9dmb

Rhesus RHA10.01 Fab in complex with HIV-1 Env BG505 DS-SOSIP trimer

Method: ELECTRON MICROSCOPY Dmax: 164.1 Å Quality: GOOD

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

BG505 DS-SOSIP glycoprotein gp41

Human immunodeficiency virus 1

UniProt Q2N0S5

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 36 PDB declaration: 12-meric(12) Consistent with protein copy count Chain E; UniProt 509–661 Chain I; UniProt 509–661 Chain J; UniProt 509–661 Not recorded RHA10.01 Light chain × 3 RHA10.01 Heavy chain × 3 Envelope glycoprotein gp120 × 3 (Q2N0S6) 2-acetamido-2-deoxy-beta-D-glucopyranose-(1-4)-2-acetamido-2-deoxy-beta-D-glucopyranose × 12 ;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 ; × 9 beta-D-mannopyranose-(1-4)-2-acetamido-2-deoxy-beta-D-glucopyranose-(1-4)-2-acetamido-2-deoxy-beta-D-glucopyranose × 15 NAG 2-acetamido-2-deoxy-beta-D-glucopyranose × 27 ELECTRON MICROSCOPY cryo-EM buffer:pH 7.4;PBS cryo-EM vitrification conditions:Cryogen ETHANE Resolution 4.27 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.

53 other PDB entries and 53 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name Q2N0S5_9HIV1
Isoform
PDB entities 3
Chains and sequence ranges Author chain E; PDBConstruct 1–153; UniProt 509–661 Author chain I; PDBConstruct 1–153; UniProt 509–661 Author chain J; PDBConstruct 1–153; UniProt 509–661

Envelope glycoprotein gp120

Human immunodeficiency virus 1

UniProt Q2N0S6

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 36 PDB declaration: 12-meric(12) Consistent with protein copy count Chain F; UniProt 30–509 Chain K; UniProt 30–509 Chain L; UniProt 30–509 Not recorded RHA10.01 Light chain × 3 RHA10.01 Heavy chain × 3 BG505 DS-SOSIP glycoprotein gp41 × 3 (Q2N0S5) 2-acetamido-2-deoxy-beta-D-glucopyranose-(1-4)-2-acetamido-2-deoxy-beta-D-glucopyranose × 12 ;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 ; × 9 beta-D-mannopyranose-(1-4)-2-acetamido-2-deoxy-beta-D-glucopyranose-(1-4)-2-acetamido-2-deoxy-beta-D-glucopyranose × 15 NAG 2-acetamido-2-deoxy-beta-D-glucopyranose × 27 ELECTRON MICROSCOPY cryo-EM buffer:pH 7.4;PBS cryo-EM vitrification conditions:Cryogen ETHANE Resolution 4.27 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.

186 other PDB entries and 199 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name Q2N0S6_9HIV1
Isoform
PDB entities 4
Chains and sequence ranges Author chain F; PDBConstruct 1–480; UniProt 30–509 Author chain K; PDBConstruct 1–480; UniProt 30–509 Author chain L; PDBConstruct 1–480; UniProt 30–509

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 9dmb

P(r) Distance Distribution P(r) Distribution

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

Entry ID entry_id9dmb
Deposition date deposition_date2024-09-12
Structure title titleRhesus RHA10.01 Fab in complex with HIV-1 Env BG505 DS-SOSIP trimer
Keywords keywordsCD4, HIV-1, SHIV, T681, rhesus macaque, IMMUNE SYSTEM; IMMUNE SYSTEM
Experimental Method methodELECTRON MICROSCOPY

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

Radius of gyration Rg (Guinier) rg_guinier50.87
Radius of gyration Rg (electron density) rg_electron50.66
Forward intensity I(0) i01349600000.00
Molecular weight molecular_weight300170.0 kDa
Excluded volume excluded_volume373740 ų
Envelope volume envelope_volume584750 ų
Hydration-shell volume shell_volume96967 ų
Envelope diameter envelope_diameter168.5
Shell Rg shell_rg54.39
Envelope Rg envelope_rg49.37
Shape Rg shape_rg50.67
Total Rg total_rg50.78
Total atoms total_atoms21021
Residues n_residues2379
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 dmax164.1
Rg (real space) rg_real50.71
Rg uncertainty (real space) rg_real_error1.68
I(0) (real space) i0_real1.3500e+09
I(0) uncertainty (real space) i0_real_error2.4960e+07
Rg (reciprocal space) rg_reciprocal50.99
I(0) (reciprocal space) i0_reciprocal1350000000.0000
Solution quality estimate total_estimate0.8931
Solution quality rating solution_quality GOOD a GOOD solution
P(r) peaks n_peaks2
Primary peak position r_peak_primary63.5
Skewness Skewness skewness0.148
Kurtosis Kurtosis kurtosis-0.509
Angular range angular_range— – 0.1550 −1
Current regularization parameter α current_alpha0.0000
Highest regularization parameter α highest_alpha108000000.0000
Real-space data points n_real_points32
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.908; Stabil: 1.000; Sysdev: 1.000; Positv: 1.000; Valcen: 0.994; Smooth: 0.889

5. Crystallography and Experiment 5. Crystallography & Experiment

6. Entities and Polymers Entities & Polymers (8)

8. Citations (1)

9. Files and Curves (10)