4tpr

Structure of Tau5 antibody Fab fragment

Method: X-RAY DIFFRACTION Dmax: 79.0 Å Quality: EXCELLENT

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

If kappa light chain

OrganismNot specified

UniProt A2NHM3

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 × 2 PDB declaration: Dimeric(2) Consistent with protein copy count Chain L; UniProt 1–218 Not recorded Fab heavy chain × 1 PG4 TETRAETHYLENE GLYCOL × 2 CL CHLORIDE ION × 5 PGE TRIETHYLENE GLYCOL × 1 NA SODIUM ION × 1 PEG DI(HYDROXYETHYL)ETHER × 5 TRS 2-AMINO-2-HYDROXYMETHYL-PROPANE-1,3-DIOL × 1 33O 3,6,9,12,15,18,21,24,27,30,33,36-dodecaoxaoctatriacontane-1,38-diol × 1 X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, SITTING DROP;pH 5.5;295 K;0.2 M NaCl, 0.1 M Bis-Tris, 25 % w/v PEG 3350 Resolution 1.60 Å R-free 0.191

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.

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

View Construct and Data Evidence
UniProt name A2NHM3_MOUSE
Isoform
PDB entities 1
Chains and sequence ranges Author chain L; PDBConstruct 1–218; UniProt 1–218

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 4tpr

P(r) Distance Distribution P(r) Distribution

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

Entry ID entry_id4tpr
Deposition date deposition_date2014-06-09
Structure title titleStructure of Tau5 antibody Fab fragment
Keywords keywordsImmune system, monoclonal antibody; IMMUNE SYSTEM
Experimental Method methodX-RAY DIFFRACTION

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

Radius of gyration Rg (Guinier) rg_guinier25.73
Radius of gyration Rg (electron density) rg_electron24.61
Forward intensity I(0) i042258600.00
Molecular weight molecular_weight49827.0 kDa
Excluded volume excluded_volume62091 ų
Envelope volume envelope_volume75883 ų
Hydration-shell volume shell_volume25762 ų
Envelope diameter envelope_diameter81.2
Shell Rg shell_rg31.79
Envelope Rg envelope_rg24.47
Shape Rg shape_rg24.59
Total Rg total_rg25.47
Total atoms total_atoms3494
Residues n_residues439
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 dmax79.0
Rg (real space) rg_real25.70
Rg uncertainty (real space) rg_real_error0.54
I(0) (real space) i0_real4.2260e+07
I(0) uncertainty (real space) i0_real_error6.2580e+05
Rg (reciprocal space) rg_reciprocal25.71
I(0) (reciprocal space) i0_reciprocal42260000.0000
Solution quality estimate total_estimate0.9128
Solution quality rating solution_quality EXCELLENT a EXCELLENT solution
P(r) peaks n_peaks2
Primary peak position r_peak_primary29.3
Skewness Skewness skewness0.264
Kurtosis Kurtosis kurtosis-0.546
Angular range angular_range— – 0.3100 −1
Current regularization parameter α current_alpha0.0000
Highest regularization parameter α highest_alpha7495000.0000
Real-space data points n_real_points63
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.971; Stabil: 1.000; Sysdev: 1.000; Positv: 1.000; Valcen: 0.996; Smooth: 0.953

5. Crystallography and Experiment 5. Crystallography & Experiment

6. Entities and Polymers Entities & Polymers (10)

7. Fold Classification (SCOP + CATH) 7 domains

SCOP 2.08 (3 domains)

Domain ID domain_idd4tprh_
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_idd4tprl1
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_idd4tprl2
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 (4 domains)

Domain ID domain_id4tprH01
Class class2 — Mainly Beta
Architecture architecture60 — Sandwich
Topology topology40 — Immunoglobulin-like
Homologous superfamily homologous superfamily10 — Immunoglobulins
Domain ID domain_id4tprH02
Class class2 — Mainly Beta
Architecture architecture60 — Sandwich
Topology topology40 — Immunoglobulin-like
Homologous superfamily homologous superfamily10 — Immunoglobulins
Domain ID domain_id4tprL01
Class class2 — Mainly Beta
Architecture architecture60 — Sandwich
Topology topology40 — Immunoglobulin-like
Homologous superfamily homologous superfamily10 — Immunoglobulins
Domain ID domain_id4tprL02
Class class2 — Mainly Beta
Architecture architecture60 — Sandwich
Topology topology40 — Immunoglobulin-like
Homologous superfamily homologous superfamily10 — Immunoglobulins

8. Citations (1)

9. Files and Curves (10)