4nf9

Structure of the Knl1/Nsl1 complex

Method: X-RAY DIFFRACTION Dmax: 100.7 Å Quality: GOOD

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

Protein CASC5

Homo sapiens

UniProt Q8NG31

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 A; UniProt 2117–2337 Fragment:Knl1 C-terminal domain, UNP residues 2117-2337 Non-standard monomer:Yes (specific site not provided by mmCIF) Kinetochore-associated protein NSL1 homolog × 1 (Q96IY1) CL CHLORIDE ION × 1 X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, HANGING DROP;pH 7;293 K;16-20 % (v/v) PEG 3350, 220 mM sodium citrate and 100 mM MES (pH 6 or 6.5) and 100 mM Hepes (pH 7), VAPOR DIFFUSION, HANGING DROP, temperature 293K Resolution 2.80 Å R-free 0.265
2 Protein heterocomplex Heteromer Protein × 2 PDB declaration: dimeric(2) Consistent with protein copy count Chain B; UniProt 2117–2337 Fragment:Knl1 C-terminal domain, UNP residues 2117-2337 Non-standard monomer:Yes (specific site not provided by mmCIF) Kinetochore-associated protein NSL1 homolog × 1 (Q96IY1) X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, HANGING DROP;pH 7;293 K;16-20 % (v/v) PEG 3350, 220 mM sodium citrate and 100 mM MES (pH 6 or 6.5) and 100 mM Hepes (pH 7), VAPOR DIFFUSION, HANGING DROP, temperature 293K Resolution 2.80 Å R-free 0.265

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 9 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name CASC5_HUMAN
Isoform
PDB entities 1
Chains and sequence ranges Author chain A; PDBConstruct 1–221; UniProt 2117–2337 Author chain B; PDBConstruct 1–221; UniProt 2117–2337

Kinetochore-associated protein NSL1 homolog

OrganismNot specified

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 C; UniProt 256–281 Fragment:Nsl1 C-terminal tail, UNP residues 256-281 Protein CASC5 × 1 (Q8NG31) CL CHLORIDE ION × 1 X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, HANGING DROP;pH 7;293 K;16-20 % (v/v) PEG 3350, 220 mM sodium citrate and 100 mM MES (pH 6 or 6.5) and 100 mM Hepes (pH 7), VAPOR DIFFUSION, HANGING DROP, temperature 293K Resolution 2.80 Å R-free 0.265
2 Protein heterocomplex Heteromer Protein × 2 PDB declaration: dimeric(2) Consistent with protein copy count Chain D; UniProt 256–281 Fragment:Nsl1 C-terminal tail, UNP residues 256-281 Protein CASC5 × 1 (Q8NG31) X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, HANGING DROP;pH 7;293 K;16-20 % (v/v) PEG 3350, 220 mM sodium citrate and 100 mM MES (pH 6 or 6.5) and 100 mM Hepes (pH 7), VAPOR DIFFUSION, HANGING DROP, temperature 293K Resolution 2.80 Å R-free 0.265

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 6 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 C; PDBConstruct 1–26; UniProt 256–281 Author chain D; PDBConstruct 1–26; UniProt 256–281

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 4nf9

P(r) Distance Distribution P(r) Distribution

P(r) distribution for 4nf9
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2. Structure Basics 2. Structure Basics

Entry ID entry_id4nf9
Deposition date deposition_date2013-10-31
Structure title titleStructure of the Knl1/Nsl1 complex
Keywords keywordsRWD domain, 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_guinier30.31
Radius of gyration Rg (electron density) rg_electron29.70
Forward intensity I(0) i041189000.00
Molecular weight molecular_weight52027.0 kDa
Excluded volume excluded_volume65715 ų
Envelope volume envelope_volume85049 ų
Hydration-shell volume shell_volume25347 ų
Envelope diameter envelope_diameter109.2
Shell Rg shell_rg34.80
Envelope Rg envelope_rg29.39
Shape Rg shape_rg29.68
Total Rg total_rg30.26
Total atoms total_atoms3670
Residues n_residues437
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 dmax100.7
Rg (real space) rg_real30.46
Rg uncertainty (real space) rg_real_error0.68
I(0) (real space) i0_real4.1190e+07
I(0) uncertainty (real space) i0_real_error5.8480e+05
Rg (reciprocal space) rg_reciprocal30.40
I(0) (reciprocal space) i0_reciprocal41190000.0000
Solution quality estimate total_estimate0.8708
Solution quality rating solution_quality GOOD a GOOD solution
P(r) peaks n_peaks2
Primary peak position r_peak_primary25.2
Skewness Skewness skewness0.378
Kurtosis Kurtosis kurtosis-0.461
Angular range angular_range— – 0.2600 −1
Current regularization parameter α current_alpha0.0001
Highest regularization parameter α highest_alpha10410000.0000
Real-space data points n_real_points53
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.877; Stabil: 1.000; Sysdev: 1.000; Positv: 1.000; Valcen: 0.803; Smooth: 0.882

5. Crystallography and Experiment 5. Crystallography & Experiment

6. Entities and Polymers Entities & Polymers (4)

8. Citations (1)

9. Files and Curves (10)