2aff

The solution structure of the Ki67FHA/hNIFK(226-269)3P complex

Method: SOLUTION NMR Dmax: 48.4 Å Quality: GOOD

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

Antigen KI-67

Homo sapiens

UniProt P46013

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 1–120 Fragment:FHA domain MKI67 FHA domain interacting nucleolar phosphoprotein × 1 (Q9BYG3) SOLUTION NMR NMR measurement conditions:pH 7.4;293 K;Ionic strength (raw mmCIF value) 150 mM NaCl;Pressure ambient NMR sample composition:0.9 mM Ki67 FHA U-15N,13C; 1 mM hNIFK(226-269)3P unlabeled 5 mM HEPES, 5 mM DTT, 1 mM EDTA, 150 mM NaCl, pH 7.4 | 93% H2O/7% D2O NMR sample composition:0.9 mM Ki67 FHA U-15N,13C; 1 mM hNIFK(226-269)3P unlabeled 5 mM HEPES, 5 mM DTT, 1 mM EDTA, 150 mM NaCl, pH 7.4 | 100% D2O NMR sample composition:1 mM Ki67 FHA unlabled; 0.9 mM hNIFK(226-269)3P U-15N,13C 5 mM HEPES, 5 mM DTT, 1 mM EDTA, 150 mM NaCl, pH 7.4 | 93% H2O/7% D2O NMR sample composition:1 mM Ki67 FHA unlabled; 0.9 mM hNIFK(226-269)3P U-15N,13C 5 mM HEPES, 5 mM DTT, 1 mM EDTA, 150 mM NaCl, pH 7.4 | 100% D2O Resolution not provided

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 3 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name KI67_HUMAN
Isoform
PDB entities 1
Chains and sequence ranges Author chain A; PDBConstruct 1–120; UniProt 1–120

MKI67 FHA domain interacting nucleolar phosphoprotein

Homo sapiens

UniProt Q9BYG3

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 B; UniProt 226–269 Fragment:residues 226-269 Non-standard monomer:Yes (specific site not provided by mmCIF) Antigen KI-67 × 1 (P46013) SOLUTION NMR NMR measurement conditions:pH 7.4;293 K;Ionic strength (raw mmCIF value) 150 mM NaCl;Pressure ambient NMR sample composition:0.9 mM Ki67 FHA U-15N,13C; 1 mM hNIFK(226-269)3P unlabeled 5 mM HEPES, 5 mM DTT, 1 mM EDTA, 150 mM NaCl, pH 7.4 | 93% H2O/7% D2O NMR sample composition:0.9 mM Ki67 FHA U-15N,13C; 1 mM hNIFK(226-269)3P unlabeled 5 mM HEPES, 5 mM DTT, 1 mM EDTA, 150 mM NaCl, pH 7.4 | 100% D2O NMR sample composition:1 mM Ki67 FHA unlabled; 0.9 mM hNIFK(226-269)3P U-15N,13C 5 mM HEPES, 5 mM DTT, 1 mM EDTA, 150 mM NaCl, pH 7.4 | 93% H2O/7% D2O NMR sample composition:1 mM Ki67 FHA unlabled; 0.9 mM hNIFK(226-269)3P U-15N,13C 5 mM HEPES, 5 mM DTT, 1 mM EDTA, 150 mM NaCl, pH 7.4 | 100% D2O Resolution not provided

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.

24 other PDB entries and 24 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name MK67I_HUMAN
Isoform
PDB entities 2
Chains and sequence ranges Author chain B; PDBConstruct 1–44; UniProt 226–269

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 2aff

P(r) Distance Distribution P(r) Distribution

P(r) distribution for 2aff
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2. Structure Basics 2. Structure Basics

Entry ID entry_id2aff
Deposition date deposition_date2005-07-25
Structure title titleThe solution structure of the Ki67FHA/hNIFK(226-269)3P complex
Keywords keywordsKi67; FHA; NIFK; NMR; Phosphoprotein, CELL CYCLE; CELL CYCLE
Experimental Method methodSOLUTION NMR

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

Radius of gyration Rg (Guinier) rg_guinier15.15
Radius of gyration Rg (electron density) rg_electron14.70
Forward intensity I(0) i037653700000.00
Molecular weight molecular_weight1584200.0 kDa
Excluded volume excluded_volume1953000 ų
Envelope volume envelope_volume33045 ų
Hydration-shell volume shell_volume16663 ų
Envelope diameter envelope_diameter55.5
Shell Rg shell_rg22.72
Envelope Rg envelope_rg16.81
Shape Rg shape_rg14.69
Total Rg total_rg14.77
Total atoms total_atoms220300
Residues n_residues13500
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 dmax48.4
Rg (real space) rg_real15.05
Rg uncertainty (real space) rg_real_error0.36
I(0) (real space) i0_real3.7650e+10
I(0) uncertainty (real space) i0_real_error4.7720e+08
Rg (reciprocal space) rg_reciprocal15.06
I(0) (reciprocal space) i0_reciprocal37650000000.0000
Solution quality estimate total_estimate0.8897
Solution quality rating solution_quality GOOD a GOOD solution
P(r) peaks n_peaks2
Primary peak position r_peak_primary20.2
Skewness Skewness skewness0.145
Kurtosis Kurtosis kurtosis-0.304
Angular range angular_range— – 0.5000 −1
Current regularization parameter α current_alpha0.0000
Highest regularization parameter α highest_alpha383400.0000
Real-space data points n_real_points80
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.858; Stabil: 0.999; Sysdev: 1.000; Positv: 1.000; Valcen: 0.998; Smooth: 0.993

5. Crystallography and Experiment 5. Crystallography & Experiment

6. Entities and Polymers Entities & Polymers (2)

7. Fold Classification (SCOP + CATH) 2 domains

SCOP 2.08 (1 domains)

Domain ID domain_idd2affa_
Class classb — All beta proteins
Fold Fold foldb.26 — SMAD/FHA domain
Superfamily Superfamily superfamilyb.26.1 — SMAD/FHA domain
Family Family familyb.26.1.2 — FHA domain

CATH v4.4 (1 domains)

Domain ID domain_id2affA00
Class class2 — Mainly Beta
Architecture architecture60 — Sandwich
Topology topology200 — Tumour Suppressor Smad4
Homologous superfamily homologous superfamily20

8. Citations (2)

9. Files and Curves (10)