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9c1w

Structure of AKT2 with compound 3

Method: X-RAY DIFFRACTION Dmax: 69.7 Å Quality: EXCELLENT
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1. Protein Identity and Related Structures Protein Identity & Related Structures

RAC-beta serine/threonine-protein kinase

Homo sapiens

UniProt P31751

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 2–447 Mutation：P115A, G116A XOO 4-{2-[({4-[(2P)-2-(2-aminopyridin-3-yl)-5-phenyl-3H-imidazo[4,5-b]pyridin-3-yl]phenyl}methyl)amino]ethyl}-2-hydroxybenzaldehyde × 1 EDO 1,2-ETHANEDIOL × 6 X-RAY DIFFRACTION X-ray crystallization conditions：VAPOR DIFFUSION, HANGING DROP；277 K；0.1 M HEPES pH 7.5, 20 % w/v PEG 8000 Resolution 2.00 Å R-free 0.242

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 9C1W Assembly / Oligomeric State Construct Mutations and Modifications Ligands, Ions and Non-polymers Method and Experimental Conditions Structure Quality
1GZK Molecular mechanism for the regulation of protein kinase B/Akt by hydrophobic motif phosphorylation Deposited 2002-05-23 Different construct Different mutation/modification Different ligand/ion Different experimental conditions Different structure-quality metrics Assembly 1 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric
Chain A 146–460（315 aa） Fragment：KINASE DOMAIN, RESIDUES (146 - 460)
Not recorded No recorded non-water small molecule X-RAY DIFFRACTION
X-ray crystallization conditions pH 7.5；10MG/ML PROTEIN, 30% PEG4K, 0.2 M LITHIUM SULPHATE, 0.1 M TRIS, pH 7.50
Resolution 2.30 Å R-free 0.319
1GZN Structure of PKB kinase domain Deposited 2002-05-24 Different construct Different mutation/modification Different ligand/ion Different experimental conditions Different structure-quality metrics Assembly 1 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric
Chain A 146–480（335 aa） Fragment：KINASE DOMAIN AND HYDROPHOBIC MOTIF, RESIDUES 146-480
Not recorded No recorded non-water small molecule X-RAY DIFFRACTION
X-ray crystallization conditions pH 7.5；30% PEG 8K, 0.2 M LITHIUM SULPHATE 0.1 M TRIS, 10 MG/ML PROTEIN, pH 7.50
Resolution 2.50 Å R-free 0.319
1GZO Structure of protein kinase B unphosphorylated Deposited 2002-05-24 Different construct Different mutation/modification Different ligand/ion Different experimental conditions Different structure-quality metrics Assembly 1 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric
Chain A 146–460（315 aa） Fragment：KINASE DOMAIN WITHOUT HYDROPHOBIC MOTIF, RESIDUES 146-460
Not recorded No recorded non-water small molecule X-RAY DIFFRACTION
X-ray crystallization conditions pH 7.5；30% PEG 8000, 0.2 M LITHIUM SULPHATE, 0.1 M TRIS, 10MG/ML PROTEIN, pH 7.50
Resolution 2.75 Å R-free 0.310
1MRV crystal structure of an inactive Akt2 kinase domain Deposited 2002-09-18 Different construct Different mutation/modification Different ligand/ion Different experimental conditions Different structure-quality metrics Assembly 1 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric
Chain A 143–481（339 aa） Fragment：kinase domain
Not recorded No recorded non-water small molecule X-RAY DIFFRACTION
X-ray crystallization conditions VAPOR DIFFUSION, HANGING DROP；pH 8.5；277 K；Li2SO4, PEG4000, pH 8.5, VAPOR DIFFUSION, HANGING DROP, temperature 277K
Resolution 2.80 Å R-free 0.295
1MRY crystal structure of an inactive akt2 kinase domain Deposited 2002-09-18 Different construct Different mutation/modification Different ligand/ion Different experimental conditions Different structure-quality metrics Assembly 1 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric
Chain A 143–481（339 aa） Fragment：kinase domain
Not recorded No recorded non-water small molecule X-RAY DIFFRACTION
X-ray crystallization conditions VAPOR DIFFUSION, HANGING DROP；pH 8.5；277 K；Li2SO4, PEG 4000, pH 8.5, VAPOR DIFFUSION, HANGING DROP, temperature 277K
Resolution 2.80 Å R-free 0.272
1O6K Structure of activated form of PKB kinase domain S474D with GSK3 peptide and AMP-PNP Deposited 2002-10-08 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 146–481（336 aa） Fragment：KINASE DOMAIN, RESIDUES 146-481
Mutation：YES Non-standard monomer：Yes (specific site not provided by mmCIF) ANP PHOSPHOAMINOPHOSPHONIC ACID-ADENYLATE ESTER × 1 MN MANGANESE (II) ION × 2 X-RAY DIFFRACTION
X-ray crystallization conditions pH 7.5；10 MG/ML PROTEIN 20 PEG 4K, 10% ISOPROPONAL, 5 MM DTT, pH 7.50
Resolution 1.70 Å R-free 0.234
1O6L Crystal structure of an activated Akt/protein kinase B (PKB-PIF chimera) ternary complex with AMP-PNP and GSK3 peptide Deposited 2002-10-08 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 146–467（322 aa） Fragment：KINASE DOMAIN, RESIDUES 146 - 467
Mutation：YES Non-standard monomer：Yes (specific site not provided by mmCIF) ANP PHOSPHOAMINOPHOSPHONIC ACID-ADENYLATE ESTER × 1 MN MANGANESE (II) ION × 2 X-RAY DIFFRACTION
X-ray crystallization conditions pH 7.5；10 MG/ML PROTEIN, 20% (W/V) POLYETHYLENE, GLYCOL 4000, 10% (V/V) ISOPROPANOL, 0.1 M HEPES (PH 7.5), 5 MM DTT
Resolution 1.60 Å R-free 0.227
1P6S Solution Structure of the Pleckstrin Homology Domain of Human Protein Kinase B beta (Pkb/Akt) Deposited 2003-04-30 Different construct Different mutation/modification Different ligand/ion Different experimental method Different experimental conditions Different structure-quality metrics Assembly 1 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric
Chain A 1–111（111 aa） Fragment：Pleckstrin Homology Domain (residues 1-111)
Not recorded No recorded non-water small molecule SOLUTION NMR
NMR measurement conditions pH 7.4；286 K；Ionic strength (raw mmCIF value) 0.3；Pressure ambient
NMR measurement conditions pH 7.4；286 K；Ionic strength (raw mmCIF value) 0.3；Pressure ambient
NMR sample composition 0.4mM PKBbeta-PH U-15N,13C; 10mM Tris-HCl; 300mM NaCl; 0.1mM Benzamidine; 0.1mM EDTA; 4mM Inositol-1,4,5-trisphosphate; 90% H2O, 10% D2O | 90% H2O/10% D2O
NMR sample composition 0.4mM PKBbeta-PH U-15N; 10mM Tris-HCl; 300mM NaCl; 0.1mM Benzamidine; 0.1mM EDTA; 4mM Inositol-1,4,5-trisphosphate; 90% H2O, 10% D2O | 90% H2O/10% D2O
Resolution not provided
2JDO STRUCTURE OF PKB-BETA (AKT2) COMPLEXED WITH ISOQUINOLINE-5-SULFONIC ACID (2-(2-(4-CHLOROBENZYLOXY) ETHYLAMINO)ETHYL)AMIDE Deposited 2007-01-11 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 146–467（322 aa） Fragment：KINASE CATALYTIC DOMAIN, RESIDUES 146-467
Non-standard monomer：Yes (specific site not provided by mmCIF) I5S ISOQUINOLINE-5-SULFONIC ACID (2-(2-(4-CHLOROBENZYLOXY)ETHYLAMINO)ETHYL)AMIDE × 1 EDO 1,2-ETHANEDIOL × 1 X-RAY DIFFRACTION mmCIF provides none of the parsed conditions Resolution 1.80 Å R-free 0.210
2JDR STRUCTURE OF PKB-BETA (AKT2) COMPLEXED WITH THE INHIBITOR A-443654 Deposited 2007-01-12 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 146–467（322 aa） Fragment：KINASE CATALYTIC DOMAIN, RESIDUES 146-467
Non-standard monomer：Yes (specific site not provided by mmCIF) L20 (2S)-1-(1H-INDOL-3-YL)-3-{[5-(3-METHYL-1H-INDAZOL-5-YL)PYRIDIN-3-YL]OXY}PROPAN-2-AMINE × 1 X-RAY DIFFRACTION mmCIF provides none of the parsed conditions Resolution 2.30 Å R-free 0.252
2UW9 STRUCTURE OF PKB-BETA (AKT2) COMPLEXED WITH 4-(4-chloro-phenyl)-4-(4-(1H-pyrazol-4-yl)-phenyl)-piperidine Deposited 2007-03-19 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 146–467（322 aa） Fragment：KINASE CATALYTIC DOMAIN, RESIDUES 146-467
Non-standard monomer：Yes (specific site not provided by mmCIF) GVP 4-(4-CHLOROPHENYL)-4-[4-(1H-PYRAZOL-4-YL)PHENYL]PIPERIDINE × 1 X-RAY DIFFRACTION mmCIF provides none of the parsed conditions Resolution 2.10 Å R-free 0.305
2X39 Structure of 4-Amino-N-(4-chlorobenzyl)-1-(7H-pyrrolo(2,3-d)pyrimidin- 4-yl)piperidine-4-carboxamide bound to PKB Deposited 2010-01-22 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 146–467（322 aa） Fragment：KINASE CATALYTIC DOMAIN, RESIDUES 146-467
Non-standard monomer：Yes (specific site not provided by mmCIF) X39 4-AMINO-N-(4-CHLOROBENZYL)-1-(7H-PYRROLO[2,3-D]PYRIMIDIN-4-YL)PIPERIDINE-4-CARBOXAMIDE × 1 X-RAY DIFFRACTION mmCIF provides none of the parsed conditions Resolution 1.93 Å R-free 0.226
2XH5 Structure of 4-(4-tert-Butylbenzyl)-1-(7H-pyrrolo(2,3-d)pyrimidin-4- yl)piperidin-4-amine bound to PKB Deposited 2010-06-09 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 146–479（334 aa） Fragment：KINASE CATALYTIC DOMAIN, RESIDUES 146-467
Mutation：YES Non-standard monomer：Yes (specific site not provided by mmCIF) X37 4-(4-tert-butylbenzyl)-1-(7H-pyrrolo[2,3-d]pyrimidin-4-yl)piperidin-4-aminium × 1 X-RAY DIFFRACTION mmCIF provides none of the parsed conditions Resolution 2.72 Å R-free 0.305
3D0E Crystal structure of human Akt2 in complex with GSK690693 Deposited 2008-05-01 Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental conditions Different structure-quality metrics Assembly 1 Protein homooligomer Homooligomer；Protein × 2 PDB declaration: dimeric
Chain A 146–480（335 aa） Fragment：kinase domain
Chain B 146–480（335 aa） Fragment：kinase domain
Mutation：S474D Non-standard monomer：Yes (specific site not provided by mmCIF) Mutation：S474D Non-standard monomer：Yes (specific site not provided by mmCIF) G93 4-{2-(4-amino-1,2,5-oxadiazol-3-yl)-1-ethyl-7-[(3S)-piperidin-3-ylmethoxy]-1H-imidazo[4,5-c]pyridin-4-yl}-2-methylbut-3 -yn-2-ol × 2 X-RAY DIFFRACTION
X-ray crystallization conditions VAPOR DIFFUSION；pH 8；298 K；14% PEG 4K, 10% isopropanol, pH 8.0, vapor diffusion, temperature 298K
Resolution 2.00 Å R-free 0.246
3D0E Crystal structure of human Akt2 in complex with GSK690693 Deposited 2008-05-01 Different construct Different mutation/modification Different ligand/ion Different experimental conditions Different structure-quality metrics Assembly 2 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric
Chain A 146–480（335 aa） Fragment：kinase domain
Mutation：S474D Non-standard monomer：Yes (specific site not provided by mmCIF) G93 4-{2-(4-amino-1,2,5-oxadiazol-3-yl)-1-ethyl-7-[(3S)-piperidin-3-ylmethoxy]-1H-imidazo[4,5-c]pyridin-4-yl}-2-methylbut-3 -yn-2-ol × 1 X-RAY DIFFRACTION
X-ray crystallization conditions VAPOR DIFFUSION；pH 8；298 K；14% PEG 4K, 10% isopropanol, pH 8.0, vapor diffusion, temperature 298K
Resolution 2.00 Å R-free 0.246
3D0E Crystal structure of human Akt2 in complex with GSK690693 Deposited 2008-05-01 Different construct Different mutation/modification Different ligand/ion Different experimental conditions Different structure-quality metrics Assembly 3 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric
Chain B 146–480（335 aa） Fragment：kinase domain
Mutation：S474D Non-standard monomer：Yes (specific site not provided by mmCIF) G93 4-{2-(4-amino-1,2,5-oxadiazol-3-yl)-1-ethyl-7-[(3S)-piperidin-3-ylmethoxy]-1H-imidazo[4,5-c]pyridin-4-yl}-2-methylbut-3 -yn-2-ol × 1 X-RAY DIFFRACTION
X-ray crystallization conditions VAPOR DIFFUSION；pH 8；298 K；14% PEG 4K, 10% isopropanol, pH 8.0, vapor diffusion, temperature 298K
Resolution 2.00 Å R-free 0.246
3E87 Crystal structures of the kinase domain of AKT2 in complex with ATP-competitive inhibitors Deposited 2008-08-19 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 146–480（335 aa） Fragment：Akt2 kinase domain (146-480)
Mutation：S474D Non-standard monomer：Yes (specific site not provided by mmCIF) G95 N-[(1S)-2-amino-1-phenylethyl]-5-(1H-pyrrolo[2,3-b]pyridin-4-yl)thiophene-2-carboxamide × 1 X-RAY DIFFRACTION
X-ray crystallization conditions VAPOR DIFFUSION；pH 8；298 K；14% PEG 2KMME, 100 mM Tris pH 8.0 and 10% ethanol diffused in. Seeded., vapor diffusion, temperature 298K
Resolution 2.30 Å R-free 0.246
3E87 Crystal structures of the kinase domain of AKT2 in complex with ATP-competitive inhibitors Deposited 2008-08-19 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 146–480（335 aa） Fragment：Akt2 kinase domain (146-480)
Mutation：S474D Non-standard monomer：Yes (specific site not provided by mmCIF) G95 N-[(1S)-2-amino-1-phenylethyl]-5-(1H-pyrrolo[2,3-b]pyridin-4-yl)thiophene-2-carboxamide × 1 X-RAY DIFFRACTION
X-ray crystallization conditions VAPOR DIFFUSION；pH 8；298 K；14% PEG 2KMME, 100 mM Tris pH 8.0 and 10% ethanol diffused in. Seeded., vapor diffusion, temperature 298K
Resolution 2.30 Å R-free 0.246
3E88 Crystal structures of the kinase domain of AKT2 in complex with ATP-competitive inhibitors Deposited 2008-08-19 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 146–480（335 aa） Fragment：Akt2 kinase domain (146-480)
Mutation：S474D Non-standard monomer：Yes (specific site not provided by mmCIF) G96 4-[2-(4-amino-1,2,5-oxadiazol-3-yl)-6-{[(2R)-2-amino-3-phenylpropyl]oxy}-1-ethyl-1H-imidazo[4,5-c]pyridin-4-yl]-2-methylbut-3-yn-2-ol × 1 X-RAY DIFFRACTION
X-ray crystallization conditions VAPOR DIFFUSION；pH 8；298 K；14% PEG 2KMME, 100 mM Tris pH 8.0 and 10% ethanol diffused in. Seeded., vapor diffusion, temperature 298K
Resolution 2.50 Å R-free 0.273
3E88 Crystal structures of the kinase domain of AKT2 in complex with ATP-competitive inhibitors Deposited 2008-08-19 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 146–480（335 aa） Fragment：Akt2 kinase domain (146-480)
Mutation：S474D Non-standard monomer：Yes (specific site not provided by mmCIF) G96 4-[2-(4-amino-1,2,5-oxadiazol-3-yl)-6-{[(2R)-2-amino-3-phenylpropyl]oxy}-1-ethyl-1H-imidazo[4,5-c]pyridin-4-yl]-2-methylbut-3-yn-2-ol × 1 X-RAY DIFFRACTION
X-ray crystallization conditions VAPOR DIFFUSION；pH 8；298 K；14% PEG 2KMME, 100 mM Tris pH 8.0 and 10% ethanol diffused in. Seeded., vapor diffusion, temperature 298K
Resolution 2.50 Å R-free 0.273
3E8D Crystal structures of the kinase domain of AKT2 in complex with ATP-competitive inhibitors Deposited 2008-08-19 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 146–480（335 aa） Fragment：Akt2 kinase domain (UNP residues 146-480)
Mutation：S474D Non-standard monomer：Yes (specific site not provided by mmCIF) G98 4-[2-(4-amino-2,5-dihydro-1,2,5-oxadiazol-3-yl)-6-{[(1S)-3-amino-1-phenylpropyl]oxy}-1-ethyl-1H-imidazo[4,5-c]pyridin-4-yl]-2-methylbut-3-yn-2-ol × 1 X-RAY DIFFRACTION
X-ray crystallization conditions VAPOR DIFFUSION；pH 8；298 K；14% PEG 2KMME, 100 mM Tris pH 8.0 and 10% ethanol diffused in. Seeded., vapor diffusion, temperature 298K
Resolution 2.70 Å R-free 0.268
3E8D Crystal structures of the kinase domain of AKT2 in complex with ATP-competitive inhibitors Deposited 2008-08-19 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 146–480（335 aa） Fragment：Akt2 kinase domain (UNP residues 146-480)
Mutation：S474D Non-standard monomer：Yes (specific site not provided by mmCIF) G98 4-[2-(4-amino-2,5-dihydro-1,2,5-oxadiazol-3-yl)-6-{[(1S)-3-amino-1-phenylpropyl]oxy}-1-ethyl-1H-imidazo[4,5-c]pyridin-4-yl]-2-methylbut-3-yn-2-ol × 1 X-RAY DIFFRACTION
X-ray crystallization conditions VAPOR DIFFUSION；pH 8；298 K；14% PEG 2KMME, 100 mM Tris pH 8.0 and 10% ethanol diffused in. Seeded., vapor diffusion, temperature 298K
Resolution 2.70 Å R-free 0.268
8Q61 Co-crystal structure of human AKT2 with compound 3 Deposited 2023-08-10 Different construct Different mutation/modification Different ligand/ion Different experimental conditions Different structure-quality metrics Assembly 1 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric
Chain A 1–481（481 aa）
Mutation：N2D K06 6-[4-(1-azanyl-3-methyl-3-oxidanyl-cyclobutyl)phenyl]-7-phenyl-1-propyl-pyrido[2,3-b][1,4]oxazin-2-one × 1 GOL GLYCEROL × 1 PO4 PHOSPHATE ION × 3 MES 2-(N-MORPHOLINO)-ETHANESULFONIC ACID × 1 X-RAY DIFFRACTION
X-ray crystallization conditions VAPOR DIFFUSION, HANGING DROP；pH 6.5；298 K；0.1 M MES, 1.5 M NaH2PO4
Resolution 2.32 Å R-free 0.263

18 other PDB entries and 23 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name AKT2_HUMAN
Isoform —
PDB entities 1
Chains and sequence ranges Author chain A； PDBConstruct 1–446； UniProt 2–447

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 9c1w

P(r) Distance Distribution P(r) Distribution

P(r) distribution for 9c1w
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2. Structure Basics 2. Structure Basics

Entry ID entry_id9c1w
Deposition date deposition_date2024-05-29
Structure title titleStructure of AKT2 with compound 3
Keywords keywordsInhibitor, Kinase, TRANSFERASE, TRANSFERASE-INHIBITOR complex; TRANSFERASE/INHIBITOR
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_guinier23.04 Å
Radius of gyration Rg (electron density) rg_electron21.75 Å
Forward intensity I(0) i034123800.00
Molecular weight molecular_weight46152.0 kDa
Excluded volume excluded_volume58296 ų
Envelope volume envelope_volume69222 ų
Hydration-shell volume shell_volume26038 ų
Envelope diameter envelope_diameter71.5 Å
Shell Rg shell_rg28.81 Å
Envelope Rg envelope_rg21.82 Å
Shape Rg shape_rg21.73 Å
Total Rg total_rg22.71 Å
Total atoms total_atoms3320
Residues n_residues388
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 dmax69.7 Å
Rg (real space) rg_real22.90 Å
Rg uncertainty (real space) rg_real_error0.33 Å
I(0) (real space) i0_real3.4120e+07
I(0) uncertainty (real space) i0_real_error4.2850e+05
Rg (reciprocal space) rg_reciprocal22.94 Å
I(0) (reciprocal space) i0_reciprocal34120000.0000
Solution quality estimate total_estimate0.9107
Solution quality rating solution_quality EXCELLENT a EXCELLENT solution
P(r) peaks n_peaks1
Primary peak position r_peak_primary68.6 Å
Skewness Skewness skewness0.137
Kurtosis Kurtosis kurtosis-0.550
Angular range angular_range— – 0.3450 Å−1
Current regularization parameter α current_alpha0.0000
Highest regularization parameter α highest_alpha9745000.0000
Real-space data points n_real_points66
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.956; Stabil: 1.000; Sysdev: 1.000; Positv: 1.000; Valcen: 0.991; Smooth: 0.977
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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)