9cpl

The ubiquitin-associated domain of human thirty-eight negative kinase 1, fused to the 2TEL crystallization chaperone via a 2-glycine linker

Method: X-RAY DIFFRACTION Dmax: 67.6 Å Quality: REASONABLE

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

2TEL/Non-receptor tyrosine-protein kinase TNK1 fusion 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 47–124 Chain A; UniProt 47–121 Mutation:First TELSAM:R80S,V112E,Second TELSAM: R80S,UBA Domain: C610A,C644A FMT FORMIC ACID × 1 X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, SITTING DROP;pH 6;298 K;100mM BisTris, pH 6.0, 960mM Mg-formate Resolution 2.40 Å R-free 0.263

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 13–90; UniProt 47–124 Author chain A; PDBConstruct 98–172; UniProt 47–121

2TEL/Non-receptor tyrosine-protein kinase TNK1 fusion protein

Homo sapiens

UniProt Q13470

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 590–666 Mutation:First TELSAM:R80S,V112E,Second TELSAM: R80S,UBA Domain: C610A,C644A FMT FORMIC ACID × 1 X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, SITTING DROP;pH 6;298 K;100mM BisTris, pH 6.0, 960mM Mg-formate Resolution 2.40 Å R-free 0.263

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.

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

View Construct and Data Evidence
UniProt name TNK1_HUMAN
Isoform
PDB entities 1
Chains and sequence ranges Author chain A; PDBConstruct 175–251; UniProt 590–666

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 9cpl

P(r) Distance Distribution P(r) Distribution

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

Entry ID entry_id9cpl
Deposition date deposition_date2024-07-18
最后修订 last_revision2024-08-14
Structure title titleThe ubiquitin-associated domain of human thirty-eight negative kinase 1, fused to the 2TEL crystallization chaperone via a 2-glycine linker
Keywords keywordsTELSAM, 2TEL, Pointed Domain, ETS, TEL, TNK1, UBA Domain, Broken Periodicity, ONCOPROTEIN; ONCOPROTEIN
Experimental Method methodX-RAY DIFFRACTION

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

Radius of gyration Rg (Guinier) rg_guinier24.80
Radius of gyration Rg (electron density) rg_electron24.35
Forward intensity I(0) i010630300.00
Molecular weight molecular_weight24998.0 kDa
Excluded volume excluded_volume31374 ų
Envelope volume envelope_volume40710 ų
Hydration-shell volume shell_volume15586 ų
Envelope diameter envelope_diameter86.7
Shell Rg shell_rg28.27
Envelope Rg envelope_rg24.28
Shape Rg shape_rg24.37
Total Rg total_rg24.83
Total atoms total_atoms1780
Residues n_residues234
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 dmax67.6
Rg (real space) rg_real23.73
Rg uncertainty (real space) rg_real_error0.15
I(0) (real space) i0_real1.0180e+07
I(0) uncertainty (real space) i0_real_error1.1170e+05
Rg (reciprocal space) rg_reciprocal25.06
I(0) (reciprocal space) i0_reciprocal10630000.0000
Solution quality estimate total_estimate0.6630
Solution quality rating solution_quality REASONABLE a REASONABLE solution
P(r) peaks n_peaks1
Primary peak position r_peak_primary20.4
Skewness Skewness skewness0.389
Kurtosis Kurtosis kurtosis-0.691
Angular range angular_range— – 0.3200 −1
Current regularization parameter α current_alpha3.8840
Highest regularization parameter α highest_alpha1787000.0000
Real-space data points n_real_points64
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.963; Stabil: 0.979; Sysdev: 0.000; Positv: 1.000; Valcen: 0.794; Smooth: 0.000

5. Crystallography and Experiment 5. Crystallography & Experiment

6. Entities and Polymers Entities & Polymers (3)

8. Citations (1)

9. Files and Curves (10)