8um7

Site-specific Aspartic Acid Dehydration and Isomerization in Streptococcal Protein GB1: Wild-type Protein

Method: SOLUTION NMR Dmax: 36.6 Å Quality: GOOD

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

Immunoglobulin G-binding protein G

OrganismNot specified

UniProt P19909

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 304–357 Not recorded No other associated polymer SOLUTION NMR NMR measurement conditions:pH 7;298 K;Ionic strength (raw mmCIF value) 41;Pressure 1 NMR sample composition:0.12 mM B1 Domain of Streptococcal Protein G, 20 mM sodium phosphate, 0.1 mM DSS, 90% H2O/10% D2O | 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.

76 other PDB entries and 116 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name SPG2_STRSG
Isoform
PDB entities 1
Chains and sequence ranges Author chain A; PDBConstruct 3–56; UniProt 304–357

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 8um7

P(r) Distance Distribution P(r) Distribution

P(r) distribution for 8um7
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2. Structure Basics 2. Structure Basics

Entry ID entry_id8um7
Deposition date deposition_date2023-10-17
最后修订 last_revision2024-05-01
Structure title titleSite-specific Aspartic Acid Dehydration and Isomerization in Streptococcal Protein GB1: Wild-type Protein
Keywords keywordsimmunoglobulin binding domain, IMMUNE SYSTEM; IMMUNE SYSTEM
Experimental Method methodSOLUTION NMR

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

Radius of gyration Rg (Guinier) rg_guinier10.83
Radius of gyration Rg (electron density) rg_electron10.58
Forward intensity I(0) i057621600.00
Molecular weight molecular_weight62188.0 kDa
Excluded volume excluded_volume77324 ų
Envelope volume envelope_volume11500 ų
Hydration-shell volume shell_volume8713 ų
Envelope diameter envelope_diameter40.3
Shell Rg shell_rg16.89
Envelope Rg envelope_rg11.97
Shape Rg shape_rg10.50
Total Rg total_rg11.11
Total atoms total_atoms8580
Residues n_residues560
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 dmax36.6
Rg (real space) rg_real10.77
Rg uncertainty (real space) rg_real_error0.38
I(0) (real space) i0_real5.7620e+07
I(0) uncertainty (real space) i0_real_error5.6540e+05
Rg (reciprocal space) rg_reciprocal10.78
I(0) (reciprocal space) i0_reciprocal57620000.0000
Solution quality estimate total_estimate0.8202
Solution quality rating solution_quality GOOD a GOOD solution
P(r) peaks n_peaks2
Primary peak position r_peak_primary13.9
Skewness Skewness skewness0.119
Kurtosis Kurtosis kurtosis-0.332
Angular range angular_range— – 0.5000 −1
Current regularization parameter α current_alpha0.0000
Highest regularization parameter α highest_alpha57010.0000
Real-space data points n_real_points80
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.631; Stabil: 0.995; Sysdev: 1.000; Positv: 1.000; Valcen: 1.000; Smooth: 0.783

5. Crystallography and Experiment 5. Crystallography & Experiment

6. Entities and Polymers Entities & Polymers (1)

8. Citations (1)

9. Files and Curves (10)