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1guw

STRUCTURE OF THE CHROMODOMAIN FROM MOUSE HP1beta IN COMPLEX WITH THE LYSINE 9-METHYL HISTONE H3 N-TERMINAL PEPTIDE, NMR, 25 STRUCTURES

Method: SOLUTION NMR Dmax: 42.4 Å Quality: REASONABLE
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1. Protein Identity and Related Structures Protein Identity & Related Structures

CHROMOBOX PROTEIN HOMOLOG 1

MUS MUSCULUS

UniProt P23197

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 10–80 Fragment：CHROMODOMAIN, RESIDUES 8 - 80 HISTONE H3.1 × 1 （P16106） SOLUTION NMR NMR measurement conditions：pH 5.5；298 K；Pressure 1 NMR sample composition：150 mM NACL, 20 mM PHOSPHATE BUFFER, 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.

Other PDB Difference from Current Entry 1GUW Assembly / Oligomeric State Construct Mutations and Modifications Ligands, Ions and Non-polymers Method and Experimental Conditions Structure Quality
1S4Z HP1 chromo shadow domain in complex with PXVXL motif of CAF-1 Deposited 2004-01-19 Different construct Different mutation/modification Different oligomeric state Different experimental conditions Assembly 1 Protein heterocomplex Heteromer；Protein × 3 PDB declaration: trimeric
Chain A 104–176（73 aa） Fragment：chromo shadow domain
Chain B 104–176（73 aa） Fragment：chromo shadow domain
Not recorded No recorded non-water small molecule SOLUTION NMR
NMR measurement conditions pH 7.5；298 K；Ionic strength (raw mmCIF value) 150mM；Pressure 1
NMR measurement conditions pH 7.5；298 K；Ionic strength (raw mmCIF value) 150mM；Pressure 1
NMR sample composition 15N-labelled and 13C,15N labelled material complexed with unlabelled peptide | H2O
NMR sample composition 15N labelled peptide complexed with unlabelled protein | H2O
Resolution not provided

1 other PDB entries and 1 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name CBX1_HUMAN
Isoform —
PDB entities 1
Chains and sequence ranges Author chain A； PDBConstruct 3–73； UniProt 10–80

HISTONE H3.1

OrganismNot specified

UniProt P16106

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 1–16 Fragment：N-TERMINAL TAIL, RESIDUES 1-18 Non-standard monomer：Yes (specific site not provided by mmCIF) CHROMOBOX PROTEIN HOMOLOG 1 × 1 （P23197） SOLUTION NMR NMR measurement conditions：pH 5.5；298 K；Pressure 1 NMR sample composition：150 mM NACL, 20 mM PHOSPHATE BUFFER, 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.

Other PDB Difference from Current Entry 1GUW Assembly / Oligomeric State Construct Mutations and Modifications Ligands, Ions and Non-polymers Method and Experimental Conditions Structure Quality
1CS9 SOLUTION STRUCTURE OF CGGIRGERA IN CONTACT WITH THE MONOCLONAL ANTIBODY MAB 4X11, NMR, 7 STRUCTURES Deposited 1999-08-18 Different construct Different mutation/modification Different oligomeric state Different experimental conditions Assembly 1 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric
Chain A 130–135（6 aa） Fragment：C-TERMINAL REGION 130-135
Not recorded No recorded non-water small molecule SOLUTION NMR
NMR measurement conditions pH 7；277 K；Ionic strength (raw mmCIF value) 0.1M PHOSPHATE；Pressure 1
NMR sample composition 5 MM PEPTIDE, 0.1MM MAB; 100 MM PHOSPHATE BUFFER CONTAINING 0.02% SODIUM AZIDE
Resolution not provided
1CT6 SOLUTION STRUCTURE OF CGGIRGERG IN CONTACT WITH THE MONOCLONAL ANTIBODY MAB 4X11, NMR, 11 STRUCTURES Deposited 1999-08-19 Different construct Different mutation/modification Different oligomeric state Different experimental conditions Assembly 1 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric
Chain A 130–135（6 aa） Fragment：C-TERMINAL REGION 130-135
Not recorded No recorded non-water small molecule SOLUTION NMR
NMR measurement conditions pH 7；277 K；Ionic strength (raw mmCIF value) 0.1M PHOSPHATE；Pressure 1
NMR sample composition 5 MM PEPTIDE, 0.1 MM MAB; 100 MM PHOSPHTE BUFFER CONTAINING 0.02% SODIUM AZIDE
Resolution not provided
1Q3L Chromodomain Of HP1 Complexed With Histone H3 Tail Containing monomethyllysine 9. Deposited 2003-07-30 Different construct Different experimental method Different experimental conditions Different structure-quality metrics Assembly 1 Protein heterocomplex Heteromer；Protein × 2 PDB declaration: dimeric
Chain P 1–16（16 aa） Fragment：tail residues 1-16
Non-standard monomer：Yes (specific site not provided by mmCIF) No recorded non-water small molecule X-RAY DIFFRACTION
X-ray crystallization conditions VAPOR DIFFUSION, SITTING DROP；pH 6.1；283 K；Ammonium Sulfate, MES, pH 6.1, VAPOR DIFFUSION, SITTING DROP, temperature 283K
Resolution 1.64 Å R-free 0.241

3 other PDB entries and 3 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name H31_HUMAN
Isoform —
PDB entities 2
Chains and sequence ranges Author chain B； PDBConstruct 1–16； UniProt 1–16

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 1guw

P(r) Distance Distribution P(r) Distribution

P(r) distribution for 1guw
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2. Structure Basics 2. Structure Basics

Entry ID entry_id1guw
Deposition date deposition_date2002-02-01
Structure title titleSTRUCTURE OF THE CHROMODOMAIN FROM MOUSE HP1beta IN COMPLEX WITH THE LYSINE 9-METHYL HISTONE H3 N-TERMINAL PEPTIDE, NMR, 25 STRUCTURES
Keywords keywordsCHROMATIN-BINDING, LYSINE METHYLATION, HETEROCHROMATIN, HISTONE MODIFICATION; CHROMATIN-BINDING
Experimental Method methodSOLUTION NMR
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3. SAXS Parameters (CRYSOL theoretical calculation) 3. SAXS Parameters (CRYSOL)

Radius of gyration Rg (Guinier) rg_guinier16.00 Å
Radius of gyration Rg (electron density) rg_electron15.61 Å
Forward intensity I(0) i01027010000.00
Molecular weight molecular_weight262590.0 kDa
Excluded volume excluded_volume325340 ų
Envelope volume envelope_volume60563 ų
Hydration-shell volume shell_volume22932 ų
Envelope diameter envelope_diameter77.7 Å
Shell Rg shell_rg29.16 Å
Envelope Rg envelope_rg22.75 Å
Shape Rg shape_rg15.55 Å
Total Rg total_rg16.18 Å
Total atoms total_atoms36525
Residues n_residues2225
Spherical-harmonic order n_harmonics20
q range q_range— – 0.5000 Å−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
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4. P(r) Distance Distribution (GNOM inversion) 4. P(r) Analysis (GNOM)

Maximum dimension Dmax dmax42.4 Å
Rg (real space) rg_real14.92 Å
Rg uncertainty (real space) rg_real_error0.07 Å
I(0) (real space) i0_real9.7470e+08
I(0) uncertainty (real space) i0_real_error8.2660e+06
Rg (reciprocal space) rg_reciprocal16.17 Å
I(0) (reciprocal space) i0_reciprocal1027000000.0000
Solution quality estimate total_estimate0.6871
Solution quality rating solution_quality REASONABLE a REASONABLE solution
P(r) peaks n_peaks1
Primary peak position r_peak_primary17.7 Å
Skewness Skewness skewness0.286
Kurtosis Kurtosis kurtosis-0.412
Angular range angular_range— – 0.4950 Å−1
Current regularization parameter α current_alpha4.3650
Highest regularization parameter α highest_alpha264600.0000
Real-space data points n_real_points80
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.009; Oscil: 0.996; Stabil: 0.982; Sysdev: 0.000; Positv: 1.000; Valcen: 0.998; Smooth: 0.000
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5. Crystallography and Experiment 5. Crystallography & Experiment

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6. Entities and Polymers Entities & Polymers (2)

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7. Fold Classification (SCOP + CATH) 3 domains

SCOP 2.08 (2 domains)

Domain ID domain_idd1guwa1
Class classb — All beta proteins
Fold Fold foldb.34 — SH3-like barrel
Superfamily Superfamily superfamilyb.34.13 — Chromo domain-like
Family Family familyb.34.13.2 — Chromo domain
Domain ID domain_idd1guwa2
Class classl — Artifacts
Fold Fold foldl.1 — Tags
Superfamily Superfamily superfamilyl.1.1 — Tags
Family Family familyl.1.1.1 — Tags

CATH v4.4 (1 domains)

Domain ID domain_id1guwA00
Class class2 — Mainly Beta
Architecture architecture40 — Beta Barrel
Topology topology50 — OB fold (Dihydrolipoamide Acetyltransferase, E2P)
Homologous superfamily homologous superfamily40 —
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8. Citations (2)

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9. Files and Curves (10)