2dim

Solution structure of the Myb_DNA-binding domain of human Cell division cycle 5-like protein

Method: SOLUTION NMR Dmax: 38.6 Å Quality: REASONABLE

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

Cell division cycle 5-like protein

Homo sapiens

UniProt Q99459

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 7–63 Fragment:Myb_DNA-binding domain No other associated polymer SOLUTION NMR NMR measurement conditions:pH 7;296 K;Ionic strength (raw mmCIF value) 120mM;Pressure ambient NMR sample composition:1.19mM Myb_DNA-binding domain U-15N, 13C; 20mM d-Tris HCl (pH 7.0); 100mM NaCl; 1mM d-DTT; 0.02% NaN3; 90% H2O, 10% D2O | 90% H2O/10% D2O Resolution not provided

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.

36 other PDB entries and 36 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name CDC5L_HUMAN
Isoform
PDB entities 1
Chains and sequence ranges Author chain A; PDBConstruct 8–64; UniProt 7–63

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 2dim

P(r) Distance Distribution P(r) Distribution

P(r) distribution for 2dim
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2. Structure Basics 2. Structure Basics

Entry ID entry_id2dim
Deposition date deposition_date2006-03-30
Structure title titleSolution structure of the Myb_DNA-binding domain of human Cell division cycle 5-like protein
Keywords keywords;Myb_DNA-binding domain, Cell cycle, DNA binding, Spliceosome, structural genomics, NPPSFA, National Project on Protein Structural and Functional Analyses, RIKEN Structural Genomics/Proteomics Initiative, RSGI, DNA binding protein ;; DNA BINDING PROTEIN
Experimental Method methodSOLUTION NMR

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

Radius of gyration Rg (Guinier) rg_guinier14.16
Radius of gyration Rg (electron density) rg_electron13.57
Forward intensity I(0) i0362529000.00
Molecular weight molecular_weight156060.0 kDa
Excluded volume excluded_volume193970 ų
Envelope volume envelope_volume37037 ų
Hydration-shell volume shell_volume16372 ų
Envelope diameter envelope_diameter75.5
Shell Rg shell_rg25.64
Envelope Rg envelope_rg20.72
Shape Rg shape_rg13.54
Total Rg total_rg14.06
Total atoms total_atoms21920
Residues n_residues1400
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 dmax38.6
Rg (real space) rg_real13.35
Rg uncertainty (real space) rg_real_error0.06
I(0) (real space) i0_real3.4620e+08
I(0) uncertainty (real space) i0_real_error2.6440e+06
Rg (reciprocal space) rg_reciprocal14.35
I(0) (reciprocal space) i0_reciprocal362500000.0000
Solution quality estimate total_estimate0.6734
Solution quality rating solution_quality REASONABLE a REASONABLE solution
P(r) peaks n_peaks1
Primary peak position r_peak_primary14.7
Skewness Skewness skewness0.360
Kurtosis Kurtosis kurtosis-0.372
Angular range angular_range— – 0.5000 −1
Current regularization parameter α current_alpha4.7440
Highest regularization parameter α highest_alpha174300.0000
Real-space data points n_real_points80
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.005; Oscil: 0.943; Stabil: 0.975; Sysdev: 0.000; Positv: 1.000; Valcen: 0.998; Smooth: 0.000

5. Crystallography and Experiment 5. Crystallography & Experiment

6. Entities and Polymers Entities & Polymers (1)

8. Citations (1)

9. Files and Curves (10)