9s53

Cryo-EM structure of the base of the Saccharomyces cerevisiae KMN junction complex containing the Mis12c(Mtw1c) head 2 domain

Method: ELECTRON MICROSCOPY Dmax: 142.6 Å Quality: REASONABLE

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

Kinetochore-associated protein DSN1

Saccharomyces cerevisiae S288C

UniProt P40568

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 Ds; UniProt 1–576 Not recorded Kinetochore-associated protein MTW1 × 1 (P39731) Kinetochore-associated protein NNF1 × 1 (P47149) Kinetochore-associated protein NSL1 × 1 (Q12143) ELECTRON MICROSCOPY cryo-EM buffer:pH 7.5 cryo-EM vitrification conditions:Cryogen ETHANE Resolution 6.50 Å

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.

3 other PDB entries and 3 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name DSN1_YEAST
Isoform
PDB entities 1
Chains and sequence ranges Author chain Ds; PDBConstruct 1–576; UniProt 1–576

Kinetochore-associated protein MTW1

Saccharomyces cerevisiae S288C

UniProt P39731

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 Mt; UniProt 1–289 Not recorded Kinetochore-associated protein DSN1 × 1 (P40568) Kinetochore-associated protein NNF1 × 1 (P47149) Kinetochore-associated protein NSL1 × 1 (Q12143) ELECTRON MICROSCOPY cryo-EM buffer:pH 7.5 cryo-EM vitrification conditions:Cryogen ETHANE Resolution 6.50 Å

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.

2 other PDB entries and 2 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name MTW1_YEAST
Isoform
PDB entities 2
Chains and sequence ranges Author chain Mt; PDBConstruct 1–289; UniProt 1–289

Kinetochore-associated protein NNF1

Saccharomyces cerevisiae S288C

UniProt P47149

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 Nn; UniProt 1–201 Not recorded Kinetochore-associated protein DSN1 × 1 (P40568) Kinetochore-associated protein MTW1 × 1 (P39731) Kinetochore-associated protein NSL1 × 1 (Q12143) ELECTRON MICROSCOPY cryo-EM buffer:pH 7.5 cryo-EM vitrification conditions:Cryogen ETHANE Resolution 6.50 Å

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.

2 other PDB entries and 2 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name NNF1_YEAST
Isoform
PDB entities 3
Chains and sequence ranges Author chain Nn; PDBConstruct 1–201; UniProt 1–201

Kinetochore-associated protein NSL1

Saccharomyces cerevisiae S288C

UniProt Q12143

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 Ns; UniProt 1–216 Not recorded Kinetochore-associated protein DSN1 × 1 (P40568) Kinetochore-associated protein MTW1 × 1 (P39731) Kinetochore-associated protein NNF1 × 1 (P47149) ELECTRON MICROSCOPY cryo-EM buffer:pH 7.5 cryo-EM vitrification conditions:Cryogen ETHANE Resolution 6.50 Å

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.

2 other PDB entries and 2 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name NSL1_YEAST
Isoform
PDB entities 4
Chains and sequence ranges Author chain Ns; PDBConstruct 1–216; UniProt 1–216

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 9s53

P(r) Distance Distribution P(r) Distribution

P(r) distribution for 9s53
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2. Structure Basics 2. Structure Basics

Entry ID entry_id9s53
Deposition date deposition_date2025-07-29
Structure title titleCryo-EM structure of the base of the Saccharomyces cerevisiae KMN junction complex containing the Mis12c(Mtw1c) head 2 domain
Keywords keywordsKinetochore, chromosome segregation, mitosis, cell cycle; CELL CYCLE
Experimental Method methodELECTRON MICROSCOPY

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

Radius of gyration Rg (Guinier) rg_guinier36.44
Radius of gyration Rg (electron density) rg_electron37.05
Forward intensity I(0) i082008900.00
Molecular weight molecular_weight71018.0 kDa
Excluded volume excluded_volume88622 ų
Envelope volume envelope_volume120710 ų
Hydration-shell volume shell_volume31642 ų
Envelope diameter envelope_diameter152.9
Shell Rg shell_rg36.85
Envelope Rg envelope_rg37.28
Shape Rg shape_rg37.02
Total Rg total_rg37.15
Total atoms total_atoms8379
Residues n_residues613
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 dmax142.6
Rg (real space) rg_real37.14
Rg uncertainty (real space) rg_real_error1.68
I(0) (real space) i0_real8.2010e+07
I(0) uncertainty (real space) i0_real_error1.4910e+06
Rg (reciprocal space) rg_reciprocal36.71
I(0) (reciprocal space) i0_reciprocal81970000.0000
Solution quality estimate total_estimate0.5311
Solution quality rating solution_quality REASONABLE a REASONABLE solution
P(r) peaks n_peaks1
Primary peak position r_peak_primary139.3
Skewness Skewness skewness0.754
Kurtosis Kurtosis kurtosis0.156
Angular range angular_range— – 0.2150 −1
Current regularization parameter α current_alpha0.0000
Highest regularization parameter α highest_alpha9397000.0000
Real-space data points n_real_points44
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.429; Stabil: 1.000; Sysdev: 0.159; Positv: 1.000; Valcen: 0.202; Smooth: 0.936

5. Crystallography and Experiment 5. Crystallography & Experiment

6. Entities and Polymers Entities & Polymers (4)

8. Citations (1)

9. Files and Curves (10)