9zrz

Cryo-EM structure of SHIV-elicited CI93-1365 Fab in complex with HIV Env trimer Q23-SCT27

Method: ELECTRON MICROSCOPY Dmax: 145.8 Å Quality: GOOD

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

Envelope gp120

Human immunodeficiency virus

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 Other combination Heteromer Protein × 8 其他Polymer 37 PDB declaration: octameric(8) Consistent with protein copy count Chain b; UniProt 30–497 Chain c; UniProt 502–654 Chain d; UniProt 30–497 Chain e; UniProt 502–654 Chain f; UniProt 30–497 Chain g; UniProt 502–654 Not recorded CI93-1365 heavy chain × 1 CI93-1365 light chain × 1 2-acetamido-2-deoxy-beta-D-glucopyranose-(1-4)-2-acetamido-2-deoxy-beta-D-glucopyranose × 29 beta-D-mannopyranose-(1-4)-2-acetamido-2-deoxy-beta-D-glucopyranose-(1-4)-2-acetamido-2-deoxy-beta-D-glucopyranose × 4 ;alpha-D-mannopyranose-(1-3)-[alpha-D-mannopyranose-(1-6)]beta-D-mannopyranose-(1-4)-2-acetamido-2-deoxy-beta-D-glucopyranose-(1-4)-2-acetamido-2-deoxy-beta-D-glucopyranose ; × 3 ;alpha-D-mannopyranose-(1-2)-alpha-D-mannopyranose-(1-3)-[alpha-D-mannopyranose-(1-3)-[alpha-D-mannopyranose-(1-6)]alpha-D-mannopyranose-(1-6)]beta-D-mannopyranose-(1-4)-2-acetamido-2-deoxy-beta-D-glucopyranose-(1-4)-2-acetamido-2-deoxy-beta-D-glucopyranose ; × 1 2-acetamido-2-deoxy-beta-D-glucopyranose × 32 ELECTRON MICROSCOPY mmCIF provides none of the parsed experimental conditions Resolution 2.90 Å

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_HV1
Isoform
PDB entities 3, 4
Chains and sequence ranges Author chain b; PDBConstruct 36–503; UniProt 30–497 Author chain d; PDBConstruct 36–503; UniProt 30–497 Author chain f; PDBConstruct 36–503; UniProt 30–497 Author chain c; PDBConstruct 1–153; UniProt 502–654 Author chain e; PDBConstruct 1–153; UniProt 502–654 Author chain g; PDBConstruct 1–153; UniProt 502–654

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 9zrz

P(r) Distance Distribution P(r) Distribution

P(r) distribution for 9zrz
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2. Structure Basics 2. Structure Basics

Entry ID entry_id9zrz
Deposition date deposition_date2025-12-21
Structure title titleCryo-EM structure of SHIV-elicited CI93-1365 Fab in complex with HIV Env trimer Q23-SCT27
Keywords keywordsimmune complex, neutralization, SHIV, HIV V2 apex, VIRAL PROTEIN, VIRAL PROTEIN-IMMUNE SYSTEM complex; VIRAL PROTEIN/IMMUNE SYSTEM
Experimental Method methodELECTRON MICROSCOPY

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

Radius of gyration Rg (Guinier) rg_guinier44.85
Radius of gyration Rg (electron density) rg_electron44.15
Forward intensity I(0) i0922085000.00
Molecular weight molecular_weight245760.0 kDa
Excluded volume excluded_volume305600 ų
Envelope volume envelope_volume438730 ų
Hydration-shell volume shell_volume80485 ų
Envelope diameter envelope_diameter160.9
Shell Rg shell_rg51.05
Envelope Rg envelope_rg43.58
Shape Rg shape_rg44.15
Total Rg total_rg44.42
Total atoms total_atoms17204
Residues n_residues1952
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 dmax145.8
Rg (real space) rg_real44.65
Rg uncertainty (real space) rg_real_error1.27
I(0) (real space) i0_real9.2210e+08
I(0) uncertainty (real space) i0_real_error1.8570e+07
Rg (reciprocal space) rg_reciprocal44.85
I(0) (reciprocal space) i0_reciprocal922300000.0000
Solution quality estimate total_estimate0.8778
Solution quality rating solution_quality GOOD a GOOD solution
P(r) peaks n_peaks2
Primary peak position r_peak_primary62.5
Skewness Skewness skewness0.168
Kurtosis Kurtosis kurtosis-0.335
Angular range angular_range— – 0.1750 −1
Current regularization parameter α current_alpha0.0000
Highest regularization parameter α highest_alpha117400000.0000
Real-space data points n_real_points36
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.854; Stabil: 1.000; Sysdev: 1.000; Positv: 1.000; Valcen: 0.995; Smooth: 0.849

5. Crystallography and Experiment 5. Crystallography & Experiment

6. Entities and Polymers Entities & Polymers (9)

8. Citations (1)

9. Files and Curves (10)