2bau

Solution NMR structure of the micelle-bound myristoylated N-terminal Arf6

Method: SOLUTION NMR Dmax: 11.7 Å Quality: REASONABLE

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

ADP-ribosylation factor 6

OrganismNot specified

UniProt P62330

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 1–10 Fragment:N-terminal peptide MYR MYRISTIC ACID × 1 SOLUTION NMR NMR measurement conditions:pH 5;298 K;Ionic strength (raw mmCIF value) 7;Pressure ambient NMR sample composition:5mM Myristoylated N-terminal Arf6; 5mM acetate buffer, 100mM fully deuterated dodecylphosphocholine (DPC) | 90% H2O/10% D2O Resolution not provided

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.

17 other PDB entries and 20 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name ARF6_HUMAN
Isoform
PDB entities 1
Chains and sequence ranges Author chain A; PDBConstruct 1–10; UniProt 1–10

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 2bau

P(r) Distance Distribution P(r) Distribution

P(r) distribution for 2bau
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2. Structure Basics 2. Structure Basics

Entry ID entry_id2bau
Deposition date deposition_date2005-10-14
Structure title titleSolution NMR structure of the micelle-bound myristoylated N-terminal Arf6
Keywords keywordsMicelle-bound, myristoylated peptide, SIGNALING PROTEIN; SIGNALING PROTEIN
Experimental Method methodSOLUTION NMR

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

Radius of gyration Rg (Guinier) rg_guinier3.37
Radius of gyration Rg (electron density) rg_electron6.07
Forward intensity I(0) i01708780.00
Molecular weight molecular_weight15104.0 kDa
Excluded volume excluded_volume21075 ų
Envelope volume envelope_volume3401 ų
Hydration-shell volume shell_volume4090 ų
Envelope diameter envelope_diameter29.1
Shell Rg shell_rg12.55
Envelope Rg envelope_rg8.77
Shape Rg shape_rg5.98
Total Rg total_rg7.42
Total atoms total_atoms2388
Residues n_residues120
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 dmax11.7
Rg (real space) rg_real3.71
Rg uncertainty (real space) rg_real_error0.02
I(0) (real space) i0_real1.7640e+06
I(0) uncertainty (real space) i0_real_error9.0930e+03
Rg (reciprocal space) rg_reciprocal2.81
I(0) (reciprocal space) i0_reciprocal1709000.0000
Solution quality estimate total_estimate0.6997
Solution quality rating solution_quality REASONABLE a REASONABLE solution
P(r) peaks n_peaks1
Primary peak position r_peak_primary4.0
Skewness Skewness skewness0.266
Kurtosis Kurtosis kurtosis-0.645
Angular range angular_range— – 0.5000 −1
Current regularization parameter α current_alpha1.5610
Highest regularization parameter α highest_alpha62.8900
Real-space data points n_real_points80
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.982; Stabil: 0.912; Sysdev: 0.000; Positv: 1.000; Valcen: 0.769; Smooth: 0.645

5. Crystallography and Experiment 5. Crystallography & Experiment

6. Entities and Polymers Entities & Polymers (2)

8. Citations (1)

9. Files and Curves (10)