3mlw

Crystal structure of anti-HIV-1 V3 Fab 1006-15D in complex with an MN V3 peptide

Method: X-RAY DIFFRACTION Dmax: 123.7 Å Quality: GOOD

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

HIV-1 gp120 third variable region (V3) crown

OrganismNot specified

UniProt P05877

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 P; UniProt 306–328 Not recorded Human monoclonal anti-HIV-1 gp120 V3 antibody 1006-15D Fab light chain × 1 Human monoclonal anti-HIV-1 gp120 V3 antibody 1006-15D Fab heavy chain × 1 PO4 PHOSPHATE ION × 3 X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, HANGING DROP;296 K;20% PEG 3350, K dihydrogen phosphate, VAPOR DIFFUSION, HANGING DROP, temperature 296K Resolution 2.70 Å R-free 0.291
2 Protein heterocomplex Heteromer Protein × 3 PDB declaration: trimeric(3) Consistent with protein copy count Chain Q; UniProt 306–328 Not recorded Human monoclonal anti-HIV-1 gp120 V3 antibody 1006-15D Fab light chain × 1 Human monoclonal anti-HIV-1 gp120 V3 antibody 1006-15D Fab heavy chain × 1 PO4 PHOSPHATE ION × 3 X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, HANGING DROP;296 K;20% PEG 3350, K dihydrogen phosphate, VAPOR DIFFUSION, HANGING DROP, temperature 296K Resolution 2.70 Å R-free 0.291

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.

13 other PDB entries and 19 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name ENV_HV1MN
Isoform
PDB entities 3
Chains and sequence ranges Author chain P; PDBConstruct 1–23; UniProt 306–328 Author chain Q; PDBConstruct 1–23; UniProt 306–328

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 3mlw

P(r) Distance Distribution P(r) Distribution

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

Entry ID entry_id3mlw
Deposition date deposition_date2010-04-18
Structure title titleCrystal structure of anti-HIV-1 V3 Fab 1006-15D in complex with an MN V3 peptide
Keywords keywordshuman monoclonal antibody, Fab, HIV-1, gp120, third variable loop, antibody-antigen interaction, 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_guinier36.50
Radius of gyration Rg (electron density) rg_electron36.26
Forward intensity I(0) i0163261000.00
Molecular weight molecular_weight99660.0 kDa
Excluded volume excluded_volume123400 ų
Envelope volume envelope_volume169480 ų
Hydration-shell volume shell_volume40330 ų
Envelope diameter envelope_diameter130.8
Shell Rg shell_rg40.71
Envelope Rg envelope_rg36.07
Shape Rg shape_rg36.23
Total Rg total_rg36.64
Total atoms total_atoms7009
Residues n_residues880
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 dmax123.7
Rg (real space) rg_real36.61
Rg uncertainty (real space) rg_real_error0.96
I(0) (real space) i0_real1.6330e+08
I(0) uncertainty (real space) i0_real_error2.5170e+06
Rg (reciprocal space) rg_reciprocal36.54
I(0) (reciprocal space) i0_reciprocal163300000.0000
Solution quality estimate total_estimate0.8780
Solution quality rating solution_quality GOOD a GOOD solution
P(r) peaks n_peaks1
Primary peak position r_peak_primary46.0
Skewness Skewness skewness0.363
Kurtosis Kurtosis kurtosis-0.428
Angular range angular_range— – 0.2150 −1
Current regularization parameter α current_alpha0.0000
Highest regularization parameter α highest_alpha30730000.0000
Real-space data points n_real_points44
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.872; Stabil: 1.000; Sysdev: 1.000; Positv: 1.000; Valcen: 0.872; Smooth: 0.922

5. Crystallography and Experiment 5. Crystallography & Experiment

6. Entities and Polymers Entities & Polymers (5)

7. Fold Classification (SCOP + CATH) 14 domains

SCOP 2.08 (6 domains)

Domain ID domain_idd3mlwh_
Class classb — All beta proteins
Fold Fold foldb.1 — Immunoglobulin-like beta-sandwich
Superfamily Superfamily superfamilyb.1.1 — Immunoglobulin
Family Family familyb.1.1.0 — automated matches
Domain ID domain_idd3mlwi_
Class classb — All beta proteins
Fold Fold foldb.1 — Immunoglobulin-like beta-sandwich
Superfamily Superfamily superfamilyb.1.1 — Immunoglobulin
Family Family familyb.1.1.0 — automated matches
Domain ID domain_idd3mlwl1
Class classb — All beta proteins
Fold Fold foldb.1 — Immunoglobulin-like beta-sandwich
Superfamily Superfamily superfamilyb.1.1 — Immunoglobulin
Family Family familyb.1.1.1 — V set domains (antibody variable domain-like)
Domain ID domain_idd3mlwl2
Class classb — All beta proteins
Fold Fold foldb.1 — Immunoglobulin-like beta-sandwich
Superfamily Superfamily superfamilyb.1.1 — Immunoglobulin
Family Family familyb.1.1.2 — C1 set domains (antibody constant domain-like)
Domain ID domain_idd3mlwm1
Class classb — All beta proteins
Fold Fold foldb.1 — Immunoglobulin-like beta-sandwich
Superfamily Superfamily superfamilyb.1.1 — Immunoglobulin
Family Family familyb.1.1.1 — V set domains (antibody variable domain-like)
Domain ID domain_idd3mlwm2
Class classb — All beta proteins
Fold Fold foldb.1 — Immunoglobulin-like beta-sandwich
Superfamily Superfamily superfamilyb.1.1 — Immunoglobulin
Family Family familyb.1.1.2 — C1 set domains (antibody constant domain-like)

CATH v4.4 (8 domains)

Domain ID domain_id3mlwH01
Class class2 — Mainly Beta
Architecture architecture60 — Sandwich
Topology topology40 — Immunoglobulin-like
Homologous superfamily homologous superfamily10 — Immunoglobulins
Domain ID domain_id3mlwH02
Class class2 — Mainly Beta
Architecture architecture60 — Sandwich
Topology topology40 — Immunoglobulin-like
Homologous superfamily homologous superfamily10 — Immunoglobulins
Domain ID domain_id3mlwI01
Class class2 — Mainly Beta
Architecture architecture60 — Sandwich
Topology topology40 — Immunoglobulin-like
Homologous superfamily homologous superfamily10 — Immunoglobulins
Domain ID domain_id3mlwI02
Class class2 — Mainly Beta
Architecture architecture60 — Sandwich
Topology topology40 — Immunoglobulin-like
Homologous superfamily homologous superfamily10 — Immunoglobulins
Domain ID domain_id3mlwL01
Class class2 — Mainly Beta
Architecture architecture60 — Sandwich
Topology topology40 — Immunoglobulin-like
Homologous superfamily homologous superfamily10 — Immunoglobulins
Domain ID domain_id3mlwL02
Class class2 — Mainly Beta
Architecture architecture60 — Sandwich
Topology topology40 — Immunoglobulin-like
Homologous superfamily homologous superfamily10 — Immunoglobulins
Domain ID domain_id3mlwM01
Class class2 — Mainly Beta
Architecture architecture60 — Sandwich
Topology topology40 — Immunoglobulin-like
Homologous superfamily homologous superfamily10 — Immunoglobulins
Domain ID domain_id3mlwM02
Class class2 — Mainly Beta
Architecture architecture60 — Sandwich
Topology topology40 — Immunoglobulin-like
Homologous superfamily homologous superfamily10 — Immunoglobulins

8. Citations (1)

9. Files and Curves (10)