9r3y

Solution NMR structure of N-WASP GBD in complex with EspFu R5

Method: SOLUTION NMR Dmax: 55.2 Å Quality: REASONABLE

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

Actin nucleation-promoting factor WASL

Homo sapiens

UniProt O00401

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 heterocomplex Heteromer Protein × 2 PDB declaration: dimeric(2) Consistent with protein copy count Chain A; UniProt 207–275 Not recorded Secreted effector protein EspF(U) × 1 (Q8X482) SOLUTION NMR NMR measurement conditions:pH 6.5;298 K;Ionic strength (raw mmCIF value) 0.11;Pressure ambient NMR sample composition:0.5 mM [U-13C; U-15N] N-WASP GBD, 0.6 mM EspFu R5, 20 mM sodium phosphate, 50 mM sodium chloride, 95% H2O/5% D2O | 95% H2O/5% D2O NMR sample composition:0.4 mM N-WASP GBD, 0.3 mM [U-13C; U-15N] EspFu R5, 20 mM sodium phosphate, 50 mM sodium chloride, 95% H2O/5% D2O | 95% H2O/5% 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.

7 other PDB entries and 15 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name WASL_HUMAN
Isoform
PDB entities 1
Chains and sequence ranges Author chain A; PDBConstruct 5–73; UniProt 207–275

Secreted effector protein EspF(U)

Escherichia coli

UniProt Q8X482

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 heterocomplex Heteromer Protein × 2 PDB declaration: dimeric(2) Consistent with protein copy count Chain B; UniProt 127–173 Not recorded Actin nucleation-promoting factor WASL × 1 (O00401) SOLUTION NMR NMR measurement conditions:pH 6.5;298 K;Ionic strength (raw mmCIF value) 0.11;Pressure ambient NMR sample composition:0.5 mM [U-13C; U-15N] N-WASP GBD, 0.6 mM EspFu R5, 20 mM sodium phosphate, 50 mM sodium chloride, 95% H2O/5% D2O | 95% H2O/5% D2O NMR sample composition:0.4 mM N-WASP GBD, 0.3 mM [U-13C; U-15N] EspFu R5, 20 mM sodium phosphate, 50 mM sodium chloride, 95% H2O/5% D2O | 95% H2O/5% 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.

No other PDB entry for the same UniProt protein was found.

View Construct and Data Evidence
UniProt name ESPFU_ECO57
Isoform
PDB entities 2
Chains and sequence ranges Author chain B; PDBConstruct 2–48; UniProt 127–173

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 9r3y

P(r) Distance Distribution P(r) Distribution

P(r) distribution for 9r3y
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2. Structure Basics 2. Structure Basics

Entry ID entry_id9r3y
Deposition date deposition_date2025-05-06
最后修订 last_revision2025-10-22
Structure title titleSolution NMR structure of N-WASP GBD in complex with EspFu R5
Keywords keywordsComplex, SIGNALING PROTEIN; SIGNALING PROTEIN
Experimental Method methodSOLUTION NMR

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

Radius of gyration Rg (Guinier) rg_guinier19.57
Radius of gyration Rg (electron density) rg_electron19.06
Forward intensity I(0) i01162630000.00
Molecular weight molecular_weight271660.0 kDa
Excluded volume excluded_volume333940 ų
Envelope volume envelope_volume132250 ų
Hydration-shell volume shell_volume36048 ų
Envelope diameter envelope_diameter120.5
Shell Rg shell_rg37.04
Envelope Rg envelope_rg32.63
Shape Rg shape_rg19.06
Total Rg total_rg19.67
Total atoms total_atoms37480
Residues n_residues2420
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 dmax55.2
Rg (real space) rg_real17.99
Rg uncertainty (real space) rg_real_error0.14
I(0) (real space) i0_real1.1070e+09
I(0) uncertainty (real space) i0_real_error1.0660e+07
Rg (reciprocal space) rg_reciprocal20.09
I(0) (reciprocal space) i0_reciprocal1163000000.0000
Solution quality estimate total_estimate0.6413
Solution quality rating solution_quality REASONABLE a REASONABLE solution
P(r) peaks n_peaks1
Primary peak position r_peak_primary19.4
Skewness Skewness skewness0.613
Kurtosis Kurtosis kurtosis-0.005
Angular range angular_range— – 0.4050 −1
Current regularization parameter α current_alpha1.8410
Highest regularization parameter α highest_alpha798500.0000
Real-space data points n_real_points72
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.008; Oscil: 0.809; Stabil: 0.991; Sysdev: 0.000; Positv: 1.000; Valcen: 0.973; 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)