5t6j

Structure of the MIND Complex Shows a Regulatory Focus of Yeast Kinetochore Assembly

Method: X-RAY DIFFRACTION Dmax: 55.2 Å Quality: REASONABLE

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

Kinetochore protein SPC24

Saccharomyces cerevisiae (strain ATCC 204508 / S288c)

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 × 3 PDB declaration: trimeric(3) Consistent with protein copy count Chain A; UniProt 155–213 Not recorded Kinetochore protein SPC25 × 1 (P40014) Kinetochore-associated protein DSN1 × 1 (P40568) X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, HANGING DROP;291 K;0.1 M HEPES, pH 7.0-7.5, 1.0 M potassium sodium tartrate, 0.2 M lithium sulfate Resolution 1.75 Å R-free 0.242

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 11 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name SPC24_YEAST
Isoform
PDB entities 1
Chains and sequence ranges Author chain A; PDBConstruct 1–59; UniProt 155–213

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 × 3 PDB declaration: trimeric(3) Consistent with protein copy count Chain B; UniProt 133–221 Not recorded Kinetochore protein SPC24 × 1 (Q04477) Kinetochore-associated protein DSN1 × 1 (P40568) X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, HANGING DROP;291 K;0.1 M HEPES, pH 7.0-7.5, 1.0 M potassium sodium tartrate, 0.2 M lithium sulfate Resolution 1.75 Å R-free 0.242

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 11 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name SPC25_YEAST
Isoform
PDB entities 2
Chains and sequence ranges Author chain B; PDBConstruct 4–92; UniProt 133–221

Kinetochore-associated protein DSN1

Saccharomyces cerevisiae

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 × 3 PDB declaration: trimeric(3) Consistent with protein copy count Chain C; UniProt 560–572 Not recorded Kinetochore protein SPC24 × 1 (Q04477) Kinetochore protein SPC25 × 1 (P40014) X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, HANGING DROP;291 K;0.1 M HEPES, pH 7.0-7.5, 1.0 M potassium sodium tartrate, 0.2 M lithium sulfate Resolution 1.75 Å R-free 0.242

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 3
Chains and sequence ranges Author chain C; PDBConstruct 1–13; UniProt 560–572

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 5t6j

P(r) Distance Distribution P(r) Distribution

P(r) distribution for 5t6j
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2. Structure Basics 2. Structure Basics

Entry ID entry_id5t6j
Deposition date deposition_date2016-09-01
Structure title titleStructure of the MIND Complex Shows a Regulatory Focus of Yeast Kinetochore Assembly
Keywords keywordscell cycle, kinetochore, complex, chromosome, segregation, MIND, Mis12, Mtw1, Spc24, Spc25, Ndc80, Nuf2; CELL CYCLE
Experimental Method methodX-RAY DIFFRACTION

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

Radius of gyration Rg (Guinier) rg_guinier17.18
Radius of gyration Rg (electron density) rg_electron15.59
Forward intensity I(0) i06225900.00
Molecular weight molecular_weight18234.0 kDa
Excluded volume excluded_volume22954 ų
Envelope volume envelope_volume26664 ų
Hydration-shell volume shell_volume14474 ų
Envelope diameter envelope_diameter55.1
Shell Rg shell_rg21.44
Envelope Rg envelope_rg15.85
Shape Rg shape_rg15.59
Total Rg total_rg16.69
Total atoms total_atoms2579
Residues n_residues163
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 dmax55.2
Rg (real space) rg_real17.07
Rg uncertainty (real space) rg_real_error0.36
I(0) (real space) i0_real6.2260e+06
I(0) uncertainty (real space) i0_real_error8.1040e+04
Rg (reciprocal space) rg_reciprocal17.09
I(0) (reciprocal space) i0_reciprocal6226000.0000
Solution quality estimate total_estimate0.7176
Solution quality rating solution_quality REASONABLE a REASONABLE solution
P(r) peaks n_peaks2
Primary peak position r_peak_primary22.5
Skewness Skewness skewness0.133
Kurtosis Kurtosis kurtosis-0.377
Angular range angular_range— – 0.4650 −1
Current regularization parameter α current_alpha0.0000
Highest regularization parameter α highest_alpha827500.0000
Real-space data points n_real_points77
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.857; Stabil: 1.000; Sysdev: 0.257; Positv: 1.000; Valcen: 0.996; Smooth: 0.985

5. Crystallography and Experiment 5. Crystallography & Experiment

6. Entities and Polymers Entities & Polymers (4)

7. Fold Classification (SCOP + CATH) 5 domains

SCOP 2.08 (3 domains)

Domain ID domain_idd5t6ja_
Class classd — Alpha and beta proteins (a+b)
Fold Fold foldd.300 — Kinetochore globular domain-like
Superfamily Superfamily superfamilyd.300.1 — Kinetochore globular domain
Family Family familyd.300.1.2 — Spc24-like
Domain ID domain_idd5t6jb1
Class classd — Alpha and beta proteins (a+b)
Fold Fold foldd.300 — Kinetochore globular domain-like
Superfamily Superfamily superfamilyd.300.1 — Kinetochore globular domain
Family Family familyd.300.1.1 — Spc25-like
Domain ID domain_idd5t6jb2
Class classl — Artifacts
Fold Fold foldl.1 — Tags
Superfamily Superfamily superfamilyl.1.1 — Tags
Family Family familyl.1.1.1 — Tags

CATH v4.4 (2 domains)

Domain ID domain_id5t6jA00
Class class3 — Alpha Beta
Architecture architecture30 — 2-Layer Sandwich
Topology topology160 — Double Stranded RNA Binding Domain
Homologous superfamily homologous superfamily430
Domain ID domain_id5t6jB00
Class class3 — Alpha Beta
Architecture architecture30 — 2-Layer Sandwich
Topology topology457 — Copper Amine Oxidase; Chain A, domain 1
Homologous superfamily homologous superfamily50 — Chromosome segregation protein Spc25

8. Citations (1)

9. Files and Curves (10)