2kdd

Solution structure of the conserved C-terminal dimerization domain of Borealin

Method: SOLUTION NMR Dmax: 52.0 Å Quality: GOOD

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

Borealin

Homo sapiens

UniProt Q53HL2

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 homooligomer Homooligomer Protein × 2 PDB declaration: dimeric(2) Consistent with protein copy count Chain A; UniProt 207–280 Chain B; UniProt 207–280 Not recorded No other associated polymer SOLUTION NMR NMR measurement conditions:pH 7.2;299 K;Ionic strength (raw mmCIF value) 0.1;Pressure ambient NMR sample composition:0.6 mM Borealin, 40 mM sodium phosphate, 100 mM sodium chloride, 100% D2O | 100% D2O NMR sample composition:0.8 mM [U-100% 15N] Borealin, 40 mM sodium phosphate, 100 mM sodium chloride, 95% H2O/5% D2O | 95% H2O/5% D2O NMR sample composition:0.7 mM [U-100% 13C; U-100% 15N] Borealin, 40 mM sodium phosphate, 100 mM sodium chloride, 95% H2O/5% D2O | 95% H2O/5% D2O NMR sample composition:0.7 mM [U-100% 13C; U-100% 15N] Borealin, 40 mM sodium phosphate, 100 mM sodium chloride, 100% D2O | 100% D2O NMR sample composition:0.8 mM 50% [U-100% 13C; U-100% 15N], 50% natural abundance Borealin, 40 mM sodium phosphate, 100 mM sodium chloride, 100% D2O | 100% 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.

14 other PDB entries and 17 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name BOREA_HUMAN
Isoform
PDB entities 1
Chains and sequence ranges Author chain A; PDBConstruct 3–76; UniProt 207–280 Author chain B; PDBConstruct 3–76; UniProt 207–280

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 2kdd

P(r) Distance Distribution P(r) Distribution

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

Entry ID entry_id2kdd
Deposition date deposition_date2009-01-06
Structure title titleSolution structure of the conserved C-terminal dimerization domain of Borealin
Keywords keywords;protein dimer, Cell cycle, Cell division, Centromere, Chromosomal protein, Cytoplasm, Mitosis, Nucleus, Phosphoprotein, Polymorphism ;; CELL CYCLE
Experimental Method methodSOLUTION NMR

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

Radius of gyration Rg (Guinier) rg_guinier15.17
Radius of gyration Rg (electron density) rg_electron14.40
Forward intensity I(0) i0221709000.00
Molecular weight molecular_weight124280.0 kDa
Excluded volume excluded_volume156300 ų
Envelope volume envelope_volume28380 ų
Hydration-shell volume shell_volume14872 ų
Envelope diameter envelope_diameter58.7
Shell Rg shell_rg22.15
Envelope Rg envelope_rg16.94
Shape Rg shape_rg14.41
Total Rg total_rg14.65
Total atoms total_atoms17980
Residues n_residues1140
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 dmax52.0
Rg (real space) rg_real15.12
Rg uncertainty (real space) rg_real_error0.36
I(0) (real space) i0_real2.2170e+08
I(0) uncertainty (real space) i0_real_error2.4280e+06
Rg (reciprocal space) rg_reciprocal15.13
I(0) (reciprocal space) i0_reciprocal221700000.0000
Solution quality estimate total_estimate0.7551
Solution quality rating solution_quality GOOD a GOOD solution
P(r) peaks n_peaks3
Primary peak position r_peak_primary19.1
Skewness Skewness skewness0.286
Kurtosis Kurtosis kurtosis-0.014
Angular range angular_range— – 0.5000 −1
Current regularization parameter α current_alpha0.0000
Highest regularization parameter α highest_alpha450100.0000
Real-space data points n_real_points80
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.606; Stabil: 0.999; Sysdev: 1.000; Positv: 1.000; Valcen: 0.996; Smooth: 0.000

5. Crystallography and Experiment 5. Crystallography & Experiment

6. Entities and Polymers Entities & Polymers (1)

7. Fold Classification (SCOP + CATH) 2 domains

CATH v4.4 (2 domains)

Domain ID domain_id2kddA00
Class class6 — Special
Architecture architecture10 — Helix non-globular
Topology topology140 — Helix Hairpins
Homologous superfamily homologous superfamily560
Domain ID domain_id2kddB00
Class class6 — Special
Architecture architecture10 — Helix non-globular
Topology topology140 — Helix Hairpins
Homologous superfamily homologous superfamily560

8. Citations (1)

9. Files and Curves (10)