family familyd.22.1.1 — Fluorescent proteins

CATH v4.4 (1 domains)

Domain ID domain_id1rmmA00
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)