5ic9

Structure of the CTD complex of Utp12 and Utp13

Method: X-RAY DIFFRACTION Dmax: 86.3 Å Quality: EXCELLENT

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

Putative uncharacterized protein

Chaetomium thermophilum (strain DSM 1495 / CBS 144.50 / IMI 039719)

UniProt G0RZL9

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 × 4 PDB declaration: tetrameric(4) Consistent with protein copy count Chain A; UniProt 748–956 Chain C; UniProt 748–956 Fragment:UNP residues 748-956 Putative uncharacterized protein × 2 (G0SG95) X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, HANGING DROP;pH 6.5;293 K;0.1M Bis-Tris-HCl, 50% Pentaerythritol, 0.35M Ammonium Sulfate, 0.2M Sodium Thiocyanate Resolution 3.70 Å R-free 0.299

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.

8 other PDB entries and 8 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name G0RZL9_CHATD
Isoform
PDB entities 1
Chains and sequence ranges Author chain A; PDBConstruct 1–209; UniProt 748–956 Author chain C; PDBConstruct 1–209; UniProt 748–956

Putative uncharacterized protein

Chaetomium thermophilum (strain DSM 1495 / CBS 144.50 / IMI 039719)

UniProt G0SG95

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 × 4 PDB declaration: tetrameric(4) Consistent with protein copy count Chain B; UniProt 738–912 Chain D; UniProt 738–912 Fragment:UNP residues 738-912 Putative uncharacterized protein × 2 (G0RZL9) X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, HANGING DROP;pH 6.5;293 K;0.1M Bis-Tris-HCl, 50% Pentaerythritol, 0.35M Ammonium Sulfate, 0.2M Sodium Thiocyanate Resolution 3.70 Å R-free 0.299

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.

8 other PDB entries and 8 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name G0SG95_CHATD
Isoform
PDB entities 2
Chains and sequence ranges Author chain B; PDBConstruct 1–175; UniProt 738–912 Author chain D; PDBConstruct 1–175; UniProt 738–912

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 5ic9

P(r) Distance Distribution P(r) Distribution

P(r) distribution for 5ic9
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2. Structure Basics 2. Structure Basics

Entry ID entry_id5ic9
Deposition date deposition_date2016-02-23
Structure title titleStructure of the CTD complex of Utp12 and Utp13
Keywords keywordssolenoid structure, rRNA processing, 90S preribosome, protein binding, STRUCTURAL PROTEIN; STRUCTURAL PROTEIN
Experimental Method methodX-RAY DIFFRACTION

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

Radius of gyration Rg (Guinier) rg_guinier27.82
Radius of gyration Rg (electron density) rg_electron26.95
Forward intensity I(0) i050826300.00
Molecular weight molecular_weight56977.0 kDa
Excluded volume excluded_volume72329 ų
Envelope volume envelope_volume97015 ų
Hydration-shell volume shell_volume29979 ų
Envelope diameter envelope_diameter90.2
Shell Rg shell_rg34.11
Envelope Rg envelope_rg27.11
Shape Rg shape_rg26.94
Total Rg total_rg27.85
Total atoms total_atoms4015
Residues n_residues498
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 dmax86.3
Rg (real space) rg_real27.75
Rg uncertainty (real space) rg_real_error0.44
I(0) (real space) i0_real5.0830e+07
I(0) uncertainty (real space) i0_real_error7.3110e+05
Rg (reciprocal space) rg_reciprocal27.78
I(0) (reciprocal space) i0_reciprocal50830000.0000
Solution quality estimate total_estimate0.9105
Solution quality rating solution_quality EXCELLENT a EXCELLENT solution
P(r) peaks n_peaks2
Primary peak position r_peak_primary31.8
Skewness Skewness skewness0.248
Kurtosis Kurtosis kurtosis-0.486
Angular range angular_range— – 0.2850 −1
Current regularization parameter α current_alpha0.0000
Highest regularization parameter α highest_alpha16670000.0000
Real-space data points n_real_points58
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.957; Stabil: 1.000; Sysdev: 1.000; Positv: 1.000; Valcen: 1.000; Smooth: 0.962

5. Crystallography and Experiment 5. Crystallography & Experiment

6. Entities and Polymers Entities & Polymers (2)

8. Citations (1)

9. Files and Curves (10)