3mnw

Crystal structure of the non-neutralizing HIV antibody 13H11 Fab fragment with a gp41 MPER-derived peptide in a helical conformation

Method: X-RAY DIFFRACTION Dmax: 87.9 Å Quality: GOOD

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

ANTI-HIV-1 ANTIBODY 13H11 LIGHT CHAIN

Homo sapiens

UniProt Q8TCD0

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 A; UniProt 126–239 Fragment:mouse Fv,human Fc Gp41 × 1 ANTI-HIV-1 ANTIBODY 13H11 HEAVY CHAIN × 1 (S6B291) EDO 1,2-ETHANEDIOL × 1 X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION;pH 7.2;298 K;Reservoir: Qiagen Classics II screen H10 (0.2 M K Na tartrate, 20% PEG 3350). Drop: 0.6 uL protein + 0.4 uL reservoir., pH 7.2, VAPOR DIFFUSION, temperature 298K Resolution 2.20 Å R-free 0.253
2 Protein heterocomplex Heteromer Protein × 6 PDB declaration: hexameric(6) Consistent with protein copy count Chain A; UniProt 126–239 Fragment:mouse Fv,human Fc Gp41 × 2 ANTI-HIV-1 ANTIBODY 13H11 HEAVY CHAIN × 2 (S6B291) EDO 1,2-ETHANEDIOL × 2 X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION;pH 7.2;298 K;Reservoir: Qiagen Classics II screen H10 (0.2 M K Na tartrate, 20% PEG 3350). Drop: 0.6 uL protein + 0.4 uL reservoir., pH 7.2, VAPOR DIFFUSION, temperature 298K Resolution 2.20 Å R-free 0.253

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.

39 other PDB entries and 65 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name Q8TCD0_HUMAN
Isoform
PDB entities 2
Chains and sequence ranges Author chain A; PDBConstruct 109–222; UniProt 126–239

ANTI-HIV-1 ANTIBODY 13H11 HEAVY CHAIN

Homo sapiens

UniProt S6B291

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 B; UniProt 133–241 Fragment:mouse Fv,human Fc Gp41 × 1 ANTI-HIV-1 ANTIBODY 13H11 LIGHT CHAIN × 1 (Q8TCD0) EDO 1,2-ETHANEDIOL × 1 X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION;pH 7.2;298 K;Reservoir: Qiagen Classics II screen H10 (0.2 M K Na tartrate, 20% PEG 3350). Drop: 0.6 uL protein + 0.4 uL reservoir., pH 7.2, VAPOR DIFFUSION, temperature 298K Resolution 2.20 Å R-free 0.253
2 Protein heterocomplex Heteromer Protein × 6 PDB declaration: hexameric(6) Consistent with protein copy count Chain B; UniProt 133–241 Fragment:mouse Fv,human Fc Gp41 × 2 ANTI-HIV-1 ANTIBODY 13H11 LIGHT CHAIN × 2 (Q8TCD0) EDO 1,2-ETHANEDIOL × 2 X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION;pH 7.2;298 K;Reservoir: Qiagen Classics II screen H10 (0.2 M K Na tartrate, 20% PEG 3350). Drop: 0.6 uL protein + 0.4 uL reservoir., pH 7.2, VAPOR DIFFUSION, temperature 298K Resolution 2.20 Å R-free 0.253

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.

27 other PDB entries and 47 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name S6B291_HUMAN
Isoform
PDB entities 3
Chains and sequence ranges Author chain B; PDBConstruct 111–219; UniProt 133–241

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 3mnw

P(r) Distance Distribution P(r) Distribution

P(r) distribution for 3mnw
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2. Structure Basics 2. Structure Basics

Entry ID entry_id3mnw
Deposition date deposition_date2010-04-22
Structure title titleCrystal structure of the non-neutralizing HIV antibody 13H11 Fab fragment with a gp41 MPER-derived peptide in a helical conformation
Keywords keywordsHIV-1, HIV gp41, MPER, 13H11, 2F5, Z13, 4E10, Fab antibody, 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_guinier26.11
Radius of gyration Rg (electron density) rg_electron25.21
Forward intensity I(0) i038780000.00
Molecular weight molecular_weight48395.0 kDa
Excluded volume excluded_volume60581 ų
Envelope volume envelope_volume75598 ų
Hydration-shell volume shell_volume25444 ų
Envelope diameter envelope_diameter90.3
Shell Rg shell_rg32.08
Envelope Rg envelope_rg24.86
Shape Rg shape_rg25.19
Total Rg total_rg26.03
Total atoms total_atoms3413
Residues n_residues429
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 dmax87.9
Rg (real space) rg_real26.10
Rg uncertainty (real space) rg_real_error0.65
I(0) (real space) i0_real3.8780e+07
I(0) uncertainty (real space) i0_real_error5.7300e+05
Rg (reciprocal space) rg_reciprocal26.11
I(0) (reciprocal space) i0_reciprocal38780000.0000
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_primary30.2
Skewness Skewness skewness0.292
Kurtosis Kurtosis kurtosis-0.463
Angular range angular_range— – 0.3050 −1
Current regularization parameter α current_alpha0.0000
Highest regularization parameter α highest_alpha5925000.0000
Real-space data points n_real_points62
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.886; Stabil: 1.000; Sysdev: 1.000; Positv: 1.000; Valcen: 0.963; Smooth: 0.985

5. Crystallography and Experiment 5. Crystallography & Experiment

6. Entities and Polymers Entities & Polymers (5)

7. Fold Classification (SCOP + CATH) 4 domains

CATH v4.4 (4 domains)

Domain ID domain_id3mnwA01
Class class2 — Mainly Beta
Architecture architecture60 — Sandwich
Topology topology40 — Immunoglobulin-like
Homologous superfamily homologous superfamily10 — Immunoglobulins
Domain ID domain_id3mnwA02
Class class2 — Mainly Beta
Architecture architecture60 — Sandwich
Topology topology40 — Immunoglobulin-like
Homologous superfamily homologous superfamily10 — Immunoglobulins
Domain ID domain_id3mnwB01
Class class2 — Mainly Beta
Architecture architecture60 — Sandwich
Topology topology40 — Immunoglobulin-like
Homologous superfamily homologous superfamily10 — Immunoglobulins
Domain ID domain_id3mnwB02
Class class2 — Mainly Beta
Architecture architecture60 — Sandwich
Topology topology40 — Immunoglobulin-like
Homologous superfamily homologous superfamily10 — Immunoglobulins

8. Citations (1)

9. Files and Curves (10)