9b7j

Cryo-EM structure of human dynactin complex bound to Chlamydia effector Dre1

Method: ELECTRON MICROSCOPY Dmax: 276.4 Å Quality: EXCELLENT

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

Alpha-centractin

OrganismNot specified

UniProt P61163

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 × 25 PDB declaration: 25-meric(25) Consistent with protein copy count Chain A; UniProt 1–376 Chain B; UniProt 1–376 Chain C; UniProt 1–376 Chain D; UniProt 1–376 Chain E; UniProt 1–376 Chain F; UniProt 1–376 Chain G; UniProt 1–376 Chain I; UniProt 1–376 Not recorded Actin, cytoplasmic 1 × 1 (P60709) Actin-related protein 10 × 1 (Q9NZ32) Dynactin subunit 4 × 1 (Q9UJW0) Dynactin subunit 5 × 1 (Q9BTE1) Dynactin subunit 6 × 1 (O00399) F-actin-capping protein subunit alpha-1 × 1 (P52907) F-actin-capping protein subunit beta × 1 (P47756) Dynactin subunit 2 × 4 (Q13561) Dynactin subunit 3 × 2 (O75935) Dynactin subunit 1 × 1 (Q14203) Dynactin subunit 1, p150-glued × 1 Dynactin subunit 2, p50 dynamitin × 1 Dynactin subunit 1 × 1 (Q14203) ADP ADENOSINE-5'-DIPHOSPHATE × 8 ANP PHOSPHOAMINOPHOSPHONIC ACID-ADENYLATE ESTER × 1 ZN ZINC ION × 3 ELECTRON MICROSCOPY cryo-EM buffer:pH 7.5 cryo-EM vitrification conditions:Cryogen ETHANE Resolution 3.49 Å

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.

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

View Construct and Data Evidence
UniProt name ACTZ_HUMAN
Isoform
PDB entities 1
Chains and sequence ranges Author chain A; PDBConstruct 1–376; UniProt 1–376 Author chain B; PDBConstruct 1–376; UniProt 1–376 Author chain C; PDBConstruct 1–376; UniProt 1–376 Author chain D; PDBConstruct 1–376; UniProt 1–376 Author chain E; PDBConstruct 1–376; UniProt 1–376 Author chain F; PDBConstruct 1–376; UniProt 1–376 Author chain G; PDBConstruct 1–376; UniProt 1–376 Author chain I; PDBConstruct 1–376; UniProt 1–376

Actin, cytoplasmic 1

OrganismNot specified

UniProt P60709

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 × 25 PDB declaration: 25-meric(25) Consistent with protein copy count Chain H; UniProt 1–375 Not recorded Alpha-centractin × 8 (P61163) Actin-related protein 10 × 1 (Q9NZ32) Dynactin subunit 4 × 1 (Q9UJW0) Dynactin subunit 5 × 1 (Q9BTE1) Dynactin subunit 6 × 1 (O00399) F-actin-capping protein subunit alpha-1 × 1 (P52907) F-actin-capping protein subunit beta × 1 (P47756) Dynactin subunit 2 × 4 (Q13561) Dynactin subunit 3 × 2 (O75935) Dynactin subunit 1 × 1 (Q14203) Dynactin subunit 1, p150-glued × 1 Dynactin subunit 2, p50 dynamitin × 1 Dynactin subunit 1 × 1 (Q14203) ADP ADENOSINE-5'-DIPHOSPHATE × 8 ANP PHOSPHOAMINOPHOSPHONIC ACID-ADENYLATE ESTER × 1 ZN ZINC ION × 3 ELECTRON MICROSCOPY cryo-EM buffer:pH 7.5 cryo-EM vitrification conditions:Cryogen ETHANE Resolution 3.49 Å

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.

72 other PDB entries and 83 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name ACTB_HUMAN
Isoform
PDB entities 2
Chains and sequence ranges Author chain H; PDBConstruct 1–375; UniProt 1–375

Actin-related protein 10

OrganismNot specified

UniProt Q9NZ32

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 × 25 PDB declaration: 25-meric(25) Consistent with protein copy count Chain J; UniProt 1–417 Not recorded Alpha-centractin × 8 (P61163) Actin, cytoplasmic 1 × 1 (P60709) Dynactin subunit 4 × 1 (Q9UJW0) Dynactin subunit 5 × 1 (Q9BTE1) Dynactin subunit 6 × 1 (O00399) F-actin-capping protein subunit alpha-1 × 1 (P52907) F-actin-capping protein subunit beta × 1 (P47756) Dynactin subunit 2 × 4 (Q13561) Dynactin subunit 3 × 2 (O75935) Dynactin subunit 1 × 1 (Q14203) Dynactin subunit 1, p150-glued × 1 Dynactin subunit 2, p50 dynamitin × 1 Dynactin subunit 1 × 1 (Q14203) ADP ADENOSINE-5'-DIPHOSPHATE × 8 ANP PHOSPHOAMINOPHOSPHONIC ACID-ADENYLATE ESTER × 1 ZN ZINC ION × 3 ELECTRON MICROSCOPY cryo-EM buffer:pH 7.5 cryo-EM vitrification conditions:Cryogen ETHANE Resolution 3.49 Å

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.

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

View Construct and Data Evidence
UniProt name ARP10_HUMAN
Isoform
PDB entities 3
Chains and sequence ranges Author chain J; PDBConstruct 1–417; UniProt 1–417

Dynactin subunit 4

OrganismNot specified

UniProt Q9UJW0

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 × 25 PDB declaration: 25-meric(25) Consistent with protein copy count Chain K; UniProt 1–460 Not recorded Alpha-centractin × 8 (P61163) Actin, cytoplasmic 1 × 1 (P60709) Actin-related protein 10 × 1 (Q9NZ32) Dynactin subunit 5 × 1 (Q9BTE1) Dynactin subunit 6 × 1 (O00399) F-actin-capping protein subunit alpha-1 × 1 (P52907) F-actin-capping protein subunit beta × 1 (P47756) Dynactin subunit 2 × 4 (Q13561) Dynactin subunit 3 × 2 (O75935) Dynactin subunit 1 × 1 (Q14203) Dynactin subunit 1, p150-glued × 1 Dynactin subunit 2, p50 dynamitin × 1 Dynactin subunit 1 × 1 (Q14203) ADP ADENOSINE-5'-DIPHOSPHATE × 8 ANP PHOSPHOAMINOPHOSPHONIC ACID-ADENYLATE ESTER × 1 ZN ZINC ION × 3 ELECTRON MICROSCOPY cryo-EM buffer:pH 7.5 cryo-EM vitrification conditions:Cryogen ETHANE Resolution 3.49 Å

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.

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

View Construct and Data Evidence
UniProt name DCTN4_HUMAN
Isoform
PDB entities 4
Chains and sequence ranges Author chain K; PDBConstruct 1–460; UniProt 1–460

Dynactin subunit 5

OrganismNot specified

UniProt Q9BTE1

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 × 25 PDB declaration: 25-meric(25) Consistent with protein copy count Chain L; UniProt 1–182 Not recorded Alpha-centractin × 8 (P61163) Actin, cytoplasmic 1 × 1 (P60709) Actin-related protein 10 × 1 (Q9NZ32) Dynactin subunit 4 × 1 (Q9UJW0) Dynactin subunit 6 × 1 (O00399) F-actin-capping protein subunit alpha-1 × 1 (P52907) F-actin-capping protein subunit beta × 1 (P47756) Dynactin subunit 2 × 4 (Q13561) Dynactin subunit 3 × 2 (O75935) Dynactin subunit 1 × 1 (Q14203) Dynactin subunit 1, p150-glued × 1 Dynactin subunit 2, p50 dynamitin × 1 Dynactin subunit 1 × 1 (Q14203) ADP ADENOSINE-5'-DIPHOSPHATE × 8 ANP PHOSPHOAMINOPHOSPHONIC ACID-ADENYLATE ESTER × 1 ZN ZINC ION × 3 ELECTRON MICROSCOPY cryo-EM buffer:pH 7.5 cryo-EM vitrification conditions:Cryogen ETHANE Resolution 3.49 Å

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.

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

View Construct and Data Evidence
UniProt name DCTN5_HUMAN
Isoform
PDB entities 5
Chains and sequence ranges Author chain L; PDBConstruct 1–182; UniProt 1–182

Dynactin subunit 6

OrganismNot specified

UniProt O00399

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 × 25 PDB declaration: 25-meric(25) Consistent with protein copy count Chain M; UniProt 1–190 Not recorded Alpha-centractin × 8 (P61163) Actin, cytoplasmic 1 × 1 (P60709) Actin-related protein 10 × 1 (Q9NZ32) Dynactin subunit 4 × 1 (Q9UJW0) Dynactin subunit 5 × 1 (Q9BTE1) F-actin-capping protein subunit alpha-1 × 1 (P52907) F-actin-capping protein subunit beta × 1 (P47756) Dynactin subunit 2 × 4 (Q13561) Dynactin subunit 3 × 2 (O75935) Dynactin subunit 1 × 1 (Q14203) Dynactin subunit 1, p150-glued × 1 Dynactin subunit 2, p50 dynamitin × 1 Dynactin subunit 1 × 1 (Q14203) ADP ADENOSINE-5'-DIPHOSPHATE × 8 ANP PHOSPHOAMINOPHOSPHONIC ACID-ADENYLATE ESTER × 1 ZN ZINC ION × 3 ELECTRON MICROSCOPY cryo-EM buffer:pH 7.5 cryo-EM vitrification conditions:Cryogen ETHANE Resolution 3.49 Å

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.

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

View Construct and Data Evidence
UniProt name DCTN6_HUMAN
Isoform
PDB entities 6
Chains and sequence ranges Author chain M; PDBConstruct 1–190; UniProt 1–190

F-actin-capping protein subunit alpha-1

OrganismNot specified

UniProt P52907

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 × 25 PDB declaration: 25-meric(25) Consistent with protein copy count Chain N; UniProt 1–286 Not recorded Alpha-centractin × 8 (P61163) Actin, cytoplasmic 1 × 1 (P60709) Actin-related protein 10 × 1 (Q9NZ32) Dynactin subunit 4 × 1 (Q9UJW0) Dynactin subunit 5 × 1 (Q9BTE1) Dynactin subunit 6 × 1 (O00399) F-actin-capping protein subunit beta × 1 (P47756) Dynactin subunit 2 × 4 (Q13561) Dynactin subunit 3 × 2 (O75935) Dynactin subunit 1 × 1 (Q14203) Dynactin subunit 1, p150-glued × 1 Dynactin subunit 2, p50 dynamitin × 1 Dynactin subunit 1 × 1 (Q14203) ADP ADENOSINE-5'-DIPHOSPHATE × 8 ANP PHOSPHOAMINOPHOSPHONIC ACID-ADENYLATE ESTER × 1 ZN ZINC ION × 3 ELECTRON MICROSCOPY cryo-EM buffer:pH 7.5 cryo-EM vitrification conditions:Cryogen ETHANE Resolution 3.49 Å

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.

9 other PDB entries and 9 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name CAZA1_HUMAN
Isoform
PDB entities 7
Chains and sequence ranges Author chain N; PDBConstruct 1–286; UniProt 1–286

F-actin-capping protein subunit beta

OrganismNot specified

UniProt P47756

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 × 25 PDB declaration: 25-meric(25) Consistent with protein copy count Chain O; UniProt 1–272 Not recorded Alpha-centractin × 8 (P61163) Actin, cytoplasmic 1 × 1 (P60709) Actin-related protein 10 × 1 (Q9NZ32) Dynactin subunit 4 × 1 (Q9UJW0) Dynactin subunit 5 × 1 (Q9BTE1) Dynactin subunit 6 × 1 (O00399) F-actin-capping protein subunit alpha-1 × 1 (P52907) Dynactin subunit 2 × 4 (Q13561) Dynactin subunit 3 × 2 (O75935) Dynactin subunit 1 × 1 (Q14203) Dynactin subunit 1, p150-glued × 1 Dynactin subunit 2, p50 dynamitin × 1 Dynactin subunit 1 × 1 (Q14203) ADP ADENOSINE-5'-DIPHOSPHATE × 8 ANP PHOSPHOAMINOPHOSPHONIC ACID-ADENYLATE ESTER × 1 ZN ZINC ION × 3 ELECTRON MICROSCOPY cryo-EM buffer:pH 7.5 cryo-EM vitrification conditions:Cryogen ETHANE Resolution 3.49 Å

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.

7 other PDB entries and 7 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name CAPZB_HUMAN
Isoform
PDB entities 8
Chains and sequence ranges Author chain O; PDBConstruct 1–272; UniProt 1–272

Dynactin subunit 2

OrganismNot specified

UniProt Q13561

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 × 25 PDB declaration: 25-meric(25) Consistent with protein copy count Chain P; UniProt 1–401 Chain Q; UniProt 1–401 Chain p; UniProt 1–401 Chain q; UniProt 1–401 Not recorded Alpha-centractin × 8 (P61163) Actin, cytoplasmic 1 × 1 (P60709) Actin-related protein 10 × 1 (Q9NZ32) Dynactin subunit 4 × 1 (Q9UJW0) Dynactin subunit 5 × 1 (Q9BTE1) Dynactin subunit 6 × 1 (O00399) F-actin-capping protein subunit alpha-1 × 1 (P52907) F-actin-capping protein subunit beta × 1 (P47756) Dynactin subunit 3 × 2 (O75935) Dynactin subunit 1 × 1 (Q14203) Dynactin subunit 1, p150-glued × 1 Dynactin subunit 2, p50 dynamitin × 1 Dynactin subunit 1 × 1 (Q14203) ADP ADENOSINE-5'-DIPHOSPHATE × 8 ANP PHOSPHOAMINOPHOSPHONIC ACID-ADENYLATE ESTER × 1 ZN ZINC ION × 3 ELECTRON MICROSCOPY cryo-EM buffer:pH 7.5 cryo-EM vitrification conditions:Cryogen ETHANE Resolution 3.49 Å

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.

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

View Construct and Data Evidence
UniProt name DCTN2_HUMAN
Isoform
PDB entities 9
Chains and sequence ranges Author chain P; PDBConstruct 1–401; UniProt 1–401 Author chain Q; PDBConstruct 1–401; UniProt 1–401 Author chain p; PDBConstruct 1–401; UniProt 1–401 Author chain q; PDBConstruct 1–401; UniProt 1–401

Dynactin subunit 3

OrganismNot specified

UniProt O75935

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 × 25 PDB declaration: 25-meric(25) Consistent with protein copy count Chain R; UniProt 1–186 Chain r; UniProt 1–186 Not recorded Alpha-centractin × 8 (P61163) Actin, cytoplasmic 1 × 1 (P60709) Actin-related protein 10 × 1 (Q9NZ32) Dynactin subunit 4 × 1 (Q9UJW0) Dynactin subunit 5 × 1 (Q9BTE1) Dynactin subunit 6 × 1 (O00399) F-actin-capping protein subunit alpha-1 × 1 (P52907) F-actin-capping protein subunit beta × 1 (P47756) Dynactin subunit 2 × 4 (Q13561) Dynactin subunit 1 × 1 (Q14203) Dynactin subunit 1, p150-glued × 1 Dynactin subunit 2, p50 dynamitin × 1 Dynactin subunit 1 × 1 (Q14203) ADP ADENOSINE-5'-DIPHOSPHATE × 8 ANP PHOSPHOAMINOPHOSPHONIC ACID-ADENYLATE ESTER × 1 ZN ZINC ION × 3 ELECTRON MICROSCOPY cryo-EM buffer:pH 7.5 cryo-EM vitrification conditions:Cryogen ETHANE Resolution 3.49 Å

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.

No other PDB entry for the same UniProt protein was found.

View Construct and Data Evidence
UniProt name DCTN3_HUMAN
Isoform
PDB entities 10
Chains and sequence ranges Author chain R; PDBConstruct 1–186; UniProt 1–186 Author chain r; PDBConstruct 1–186; UniProt 1–186

Dynactin subunit 1

OrganismNot specified

UniProt Q14203

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 × 25 PDB declaration: 25-meric(25) Consistent with protein copy count Chain S; UniProt 1–1278 Chain s; UniProt 1–1278 Not recorded Alpha-centractin × 8 (P61163) Actin, cytoplasmic 1 × 1 (P60709) Actin-related protein 10 × 1 (Q9NZ32) Dynactin subunit 4 × 1 (Q9UJW0) Dynactin subunit 5 × 1 (Q9BTE1) Dynactin subunit 6 × 1 (O00399) F-actin-capping protein subunit alpha-1 × 1 (P52907) F-actin-capping protein subunit beta × 1 (P47756) Dynactin subunit 2 × 4 (Q13561) Dynactin subunit 3 × 2 (O75935) Dynactin subunit 1, p150-glued × 1 Dynactin subunit 2, p50 dynamitin × 1 ADP ADENOSINE-5'-DIPHOSPHATE × 8 ANP PHOSPHOAMINOPHOSPHONIC ACID-ADENYLATE ESTER × 1 ZN ZINC ION × 3 ELECTRON MICROSCOPY cryo-EM buffer:pH 7.5 cryo-EM vitrification conditions:Cryogen ETHANE Resolution 3.49 Å

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.

12 other PDB entries and 20 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name DCTN1_HUMAN
Isoform
PDB entities 11, 14
Chains and sequence ranges Author chain S; PDBConstruct 1–1278; UniProt 1–1278 Author chain s; PDBConstruct 1–1278; UniProt 1–1278

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 9b7j

P(r) Distance Distribution P(r) Distribution

P(r) distribution for 9b7j
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2. Structure Basics 2. Structure Basics

Entry ID entry_id9b7j
Deposition date deposition_date2024-03-27
最后修订 last_revision2025-04-16
Structure title titleCryo-EM structure of human dynactin complex bound to Chlamydia effector Dre1
Keywords keywordsHuman dynactin, Chlamydia effector, host-pathogen interaction, MOTOR PROTEIN; MOTOR PROTEIN
Experimental Method methodELECTRON MICROSCOPY

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

Radius of gyration Rg (Guinier) rg_guinier98.61
Radius of gyration Rg (electron density) rg_electron101.50
Forward intensity I(0) i08696400000.00
Molecular weight molecular_weight800560.0 kDa
Excluded volume excluded_volume1006200 ų
Envelope volume envelope_volume1770300 ų
Hydration-shell volume shell_volume167170 ų
Envelope diameter envelope_diameter389.1
Shell Rg shell_rg73.47
Envelope Rg envelope_rg100.80
Shape Rg shape_rg101.40
Total Rg total_rg101.40
Total atoms total_atoms113042
Residues n_residues7116
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 dmax276.4
Rg (real space) rg_real92.00
Rg uncertainty (real space) rg_real_error1.46
I(0) (real space) i0_real8.3100e+09
I(0) uncertainty (real space) i0_real_error1.7670e+08
Rg (reciprocal space) rg_reciprocal89.35
I(0) (reciprocal space) i0_reciprocal8441000000.0000
Solution quality estimate total_estimate0.9066
Solution quality rating solution_quality EXCELLENT a EXCELLENT solution
P(r) peaks n_peaks1
Primary peak position r_peak_primary69.1
Skewness Skewness skewness0.453
Kurtosis Kurtosis kurtosis-0.620
Angular range angular_range— – 0.0800 −1
Current regularization parameter α current_alpha0.7303
Highest regularization parameter α highest_alpha277700000.0000
Real-space data points n_real_points17
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.009; Oscil: 0.949; Stabil: 0.980; Sysdev: 1.000; Positv: 1.000; Valcen: 0.997; Smooth: 0.004

5. Crystallography and Experiment 5. Crystallography & Experiment

6. Entities and Polymers Entities & Polymers (17)

8. Citations (1)

9. Files and Curves (10)