4nfa

Structure of the C-terminal doamin of Knl1

Method: X-RAY DIFFRACTION Dmax: 75.6 Å Quality: GOOD

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

Protein CASC5

Homo sapiens

UniProt Q8NG31

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 monomer Monomer Protein × 1 PDB declaration: monomeric(1) Consistent with protein copy count Chain A; UniProt 2117–2323 Fragment:Knl1 C-terminal domain, UNP residues 2131-2337 CL CHLORIDE ION × 1 GOL GLYCEROL × 3 X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, HANGING DROP;pH 9;293 K;120-300 KSCN, 100 mM BisTris Propane (pH 8.6-9.2), 17 % (v/v) PEG 3350 and 1 mM DTT, VAPOR DIFFUSION, HANGING DROP, temperature 293K Resolution 2.50 Å R-free 0.242

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.

5 other PDB entries and 10 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name CASC5_HUMAN
Isoform
PDB entities 1
Chains and sequence ranges Author chain A; PDBConstruct 1–207; UniProt 2117–2323

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 4nfa

P(r) Distance Distribution P(r) Distribution

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

Entry ID entry_id4nfa
Deposition date deposition_date2013-10-31
Structure title titleStructure of the C-terminal doamin of Knl1
Keywords keywordsRWD domain, CELL CYCLE; CELL CYCLE
Experimental Method methodX-RAY DIFFRACTION

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

Radius of gyration Rg (Guinier) rg_guinier21.46
Radius of gyration Rg (electron density) rg_electron20.58
Forward intensity I(0) i09735240.00
Molecular weight molecular_weight24069.0 kDa
Excluded volume excluded_volume30471 ų
Envelope volume envelope_volume36494 ų
Hydration-shell volume shell_volume16086 ų
Envelope diameter envelope_diameter74.3
Shell Rg shell_rg25.51
Envelope Rg envelope_rg20.93
Shape Rg shape_rg20.59
Total Rg total_rg21.35
Total atoms total_atoms1703
Residues n_residues204
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 dmax75.6
Rg (real space) rg_real21.65
Rg uncertainty (real space) rg_real_error0.79
I(0) (real space) i0_real9.7350e+06
I(0) uncertainty (real space) i0_real_error1.4320e+05
Rg (reciprocal space) rg_reciprocal21.62
I(0) (reciprocal space) i0_reciprocal9735000.0000
Solution quality estimate total_estimate0.8101
Solution quality rating solution_quality GOOD a GOOD solution
P(r) peaks n_peaks1
Primary peak position r_peak_primary74.5
Skewness Skewness skewness0.556
Kurtosis Kurtosis kurtosis-0.215
Angular range angular_range— – 0.3700 −1
Current regularization parameter α current_alpha0.0000
Highest regularization parameter α highest_alpha3250000.0000
Real-space data points n_real_points69
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.604; Stabil: 1.000; Sysdev: 1.000; Positv: 1.000; Valcen: 0.727; Smooth: 0.990

5. Crystallography and Experiment 5. Crystallography & Experiment

6. Entities and Polymers Entities & Polymers (4)

8. Citations (1)

9. Files and Curves (10)