6tdb

Neuropilin2-b1 domain in a complex with the C-terminal VEGFB167 peptide

Method: X-RAY DIFFRACTION Dmax: 101.1 Å Quality: GOOD

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

Neuropilin-2

Homo sapiens

UniProt O60462

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 A; UniProt 275–430 Not recorded C-terminal VEGFB167 peptide × 1 EDO 1,2-ETHANEDIOL × 1 ACE ACETYL GROUP × 1 X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION;293 K;N2b1-apo 0.05 M KCl, 0.01 M MgCl2 and 15 % (w/v) PEG600 N2b1/VEGFB167 0.1 M HEPES pH 7.5, 10 % (w/v) PEG4000, 20 % (w/v) isopropanol Resolution 2.45 Å R-free 0.250
2 Protein heterocomplex Heteromer Protein × 2 PDB declaration: dimeric(2) Consistent with protein copy count Chain B; UniProt 275–430 Not recorded C-terminal VEGFB167 peptide × 1 EDO 1,2-ETHANEDIOL × 1 ACE ACETYL GROUP × 1 X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION;293 K;N2b1-apo 0.05 M KCl, 0.01 M MgCl2 and 15 % (w/v) PEG600 N2b1/VEGFB167 0.1 M HEPES pH 7.5, 10 % (w/v) PEG4000, 20 % (w/v) isopropanol Resolution 2.45 Å R-free 0.250
3 Protein heterocomplex Heteromer Protein × 2 PDB declaration: dimeric(2) Consistent with protein copy count Chain C; UniProt 275–430 Not recorded C-terminal VEGFB167 peptide × 1 EDO 1,2-ETHANEDIOL × 1 X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION;293 K;N2b1-apo 0.05 M KCl, 0.01 M MgCl2 and 15 % (w/v) PEG600 N2b1/VEGFB167 0.1 M HEPES pH 7.5, 10 % (w/v) PEG4000, 20 % (w/v) isopropanol Resolution 2.45 Å R-free 0.250
4 Protein heterocomplex Heteromer Protein × 2 PDB declaration: dimeric(2) Consistent with protein copy count Chain D; UniProt 275–430 Not recorded C-terminal VEGFB167 peptide × 1 X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION;293 K;N2b1-apo 0.05 M KCl, 0.01 M MgCl2 and 15 % (w/v) PEG600 N2b1/VEGFB167 0.1 M HEPES pH 7.5, 10 % (w/v) PEG4000, 20 % (w/v) isopropanol Resolution 2.45 Å R-free 0.250

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.

15 other PDB entries and 28 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name NRP2_HUMAN
Isoform
PDB entities 1
Chains and sequence ranges Author chain A; PDBConstruct 4–159; UniProt 275–430 Author chain B; PDBConstruct 4–159; UniProt 275–430 Author chain C; PDBConstruct 4–159; UniProt 275–430 Author chain D; PDBConstruct 4–159; UniProt 275–430

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 6tdb

P(r) Distance Distribution P(r) Distribution

P(r) distribution for 6tdb
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2. Structure Basics 2. Structure Basics

Entry ID entry_id6tdb
Deposition date deposition_date2019-11-08
Structure title titleNeuropilin2-b1 domain in a complex with the C-terminal VEGFB167 peptide
Keywords keywordsVEGF-binding, NRP2, angiogenesis, immunomodulation, SIGNALING PROTEIN; SIGNALING PROTEIN
Experimental Method methodX-RAY DIFFRACTION

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

Radius of gyration Rg (Guinier) rg_guinier30.18
Radius of gyration Rg (electron density) rg_electron29.64
Forward intensity I(0) i092358900.00
Molecular weight molecular_weight72914.0 kDa
Excluded volume excluded_volume90080 ų
Envelope volume envelope_volume116750 ų
Hydration-shell volume shell_volume33001 ų
Envelope diameter envelope_diameter111.8
Shell Rg shell_rg36.28
Envelope Rg envelope_rg29.57
Shape Rg shape_rg29.58
Total Rg total_rg30.44
Total atoms total_atoms5154
Residues n_residues641
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 dmax101.1
Rg (real space) rg_real30.07
Rg uncertainty (real space) rg_real_error0.93
I(0) (real space) i0_real9.2360e+07
I(0) uncertainty (real space) i0_real_error1.5280e+06
Rg (reciprocal space) rg_reciprocal30.12
I(0) (reciprocal space) i0_reciprocal92360000.0000
Solution quality estimate total_estimate0.8059
Solution quality rating solution_quality GOOD a GOOD solution
P(r) peaks n_peaks3
Primary peak position r_peak_primary42.0
Skewness Skewness skewness0.141
Kurtosis Kurtosis kurtosis-0.477
Angular range angular_range— – 0.2650 −1
Current regularization parameter α current_alpha0.0000
Highest regularization parameter α highest_alpha24270000.0000
Real-space data points n_real_points54
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.827; Stabil: 1.000; Sysdev: 1.000; Positv: 1.000; Valcen: 0.993; Smooth: 0.000

5. Crystallography and Experiment 5. Crystallography & Experiment

6. Entities and Polymers Entities & Polymers (5)

8. Citations (2)

9. Files and Curves (10)