5lsi

CRYSTAL STRUCTURE OF THE KINETOCHORE MIS12 COMPLEX HEAD2 SUBDOMAIN CONTAINING DSN1 AND NSL1 FRAGMENTS

Method: X-RAY DIFFRACTION Dmax: 48.1 Å Quality: REASONABLE

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

Kinetochore-associated protein DSN1 homolog

Homo sapiens

UniProt Q9H410

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 × 2 PDB declaration: dimeric(2) Consistent with protein copy count Chain D; UniProt 68–200 Fragment:head2 domain, UNP residues 68-200 Kinetochore-associated protein NSL1 homolog × 1 (Q96IY1) SO4 SULFATE ION × 1 X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION;pH 5.6;293 K;2M ammonium sulfate, 0.2M potassium sodium phosphate, 0.1M sodium citrate pH 5.6 Resolution 2.00 Å R-free 0.246

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.

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

View Construct and Data Evidence
UniProt name DSN1_HUMAN
Isoform
PDB entities 1
Chains and sequence ranges Author chain D; PDBConstruct 2–134; UniProt 68–200

Kinetochore-associated protein NSL1 homolog

Homo sapiens

UniProt Q96IY1

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 × 2 PDB declaration: dimeric(2) Consistent with protein copy count Chain E; UniProt 29–99 Fragment:UNP residues 29-99 Kinetochore-associated protein DSN1 homolog × 1 (Q9H410) SO4 SULFATE ION × 1 X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION;pH 5.6;293 K;2M ammonium sulfate, 0.2M potassium sodium phosphate, 0.1M sodium citrate pH 5.6 Resolution 2.00 Å R-free 0.246

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 7 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name NSL1_HUMAN
Isoform
PDB entities 2
Chains and sequence ranges Author chain E; PDBConstruct 6–76; UniProt 29–99

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 5lsi

P(r) Distance Distribution P(r) Distribution

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

Entry ID entry_id5lsi
Deposition date deposition_date2016-09-02
Structure title titleCRYSTAL STRUCTURE OF THE KINETOCHORE MIS12 COMPLEX HEAD2 SUBDOMAIN CONTAINING DSN1 AND NSL1 FRAGMENTS
Keywords keywordsALPHA-HELICAL, 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_guinier18.69
Radius of gyration Rg (electron density) rg_electron17.64
Forward intensity I(0) i06399180.00
Molecular weight molecular_weight17598.0 kDa
Excluded volume excluded_volume21757 ų
Envelope volume envelope_volume27460 ų
Hydration-shell volume shell_volume13967 ų
Envelope diameter envelope_diameter81.2
Shell Rg shell_rg22.86
Envelope Rg envelope_rg18.81
Shape Rg shape_rg17.61
Total Rg total_rg18.63
Total atoms total_atoms1235
Residues n_residues158
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 dmax48.1
Rg (real space) rg_real17.40
Rg uncertainty (real space) rg_real_error0.06
I(0) (real space) i0_real6.0540e+06
I(0) uncertainty (real space) i0_real_error5.7410e+04
Rg (reciprocal space) rg_reciprocal18.82
I(0) (reciprocal space) i0_reciprocal6399000.0000
Solution quality estimate total_estimate0.6867
Solution quality rating solution_quality REASONABLE a REASONABLE solution
P(r) peaks n_peaks1
Primary peak position r_peak_primary19.8
Skewness Skewness skewness0.261
Kurtosis Kurtosis kurtosis-0.479
Angular range angular_range— – 0.4250 −1
Current regularization parameter α current_alpha3.1010
Highest regularization parameter α highest_alpha1036000.0000
Real-space data points n_real_points74
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.005; Oscil: 0.995; Stabil: 0.981; Sysdev: 0.000; Positv: 1.000; Valcen: 1.000; Smooth: 0.000

5. Crystallography and Experiment 5. Crystallography & Experiment

6. Entities and Polymers Entities & Polymers (4)

8. Citations (1)

9. Files and Curves (10)