6cnv

INFLUENZA B/BRISBANE HEMAGGLUTININ FAB CR9115 SD84H COMPLEX

Method: X-RAY DIFFRACTION Dmax: 143.3 Å Quality: GOOD

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

Hemagglutinin

Influenza B virus

UniProt U3RVK6

State in the Current Structure

Assembly Oligomeric State Construct Mutations and Modifications Ligands, Ions and Associated Components Method and Experimental Conditions Structure Quality
1 Insufficient information Heteromer Protein × 15 其他Polymer 12 PDB declaration: pentadecameric(15) Consistent with protein copy count Chain A; UniProt 16–362 Not recorded Envelope glycoprotein × 3 (G4WYG8,M1E1E4) SD84h × 3 CR9114 Light chain × 3 CR9114 Fab heavy chain × 3 2-acetamido-2-deoxy-beta-D-glucopyranose-(1-4)-2-acetamido-2-deoxy-beta-D-glucopyranose × 12 NAG 2-acetamido-2-deoxy-beta-D-glucopyranose × 3 X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, SITTING DROP;pH 4.5;295 K;100 mM sodium acetate, pH 4.5, 5.5 M sodium formate, and 5% MPD Resolution 4.10 Å R-free 0.276

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 U3RVK6_9INFB
Isoform
PDB entities 1
Chains and sequence ranges Author chain A; PDBConstruct 1–347; UniProt 16–362

Envelope glycoprotein

Human immunodeficiency virus 1

UniProt G4WYG8

State in the Current Structure

Assembly Oligomeric State Construct Mutations and Modifications Ligands, Ions and Associated Components Method and Experimental Conditions Structure Quality
1 Insufficient information Heteromer Protein × 15 其他Polymer 12 PDB declaration: pentadecameric(15) Consistent with protein copy count Chain B; UniProt 363–536 Not recorded Hemagglutinin × 3 (U3RVK6) SD84h × 3 CR9114 Light chain × 3 CR9114 Fab heavy chain × 3 2-acetamido-2-deoxy-beta-D-glucopyranose-(1-4)-2-acetamido-2-deoxy-beta-D-glucopyranose × 12 NAG 2-acetamido-2-deoxy-beta-D-glucopyranose × 3 X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, SITTING DROP;pH 4.5;295 K;100 mM sodium acetate, pH 4.5, 5.5 M sodium formate, and 5% MPD Resolution 4.10 Å R-free 0.276

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 G4WYG8_9INFB
Isoform
PDB entities 2
Chains and sequence ranges Author chain B; PDBConstruct 1–174; UniProt 363–536

Envelope glycoprotein

Human immunodeficiency virus 1

UniProt M1E1E4

State in the Current Structure

Assembly Oligomeric State Construct Mutations and Modifications Ligands, Ions and Associated Components Method and Experimental Conditions Structure Quality
1 Insufficient information Heteromer Protein × 15 其他Polymer 12 PDB declaration: pentadecameric(15) Consistent with protein copy count Chain B; UniProt 1–28 Not recorded Hemagglutinin × 3 (U3RVK6) SD84h × 3 CR9114 Light chain × 3 CR9114 Fab heavy chain × 3 2-acetamido-2-deoxy-beta-D-glucopyranose-(1-4)-2-acetamido-2-deoxy-beta-D-glucopyranose × 12 NAG 2-acetamido-2-deoxy-beta-D-glucopyranose × 3 X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, SITTING DROP;pH 4.5;295 K;100 mM sodium acetate, pH 4.5, 5.5 M sodium formate, and 5% MPD Resolution 4.10 Å R-free 0.276

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.

24 other PDB entries and 27 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name M1E1E4_9HIV1
Isoform
PDB entities 2
Chains and sequence ranges Author chain B; PDBConstruct 187–214; UniProt 1–28

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 6cnv

P(r) Distance Distribution P(r) Distribution

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

Entry ID entry_id6cnv
Deposition date deposition_date2018-03-09
Structure title titleINFLUENZA B/BRISBANE HEMAGGLUTININ FAB CR9115 SD84H COMPLEX
Keywords keywordsVIRAL PROTEIN-IMMUNE SYSTEM complex, influenza, Single domain antibody, hemagglutinin, humanization, VIRAL PROTEIN; VIRAL PROTEIN
Experimental Method methodX-RAY DIFFRACTION

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

Radius of gyration Rg (Guinier) rg_guinier42.27
Radius of gyration Rg (electron density) rg_electron42.06
Forward intensity I(0) i0197418000.00
Molecular weight molecular_weight112410.0 kDa
Excluded volume excluded_volume139830 ų
Envelope volume envelope_volume200540 ų
Hydration-shell volume shell_volume41013 ų
Envelope diameter envelope_diameter144.9
Shell Rg shell_rg45.46
Envelope Rg envelope_rg40.89
Shape Rg shape_rg42.07
Total Rg total_rg42.24
Total atoms total_atoms7901
Residues n_residues1019
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 dmax143.3
Rg (real space) rg_real42.39
Rg uncertainty (real space) rg_real_error1.66
I(0) (real space) i0_real1.9740e+08
I(0) uncertainty (real space) i0_real_error4.1260e+06
Rg (reciprocal space) rg_reciprocal42.27
I(0) (reciprocal space) i0_reciprocal197400000.0000
Solution quality estimate total_estimate0.8715
Solution quality rating solution_quality GOOD a GOOD solution
P(r) peaks n_peaks1
Primary peak position r_peak_primary34.9
Skewness Skewness skewness0.260
Kurtosis Kurtosis kurtosis-0.721
Angular range angular_range— – 0.1850 −1
Current regularization parameter α current_alpha0.0000
Highest regularization parameter α highest_alpha13380000.0000
Real-space data points n_real_points38
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.855; Stabil: 1.000; Sysdev: 1.000; Positv: 1.000; Valcen: 0.853; Smooth: 0.908

5. Crystallography and Experiment 5. Crystallography & Experiment

6. Entities and Polymers Entities & Polymers (7)

8. Citations (1)

9. Files and Curves (10)