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8vlh

Crystal structure of Ash1L PHD-BAH domains

Method: X-RAY DIFFRACTION Dmax: 119.8 Å Quality: GOOD
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1. Protein Identity and Related Structures Protein Identity & Related Structures

Histone-lysine N-methyltransferase ASH1L

Homo sapiens

UniProt Q9NR48

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 homooligomer Homooligomer Protein × 2 PDB declaration: dimeric（2） Consistent with protein copy count Chain A； UniProt 2584–2839 Chain B； UniProt 2584–2839 Not recorded ZN ZINC ION × 4 SR STRONTIUM ION × 1 X-RAY DIFFRACTION X-ray crystallization conditions：VAPOR DIFFUSION, SITTING DROP；291 K；0.1 M Bis-Tris propane pH 10, 0.25 M strontium chloride, 0.01 M ammonium sulfate, and 25% PEG 8000 Resolution 2.40 Å R-free 0.284

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 8VLH Assembly / Oligomeric State Construct Mutations and Modifications Ligands, Ions and Non-polymers Method and Experimental Conditions Structure Quality
3MQM Crystal Structure of the Bromodomain of human ASH1L Deposited 2010-04-28 Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental conditions Different structure-quality metrics Assembly 1 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric
Chain A 2438–2564（127 aa） Fragment：BROMODOMAIN of human ASH1L (UNP RESIDUES 2438:2564)
Not recorded No recorded non-water small molecule X-RAY DIFFRACTION
X-ray crystallization conditions VAPOR DIFFUSION, SITTING DROP；pH 7.5；277 K；0.15M NaNO3 20% PEG3350 10% EtGly, pH 7.5, VAPOR DIFFUSION, SITTING DROP, temperature 277K
Resolution 2.54 Å R-free 0.259
3MQM Crystal Structure of the Bromodomain of human ASH1L Deposited 2010-04-28 Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental conditions Different structure-quality metrics Assembly 2 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric
Chain B 2438–2564（127 aa） Fragment：BROMODOMAIN of human ASH1L (UNP RESIDUES 2438:2564)
Not recorded No recorded non-water small molecule X-RAY DIFFRACTION
X-ray crystallization conditions VAPOR DIFFUSION, SITTING DROP；pH 7.5；277 K；0.15M NaNO3 20% PEG3350 10% EtGly, pH 7.5, VAPOR DIFFUSION, SITTING DROP, temperature 277K
Resolution 2.54 Å R-free 0.259
3MQM Crystal Structure of the Bromodomain of human ASH1L Deposited 2010-04-28 Different construct Different ligand/ion Different experimental conditions Different structure-quality metrics Assembly 3 Protein homooligomer Homooligomer；Protein × 2 PDB declaration: dimeric
Chain A 2438–2564（127 aa） Fragment：BROMODOMAIN of human ASH1L (UNP RESIDUES 2438:2564)
Chain B 2438–2564（127 aa） Fragment：BROMODOMAIN of human ASH1L (UNP RESIDUES 2438:2564)
Not recorded No recorded non-water small molecule X-RAY DIFFRACTION
X-ray crystallization conditions VAPOR DIFFUSION, SITTING DROP；pH 7.5；277 K；0.15M NaNO3 20% PEG3350 10% EtGly, pH 7.5, VAPOR DIFFUSION, SITTING DROP, temperature 277K
Resolution 2.54 Å R-free 0.259
3OPE Structural Basis of Auto-inhibitory mechanism of Histone methyltransferase Deposited 2010-08-31 Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental conditions Different structure-quality metrics Assembly 1 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric
Chain A 2074–2293（220 aa） Fragment：SET domain (UNP RESIDUES 2074-2293)
Not recorded ZN ZINC ION × 3 SAM S-ADENOSYLMETHIONINE × 1 X-RAY DIFFRACTION
X-ray crystallization conditions VAPOR DIFFUSION, HANGING DROP；pH 7.5；291 K；Bistrisprofane, PEG, pH 7.5, VAPOR DIFFUSION, HANGING DROP, temperature 291K
Resolution 2.90 Å R-free 0.299
3OPE Structural Basis of Auto-inhibitory mechanism of Histone methyltransferase Deposited 2010-08-31 Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental conditions Different structure-quality metrics Assembly 2 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric
Chain B 2074–2293（220 aa） Fragment：SET domain (UNP RESIDUES 2074-2293)
Not recorded ZN ZINC ION × 3 SAM S-ADENOSYLMETHIONINE × 1 X-RAY DIFFRACTION
X-ray crystallization conditions VAPOR DIFFUSION, HANGING DROP；pH 7.5；291 K；Bistrisprofane, PEG, pH 7.5, VAPOR DIFFUSION, HANGING DROP, temperature 291K
Resolution 2.90 Å R-free 0.299
4YNM ASH1L wild-type SET domain in complex with S-adenosyl methionine (SAM) Deposited 2015-03-10 Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental conditions Different structure-quality metrics Assembly 1 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric
Chain A 2074–2293（220 aa） Fragment：SET domain (UNP residues 2074-2293)
Not recorded ZN ZINC ION × 3 SAM S-ADENOSYLMETHIONINE × 1 X-RAY DIFFRACTION
X-ray crystallization conditions VAPOR DIFFUSION, SITTING DROP；277 K；PEG 3350, 20 mM Tris
Resolution 2.19 Å R-free 0.278
4YNM ASH1L wild-type SET domain in complex with S-adenosyl methionine (SAM) Deposited 2015-03-10 Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental conditions Different structure-quality metrics Assembly 2 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric
Chain B 2074–2293（220 aa） Fragment：SET domain (UNP residues 2074-2293)
Not recorded ZN ZINC ION × 3 SAM S-ADENOSYLMETHIONINE × 1 X-RAY DIFFRACTION
X-ray crystallization conditions VAPOR DIFFUSION, SITTING DROP；277 K；PEG 3350, 20 mM Tris
Resolution 2.19 Å R-free 0.278
4YNP ASH1L SET domain S2259M mutant in complex with S-adenosyl methionine (SAM) Deposited 2015-03-10 Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental conditions Different structure-quality metrics Assembly 1 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric
Chain A 2074–2293（220 aa） Fragment：SET domain (UNP residues 2074-2293)
Mutation：S2259M ZN ZINC ION × 3 SAM S-ADENOSYLMETHIONINE × 1 X-RAY DIFFRACTION
X-ray crystallization conditions VAPOR DIFFUSION, SITTING DROP；277 K；PEG 3350, 20 mM Tris
Resolution 2.90 Å R-free 0.319
4YNP ASH1L SET domain S2259M mutant in complex with S-adenosyl methionine (SAM) Deposited 2015-03-10 Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental conditions Different structure-quality metrics Assembly 2 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric
Chain B 2074–2293（220 aa） Fragment：SET domain (UNP residues 2074-2293)
Mutation：S2259M ZN ZINC ION × 3 SAM S-ADENOSYLMETHIONINE × 1 X-RAY DIFFRACTION
X-ray crystallization conditions VAPOR DIFFUSION, SITTING DROP；277 K；PEG 3350, 20 mM Tris
Resolution 2.90 Å R-free 0.319
4YPA ASH1L SET domain Q2265A mutant in complex with S-adenosyl methionine (SAM) Deposited 2015-03-12 Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental conditions Different structure-quality metrics Assembly 1 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric
Chain A 2074–2293（220 aa） Fragment：SET domain (UNP residues 2074-2293)
Mutation：Q2265A ZN ZINC ION × 3 SAM S-ADENOSYLMETHIONINE × 1 X-RAY DIFFRACTION
X-ray crystallization conditions VAPOR DIFFUSION, SITTING DROP；290 K；PEG 4000, magnesium chloride, Tris
Resolution 2.30 Å R-free 0.303
4YPA ASH1L SET domain Q2265A mutant in complex with S-adenosyl methionine (SAM) Deposited 2015-03-12 Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental conditions Different structure-quality metrics Assembly 2 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric
Chain B 2074–2293（220 aa） Fragment：SET domain (UNP residues 2074-2293)
Mutation：Q2265A ZN ZINC ION × 3 SAM S-ADENOSYLMETHIONINE × 1 X-RAY DIFFRACTION
X-ray crystallization conditions VAPOR DIFFUSION, SITTING DROP；290 K；PEG 4000, magnesium chloride, Tris
Resolution 2.30 Å R-free 0.303
4YPA ASH1L SET domain Q2265A mutant in complex with S-adenosyl methionine (SAM) Deposited 2015-03-12 Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental conditions Different structure-quality metrics Assembly 3 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric
Chain C 2074–2293（220 aa） Fragment：SET domain (UNP residues 2074-2293)
Mutation：Q2265A ZN ZINC ION × 3 SAM S-ADENOSYLMETHIONINE × 1 X-RAY DIFFRACTION
X-ray crystallization conditions VAPOR DIFFUSION, SITTING DROP；290 K；PEG 4000, magnesium chloride, Tris
Resolution 2.30 Å R-free 0.303
4YPA ASH1L SET domain Q2265A mutant in complex with S-adenosyl methionine (SAM) Deposited 2015-03-12 Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental conditions Different structure-quality metrics Assembly 4 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric
Chain D 2074–2293（220 aa） Fragment：SET domain (UNP residues 2074-2293)
Mutation：Q2265A ZN ZINC ION × 3 SAM S-ADENOSYLMETHIONINE × 1 X-RAY DIFFRACTION
X-ray crystallization conditions VAPOR DIFFUSION, SITTING DROP；290 K；PEG 4000, magnesium chloride, Tris
Resolution 2.30 Å R-free 0.303
4YPE ASH1L SET domain H2193F mutant in complex with S-adenosyl methionine (SAM) Deposited 2015-03-12 Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental conditions Different structure-quality metrics Assembly 1 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric
Chain A 2074–2293（220 aa） Fragment：SET domain (UNP residues 2074-2293)
Mutation：H2193F ZN ZINC ION × 3 SAM S-ADENOSYLMETHIONINE × 1 X-RAY DIFFRACTION
X-ray crystallization conditions VAPOR DIFFUSION, SITTING DROP；277 K；PEG 3350, 20 mM Tris
Resolution 2.20 Å R-free 0.263
4YPE ASH1L SET domain H2193F mutant in complex with S-adenosyl methionine (SAM) Deposited 2015-03-12 Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental conditions Different structure-quality metrics Assembly 2 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric
Chain B 2074–2293（220 aa） Fragment：SET domain (UNP residues 2074-2293)
Mutation：H2193F ZN ZINC ION × 3 SAM S-ADENOSYLMETHIONINE × 1 X-RAY DIFFRACTION
X-ray crystallization conditions VAPOR DIFFUSION, SITTING DROP；277 K；PEG 3350, 20 mM Tris
Resolution 2.20 Å R-free 0.263
4YPU ASH1L SET domain K2264L mutant in complex with S-adenosyl methionine (SAM) Deposited 2015-03-13 Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental conditions Different structure-quality metrics Assembly 1 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric
Chain A 2074–2293（220 aa） Fragment：SET domain (UNP residues 2074-2293)
Mutation：K2264L ZN ZINC ION × 3 SAM S-ADENOSYLMETHIONINE × 1 X-RAY DIFFRACTION
X-ray crystallization conditions VAPOR DIFFUSION, SITTING DROP；277 K；PEG 3350, 20 mm Tris
Resolution 2.60 Å R-free 0.305
4YPU ASH1L SET domain K2264L mutant in complex with S-adenosyl methionine (SAM) Deposited 2015-03-13 Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental conditions Different structure-quality metrics Assembly 2 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric
Chain B 2074–2293（220 aa） Fragment：SET domain (UNP residues 2074-2293)
Mutation：K2264L ZN ZINC ION × 3 SAM S-ADENOSYLMETHIONINE × 1 X-RAY DIFFRACTION
X-ray crystallization conditions VAPOR DIFFUSION, SITTING DROP；277 K；PEG 3350, 20 mm Tris
Resolution 2.60 Å R-free 0.305
6AGO Crystal structure of MRG15-ASH1L Histone methyltransferase complex Deposited 2018-08-13 Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental conditions Different structure-quality metrics Assembly 1 Protein heterocomplex Heteromer；Protein × 2 PDB declaration: dimeric
Chain A 2039–2293（255 aa）
Not recorded SAM S-ADENOSYLMETHIONINE × 1 ZN ZINC ION × 3 X-RAY DIFFRACTION
X-ray crystallization conditions EVAPORATION；295 K；Ammonium Acetate
Resolution 3.10 Å R-free 0.272
6AGO Crystal structure of MRG15-ASH1L Histone methyltransferase complex Deposited 2018-08-13 Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental conditions Different structure-quality metrics Assembly 2 Protein heterocomplex Heteromer；Protein × 2 PDB declaration: dimeric
Chain B 2039–2293（255 aa）
Not recorded ZN ZINC ION × 3 X-RAY DIFFRACTION
X-ray crystallization conditions EVAPORATION；295 K；Ammonium Acetate
Resolution 3.10 Å R-free 0.272
6INE Crystal Structure of human ASH1L-MRG15 complex Deposited 2018-10-25 Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental conditions Different structure-quality metrics Assembly 1 Protein heterocomplex Heteromer；Protein × 2 PDB declaration: dimeric
Chain A 2026–2288（263 aa）
Not recorded ZN ZINC ION × 3 SAM S-ADENOSYLMETHIONINE × 1 GOL GLYCEROL × 1 X-RAY DIFFRACTION
X-ray crystallization conditions VAPOR DIFFUSION, SITTING DROP；pH 8.5；277 K；0.1 M Tris-HCl pH 8.5, 20 % PEG 6000, 0.2 M Trimethylamine-N-oxide
Resolution 2.60 Å R-free 0.237
6WZW Ash1L SET domain in complex with AS-85 Deposited 2020-05-14 Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental conditions Different structure-quality metrics Assembly 1 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric
Chain A 2074–2293（220 aa）
Not recorded EPE 4-(2-HYDROXYETHYL)-1-PIPERAZINE ETHANESULFONIC ACID × 1 SAM S-ADENOSYLMETHIONINE × 1 ZN ZINC ION × 3 UG7 N-{[3-(3-carbamothioylphenyl)-1-{1-[(trifluoromethyl)sulfonyl]piperidin-4-yl}-1H-indol-6-yl]methyl}azetidine-3-carboxamide × 1 X-RAY DIFFRACTION
X-ray crystallization conditions VAPOR DIFFUSION, SITTING DROP；pH 7.5；290 K；0.1 M HEPES pH 7.5, 30% PEG3350
Resolution 1.69 Å R-free 0.206
6X0P Ash1L SET domain Q2265A mutant in complex with AS-5 Deposited 2020-05-17 Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental conditions Different structure-quality metrics Assembly 1 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric
Chain A 2074–2293（220 aa）
Mutation：Q2265A UK7 3-[6-(aminomethyl)-1-(2-hydroxyethyl)-1H-indol-3-yl]benzene-1-carbothioamide × 1 ZN ZINC ION × 3 SAM S-ADENOSYLMETHIONINE × 1 X-RAY DIFFRACTION
X-ray crystallization conditions VAPOR DIFFUSION, SITTING DROP；pH 8.5；290 K；0.1 M Tris pH 8.5, 0.2 M MgCl2, 30% PEG4000
Resolution 1.69 Å R-free 0.213
6X0P Ash1L SET domain Q2265A mutant in complex with AS-5 Deposited 2020-05-17 Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental conditions Different structure-quality metrics Assembly 2 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric
Chain B 2074–2293（220 aa）
Mutation：Q2265A UK7 3-[6-(aminomethyl)-1-(2-hydroxyethyl)-1H-indol-3-yl]benzene-1-carbothioamide × 1 ZN ZINC ION × 3 SAM S-ADENOSYLMETHIONINE × 1 X-RAY DIFFRACTION
X-ray crystallization conditions VAPOR DIFFUSION, SITTING DROP；pH 8.5；290 K；0.1 M Tris pH 8.5, 0.2 M MgCl2, 30% PEG4000
Resolution 1.69 Å R-free 0.213
6X0P Ash1L SET domain Q2265A mutant in complex with AS-5 Deposited 2020-05-17 Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental conditions Different structure-quality metrics Assembly 3 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric
Chain C 2074–2293（220 aa）
Mutation：Q2265A UK7 3-[6-(aminomethyl)-1-(2-hydroxyethyl)-1H-indol-3-yl]benzene-1-carbothioamide × 1 ZN ZINC ION × 3 SAM S-ADENOSYLMETHIONINE × 1 X-RAY DIFFRACTION
X-ray crystallization conditions VAPOR DIFFUSION, SITTING DROP；pH 8.5；290 K；0.1 M Tris pH 8.5, 0.2 M MgCl2, 30% PEG4000
Resolution 1.69 Å R-free 0.213
6X0P Ash1L SET domain Q2265A mutant in complex with AS-5 Deposited 2020-05-17 Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental conditions Different structure-quality metrics Assembly 4 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric
Chain D 2074–2293（220 aa）
Mutation：Q2265A UK7 3-[6-(aminomethyl)-1-(2-hydroxyethyl)-1H-indol-3-yl]benzene-1-carbothioamide × 1 ZN ZINC ION × 3 SAM S-ADENOSYLMETHIONINE × 1 X-RAY DIFFRACTION
X-ray crystallization conditions VAPOR DIFFUSION, SITTING DROP；pH 8.5；290 K；0.1 M Tris pH 8.5, 0.2 M MgCl2, 30% PEG4000
Resolution 1.69 Å R-free 0.213
7Y0I Solution structures of ASH1L PHD domain in complex with H3K4me2 peptide Deposited 2022-06-05 Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental method Different experimental conditions Different structure-quality metrics Assembly 1 Protein heterocomplex Heteromer；Protein × 2 PDB declaration: dimeric
Chain A 2584–2635（52 aa）
Not recorded ZN ZINC ION × 2 SOLUTION NMR
NMR measurement conditions pH 7.2；298 K；Ionic strength (raw mmCIF value) null；Pressure 1
NMR sample composition 50 mM sodium phosphate, 100 mM sodium chloride, 100 uM ZINC ION, 2.0 mM [U-100% 2H] DTT, 90% H2O/10% D2O | 90% H2O/10% D2O
NMR sample composition 50 mM sodium phosphate, 100 mM sodium chloride, 100 uM ZINC ION, 2.0 mM [U-100% 2H] DTT, 100% D2O | 100% D2O
Resolution not provided
8VLD Crystal structure of Ash1L PHD finger in complex with histone H3K4me2 Deposited 2024-01-11 Different construct Different oligomeric state Different ligand/ion Different experimental conditions Different structure-quality metrics Assembly 1 Protein heterocomplex Heteromer；Protein × 4 PDB declaration: tetrameric
Chain A 2584–2636（53 aa）
Chain B 2584–2636（53 aa）
Not recorded ZN ZINC ION × 4 X-RAY DIFFRACTION
X-ray crystallization conditions VAPOR DIFFUSION, HANGING DROP；277 K；1.6 M sodium citrate pH 6.5
Resolution 1.92 Å R-free 0.249
8VLF Crystal structure of Ash1L PHD finger in complex with histone H3K4me3 Deposited 2024-01-11 Different construct Different oligomeric state Different ligand/ion Different experimental conditions Different structure-quality metrics Assembly 1 Protein heterocomplex Heteromer；Protein × 4 PDB declaration: tetrameric
Chain A 2584–2636（53 aa）
Chain B 2584–2636（53 aa）
Not recorded ZN ZINC ION × 4 X-RAY DIFFRACTION
X-ray crystallization conditions VAPOR DIFFUSION, HANGING DROP；277 K；1.6 M sodium citrate pH 6.5
Resolution 1.34 Å R-free 0.188

14 other PDB entries and 28 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name ASH1L_HUMAN
Isoform —
PDB entities 1
Chains and sequence ranges Author chain A； PDBConstruct 4–259； UniProt 2584–2839 Author chain B； PDBConstruct 4–259； UniProt 2584–2839

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 8vlh

P(r) Distance Distribution P(r) Distribution

P(r) distribution for 8vlh
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2. Structure Basics 2. Structure Basics

Entry ID entry_id8vlh
Deposition date deposition_date2024-01-11
Structure title titleCrystal structure of Ash1L PHD-BAH domains
Keywords keywordsAsh1L, methyltransferase, zinc finger, PHD, BAH, TRANSFERASE; TRANSFERASE
Experimental Method methodX-RAY DIFFRACTION
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3. SAXS Parameters (CRYSOL theoretical calculation) 3. SAXS Parameters (CRYSOL)

Radius of gyration Rg (Guinier) rg_guinier35.35 Å
Radius of gyration Rg (electron density) rg_electron35.74 Å
Forward intensity I(0) i056573800.00
Molecular weight molecular_weight58767.0 kDa
Excluded volume excluded_volume73032 ų
Envelope volume envelope_volume104450 ų
Hydration-shell volume shell_volume26361 ų
Envelope diameter envelope_diameter122.8 Å
Shell Rg shell_rg38.36 Å
Envelope Rg envelope_rg35.16 Å
Shape Rg shape_rg35.92 Å
Total Rg total_rg35.37 Å
Total atoms total_atoms4106
Residues n_residues490
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 dmax119.8 Å
Rg (real space) rg_real35.75 Å
Rg uncertainty (real space) rg_real_error1.57 Å
I(0) (real space) i0_real5.6570e+07
I(0) uncertainty (real space) i0_real_error1.1500e+06
Rg (reciprocal space) rg_reciprocal35.51 Å
I(0) (reciprocal space) i0_reciprocal56560000.0000
Solution quality estimate total_estimate0.7796
Solution quality rating solution_quality GOOD a GOOD solution
P(r) peaks n_peaks1
Primary peak position r_peak_primary29.3 Å
Skewness Skewness skewness0.469
Kurtosis Kurtosis kurtosis-0.693
Angular range angular_range— – 0.2250 Å−1
Current regularization parameter α current_alpha0.0000
Highest regularization parameter α highest_alpha5119000.0000
Real-space data points n_real_points46
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.613; Stabil: 1.000; Sysdev: 1.000; Positv: 1.000; Valcen: 0.501; Smooth: 0.792
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5. Crystallography and Experiment 5. Crystallography & Experiment

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6. Entities and Polymers Entities & Polymers (4)

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8. Citations (1)

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9. Files and Curves (10)