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5ghc

SOLUTION STRUCTURE OF LYS33 ACETYLATED HUMAN SUMO2

Method: SOLUTION NMR Dmax: 43.7 Å Quality: REASONABLE
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1. Protein Identity and Related Structures Protein Identity & Related Structures

Small ubiquitin-related modifier 2

Homo sapiens

UniProt P61956

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 monomer Monomer Protein × 1 PDB declaration: monomeric（1） Consistent with protein copy count Chain A； UniProt 1–93 Fragment：UNP RESIDUES 1-93 Non-standard monomer：Yes (specific site not provided by mmCIF) No other associated polymer SOLUTION NMR NMR measurement conditions：pH 6.5；290 K；Ionic strength (raw mmCIF value) 100 mM KCl；Pressure AMBIENT NMR sample composition：1 mM SUMO2 K33Ac, 10 mM potassium phosphate, 100 mM potassium chloride, 2 mM DTT, 0.1 mM EDTA, 0.001 % sodium azide, 90% H2O/10% D2O | 90% H2O/10% D2O NMR sample composition：1 mM SUMO2 K33Ac, 10 mM potassium phosphate, 100 mM potassium chloride, 2 mM DTT, 0.1 mM EDTA, 0.001 % sodium azide, 90% H2O/10% D2O | 90% H2O/10% D2O NMR sample composition：1 mM SUMO2 K33Ac, 10 mM potassium phosphate, 100 mM potassium chloride, 2 mM DTT, 0.1 mM EDTA, 0.001 % sodium azide, 10 mg/mL Pf1 phage, 90% H2O/10% D2O | 90% H2O/10% D2O NMR sample composition：1 mM SUMO2 K33Ac, 10 mM potassium phosphate, 100 mM potassium chloride, 2 mM DTT, 0.1 mM EDTA, 0.001 % sodium azide, 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.

Other PDB Difference from Current Entry 5GHC Assembly / Oligomeric State Construct Mutations and Modifications Ligands, Ions and Non-polymers Method and Experimental Conditions Structure Quality
1WM2 Crystal structure of human SUMO-2 protein Deposited 2004-07-02 Different construct Different mutation/modification Different oligomeric state Different experimental method Different experimental conditions Different structure-quality metrics Assembly 1 Protein homooligomer Homooligomer；Protein × 3 PDB declaration: trimeric
Chain A 12–89（78 aa） Fragment：no N-terminal arm(residues 12-89)
Not recorded No recorded non-water small molecule X-RAY DIFFRACTION
X-ray crystallization conditions VAPOR DIFFUSION, HANGING DROP；pH 8；298 K；40% PEG600, 0.1M CHES, 0.1M Tris-HCl, pH 8.0, VAPOR DIFFUSION, HANGING DROP, temperature 298.0K
Resolution 1.60 Å R-free 0.190
1WM3 Crystal structure of human SUMO-2 protein Deposited 2004-07-02 Different construct Different mutation/modification Different oligomeric state Different experimental method Different experimental conditions Different structure-quality metrics Assembly 1 Protein homooligomer Homooligomer；Protein × 3 PDB declaration: trimeric
Chain A 17–88（72 aa） Fragment：no N-terminal arm(residues 17-88)
Not recorded No recorded non-water small molecule X-RAY DIFFRACTION
X-ray crystallization conditions VAPOR DIFFUSION, HANGING DROP；pH 8；298 K；40% PEG600, 0.1M CHES, 0.1M Na-HEPES, pH 8.0, VAPOR DIFFUSION, HANGING DROP, temperature 298.0K
Resolution 1.20 Å R-free 0.185
1WZ0 Solution Structure of Human SUMO-2 (SMT3B), a Ubiquitin-like Protein Deposited 2005-02-21 Different construct Different mutation/modification Different experimental conditions Assembly 1 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric
Chain A 1–91（91 aa） Fragment：ubiquitin-like molecule
Not recorded No recorded non-water small molecule SOLUTION NMR
NMR measurement conditions pH 7；298 K；Ionic strength (raw mmCIF value) 100mM；Pressure ambient
NMR sample composition 1.21mM protein U-15N, 13C; 20mM d-Tris-HCl (pH7.0); 100mM NaCl; 1mM d-DTT; 0.02% NaN3; 10% D2O | 90% H2O/10% D2O
Resolution not provided
2AWT Solution Structure of Human Small Ubiquitin-Like Modifier Protein Isoform 2 (SUMO-2) Deposited 2005-09-02 Different construct Different mutation/modification Different experimental conditions Assembly 1 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric
Chain A 1–95（95 aa）
Not recorded No recorded non-water small molecule SOLUTION NMR
NMR measurement conditions pH 6；303 K；Ionic strength (raw mmCIF value) 50mM sodium phosphate, 150mM NaCl；Pressure ambient
NMR sample composition 0.8mM SUMO-2 U-15N, 13C; 50mM phosphate buffer pH 6.0; 150mM NaCl; 1mM EDTA; 1mM DSS; 0.01% sodium azide; 90% H2O, 10% D2O | 90% H2O/10% D2O
Resolution not provided
2CKH SENP1-SUMO2 complex Deposited 2006-04-18 Different construct Different mutation/modification Different oligomeric state Different experimental method Different experimental conditions Different structure-quality metrics Assembly 1 Protein heterocomplex Heteromer；Protein × 2 PDB declaration: dimeric
Chain B 15–93（79 aa）
Not recorded No recorded non-water small molecule X-RAY DIFFRACTION
X-ray crystallization conditions pH 5；pH 5.00
Resolution 3.20 Å R-free 0.294
2D07 Crystal Structure of SUMO-3-modified Thymine-DNA Glycosylase Deposited 2005-07-26 Different construct Different mutation/modification Different oligomeric state Different experimental method Different experimental conditions Different structure-quality metrics Assembly 1 Protein heterocomplex Heteromer；Protein × 2 PDB declaration: dimeric
Chain B 1–93（93 aa）
Not recorded No recorded non-water small molecule X-RAY DIFFRACTION
X-ray crystallization conditions VAPOR DIFFUSION, HANGING DROP；pH 5；293 K；1.5M sodium malonate, pH 5.0, VAPOR DIFFUSION, HANGING DROP, temperature 293K
Resolution 2.10 Å R-free 0.241
2IO0 Crystal structure of human Senp2 in complex with preSUMO-2 Deposited 2006-10-09 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 B 15–95（81 aa）
Not recorded SO4 SULFATE ION × 3 X-RAY DIFFRACTION
X-ray crystallization conditions VAPOR DIFFUSION, HANGING DROP；pH 8；291 K；15% PEG 4000, 0.2M Lithium sulfate, 0.1mM Tris-HCl, pH 8.0, VAPOR DIFFUSION, HANGING DROP, temperature 291K
Resolution 2.30 Å R-free 0.249
2IO3 Crystal structure of human Senp2 in complex with RanGAP1-SUMO-2 Deposited 2006-10-09 Different construct Different mutation/modification Different oligomeric state Different experimental method Different experimental conditions Different structure-quality metrics Assembly 1 Protein heterocomplex Heteromer；Protein × 12 PDB declaration: dodecameric
Chain B 15–93（79 aa）
Not recorded No recorded non-water small molecule X-RAY DIFFRACTION
X-ray crystallization conditions VAPOR DIFFUSION, HANGING DROP；pH 8.5；291 K；12% PEG 4000, 0.1M Lithium chloride, 0.1M Tris-HCl, pH 8.5, VAPOR DIFFUSION, HANGING DROP, temperature 291K
Resolution 3.20 Å R-free 0.306
2IYD SENP1 covalent complex with SUMO-2 Deposited 2006-07-14 Different construct Different mutation/modification Different oligomeric state Different experimental method Different experimental conditions Different structure-quality metrics Assembly 1 Protein heterocomplex Heteromer；Protein × 2 PDB declaration: dimeric
Chain B 15–95（81 aa） Fragment：CATALYTIC FRAGMENT, RESIDUES 15-95
Not recorded No recorded non-water small molecule X-RAY DIFFRACTION mmCIF provides none of the parsed conditions Resolution 3.20 Å R-free 0.288
2N1W Solution structure of human SUMO2 Deposited 2015-04-24 Different construct Different mutation/modification Different experimental conditions Assembly 1 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric
Chain A 1–93（93 aa） Fragment：UNP residues 1-93
Not recorded No recorded non-water small molecule SOLUTION NMR
NMR measurement conditions pH 6.5；290 K；Pressure ambient
NMR sample composition 0.5-1 mM [U-100% 13C; U-100% 15N] SUMO2-1, 10 mM potassium phosphate-2, 100 mM potassium chloride-3, 2 mM DTT-4, 0.1 mM EDTA-5, 0.001 % sodium azide-6, 90% H2O/10% D2O | 90% H2O/10% D2O
NMR sample composition 0.5-1 mM [U-100% 15N] SUMO2-7, 10 mM potassium phosphate-8, 100 mM potassium chloride-9, 2 mM DTT-10, 0.1 mM EDTA-11, 0.001 % sodium azide-12, 90% H2O/10% D2O | 90% H2O/10% D2O
NMR sample composition 0.5-1 mM [U-100% 15N] SUMO2-13, 10 mM potassium phosphate-14, 100 mM potassium chloride-15, 2 mM DTT-16, 0.1 mM EDTA-17, 0.001 % sodium azide-18, 10 w/v Pf1 phage-19, 90% H2O/10% D2O | 90% H2O/10% D2O
NMR sample composition 0.5-1 mM SUMO2-20, 10 mM potassium phosphate-21, 100 mM potassium chloride-22, 2 mM DTT-23, 0.1 mM EDTA-24, 0.001 % sodium azide-25, 90% H2O/10% D2O | 90% H2O/10% D2O
Resolution not provided
2N9E Structure of SUMO-2 bound to phosphorylated RAP80 SIM Deposited 2015-11-15 Different construct Different mutation/modification Different oligomeric state Different experimental conditions Assembly 1 Protein heterocomplex Heteromer；Protein × 2 PDB declaration: dimeric
Chain B 1–95（95 aa）
Not recorded No recorded non-water small molecule SOLUTION NMR
NMR measurement conditions pH 7.3；298 K；Ionic strength (raw mmCIF value) 25；Pressure ambient
NMR sample composition 1.2 mM peptide, 0.4 mM [U-100% 13C; U-100% 15N] protein, 90% H2O/10% D2O | 90% H2O/10% D2O
Resolution not provided
2RPQ Solution Structure of a SUMO-interacting motif of MBD1-containing chromatin-associated factor 1 bound to SUMO-3 Deposited 2008-07-07 Different construct Different mutation/modification Different oligomeric state Different experimental conditions Assembly 1 Protein heterocomplex Heteromer；Protein × 2 PDB declaration: dimeric
Chain A 1–93（93 aa）
Not recorded No recorded non-water small molecule SOLUTION NMR
NMR measurement conditions pH 6.8；298 K；Ionic strength (raw mmCIF value) 0；Pressure ambient
NMR sample composition 0.7 mM [U-100% 13C; U-100% 15N] SIMMCAF1, 90% H2O/10% D2O | 90% H2O/10% D2O
Resolution not provided
3UIN Complex between human RanGAP1-SUMO2, UBC9 and the IR1 domain from RanBP2 Deposited 2011-11-05 Different construct Different mutation/modification Different oligomeric state Different experimental method Different experimental conditions Different structure-quality metrics Assembly 1 Protein heterocomplex Heteromer；Protein × 4 PDB declaration: tetrameric
Chain B 14–93（80 aa） Fragment：UNP residues 14-93
Not recorded No recorded non-water small molecule X-RAY DIFFRACTION
X-ray crystallization conditions VAPOR DIFFUSION, HANGING DROP；pH 7.5；279 K；100 mM HEPES pH 7.5, 400 mM ammonium citrate, 2% isopropanol, VAPOR DIFFUSION, HANGING DROP, temperature 279K
Resolution 2.60 Å R-free 0.264
3UIO Complex between human RanGAP1-SUMO2, UBC9 and the IR1 domain from RanBP2 containing IR2 Motif II Deposited 2011-11-05 Different construct Different mutation/modification Different oligomeric state Different experimental method Different experimental conditions Different structure-quality metrics Assembly 1 Protein heterocomplex Heteromer；Protein × 4 PDB declaration: tetrameric
Chain B 14–93（80 aa） Fragment：UNP residues 14-93
Not recorded No recorded non-water small molecule X-RAY DIFFRACTION
X-ray crystallization conditions VAPOR DIFFUSION, HANGING DROP；pH 6；279 K；14% PEG4000, 100 mM sodium citrate pH 6.0, 200 mM ammonium acetate, vapor diffusion, hanging drop, temperature 279K
Resolution 2.60 Å R-free 0.251
3ZO5 Structure of SENP2-Loop1 in complex with preSUMO-2 Deposited 2013-02-20 Different construct Different mutation/modification Different oligomeric state Different experimental method Different experimental conditions Different structure-quality metrics Assembly 1 Protein heterocomplex Heteromer；Protein × 2 PDB declaration: dimeric
Chain B 16–95（80 aa） Fragment：RESIDUES 16-95
Not recorded No recorded non-water small molecule X-RAY DIFFRACTION mmCIF provides none of the parsed conditions Resolution 2.15 Å R-free 0.236
4BKG crystal structure of human diSUMO-2 Deposited 2013-04-25 Different construct Different mutation/modification Different oligomeric state Different experimental method Different experimental conditions Different structure-quality metrics Assembly 1 Protein homooligomer Homooligomer；Protein × 2 PDB declaration: dimeric
Chain A 12–93（82 aa） Fragment：SUMO-2DELTAN11, RESIDUES 12-93
Not recorded No recorded non-water small molecule X-RAY DIFFRACTION
X-ray crystallization conditions pH 8；0.1 M TRIS/HCL PH 8.0, 28% PEG 350MME,0.05% DIOXANE
Resolution 2.11 Å R-free 0.231
4NPN Crystal structure of human tetra-SUMO-2 Deposited 2013-11-22 Different construct Different mutation/modification Different oligomeric state Different experimental method Different experimental conditions Different structure-quality metrics Assembly 1 Protein homooligomer Homooligomer；Protein × 4 PDB declaration: tetrameric
Chain A 12–93（82 aa） Fragment：DELTAN11SUMO-2, UNP RESIDUES 12-93
Not recorded No recorded non-water small molecule X-RAY DIFFRACTION
X-ray crystallization conditions VAPOR DIFFUSION, HANGING DROP；pH 9.4；289 K；0.1M Tris-HCl, 0.1M CHES, 30% PEG 600, pH 9.4, VAPOR DIFFUSION, HANGING DROP, temperature 289K
Resolution 1.63 Å R-free 0.218
4NPN Crystal structure of human tetra-SUMO-2 Deposited 2013-11-22 Different construct Different mutation/modification Different experimental method Different experimental conditions Different structure-quality metrics Assembly 2 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric
Chain A 12–93（82 aa） Fragment：DELTAN11SUMO-2, UNP RESIDUES 12-93
Not recorded No recorded non-water small molecule X-RAY DIFFRACTION
X-ray crystallization conditions VAPOR DIFFUSION, HANGING DROP；pH 9.4；289 K；0.1M Tris-HCl, 0.1M CHES, 30% PEG 600, pH 9.4, VAPOR DIFFUSION, HANGING DROP, temperature 289K
Resolution 1.63 Å R-free 0.218
5D2M Complex between human SUMO2-RANGAP1, UBC9 and ZNF451 Deposited 2015-08-05 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 × 5 PDB declaration: pentameric
Chain B 15–93（79 aa） Fragment：UNP residues 15-93
Chain E 15–93（79 aa） Fragment：UNP residues 15-93
Not recorded EDO 1,2-ETHANEDIOL × 3 X-RAY DIFFRACTION
X-ray crystallization conditions VAPOR DIFFUSION, HANGING DROP；pH 7.5；291 K；6 % (w/v) PEG 8000, 0.2 M ammonium citrate and 0.1 M HEPES pH 7.5
Resolution 2.40 Å R-free 0.234
5ELU Isoform-specific inhibition of SUMO-dependent protein-protein interactions Deposited 2015-11-05 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 B 14–89（76 aa）
Not recorded SO4 SULFATE ION × 3 X-RAY DIFFRACTION
X-ray crystallization conditions VAPOR DIFFUSION, SITTING DROP；pH 6.5；291 K；0.1 M sodium cacodylate pH 6.5, 0.2 M sodium chloride and 2.0 M ammonium sulphate
Resolution 2.35 Å R-free 0.207
5EQL Isoform-specific inhibition of SUMO-dependent protein-protein interactions Deposited 2015-11-13 Different construct Different mutation/modification Different oligomeric state Different experimental method Different experimental conditions Different structure-quality metrics Assembly 1 Protein heterocomplex Heteromer；Protein × 2 PDB declaration: dimeric
Chain B 14–89（76 aa） Fragment：UNP residues 14-89
Not recorded No recorded non-water small molecule X-RAY DIFFRACTION
X-ray crystallization conditions VAPOR DIFFUSION, SITTING DROP；pH 7.6；291 K；0.1 M HEPES sodium salt pH 7.6, 22% w/v polyethylene glycol 3350
Resolution 2.49 Å R-free 0.243
5GHB SOLUTION STRUCTURE OF LYS42 ACETYLATED HUMAN SUMO2 Deposited 2016-06-19 Different experimental conditions Assembly 1 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric
Chain A 1–93（93 aa） Fragment：UNP RESIDUES 1-93
Non-standard monomer：Yes (specific site not provided by mmCIF) No recorded non-water small molecule SOLUTION NMR
NMR measurement conditions pH 6.5；290 K；Ionic strength (raw mmCIF value) 100 mM KCl；Pressure AMBIENT
NMR sample composition 1 mM [U-100% 13C; U-100% 15N; U-80% 2H] SUMO2 K42Ac, 10 mM potassium phosphate, 100 mM potassium chloride, 2 mM DTT, 0.1 mM EDTA, 0.001 % sodium azide, 90% H2O/10% D2O | 90% H2O/10% D2O
NMR sample composition 1 mM [U-100% 15N] SUMO2 K42Ac, 10 mM potassium phosphate, 100 mM potassium chloride, 2 mM DTT, 0.1 mM EDTA, 0.001 % sodium azide, 90% H2O/10% D2O | 90% H2O/10% D2O
NMR sample composition 1 mM [U-100% 15N] SUMO2 K42Ac, 10 mM potassium phosphate, 100 mM potassium chloride, 2 mM DTT, 0.1 mM EDTA, 0.001 % sodium azide, 10 mg/mL Pf1 phage, 90% H2O/10% D2O | 90% H2O/10% D2O
NMR sample composition 1 mM K42Ac SUMO2, 10 mM potassium phosphate, 100 mM potassium chloride, 2 mM DTT, 0.1 mM EDTA, 0.001 % sodium azide, 90% H2O/10% D2O | 90% H2O/10% D2O
Resolution not provided
6JXW Complex of SUMO2 bound SLS4 from ICP0. Deposited 2019-04-25 Different construct Different mutation/modification Different oligomeric state Different experimental conditions Assembly 1 Protein heterocomplex Heteromer；Protein × 2 PDB declaration: dimeric
Chain A 1–95（95 aa）
Not recorded No recorded non-water small molecule SOLUTION NMR
NMR measurement conditions pH 7.4；298 K；Ionic strength (raw mmCIF value) 137；Pressure 1
NMR sample composition 0.5 mM [U-98% 15N] SUMO2, 2.0 mM SLS4-SIM from Ubiquitin E3 ligase ICP0, 90% H2O/10% D2O | 90% H2O/10% D2O
NMR sample composition 0.5 mM [U-100% 13C; U-100% 15N] SUMO2, 2.0 mM SLS4-SIM from Ubiquitin E3 ligase ICP0, 90% H2O/10% D2O | 90% H2O/10% D2O
NMR sample composition 0.5 mM [U-15N; U-2H] SUMO2, 2.0 mM SLS4-SIM from Ubiquitin E3 ligase ICP0, 90% H2O/10% D2O | 90% H2O/10% D2O
NMR sample composition 2.0 mM [U-15N; U-2H] SUMO2, 0.5 mM SLS4-SIM from Ubiquitin E3 ligase ICP0, 90% H2O/10% D2O | 90% H2O/10% D2O
Resolution not provided
6JXX SUMO2 bound to phosphorylated SLS4-SIM peptide from ICP0 Deposited 2019-04-25 Different construct Different mutation/modification Different oligomeric state Different experimental conditions Assembly 1 Protein heterocomplex Heteromer；Protein × 2 PDB declaration: dimeric
Chain A 1–95（95 aa）
Not recorded No recorded non-water small molecule SOLUTION NMR
NMR measurement conditions pH 7.4；298 K；Ionic strength (raw mmCIF value) 137；Pressure 1
NMR sample composition 0.5 mM [U-15N] SUMO2, 2 mM Phosphorylated SLS4 from E3 ubiquitin ligase ICP0, 90% H2O/10% D2O | 90% H2O/10% D2O
NMR sample composition 0.7 mM [U-13C; U-15N] SUMO2, 1.5 mM Phosphorylated SLS4 from E3 ubiquitin ligase ICP0, 90% H2O/10% D2O | 90% H2O/10% D2O
Resolution not provided
7ZJV Structure of human USPL1 in covalent complex with DeltaN-SUMO2/3-PA probe Deposited 2022-04-12 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 B 18–92（75 aa）
Not recorded ZN ZINC ION × 1 AYE prop-2-en-1-amine × 1 CL CHLORIDE ION × 5 X-RAY DIFFRACTION
X-ray crystallization conditions VAPOR DIFFUSION, SITTING DROP；pH 8.9；293 K；100 mM CHES pH 8.9, 34% PEG600
Resolution 2.40 Å R-free 0.258

24 other PDB entries and 25 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name SUMO2_HUMAN
Isoform —
PDB entities 1
Chains and sequence ranges Author chain A； PDBConstruct 15–107； UniProt 1–93

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 5ghc

P(r) Distance Distribution P(r) Distribution

P(r) distribution for 5ghc
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2. Structure Basics 2. Structure Basics

Entry ID entry_id5ghc
Deposition date deposition_date2016-06-19
Structure title titleSOLUTION STRUCTURE OF LYS33 ACETYLATED HUMAN SUMO2
Keywords keywordsUBIQUITIN-LIKE PROTEIN, ACETYLATED PROTEIN, STRUCTURAL GENOMICS; STRUCTURAL GENOMICS
Experimental Method methodSOLUTION NMR
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3. SAXS Parameters (CRYSOL theoretical calculation) 3. SAXS Parameters (CRYSOL)

Radius of gyration Rg (Guinier) rg_guinier16.02 Å
Radius of gyration Rg (electron density) rg_electron15.62 Å
Forward intensity I(0) i0718426000.00
Molecular weight molecular_weight212960.0 kDa
Excluded volume excluded_volume261520 ų
Envelope volume envelope_volume50553 ų
Hydration-shell volume shell_volume19445 ų
Envelope diameter envelope_diameter82.3 Å
Shell Rg shell_rg28.89 Å
Envelope Rg envelope_rg24.44 Å
Shape Rg shape_rg15.59 Å
Total Rg total_rg16.10 Å
Total atoms total_atoms29480
Residues n_residues1840
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 dmax43.7 Å
Rg (real space) rg_real14.89 Å
Rg uncertainty (real space) rg_real_error0.08 Å
I(0) (real space) i0_real6.8300e+08
I(0) uncertainty (real space) i0_real_error6.0170e+06
Rg (reciprocal space) rg_reciprocal16.28 Å
I(0) (reciprocal space) i0_reciprocal718400000.0000
Solution quality estimate total_estimate0.6713
Solution quality rating solution_quality REASONABLE a REASONABLE solution
P(r) peaks n_peaks1
Primary peak position r_peak_primary16.6 Å
Skewness Skewness skewness0.429
Kurtosis Kurtosis kurtosis-0.249
Angular range angular_range— – 0.4950 Å−1
Current regularization parameter α current_alpha3.6890
Highest regularization parameter α highest_alpha330700.0000
Real-space data points n_real_points80
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.011; Oscil: 0.924; Stabil: 0.986; 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 (1)

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7. Fold Classification (SCOP + CATH) 1 domains

SCOP 2.08 (1 domains)

Domain ID domain_idd5ghca_
Class classd — Alpha and beta proteins (a+b)
Fold Fold foldd.15 — beta-Grasp (ubiquitin-like)
Superfamily Superfamily superfamilyd.15.1 — Ubiquitin-like
Family Family familyd.15.1.1 — Ubiquitin-related
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8. Citations (1)

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9. Files and Curves (10)