9doc

The von Willebrand factor A domain of human capillary morphogenesis gene II, flexibly fused to the 1TEL crystallization chaperone, Thr-Val linker variant, at 1.2 Angstrom resolution

Method: X-RAY DIFFRACTION Dmax: 72.6 Å Quality: REASONABLE

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

Transcription factor ETV6,Capillary morphogenesis gene 2 protein

Homo sapiens

UniProt P41212

State in the Current Structure

Assembly Oligomeric State Construct Mutations and Modifications Ligands, Ions and Associated Components Method and Experimental Conditions Structure Quality
1 Insufficient information Monomer Protein × 1 PDB declaration: monomeric(1) Consistent with protein copy count Chain A; UniProt 47–121 Fragment:von Willebrand factor A domain of CMG2 Mutation:TELSAM: R80S,V112E (Uniprot numbering),vWA: C175A (Uniprot numbering) GOL GLYCEROL × 1 PO4 PHOSPHATE ION × 2 MG MAGNESIUM ION × 7 NA SODIUM ION × 5 X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, SITTING DROP;pH 7.25;298 K;100 mM Bis-Tris, pH 7.25, 1350 mM Sodium Potassium Phosphate Resolution 1.19 Å R-free 0.197

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.

40 other PDB entries and 64 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name ETV6_HUMAN
Isoform
PDB entities 1
Chains and sequence ranges Author chain A; PDBConstruct 13–87; UniProt 47–121

Transcription factor ETV6,Capillary morphogenesis gene 2 protein

Homo sapiens

UniProt P58335

State in the Current Structure

Assembly Oligomeric State Construct Mutations and Modifications Ligands, Ions and Associated Components Method and Experimental Conditions Structure Quality
1 Insufficient information Monomer Protein × 1 PDB declaration: monomeric(1) Consistent with protein copy count Chain A; UniProt 43–217 Fragment:von Willebrand factor A domain of CMG2 Mutation:TELSAM: R80S,V112E (Uniprot numbering),vWA: C175A (Uniprot numbering) GOL GLYCEROL × 1 PO4 PHOSPHATE ION × 2 MG MAGNESIUM ION × 7 NA SODIUM ION × 5 X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, SITTING DROP;pH 7.25;298 K;100 mM Bis-Tris, pH 7.25, 1350 mM Sodium Potassium Phosphate Resolution 1.19 Å R-free 0.197

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 24 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name ANTR2_HUMAN
Isoform
PDB entities 1
Chains and sequence ranges Author chain A; PDBConstruct 94–268; UniProt 43–217

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 9doc

P(r) Distance Distribution P(r) Distribution

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

Entry ID entry_id9doc
Deposition date deposition_date2024-09-18
最后修订 last_revision2024-11-06
Structure title titleThe von Willebrand factor A domain of human capillary morphogenesis gene II, flexibly fused to the 1TEL crystallization chaperone, Thr-Val linker variant, at 1.2 Angstrom resolution
Keywords keywords;TELSAM, 1TEL, Pointed Domain, Sterile Alpha Motif domain, ETS, TEL, CMG2, vWA Domain, Anthrax toxin receptor 2, ONCOPROTEIN, PEPTIDE BINDING PROTEIN ;; PEPTIDE BINDING PROTEIN
Experimental Method methodX-RAY DIFFRACTION

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

Radius of gyration Rg (Guinier) rg_guinier22.17
Radius of gyration Rg (electron density) rg_electron21.16
Forward intensity I(0) i014437700.00
Molecular weight molecular_weight29305.0 kDa
Excluded volume excluded_volume36931 ų
Envelope volume envelope_volume43291 ų
Hydration-shell volume shell_volume18188 ų
Envelope diameter envelope_diameter75.6
Shell Rg shell_rg26.67
Envelope Rg envelope_rg21.44
Shape Rg shape_rg21.18
Total Rg total_rg21.89
Total atoms total_atoms3961
Residues n_residues260
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 dmax72.6
Rg (real space) rg_real22.31
Rg uncertainty (real space) rg_real_error0.57
I(0) (real space) i0_real1.4440e+07
I(0) uncertainty (real space) i0_real_error1.9560e+05
Rg (reciprocal space) rg_reciprocal22.28
I(0) (reciprocal space) i0_reciprocal14440000.0000
Solution quality estimate total_estimate0.5868
Solution quality rating solution_quality REASONABLE a REASONABLE solution
P(r) peaks n_peaks2
Primary peak position r_peak_primary22.8
Skewness Skewness skewness0.471
Kurtosis Kurtosis kurtosis-0.378
Angular range angular_range— – 0.3600 −1
Current regularization parameter α current_alpha0.0000
Highest regularization parameter α highest_alpha3042000.0000
Real-space data points n_real_points68
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.768; Stabil: 0.999; Sysdev: 0.145; Positv: 1.000; Valcen: 0.888; Smooth: 0.000

5. Crystallography and Experiment 5. Crystallography & Experiment

6. Entities and Polymers Entities & Polymers (6)

8. Citations (1)

9. Files and Curves (10)