8txp

Crystal structure of 05.GC.w13.01 Fab in complex with H1 HA from A/California/04/2009(H1N1)

Method: X-RAY DIFFRACTION Dmax: 135.2 Å Quality: GOOD

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

Hemagglutinin

Influenza A virus

UniProt C3W5S1

State in the Current Structure

Assembly Oligomeric State Construct Mutations and Modifications Ligands, Ions and Associated Components Method and Experimental Conditions Structure Quality
1 Other combination Heteromer Protein × 12 其他Polymer 15 PDB declaration: dodecameric(12) Consistent with protein copy count Chain A; UniProt 18–344 Fragment:HA1 subdomain (UNP residues 18-344) Hemagglutinin × 3 (I1ZFF9) GC_w13_A, Fab heavy chain × 3 GC_w13_A, Fab light chain × 3 2-acetamido-2-deoxy-beta-D-glucopyranose-(1-4)-2-acetamido-2-deoxy-beta-D-glucopyranose × 6 beta-D-mannopyranose-(1-4)-2-acetamido-2-deoxy-beta-D-glucopyranose-(1-4)-2-acetamido-2-deoxy-beta-D-glucopyranose × 9 X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, HANGING DROP;293 K;0.2 M sodium acetate, pH 6.2, 20% PEG3350 Resolution 2.75 Å R-free 0.292

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.

21 other PDB entries and 40 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name C3W5S1_I09A0
Isoform
PDB entities 1
Chains and sequence ranges Author chain A; PDBConstruct 5–331; UniProt 18–344

Hemagglutinin

Influenza A virus

UniProt I1ZFF9

State in the Current Structure

Assembly Oligomeric State Construct Mutations and Modifications Ligands, Ions and Associated Components Method and Experimental Conditions Structure Quality
1 Other combination Heteromer Protein × 12 其他Polymer 15 PDB declaration: dodecameric(12) Consistent with protein copy count Chain B; UniProt 326–499 Fragment:HA2 subdomain (UNP residues 326-499) Hemagglutinin × 3 (C3W5S1) GC_w13_A, Fab heavy chain × 3 GC_w13_A, Fab light chain × 3 2-acetamido-2-deoxy-beta-D-glucopyranose-(1-4)-2-acetamido-2-deoxy-beta-D-glucopyranose × 6 beta-D-mannopyranose-(1-4)-2-acetamido-2-deoxy-beta-D-glucopyranose-(1-4)-2-acetamido-2-deoxy-beta-D-glucopyranose × 9 X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, HANGING DROP;293 K;0.2 M sodium acetate, pH 6.2, 20% PEG3350 Resolution 2.75 Å R-free 0.292

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.

3 other PDB entries and 4 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name I1ZFF9_9INFA
Isoform
PDB entities 2
Chains and sequence ranges Author chain B; PDBConstruct 1–174; UniProt 326–499

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 8txp

P(r) Distance Distribution P(r) Distribution

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

Entry ID entry_id8txp
Deposition date deposition_date2023-08-24
Structure title titleCrystal structure of 05.GC.w13.01 Fab in complex with H1 HA from A/California/04/2009(H1N1)
Keywords keywordsH1N1, Antibody, Hemagglutinin, VIRAL PROTEIN-IMMUNE SYSTEM complex; VIRAL PROTEIN/IMMUNE SYSTEM
Experimental Method methodX-RAY DIFFRACTION

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

Radius of gyration Rg (Guinier) rg_guinier40.93
Radius of gyration Rg (electron density) rg_electron40.88
Forward intensity I(0) i0173444000.00
Molecular weight molecular_weight105250.0 kDa
Excluded volume excluded_volume131030 ų
Envelope volume envelope_volume185340 ų
Hydration-shell volume shell_volume40291 ų
Envelope diameter envelope_diameter140.3
Shell Rg shell_rg42.90
Envelope Rg envelope_rg40.31
Shape Rg shape_rg40.90
Total Rg total_rg40.95
Total atoms total_atoms7404
Residues n_residues930
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 dmax135.2
Rg (real space) rg_real41.06
Rg uncertainty (real space) rg_real_error1.33
I(0) (real space) i0_real1.7340e+08
I(0) uncertainty (real space) i0_real_error3.2720e+06
Rg (reciprocal space) rg_reciprocal40.93
I(0) (reciprocal space) i0_reciprocal173400000.0000
Solution quality estimate total_estimate0.8538
Solution quality rating solution_quality GOOD a GOOD solution
P(r) peaks n_peaks1
Primary peak position r_peak_primary34.7
Skewness Skewness skewness0.282
Kurtosis Kurtosis kurtosis-0.722
Angular range angular_range— – 0.1950 −1
Current regularization parameter α current_alpha0.0000
Highest regularization parameter α highest_alpha14090000.0000
Real-space data points n_real_points40
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.862; Stabil: 1.000; Sysdev: 1.000; Positv: 1.000; Valcen: 0.768; Smooth: 0.742

5. Crystallography and Experiment 5. Crystallography & Experiment

6. Entities and Polymers Entities & Polymers (6)

8. Citations (1)

9. Files and Curves (10)