6qlf

Structure of inner kinetochore CCAN complex with mask1

Method: ELECTRON MICROSCOPY Dmax: 165.0 Å Quality: GOOD

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

Inner kinetochore subunit IML3

Saccharomyces cerevisiae

UniProt P38265

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 × 8 PDB declaration: octameric(8) Consistent with protein copy count Chain L; UniProt 1–245 Not recorded Inner kinetochore subunit CHL4 × 1 (P38907) Inner kinetochore subunit MCM21 × 1 (Q06675) Inner kinetochore subunit CTF19 × 1 (Q02732) Inner kinetochore subunit OKP1 × 1 (P53298) Inner kinetochore subunit AME1 × 1 (P38313) Inner kinetochore subunit NKP1 × 1 (Q12493) Inner kinetochore subunit NKP2 × 1 (Q06162) ELECTRON MICROSCOPY cryo-EM buffer:pH 8 cryo-EM vitrification conditions:Cryogen ETHANE Resolution 3.45 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.

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

View Construct and Data Evidence
UniProt name CENPL_YEAST
Isoform
PDB entities 1
Chains and sequence ranges Author chain L; PDBConstruct 1–245; UniProt 1–245

Inner kinetochore subunit CHL4

Saccharomyces cerevisiae

UniProt P38907

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 × 8 PDB declaration: octameric(8) Consistent with protein copy count Chain N; UniProt 1–458 Not recorded Inner kinetochore subunit IML3 × 1 (P38265) Inner kinetochore subunit MCM21 × 1 (Q06675) Inner kinetochore subunit CTF19 × 1 (Q02732) Inner kinetochore subunit OKP1 × 1 (P53298) Inner kinetochore subunit AME1 × 1 (P38313) Inner kinetochore subunit NKP1 × 1 (Q12493) Inner kinetochore subunit NKP2 × 1 (Q06162) ELECTRON MICROSCOPY cryo-EM buffer:pH 8 cryo-EM vitrification conditions:Cryogen ETHANE Resolution 3.45 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.

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

View Construct and Data Evidence
UniProt name CENPN_YEAST
Isoform
PDB entities 2
Chains and sequence ranges Author chain N; PDBConstruct 1–458; UniProt 1–458

Inner kinetochore subunit MCM21

Saccharomyces cerevisiae

UniProt Q06675

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 × 8 PDB declaration: octameric(8) Consistent with protein copy count Chain O; UniProt 1–368 Not recorded Inner kinetochore subunit IML3 × 1 (P38265) Inner kinetochore subunit CHL4 × 1 (P38907) Inner kinetochore subunit CTF19 × 1 (Q02732) Inner kinetochore subunit OKP1 × 1 (P53298) Inner kinetochore subunit AME1 × 1 (P38313) Inner kinetochore subunit NKP1 × 1 (Q12493) Inner kinetochore subunit NKP2 × 1 (Q06162) ELECTRON MICROSCOPY cryo-EM buffer:pH 8 cryo-EM vitrification conditions:Cryogen ETHANE Resolution 3.45 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.

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

View Construct and Data Evidence
UniProt name CENPO_YEAST
Isoform
PDB entities 3
Chains and sequence ranges Author chain O; PDBConstruct 1–368; UniProt 1–368

Inner kinetochore subunit CTF19

Saccharomyces cerevisiae

UniProt Q02732

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 × 8 PDB declaration: octameric(8) Consistent with protein copy count Chain P; UniProt 1–369 Not recorded Inner kinetochore subunit IML3 × 1 (P38265) Inner kinetochore subunit CHL4 × 1 (P38907) Inner kinetochore subunit MCM21 × 1 (Q06675) Inner kinetochore subunit OKP1 × 1 (P53298) Inner kinetochore subunit AME1 × 1 (P38313) Inner kinetochore subunit NKP1 × 1 (Q12493) Inner kinetochore subunit NKP2 × 1 (Q06162) ELECTRON MICROSCOPY cryo-EM buffer:pH 8 cryo-EM vitrification conditions:Cryogen ETHANE Resolution 3.45 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.

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

View Construct and Data Evidence
UniProt name CENPP_YEAST
Isoform
PDB entities 4
Chains and sequence ranges Author chain P; PDBConstruct 1–369; UniProt 1–369

Inner kinetochore subunit OKP1

Saccharomyces cerevisiae

UniProt P53298

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 × 8 PDB declaration: octameric(8) Consistent with protein copy count Chain Q; UniProt 1–406 Not recorded Inner kinetochore subunit IML3 × 1 (P38265) Inner kinetochore subunit CHL4 × 1 (P38907) Inner kinetochore subunit MCM21 × 1 (Q06675) Inner kinetochore subunit CTF19 × 1 (Q02732) Inner kinetochore subunit AME1 × 1 (P38313) Inner kinetochore subunit NKP1 × 1 (Q12493) Inner kinetochore subunit NKP2 × 1 (Q06162) ELECTRON MICROSCOPY cryo-EM buffer:pH 8 cryo-EM vitrification conditions:Cryogen ETHANE Resolution 3.45 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.

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

View Construct and Data Evidence
UniProt name CENPQ_YEAST
Isoform
PDB entities 5
Chains and sequence ranges Author chain Q; PDBConstruct 1–406; UniProt 1–406

Inner kinetochore subunit AME1

Saccharomyces cerevisiae

UniProt P38313

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 × 8 PDB declaration: octameric(8) Consistent with protein copy count Chain U; UniProt 1–320 Not recorded Inner kinetochore subunit IML3 × 1 (P38265) Inner kinetochore subunit CHL4 × 1 (P38907) Inner kinetochore subunit MCM21 × 1 (Q06675) Inner kinetochore subunit CTF19 × 1 (Q02732) Inner kinetochore subunit OKP1 × 1 (P53298) Inner kinetochore subunit NKP1 × 1 (Q12493) Inner kinetochore subunit NKP2 × 1 (Q06162) ELECTRON MICROSCOPY cryo-EM buffer:pH 8 cryo-EM vitrification conditions:Cryogen ETHANE Resolution 3.45 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.

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

View Construct and Data Evidence
UniProt name CENPU_YEAST
Isoform
PDB entities 6
Chains and sequence ranges Author chain U; PDBConstruct 1–320; UniProt 1–320

Inner kinetochore subunit NKP1

Saccharomyces cerevisiae

UniProt Q12493

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 × 8 PDB declaration: octameric(8) Consistent with protein copy count Chain Y; UniProt 1–238 Not recorded Inner kinetochore subunit IML3 × 1 (P38265) Inner kinetochore subunit CHL4 × 1 (P38907) Inner kinetochore subunit MCM21 × 1 (Q06675) Inner kinetochore subunit CTF19 × 1 (Q02732) Inner kinetochore subunit OKP1 × 1 (P53298) Inner kinetochore subunit AME1 × 1 (P38313) Inner kinetochore subunit NKP2 × 1 (Q06162) ELECTRON MICROSCOPY cryo-EM buffer:pH 8 cryo-EM vitrification conditions:Cryogen ETHANE Resolution 3.45 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.

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

View Construct and Data Evidence
UniProt name NKP1_YEAST
Isoform
PDB entities 7
Chains and sequence ranges Author chain Y; PDBConstruct 1–238; UniProt 1–238

Inner kinetochore subunit NKP2

Saccharomyces cerevisiae

UniProt Q06162

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 × 8 PDB declaration: octameric(8) Consistent with protein copy count Chain Z; UniProt 1–153 Not recorded Inner kinetochore subunit IML3 × 1 (P38265) Inner kinetochore subunit CHL4 × 1 (P38907) Inner kinetochore subunit MCM21 × 1 (Q06675) Inner kinetochore subunit CTF19 × 1 (Q02732) Inner kinetochore subunit OKP1 × 1 (P53298) Inner kinetochore subunit AME1 × 1 (P38313) Inner kinetochore subunit NKP1 × 1 (Q12493) ELECTRON MICROSCOPY cryo-EM buffer:pH 8 cryo-EM vitrification conditions:Cryogen ETHANE Resolution 3.45 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.

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

View Construct and Data Evidence
UniProt name NKP2_YEAST
Isoform
PDB entities 8
Chains and sequence ranges Author chain Z; PDBConstruct 1–153; UniProt 1–153

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 6qlf

P(r) Distance Distribution P(r) Distribution

P(r) distribution for 6qlf
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2. Structure Basics 2. Structure Basics

Entry ID entry_id6qlf
Deposition date deposition_date2019-01-31
Structure title titleStructure of inner kinetochore CCAN complex with mask1
Keywords keywordsinner kinetochore, CCAN, DNA BINDING PROTEIN; DNA BINDING PROTEIN
Experimental Method methodELECTRON MICROSCOPY

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

Radius of gyration Rg (Guinier) rg_guinier47.90
Radius of gyration Rg (electron density) rg_electron47.39
Forward intensity I(0) i0515622000.00
Molecular weight molecular_weight191500.0 kDa
Excluded volume excluded_volume241910 ų
Envelope volume envelope_volume362180 ų
Hydration-shell volume shell_volume66146 ų
Envelope diameter envelope_diameter179.2
Shell Rg shell_rg48.41
Envelope Rg envelope_rg48.37
Shape Rg shape_rg47.46
Total Rg total_rg47.20
Total atoms total_atoms13501
Residues n_residues1783
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 dmax165.0
Rg (real space) rg_real48.15
Rg uncertainty (real space) rg_real_error1.93
I(0) (real space) i0_real5.1560e+08
I(0) uncertainty (real space) i0_real_error1.0040e+07
Rg (reciprocal space) rg_reciprocal47.91
I(0) (reciprocal space) i0_reciprocal515500000.0000
Solution quality estimate total_estimate0.8749
Solution quality rating solution_quality GOOD a GOOD solution
P(r) peaks n_peaks2
Primary peak position r_peak_primary50.0
Skewness Skewness skewness0.417
Kurtosis Kurtosis kurtosis-0.367
Angular range angular_range— – 0.1650 −1
Current regularization parameter α current_alpha0.0000
Highest regularization parameter α highest_alpha55070000.0000
Real-space data points n_real_points34
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.854; Stabil: 1.000; Sysdev: 1.000; Positv: 1.000; Valcen: 0.970; Smooth: 0.838

5. Crystallography and Experiment 5. Crystallography & Experiment

6. Entities and Polymers Entities & Polymers (8)

8. Citations (1)

9. Files and Curves (10)