8v11

Structure of a Saccharomyces cerevisiae Ipl1 peptide Bound to dwarf Ndc80 complex

Method: X-RAY DIFFRACTION Dmax: 219.6 Å Quality: GOOD

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

Kinetochore protein NDC80

Saccharomyces cerevisiae

UniProt P40460

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 114–318 Chain A; UniProt 621–684 Not recorded Ipl1/Nuf2 chimera protein × 1 (P33895) Kinetochore protein SPC24 × 1 (Q04477) Kinetochore protein SPC25 × 1 (P40014) X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, HANGING DROP;pH 7.5;291.15 K;15% polyethylene glycol 2000 monomethyl ether,500 mM sodium chloride,50 mM Tris pH 7.5 Resolution 3.95 Å R-free 0.327
2 Protein heterocomplex Heteromer Protein × 4 PDB declaration: tetrameric(4) Consistent with protein copy count Chain E; UniProt 114–318 Chain E; UniProt 621–684 Not recorded Ipl1/Nuf2 chimera protein × 1 (P33895) Kinetochore protein SPC24 × 1 (Q04477) Kinetochore protein SPC25 × 1 (P40014) X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, HANGING DROP;pH 7.5;291.15 K;15% polyethylene glycol 2000 monomethyl ether,500 mM sodium chloride,50 mM Tris pH 7.5 Resolution 3.95 Å R-free 0.327

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.

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

View Construct and Data Evidence
UniProt name NDC80_YEAST
Isoform
PDB entities 1
Chains and sequence ranges Author chain A; PDBConstruct 4–208; UniProt 114–318 Author chain A; PDBConstruct 209–272; UniProt 621–684 Author chain E; PDBConstruct 4–208; UniProt 114–318 Author chain E; PDBConstruct 209–272; UniProt 621–684

Ipl1/Nuf2 chimera protein

Saccharomyces cerevisiae

UniProt P33895

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 2–153 Chain B; UniProt 407–451 Not recorded Kinetochore protein NDC80 × 1 (P40460) Kinetochore protein SPC24 × 1 (Q04477) Kinetochore protein SPC25 × 1 (P40014) X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, HANGING DROP;pH 7.5;291.15 K;15% polyethylene glycol 2000 monomethyl ether,500 mM sodium chloride,50 mM Tris pH 7.5 Resolution 3.95 Å R-free 0.327
2 Protein heterocomplex Heteromer Protein × 4 PDB declaration: tetrameric(4) Consistent with protein copy count Chain F; UniProt 2–153 Chain F; UniProt 407–451 Not recorded Kinetochore protein NDC80 × 1 (P40460) Kinetochore protein SPC24 × 1 (Q04477) Kinetochore protein SPC25 × 1 (P40014) X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, HANGING DROP;pH 7.5;291.15 K;15% polyethylene glycol 2000 monomethyl ether,500 mM sodium chloride,50 mM Tris pH 7.5 Resolution 3.95 Å R-free 0.327

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.

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

View Construct and Data Evidence
UniProt name NUF2_YEAST
Isoform
PDB entities 2
Chains and sequence ranges Author chain B; PDBConstruct 31–182; UniProt 2–153 Author chain B; PDBConstruct 183–227; UniProt 407–451 Author chain F; PDBConstruct 31–182; UniProt 2–153 Author chain F; PDBConstruct 183–227; UniProt 407–451

Kinetochore protein SPC24

Saccharomyces cerevisiae

UniProt Q04477

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 C; UniProt 1–48 Chain C; UniProt 162–212 Not recorded Kinetochore protein NDC80 × 1 (P40460) Ipl1/Nuf2 chimera protein × 1 (P33895) Kinetochore protein SPC25 × 1 (P40014) X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, HANGING DROP;pH 7.5;291.15 K;15% polyethylene glycol 2000 monomethyl ether,500 mM sodium chloride,50 mM Tris pH 7.5 Resolution 3.95 Å R-free 0.327
2 Protein heterocomplex Heteromer Protein × 4 PDB declaration: tetrameric(4) Consistent with protein copy count Chain G; UniProt 1–48 Chain G; UniProt 162–212 Not recorded Kinetochore protein NDC80 × 1 (P40460) Ipl1/Nuf2 chimera protein × 1 (P33895) Kinetochore protein SPC25 × 1 (P40014) X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, HANGING DROP;pH 7.5;291.15 K;15% polyethylene glycol 2000 monomethyl ether,500 mM sodium chloride,50 mM Tris pH 7.5 Resolution 3.95 Å R-free 0.327

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.

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

View Construct and Data Evidence
UniProt name SPC24_YEAST
Isoform
PDB entities 3
Chains and sequence ranges Author chain C; PDBConstruct 1–48; UniProt 1–48 Author chain C; PDBConstruct 49–99; UniProt 162–212 Author chain G; PDBConstruct 1–48; UniProt 1–48 Author chain G; PDBConstruct 49–99; UniProt 162–212

Kinetochore protein SPC25

Saccharomyces cerevisiae

UniProt P40014

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 D; UniProt 1–31 Chain D; UniProt 138–220 Not recorded Kinetochore protein NDC80 × 1 (P40460) Ipl1/Nuf2 chimera protein × 1 (P33895) Kinetochore protein SPC24 × 1 (Q04477) X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, HANGING DROP;pH 7.5;291.15 K;15% polyethylene glycol 2000 monomethyl ether,500 mM sodium chloride,50 mM Tris pH 7.5 Resolution 3.95 Å R-free 0.327
2 Protein heterocomplex Heteromer Protein × 4 PDB declaration: tetrameric(4) Consistent with protein copy count Chain H; UniProt 1–31 Chain H; UniProt 138–220 Not recorded Kinetochore protein NDC80 × 1 (P40460) Ipl1/Nuf2 chimera protein × 1 (P33895) Kinetochore protein SPC24 × 1 (Q04477) X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, HANGING DROP;pH 7.5;291.15 K;15% polyethylene glycol 2000 monomethyl ether,500 mM sodium chloride,50 mM Tris pH 7.5 Resolution 3.95 Å R-free 0.327

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.

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

View Construct and Data Evidence
UniProt name SPC25_YEAST
Isoform
PDB entities 4
Chains and sequence ranges Author chain D; PDBConstruct 1–31; UniProt 1–31 Author chain D; PDBConstruct 32–114; UniProt 138–220 Author chain H; PDBConstruct 1–31; UniProt 1–31 Author chain H; PDBConstruct 32–114; UniProt 138–220

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 8v11

P(r) Distance Distribution P(r) Distribution

P(r) distribution for 8v11
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2. Structure Basics 2. Structure Basics

Entry ID entry_id8v11
Deposition date deposition_date2023-11-19
Structure title titleStructure of a Saccharomyces cerevisiae Ipl1 peptide Bound to dwarf Ndc80 complex
Keywords keywordsStu2, tension sensing, Ndc80, kinetochore, 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_guinier84.43
Radius of gyration Rg (electron density) rg_electron87.13
Forward intensity I(0) i0359974000.00
Molecular weight molecular_weight159570.0 kDa
Excluded volume excluded_volume200580 ų
Envelope volume envelope_volume359380 ų
Hydration-shell volume shell_volume46775 ų
Envelope diameter envelope_diameter331.7
Shell Rg shell_rg51.20
Envelope Rg envelope_rg90.05
Shape Rg shape_rg87.17
Total Rg total_rg85.97
Total atoms total_atoms11239
Residues n_residues1371
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 dmax219.6
Rg (real space) rg_real76.16
Rg uncertainty (real space) rg_real_error1.59
I(0) (real space) i0_real3.4430e+08
I(0) uncertainty (real space) i0_real_error6.8120e+06
Rg (reciprocal space) rg_reciprocal76.48
I(0) (reciprocal space) i0_reciprocal352200000.0000
Solution quality estimate total_estimate0.8076
Solution quality rating solution_quality GOOD a GOOD solution
P(r) peaks n_peaks2
Primary peak position r_peak_primary48.8
Skewness Skewness skewness0.305
Kurtosis Kurtosis kurtosis-0.998
Angular range angular_range— – 0.0900 −1
Current regularization parameter α current_alpha0.1706
Highest regularization parameter α highest_alpha12120000.0000
Real-space data points n_real_points19
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.013; Oscil: 0.728; Stabil: 0.987; Sysdev: 1.000; Positv: 1.000; Valcen: 0.477; 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)