2jmj

NMR solution structure of the PHD domain from the yeast YNG1 protein in complex with H3(1-9)K4me3 peptide

Method: SOLUTION NMR Dmax: 49.4 Å Quality: REASONABLE

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

Protein YNG1

Saccharomyces cerevisiae

UniProt Q08465

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 141–219 Fragment:PHD finger Histone H3 × 1 (P61830) ZN ZINC ION × 2 SOLUTION NMR NMR measurement conditions:pH 7.5;20 K;Ionic strength (raw mmCIF value) 50;Pressure ambient NMR sample composition:0.52 mM [U-15N] YNG1_PHD, 2.5 mM H3(1-9)K4me3, 2 mM DTT, 50 mM potassium chloride, 20 mM sodium phosphate, 90% H2O, 10% D2O | 90% H2O/10% D2O NMR sample composition:0.48 mM [U-13C; U-15N] YNG1_PHD, 2.5 mM H3(1-9)K4me3, 2 mM DTT, 50 mM potassium chloride, 20 mM sodium phosphate, 90% H2O, 10% D2O | 90% H2O/10% 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.

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

View Construct and Data Evidence
UniProt name YNG1_YEAST
Isoform
PDB entities 1
Chains and sequence ranges Author chain A; PDBConstruct 12–90; UniProt 141–219

Histone H3

OrganismNot specified

UniProt P61830

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 P; UniProt 2–10 Non-standard monomer:Yes (specific site not provided by mmCIF) Protein YNG1 × 1 (Q08465) ZN ZINC ION × 2 SOLUTION NMR NMR measurement conditions:pH 7.5;20 K;Ionic strength (raw mmCIF value) 50;Pressure ambient NMR sample composition:0.52 mM [U-15N] YNG1_PHD, 2.5 mM H3(1-9)K4me3, 2 mM DTT, 50 mM potassium chloride, 20 mM sodium phosphate, 90% H2O, 10% D2O | 90% H2O/10% D2O NMR sample composition:0.48 mM [U-13C; U-15N] YNG1_PHD, 2.5 mM H3(1-9)K4me3, 2 mM DTT, 50 mM potassium chloride, 20 mM sodium phosphate, 90% H2O, 10% D2O | 90% H2O/10% 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.

37 other PDB entries and 42 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name H3_YEAST
Isoform
PDB entities 2
Chains and sequence ranges Author chain P; PDBConstruct 1–9; UniProt 2–10

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 2jmj

P(r) Distance Distribution P(r) Distribution

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

Entry ID entry_id2jmj
Deposition date deposition_date2006-11-15
Structure title titleNMR solution structure of the PHD domain from the yeast YNG1 protein in complex with H3(1-9)K4me3 peptide
Keywords keywordsHistone, PHD, H3K4me3, complex, PROTEIN BINDING; PROTEIN BINDING
Experimental Method methodSOLUTION NMR

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

Radius of gyration Rg (Guinier) rg_guinier11.91
Radius of gyration Rg (electron density) rg_electron12.09
Forward intensity I(0) i0414355000.00
Molecular weight molecular_weight162140.0 kDa
Excluded volume excluded_volume198430 ų
Envelope volume envelope_volume22292 ų
Hydration-shell volume shell_volume12375 ų
Envelope diameter envelope_diameter54.3
Shell Rg shell_rg21.14
Envelope Rg envelope_rg16.66
Shape Rg shape_rg12.11
Total Rg total_rg12.23
Total atoms total_atoms21880
Residues n_residues1360
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 dmax49.4
Rg (real space) rg_real12.01
Rg uncertainty (real space) rg_real_error0.46
I(0) (real space) i0_real4.1440e+08
I(0) uncertainty (real space) i0_real_error4.5190e+06
Rg (reciprocal space) rg_reciprocal12.00
I(0) (reciprocal space) i0_reciprocal414400000.0000
Solution quality estimate total_estimate0.7369
Solution quality rating solution_quality REASONABLE a REASONABLE solution
P(r) peaks n_peaks2
Primary peak position r_peak_primary13.8
Skewness Skewness skewness0.605
Kurtosis Kurtosis kurtosis0.329
Angular range angular_range— – 0.5000 −1
Current regularization parameter α current_alpha0.0000
Highest regularization parameter α highest_alpha75060.0000
Real-space data points n_real_points80
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.401; Stabil: 1.000; Sysdev: 1.000; Positv: 1.000; Valcen: 0.375; Smooth: 0.998

5. Crystallography and Experiment 5. Crystallography & Experiment

6. Entities and Polymers Entities & Polymers (3)

7. Fold Classification (SCOP + CATH) 1 domains

CATH v4.4 (1 domains)

Domain ID domain_id2jmjA00
Class class3 — Alpha Beta
Architecture architecture30 — 2-Layer Sandwich
Topology topology40 — Herpes Virus-1
Homologous superfamily homologous superfamily10 — Zinc/RING finger domain, C3HC4 (zinc finger)

8. Citations (1)

9. Files and Curves (10)