6okw

Solution structure of VEK50

Method: SOLUTION NMR Dmax: 34.9 Å Quality: REASONABLE

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

Plasminogen-binding group A streptococcal M-like protein PAM

Streptococcus pyogenes

UniProt P49054

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 85–133 Fragment:residues 85-133 No other associated polymer SOLUTION NMR NMR measurement conditions:pH 6.8;298 K;Ionic strength (raw mmCIF value) 20;Pressure 1 NMR sample composition:0.5 mM [U-99% 13C; U-99% 15N] VEK50, 2 ug/mL DSS, 20 mM [U-2H] Bis-Tris-d19, 1 ug/mL DTT, 1 ug/mL sodium azide, 93% H2O/7% D2O | 93% H2O/7% 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.

9 other PDB entries and 10 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name PAM_STRPY
Isoform
PDB entities 1
Chains and sequence ranges Author chain A; PDBConstruct 3–51; UniProt 85–133

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 6okw

P(r) Distance Distribution P(r) Distribution

P(r) distribution for 6okw
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2. Structure Basics 2. Structure Basics

Entry ID entry_id6okw
Deposition date deposition_date2019-04-15
Structure title titleSolution structure of VEK50
Keywords keywordsPlasminogen binding peptide, PROTEIN BINDING; PROTEIN BINDING
Experimental Method methodSOLUTION NMR

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

Radius of gyration Rg (Guinier) rg_guinier13.29
Radius of gyration Rg (electron density) rg_electron13.13
Forward intensity I(0) i068335900.00
Molecular weight molecular_weight61547.0 kDa
Excluded volume excluded_volume74929 ų
Envelope volume envelope_volume31455 ų
Hydration-shell volume shell_volume16037 ų
Envelope diameter envelope_diameter62.4
Shell Rg shell_rg22.95
Envelope Rg envelope_rg17.39
Shape Rg shape_rg13.11
Total Rg total_rg13.89
Total atoms total_atoms8570
Residues n_residues520
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 dmax34.9
Rg (real space) rg_real12.48
Rg uncertainty (real space) rg_real_error0.04
I(0) (real space) i0_real6.4950e+07
I(0) uncertainty (real space) i0_real_error4.5300e+05
Rg (reciprocal space) rg_reciprocal13.37
I(0) (reciprocal space) i0_reciprocal68340000.0000
Solution quality estimate total_estimate0.6844
Solution quality rating solution_quality REASONABLE a REASONABLE solution
P(r) peaks n_peaks1
Primary peak position r_peak_primary15.0
Skewness Skewness skewness0.219
Kurtosis Kurtosis kurtosis-0.414
Angular range angular_range— – 0.5000 −1
Current regularization parameter α current_alpha4.2750
Highest regularization parameter α highest_alpha416500.0000
Real-space data points n_real_points80
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.005; Oscil: 0.993; Stabil: 0.975; Sysdev: 0.000; Positv: 1.000; Valcen: 0.994; Smooth: 0.000

5. Crystallography and Experiment 5. Crystallography & Experiment

6. Entities and Polymers Entities & Polymers (1)

8. Citations (1)

9. Files and Curves (10)