6ptn

Structure of Ctf4 trimer in complex with two CMG helicases

Method: ELECTRON MICROSCOPY Dmax: 264.1 Å Quality: EXCELLENT

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

DNA polymerase alpha-binding protein

Saccharomyces cerevisiae

UniProt Q01454

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 E; UniProt 1–927 Chain F; UniProt 1–927 Chain G; UniProt 1–927 Not recorded DNA replication complex GINS protein PSF1 × 2 (Q12488) DNA replication complex GINS protein PSF2 × 2 (P40359) DNA replication complex GINS protein PSF3 × 2 (Q12146) DNA replication complex GINS protein SLD5 × 2 (Q03406) Cell division control protein 45 × 2 (Q08032) DNA replication licensing factor MCM2 × 2 (P29469) DNA replication licensing factor MCM3 × 2 (P24279) DNA replication licensing factor MCM4 × 2 (P30665) Minichromosome maintenance protein 5 × 2 (P29496) DNA replication licensing factor MCM6 × 2 (P53091) DNA replication licensing factor MCM7 × 2 (P38132) ATP ADENOSINE-5'-TRIPHOSPHATE × 6 ELECTRON MICROSCOPY cryo-EM buffer:pH 7.5 cryo-EM vitrification conditions:Cryogen ETHANE Resolution 5.80 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.

19 other PDB entries and 19 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name CTF4_YEAST
Isoform
PDB entities 1
Chains and sequence ranges Author chain E; PDBConstruct 1–927; UniProt 1–927 Author chain F; PDBConstruct 1–927; UniProt 1–927 Author chain G; PDBConstruct 1–927; UniProt 1–927

DNA replication complex GINS protein PSF1

Saccharomyces cerevisiae

UniProt Q12488

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 1–208 Chain a; UniProt 1–208 Not recorded DNA polymerase alpha-binding protein × 3 (Q01454) DNA replication complex GINS protein PSF2 × 2 (P40359) DNA replication complex GINS protein PSF3 × 2 (Q12146) DNA replication complex GINS protein SLD5 × 2 (Q03406) Cell division control protein 45 × 2 (Q08032) DNA replication licensing factor MCM2 × 2 (P29469) DNA replication licensing factor MCM3 × 2 (P24279) DNA replication licensing factor MCM4 × 2 (P30665) Minichromosome maintenance protein 5 × 2 (P29496) DNA replication licensing factor MCM6 × 2 (P53091) DNA replication licensing factor MCM7 × 2 (P38132) ATP ADENOSINE-5'-TRIPHOSPHATE × 6 ELECTRON MICROSCOPY cryo-EM buffer:pH 7.5 cryo-EM vitrification conditions:Cryogen ETHANE Resolution 5.80 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.

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

View Construct and Data Evidence
UniProt name PSF1_YEAST
Isoform
PDB entities 2
Chains and sequence ranges Author chain A; PDBConstruct 1–208; UniProt 1–208 Author chain a; PDBConstruct 1–208; UniProt 1–208

DNA replication complex GINS protein PSF2

Saccharomyces cerevisiae

UniProt P40359

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 B; UniProt 1–213 Chain b; UniProt 1–213 Not recorded DNA polymerase alpha-binding protein × 3 (Q01454) DNA replication complex GINS protein PSF1 × 2 (Q12488) DNA replication complex GINS protein PSF3 × 2 (Q12146) DNA replication complex GINS protein SLD5 × 2 (Q03406) Cell division control protein 45 × 2 (Q08032) DNA replication licensing factor MCM2 × 2 (P29469) DNA replication licensing factor MCM3 × 2 (P24279) DNA replication licensing factor MCM4 × 2 (P30665) Minichromosome maintenance protein 5 × 2 (P29496) DNA replication licensing factor MCM6 × 2 (P53091) DNA replication licensing factor MCM7 × 2 (P38132) ATP ADENOSINE-5'-TRIPHOSPHATE × 6 ELECTRON MICROSCOPY cryo-EM buffer:pH 7.5 cryo-EM vitrification conditions:Cryogen ETHANE Resolution 5.80 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.

27 other PDB entries and 27 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name PSF2_YEAST
Isoform
PDB entities 3
Chains and sequence ranges Author chain B; PDBConstruct 1–213; UniProt 1–213 Author chain b; PDBConstruct 1–213; UniProt 1–213

DNA replication complex GINS protein PSF3

Saccharomyces cerevisiae

UniProt Q12146

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 C; UniProt 1–194 Chain c; UniProt 1–194 Not recorded DNA polymerase alpha-binding protein × 3 (Q01454) DNA replication complex GINS protein PSF1 × 2 (Q12488) DNA replication complex GINS protein PSF2 × 2 (P40359) DNA replication complex GINS protein SLD5 × 2 (Q03406) Cell division control protein 45 × 2 (Q08032) DNA replication licensing factor MCM2 × 2 (P29469) DNA replication licensing factor MCM3 × 2 (P24279) DNA replication licensing factor MCM4 × 2 (P30665) Minichromosome maintenance protein 5 × 2 (P29496) DNA replication licensing factor MCM6 × 2 (P53091) DNA replication licensing factor MCM7 × 2 (P38132) ATP ADENOSINE-5'-TRIPHOSPHATE × 6 ELECTRON MICROSCOPY cryo-EM buffer:pH 7.5 cryo-EM vitrification conditions:Cryogen ETHANE Resolution 5.80 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.

29 other PDB entries and 29 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name PSF3_YEAST
Isoform
PDB entities 4
Chains and sequence ranges Author chain C; PDBConstruct 1–194; UniProt 1–194 Author chain c; PDBConstruct 1–194; UniProt 1–194

DNA replication complex GINS protein SLD5

Saccharomyces cerevisiae

UniProt Q03406

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 D; UniProt 1–294 Chain d; UniProt 1–294 Not recorded DNA polymerase alpha-binding protein × 3 (Q01454) DNA replication complex GINS protein PSF1 × 2 (Q12488) DNA replication complex GINS protein PSF2 × 2 (P40359) DNA replication complex GINS protein PSF3 × 2 (Q12146) Cell division control protein 45 × 2 (Q08032) DNA replication licensing factor MCM2 × 2 (P29469) DNA replication licensing factor MCM3 × 2 (P24279) DNA replication licensing factor MCM4 × 2 (P30665) Minichromosome maintenance protein 5 × 2 (P29496) DNA replication licensing factor MCM6 × 2 (P53091) DNA replication licensing factor MCM7 × 2 (P38132) ATP ADENOSINE-5'-TRIPHOSPHATE × 6 ELECTRON MICROSCOPY cryo-EM buffer:pH 7.5 cryo-EM vitrification conditions:Cryogen ETHANE Resolution 5.80 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.

33 other PDB entries and 33 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name SLD5_YEAST
Isoform
PDB entities 5
Chains and sequence ranges Author chain D; PDBConstruct 1–294; UniProt 1–294 Author chain d; PDBConstruct 1–294; UniProt 1–294

Cell division control protein 45

Saccharomyces cerevisiae

UniProt Q08032

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 1–650 Chain h; UniProt 1–650 Not recorded DNA polymerase alpha-binding protein × 3 (Q01454) DNA replication complex GINS protein PSF1 × 2 (Q12488) DNA replication complex GINS protein PSF2 × 2 (P40359) DNA replication complex GINS protein PSF3 × 2 (Q12146) DNA replication complex GINS protein SLD5 × 2 (Q03406) DNA replication licensing factor MCM2 × 2 (P29469) DNA replication licensing factor MCM3 × 2 (P24279) DNA replication licensing factor MCM4 × 2 (P30665) Minichromosome maintenance protein 5 × 2 (P29496) DNA replication licensing factor MCM6 × 2 (P53091) DNA replication licensing factor MCM7 × 2 (P38132) ATP ADENOSINE-5'-TRIPHOSPHATE × 6 ELECTRON MICROSCOPY cryo-EM buffer:pH 7.5 cryo-EM vitrification conditions:Cryogen ETHANE Resolution 5.80 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.

34 other PDB entries and 34 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name CDC45_YEAST
Isoform
PDB entities 6
Chains and sequence ranges Author chain H; PDBConstruct 1–650; UniProt 1–650 Author chain h; PDBConstruct 1–650; UniProt 1–650

DNA replication licensing factor MCM2

Saccharomyces cerevisiae

UniProt P29469

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 2; UniProt 1–868 Chain i; UniProt 1–868 Not recorded DNA polymerase alpha-binding protein × 3 (Q01454) DNA replication complex GINS protein PSF1 × 2 (Q12488) DNA replication complex GINS protein PSF2 × 2 (P40359) DNA replication complex GINS protein PSF3 × 2 (Q12146) DNA replication complex GINS protein SLD5 × 2 (Q03406) Cell division control protein 45 × 2 (Q08032) DNA replication licensing factor MCM3 × 2 (P24279) DNA replication licensing factor MCM4 × 2 (P30665) Minichromosome maintenance protein 5 × 2 (P29496) DNA replication licensing factor MCM6 × 2 (P53091) DNA replication licensing factor MCM7 × 2 (P38132) ATP ADENOSINE-5'-TRIPHOSPHATE × 6 ELECTRON MICROSCOPY cryo-EM buffer:pH 7.5 cryo-EM vitrification conditions:Cryogen ETHANE Resolution 5.80 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.

51 other PDB entries and 51 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name MCM2_YEAST
Isoform
PDB entities 7
Chains and sequence ranges Author chain 2; PDBConstruct 1–868; UniProt 1–868 Author chain i; PDBConstruct 1–868; UniProt 1–868

DNA replication licensing factor MCM3

Saccharomyces cerevisiae

UniProt P24279

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 3; UniProt 1–971 Chain j; UniProt 1–971 Not recorded DNA polymerase alpha-binding protein × 3 (Q01454) DNA replication complex GINS protein PSF1 × 2 (Q12488) DNA replication complex GINS protein PSF2 × 2 (P40359) DNA replication complex GINS protein PSF3 × 2 (Q12146) DNA replication complex GINS protein SLD5 × 2 (Q03406) Cell division control protein 45 × 2 (Q08032) DNA replication licensing factor MCM2 × 2 (P29469) DNA replication licensing factor MCM4 × 2 (P30665) Minichromosome maintenance protein 5 × 2 (P29496) DNA replication licensing factor MCM6 × 2 (P53091) DNA replication licensing factor MCM7 × 2 (P38132) ATP ADENOSINE-5'-TRIPHOSPHATE × 6 ELECTRON MICROSCOPY cryo-EM buffer:pH 7.5 cryo-EM vitrification conditions:Cryogen ETHANE Resolution 5.80 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.

59 other PDB entries and 59 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name MCM3_YEAST
Isoform
PDB entities 8
Chains and sequence ranges Author chain 3; PDBConstruct 1–971; UniProt 1–971 Author chain j; PDBConstruct 1–971; UniProt 1–971

DNA replication licensing factor MCM4

Saccharomyces cerevisiae

UniProt P30665

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 4; UniProt 1–933 Chain k; UniProt 1–933 Not recorded DNA polymerase alpha-binding protein × 3 (Q01454) DNA replication complex GINS protein PSF1 × 2 (Q12488) DNA replication complex GINS protein PSF2 × 2 (P40359) DNA replication complex GINS protein PSF3 × 2 (Q12146) DNA replication complex GINS protein SLD5 × 2 (Q03406) Cell division control protein 45 × 2 (Q08032) DNA replication licensing factor MCM2 × 2 (P29469) DNA replication licensing factor MCM3 × 2 (P24279) Minichromosome maintenance protein 5 × 2 (P29496) DNA replication licensing factor MCM6 × 2 (P53091) DNA replication licensing factor MCM7 × 2 (P38132) ATP ADENOSINE-5'-TRIPHOSPHATE × 6 ELECTRON MICROSCOPY cryo-EM buffer:pH 7.5 cryo-EM vitrification conditions:Cryogen ETHANE Resolution 5.80 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.

58 other PDB entries and 58 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name MCM4_YEAST
Isoform
PDB entities 9
Chains and sequence ranges Author chain 4; PDBConstruct 1–933; UniProt 1–933 Author chain k; PDBConstruct 1–933; UniProt 1–933

Minichromosome maintenance protein 5

Saccharomyces cerevisiae

UniProt P29496

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 5; UniProt 1–775 Chain l; UniProt 1–775 Not recorded DNA polymerase alpha-binding protein × 3 (Q01454) DNA replication complex GINS protein PSF1 × 2 (Q12488) DNA replication complex GINS protein PSF2 × 2 (P40359) DNA replication complex GINS protein PSF3 × 2 (Q12146) DNA replication complex GINS protein SLD5 × 2 (Q03406) Cell division control protein 45 × 2 (Q08032) DNA replication licensing factor MCM2 × 2 (P29469) DNA replication licensing factor MCM3 × 2 (P24279) DNA replication licensing factor MCM4 × 2 (P30665) DNA replication licensing factor MCM6 × 2 (P53091) DNA replication licensing factor MCM7 × 2 (P38132) ATP ADENOSINE-5'-TRIPHOSPHATE × 6 ELECTRON MICROSCOPY cryo-EM buffer:pH 7.5 cryo-EM vitrification conditions:Cryogen ETHANE Resolution 5.80 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.

54 other PDB entries and 54 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name MCM5_YEAST
Isoform
PDB entities 10
Chains and sequence ranges Author chain 5; PDBConstruct 1–775; UniProt 1–775 Author chain l; PDBConstruct 1–775; UniProt 1–775

DNA replication licensing factor MCM6

Saccharomyces cerevisiae

UniProt P53091

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 6; UniProt 1–1017 Chain m; UniProt 1–1017 Not recorded DNA polymerase alpha-binding protein × 3 (Q01454) DNA replication complex GINS protein PSF1 × 2 (Q12488) DNA replication complex GINS protein PSF2 × 2 (P40359) DNA replication complex GINS protein PSF3 × 2 (Q12146) DNA replication complex GINS protein SLD5 × 2 (Q03406) Cell division control protein 45 × 2 (Q08032) DNA replication licensing factor MCM2 × 2 (P29469) DNA replication licensing factor MCM3 × 2 (P24279) DNA replication licensing factor MCM4 × 2 (P30665) Minichromosome maintenance protein 5 × 2 (P29496) DNA replication licensing factor MCM7 × 2 (P38132) ATP ADENOSINE-5'-TRIPHOSPHATE × 6 ELECTRON MICROSCOPY cryo-EM buffer:pH 7.5 cryo-EM vitrification conditions:Cryogen ETHANE Resolution 5.80 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.

58 other PDB entries and 58 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name MCM6_YEAST
Isoform
PDB entities 11
Chains and sequence ranges Author chain 6; PDBConstruct 1–1017; UniProt 1–1017 Author chain m; PDBConstruct 1–1017; UniProt 1–1017

DNA replication licensing factor MCM7

Saccharomyces cerevisiae

UniProt P38132

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 7; UniProt 1–845 Chain n; UniProt 1–845 Not recorded DNA polymerase alpha-binding protein × 3 (Q01454) DNA replication complex GINS protein PSF1 × 2 (Q12488) DNA replication complex GINS protein PSF2 × 2 (P40359) DNA replication complex GINS protein PSF3 × 2 (Q12146) DNA replication complex GINS protein SLD5 × 2 (Q03406) Cell division control protein 45 × 2 (Q08032) DNA replication licensing factor MCM2 × 2 (P29469) DNA replication licensing factor MCM3 × 2 (P24279) DNA replication licensing factor MCM4 × 2 (P30665) Minichromosome maintenance protein 5 × 2 (P29496) DNA replication licensing factor MCM6 × 2 (P53091) ATP ADENOSINE-5'-TRIPHOSPHATE × 6 ELECTRON MICROSCOPY cryo-EM buffer:pH 7.5 cryo-EM vitrification conditions:Cryogen ETHANE Resolution 5.80 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.

55 other PDB entries and 55 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name MCM7_YEAST
Isoform
PDB entities 12
Chains and sequence ranges Author chain 7; PDBConstruct 1–845; UniProt 1–845 Author chain n; PDBConstruct 1–845; UniProt 1–845

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 6ptn

P(r) Distance Distribution P(r) Distribution

P(r) distribution for 6ptn
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2. Structure Basics 2. Structure Basics

Entry ID entry_id6ptn
Deposition date deposition_date2019-07-16
Structure title titleStructure of Ctf4 trimer in complex with two CMG helicases
Keywords keywordsDNA replication, Cryo-EM, CMG-Ctf4, REPLICATION; REPLICATION
Experimental Method methodELECTRON MICROSCOPY

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

Radius of gyration Rg (Guinier) rg_guinier
Radius of gyration Rg (electron density) rg_electron102.50
Forward intensity I(0) i022858000000.00
Molecular weight molecular_weight1302800.0 kDa
Excluded volume excluded_volume1635600 ų
Envelope volume envelope_volume3072700 ų
Hydration-shell volume shell_volume241600 ų
Envelope diameter envelope_diameter318.3
Shell Rg shell_rg110.30
Envelope Rg envelope_rg97.26
Shape Rg shape_rg102.40
Total Rg total_rg102.70
Total atoms total_atoms91606
Residues n_residues11517
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 dmax264.1
Rg (real space) rg_real98.90
Rg uncertainty (real space) rg_real_error0.97
I(0) (real space) i0_real2.1930e+10
I(0) uncertainty (real space) i0_real_error5.2130e+08
Rg (reciprocal space) rg_reciprocal98.92
I(0) (reciprocal space) i0_reciprocal22570000000.0000
Solution quality estimate total_estimate0.9120
Solution quality rating solution_quality EXCELLENT a EXCELLENT solution
P(r) peaks n_peaks2
Primary peak position r_peak_primary70.4
Skewness Skewness skewness0.172
Kurtosis Kurtosis kurtosis-0.987
Angular range angular_range— – 0.0750 −1
Current regularization parameter α current_alpha0.9067
Highest regularization parameter α highest_alpha3059000000.0000
Real-space data points n_real_points16
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.986; Stabil: 0.967; Sysdev: 1.000; Positv: 1.000; Valcen: 0.998; Smooth: 0.000

5. Crystallography and Experiment 5. Crystallography & Experiment

6. Entities and Polymers Entities & Polymers (13)

8. Citations (1)

9. Files and Curves (10)