4ydi

Crystal structure of broad and potently neutralizing VRC01-class antibody Z258-VRC27.01, isolated from human donor Z258, in complex with HIV-1 gp120 from clade A strain Q23.17

Method: X-RAY DIFFRACTION Dmax: 109.4 Å Quality: GOOD

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

Envelope glycoprotein gp160

Human immunodeficiency virus 1

UniProt O55774

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 × 3 PDB declaration: trimeric(3) Consistent with protein copy count Chain G; UniProt 43–122 Chain G; UniProt 191–293 Chain G; UniProt 315–482 Fragment:UNP residues 43-122, 191-293, 315-482 HEAVY CHAIN OF ANTIBODY Z258-VRC27.01 × 1 LIGHT CHAIN OF ANTIBODY Z258-VRC27.01 × 1 NAG 2-acetamido-2-deoxy-beta-D-glucopyranose × 13 SO4 SULFATE ION × 4 EDO 1,2-ETHANEDIOL × 1 X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, HANGING DROP;pH 8.5;293 K;4% PEG 400, 1.9 M (NH4)2SO4, 0.1M Tris-HCl, pH 8.5 Resolution 3.45 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.

16 other PDB entries and 16 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name O55774_9HIV1
Isoform
PDB entities 1
Chains and sequence ranges Author chain G; PDBConstruct 1–80; UniProt 43–122 Author chain G; PDBConstruct 83–185; UniProt 191–293 Author chain G; PDBConstruct 192–359; UniProt 315–482

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 4ydi

P(r) Distance Distribution P(r) Distribution

P(r) distribution for 4ydi
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2. Structure Basics 2. Structure Basics

Entry ID entry_id4ydi
Deposition date deposition_date2015-02-22
Structure title titleCrystal structure of broad and potently neutralizing VRC01-class antibody Z258-VRC27.01, isolated from human donor Z258, in complex with HIV-1 gp120 from clade A strain Q23.17
Keywords keywordsAntibody, HIV-1, IMMUNE SYSTEM; IMMUNE SYSTEM
Experimental Method methodX-RAY DIFFRACTION

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

Radius of gyration Rg (Guinier) rg_guinier32.93
Radius of gyration Rg (electron density) rg_electron32.94
Forward intensity I(0) i0126342000.00
Molecular weight molecular_weight87553.0 kDa
Excluded volume excluded_volume108750 ų
Envelope volume envelope_volume145780 ų
Hydration-shell volume shell_volume38279 ų
Envelope diameter envelope_diameter116.6
Shell Rg shell_rg38.28
Envelope Rg envelope_rg33.26
Shape Rg shape_rg32.90
Total Rg total_rg33.47
Total atoms total_atoms6150
Residues n_residues751
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 dmax109.4
Rg (real space) rg_real33.17
Rg uncertainty (real space) rg_real_error0.91
I(0) (real space) i0_real1.2630e+08
I(0) uncertainty (real space) i0_real_error1.9130e+06
Rg (reciprocal space) rg_reciprocal33.07
I(0) (reciprocal space) i0_reciprocal126300000.0000
Solution quality estimate total_estimate0.8552
Solution quality rating solution_quality GOOD a GOOD solution
P(r) peaks n_peaks2
Primary peak position r_peak_primary34.2
Skewness Skewness skewness0.507
Kurtosis Kurtosis kurtosis-0.322
Angular range angular_range— – 0.2400 −1
Current regularization parameter α current_alpha0.0000
Highest regularization parameter α highest_alpha21300000.0000
Real-space data points n_real_points49
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.797; Stabil: 1.000; Sysdev: 1.000; Positv: 1.000; Valcen: 0.925; Smooth: 0.797

5. Crystallography and Experiment 5. Crystallography & Experiment

6. Entities and Polymers Entities & Polymers (7)

7. Fold Classification (SCOP + CATH) 5 domains

CATH v4.4 (5 domains)

Domain ID domain_id4ydiG01
Class class2 — Mainly Beta
Architecture architecture170 — Beta Complex
Topology topology40 — HIV Envelope Protein Gp120; Chain G
Homologous superfamily homologous superfamily20 — Human immunodeficiency virus 1, Gp160, envelope glycoprotein
Domain ID domain_id4ydiH01
Class class2 — Mainly Beta
Architecture architecture60 — Sandwich
Topology topology40 — Immunoglobulin-like
Homologous superfamily homologous superfamily10 — Immunoglobulins
Domain ID domain_id4ydiH02
Class class2 — Mainly Beta
Architecture architecture60 — Sandwich
Topology topology40 — Immunoglobulin-like
Homologous superfamily homologous superfamily10 — Immunoglobulins
Domain ID domain_id4ydiL01
Class class2 — Mainly Beta
Architecture architecture60 — Sandwich
Topology topology40 — Immunoglobulin-like
Homologous superfamily homologous superfamily10 — Immunoglobulins
Domain ID domain_id4ydiL02
Class class2 — Mainly Beta
Architecture architecture60 — Sandwich
Topology topology40 — Immunoglobulin-like
Homologous superfamily homologous superfamily10 — Immunoglobulins

8. Citations (1)

9. Files and Curves (10)