3jc5

Structure of the eukaryotic replicative CMG helicase and pumpjack motion

Method: ELECTRON MICROSCOPY Dmax: 195.7 Å Quality: GOOD

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

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 × 11 PDB declaration: undecameric(11) Consistent with protein copy count Chain 2; UniProt 1–868 Not recorded DNA replication licensing factor MCM3 × 1 (P24279) DNA replication licensing factor MCM4 × 1 (P30665) Minichromosome maintenance protein 5 × 1 (P29496) DNA replication licensing factor MCM6 × 1 (P53091) DNA replication licensing factor MCM7 × 1 (P38132) Cell division control protein 45 × 1 (Q08032) DNA replication complex GINS protein SLD5 × 1 (Q03406) DNA replication complex GINS protein PSF2 × 1 (P40359) DNA replication complex GINS protein PSF1 × 1 (Q12488) DNA replication complex GINS protein PSF3 × 1 (Q12146) ELECTRON MICROSCOPY cryo-EM buffer:20 mM Tris acetate, pH 7.5, 40 mM potassium glutamate, 2 mM DTT, 0.1 mM EDTA;pH 7.5;20 mM Tris acetate, pH 7.5, 40 mM potassium glutamate, 2 mM DTT, 0.1 mM EDTA cryo-EM vitrification conditions:Blot for 3 seconds before plunging;Cryogen ETHANE;Blot for 3 seconds before plunging into liquid ethane (FEI VITROBOT MARK IV). Resolution 4.70 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 1
Chains and sequence ranges Author chain 2; 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 × 11 PDB declaration: undecameric(11) Consistent with protein copy count Chain 3; UniProt 1–971 Not recorded DNA replication licensing factor MCM2 × 1 (P29469) DNA replication licensing factor MCM4 × 1 (P30665) Minichromosome maintenance protein 5 × 1 (P29496) DNA replication licensing factor MCM6 × 1 (P53091) DNA replication licensing factor MCM7 × 1 (P38132) Cell division control protein 45 × 1 (Q08032) DNA replication complex GINS protein SLD5 × 1 (Q03406) DNA replication complex GINS protein PSF2 × 1 (P40359) DNA replication complex GINS protein PSF1 × 1 (Q12488) DNA replication complex GINS protein PSF3 × 1 (Q12146) ELECTRON MICROSCOPY cryo-EM buffer:20 mM Tris acetate, pH 7.5, 40 mM potassium glutamate, 2 mM DTT, 0.1 mM EDTA;pH 7.5;20 mM Tris acetate, pH 7.5, 40 mM potassium glutamate, 2 mM DTT, 0.1 mM EDTA cryo-EM vitrification conditions:Blot for 3 seconds before plunging;Cryogen ETHANE;Blot for 3 seconds before plunging into liquid ethane (FEI VITROBOT MARK IV). Resolution 4.70 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 2
Chains and sequence ranges Author chain 3; 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 × 11 PDB declaration: undecameric(11) Consistent with protein copy count Chain 4; UniProt 1–933 Not recorded DNA replication licensing factor MCM2 × 1 (P29469) DNA replication licensing factor MCM3 × 1 (P24279) Minichromosome maintenance protein 5 × 1 (P29496) DNA replication licensing factor MCM6 × 1 (P53091) DNA replication licensing factor MCM7 × 1 (P38132) Cell division control protein 45 × 1 (Q08032) DNA replication complex GINS protein SLD5 × 1 (Q03406) DNA replication complex GINS protein PSF2 × 1 (P40359) DNA replication complex GINS protein PSF1 × 1 (Q12488) DNA replication complex GINS protein PSF3 × 1 (Q12146) ELECTRON MICROSCOPY cryo-EM buffer:20 mM Tris acetate, pH 7.5, 40 mM potassium glutamate, 2 mM DTT, 0.1 mM EDTA;pH 7.5;20 mM Tris acetate, pH 7.5, 40 mM potassium glutamate, 2 mM DTT, 0.1 mM EDTA cryo-EM vitrification conditions:Blot for 3 seconds before plunging;Cryogen ETHANE;Blot for 3 seconds before plunging into liquid ethane (FEI VITROBOT MARK IV). Resolution 4.70 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 3
Chains and sequence ranges Author chain 4; 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 × 11 PDB declaration: undecameric(11) Consistent with protein copy count Chain 5; UniProt 1–775 Not recorded DNA replication licensing factor MCM2 × 1 (P29469) DNA replication licensing factor MCM3 × 1 (P24279) DNA replication licensing factor MCM4 × 1 (P30665) DNA replication licensing factor MCM6 × 1 (P53091) DNA replication licensing factor MCM7 × 1 (P38132) Cell division control protein 45 × 1 (Q08032) DNA replication complex GINS protein SLD5 × 1 (Q03406) DNA replication complex GINS protein PSF2 × 1 (P40359) DNA replication complex GINS protein PSF1 × 1 (Q12488) DNA replication complex GINS protein PSF3 × 1 (Q12146) ELECTRON MICROSCOPY cryo-EM buffer:20 mM Tris acetate, pH 7.5, 40 mM potassium glutamate, 2 mM DTT, 0.1 mM EDTA;pH 7.5;20 mM Tris acetate, pH 7.5, 40 mM potassium glutamate, 2 mM DTT, 0.1 mM EDTA cryo-EM vitrification conditions:Blot for 3 seconds before plunging;Cryogen ETHANE;Blot for 3 seconds before plunging into liquid ethane (FEI VITROBOT MARK IV). Resolution 4.70 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 4
Chains and sequence ranges Author chain 5; 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 × 11 PDB declaration: undecameric(11) Consistent with protein copy count Chain 6; UniProt 1–1017 Not recorded DNA replication licensing factor MCM2 × 1 (P29469) DNA replication licensing factor MCM3 × 1 (P24279) DNA replication licensing factor MCM4 × 1 (P30665) Minichromosome maintenance protein 5 × 1 (P29496) DNA replication licensing factor MCM7 × 1 (P38132) Cell division control protein 45 × 1 (Q08032) DNA replication complex GINS protein SLD5 × 1 (Q03406) DNA replication complex GINS protein PSF2 × 1 (P40359) DNA replication complex GINS protein PSF1 × 1 (Q12488) DNA replication complex GINS protein PSF3 × 1 (Q12146) ELECTRON MICROSCOPY cryo-EM buffer:20 mM Tris acetate, pH 7.5, 40 mM potassium glutamate, 2 mM DTT, 0.1 mM EDTA;pH 7.5;20 mM Tris acetate, pH 7.5, 40 mM potassium glutamate, 2 mM DTT, 0.1 mM EDTA cryo-EM vitrification conditions:Blot for 3 seconds before plunging;Cryogen ETHANE;Blot for 3 seconds before plunging into liquid ethane (FEI VITROBOT MARK IV). Resolution 4.70 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 5
Chains and sequence ranges Author chain 6; 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 × 11 PDB declaration: undecameric(11) Consistent with protein copy count Chain 7; UniProt 1–845 Not recorded DNA replication licensing factor MCM2 × 1 (P29469) DNA replication licensing factor MCM3 × 1 (P24279) DNA replication licensing factor MCM4 × 1 (P30665) Minichromosome maintenance protein 5 × 1 (P29496) DNA replication licensing factor MCM6 × 1 (P53091) Cell division control protein 45 × 1 (Q08032) DNA replication complex GINS protein SLD5 × 1 (Q03406) DNA replication complex GINS protein PSF2 × 1 (P40359) DNA replication complex GINS protein PSF1 × 1 (Q12488) DNA replication complex GINS protein PSF3 × 1 (Q12146) ELECTRON MICROSCOPY cryo-EM buffer:20 mM Tris acetate, pH 7.5, 40 mM potassium glutamate, 2 mM DTT, 0.1 mM EDTA;pH 7.5;20 mM Tris acetate, pH 7.5, 40 mM potassium glutamate, 2 mM DTT, 0.1 mM EDTA cryo-EM vitrification conditions:Blot for 3 seconds before plunging;Cryogen ETHANE;Blot for 3 seconds before plunging into liquid ethane (FEI VITROBOT MARK IV). Resolution 4.70 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 6
Chains and sequence ranges Author chain 7; PDBConstruct 1–845; UniProt 1–845

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 × 11 PDB declaration: undecameric(11) Consistent with protein copy count Chain c; UniProt 1–650 Not recorded DNA replication licensing factor MCM2 × 1 (P29469) DNA replication licensing factor MCM3 × 1 (P24279) DNA replication licensing factor MCM4 × 1 (P30665) Minichromosome maintenance protein 5 × 1 (P29496) DNA replication licensing factor MCM6 × 1 (P53091) DNA replication licensing factor MCM7 × 1 (P38132) DNA replication complex GINS protein SLD5 × 1 (Q03406) DNA replication complex GINS protein PSF2 × 1 (P40359) DNA replication complex GINS protein PSF1 × 1 (Q12488) DNA replication complex GINS protein PSF3 × 1 (Q12146) ELECTRON MICROSCOPY cryo-EM buffer:20 mM Tris acetate, pH 7.5, 40 mM potassium glutamate, 2 mM DTT, 0.1 mM EDTA;pH 7.5;20 mM Tris acetate, pH 7.5, 40 mM potassium glutamate, 2 mM DTT, 0.1 mM EDTA cryo-EM vitrification conditions:Blot for 3 seconds before plunging;Cryogen ETHANE;Blot for 3 seconds before plunging into liquid ethane (FEI VITROBOT MARK IV). Resolution 4.70 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 7
Chains and sequence ranges Author chain c; PDBConstruct 1–650; UniProt 1–650

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 × 11 PDB declaration: undecameric(11) Consistent with protein copy count Chain D; UniProt 1–294 Not recorded DNA replication licensing factor MCM2 × 1 (P29469) DNA replication licensing factor MCM3 × 1 (P24279) DNA replication licensing factor MCM4 × 1 (P30665) Minichromosome maintenance protein 5 × 1 (P29496) DNA replication licensing factor MCM6 × 1 (P53091) DNA replication licensing factor MCM7 × 1 (P38132) Cell division control protein 45 × 1 (Q08032) DNA replication complex GINS protein PSF2 × 1 (P40359) DNA replication complex GINS protein PSF1 × 1 (Q12488) DNA replication complex GINS protein PSF3 × 1 (Q12146) ELECTRON MICROSCOPY cryo-EM buffer:20 mM Tris acetate, pH 7.5, 40 mM potassium glutamate, 2 mM DTT, 0.1 mM EDTA;pH 7.5;20 mM Tris acetate, pH 7.5, 40 mM potassium glutamate, 2 mM DTT, 0.1 mM EDTA cryo-EM vitrification conditions:Blot for 3 seconds before plunging;Cryogen ETHANE;Blot for 3 seconds before plunging into liquid ethane (FEI VITROBOT MARK IV). Resolution 4.70 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 8
Chains and sequence ranges Author chain D; PDBConstruct 1–294; UniProt 1–294

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 × 11 PDB declaration: undecameric(11) Consistent with protein copy count Chain B; UniProt 1–213 Not recorded DNA replication licensing factor MCM2 × 1 (P29469) DNA replication licensing factor MCM3 × 1 (P24279) DNA replication licensing factor MCM4 × 1 (P30665) Minichromosome maintenance protein 5 × 1 (P29496) DNA replication licensing factor MCM6 × 1 (P53091) DNA replication licensing factor MCM7 × 1 (P38132) Cell division control protein 45 × 1 (Q08032) DNA replication complex GINS protein SLD5 × 1 (Q03406) DNA replication complex GINS protein PSF1 × 1 (Q12488) DNA replication complex GINS protein PSF3 × 1 (Q12146) ELECTRON MICROSCOPY cryo-EM buffer:20 mM Tris acetate, pH 7.5, 40 mM potassium glutamate, 2 mM DTT, 0.1 mM EDTA;pH 7.5;20 mM Tris acetate, pH 7.5, 40 mM potassium glutamate, 2 mM DTT, 0.1 mM EDTA cryo-EM vitrification conditions:Blot for 3 seconds before plunging;Cryogen ETHANE;Blot for 3 seconds before plunging into liquid ethane (FEI VITROBOT MARK IV). Resolution 4.70 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 9
Chains and sequence ranges Author chain B; PDBConstruct 1–213; UniProt 1–213

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 × 11 PDB declaration: undecameric(11) Consistent with protein copy count Chain A; UniProt 1–208 Not recorded DNA replication licensing factor MCM2 × 1 (P29469) DNA replication licensing factor MCM3 × 1 (P24279) DNA replication licensing factor MCM4 × 1 (P30665) Minichromosome maintenance protein 5 × 1 (P29496) DNA replication licensing factor MCM6 × 1 (P53091) DNA replication licensing factor MCM7 × 1 (P38132) Cell division control protein 45 × 1 (Q08032) DNA replication complex GINS protein SLD5 × 1 (Q03406) DNA replication complex GINS protein PSF2 × 1 (P40359) DNA replication complex GINS protein PSF3 × 1 (Q12146) ELECTRON MICROSCOPY cryo-EM buffer:20 mM Tris acetate, pH 7.5, 40 mM potassium glutamate, 2 mM DTT, 0.1 mM EDTA;pH 7.5;20 mM Tris acetate, pH 7.5, 40 mM potassium glutamate, 2 mM DTT, 0.1 mM EDTA cryo-EM vitrification conditions:Blot for 3 seconds before plunging;Cryogen ETHANE;Blot for 3 seconds before plunging into liquid ethane (FEI VITROBOT MARK IV). Resolution 4.70 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 10
Chains and sequence ranges Author chain A; PDBConstruct 1–208; UniProt 1–208

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 × 11 PDB declaration: undecameric(11) Consistent with protein copy count Chain C; UniProt 1–194 Not recorded DNA replication licensing factor MCM2 × 1 (P29469) DNA replication licensing factor MCM3 × 1 (P24279) DNA replication licensing factor MCM4 × 1 (P30665) Minichromosome maintenance protein 5 × 1 (P29496) DNA replication licensing factor MCM6 × 1 (P53091) DNA replication licensing factor MCM7 × 1 (P38132) Cell division control protein 45 × 1 (Q08032) DNA replication complex GINS protein SLD5 × 1 (Q03406) DNA replication complex GINS protein PSF2 × 1 (P40359) DNA replication complex GINS protein PSF1 × 1 (Q12488) ELECTRON MICROSCOPY cryo-EM buffer:20 mM Tris acetate, pH 7.5, 40 mM potassium glutamate, 2 mM DTT, 0.1 mM EDTA;pH 7.5;20 mM Tris acetate, pH 7.5, 40 mM potassium glutamate, 2 mM DTT, 0.1 mM EDTA cryo-EM vitrification conditions:Blot for 3 seconds before plunging;Cryogen ETHANE;Blot for 3 seconds before plunging into liquid ethane (FEI VITROBOT MARK IV). Resolution 4.70 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 11
Chains and sequence ranges Author chain C; PDBConstruct 1–194; UniProt 1–194

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 3jc5

P(r) Distance Distribution P(r) Distribution

P(r) distribution for 3jc5
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2. Structure Basics 2. Structure Basics

Entry ID entry_id3jc5
Deposition date deposition_date2015-11-24
Structure title titleStructure of the eukaryotic replicative CMG helicase and pumpjack motion
Keywords keywordsCMG helicase, Cryo-EM, HYDROLASE; HYDROLASE
Experimental Method methodELECTRON MICROSCOPY

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

Radius of gyration Rg (Guinier) rg_guinier58.50
Radius of gyration Rg (electron density) rg_electron58.11
Forward intensity I(0) i04479360000.00
Molecular weight molecular_weight569390.0 kDa
Excluded volume excluded_volume715800 ų
Envelope volume envelope_volume1094000 ų
Hydration-shell volume shell_volume151800 ų
Envelope diameter envelope_diameter210.2
Shell Rg shell_rg65.18
Envelope Rg envelope_rg56.33
Shape Rg shape_rg58.12
Total Rg total_rg58.25
Total atoms total_atoms40041
Residues n_residues5039
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 dmax195.7
Rg (real space) rg_real58.31
Rg uncertainty (real space) rg_real_error1.37
I(0) (real space) i0_real4.4790e+09
I(0) uncertainty (real space) i0_real_error9.1780e+07
Rg (reciprocal space) rg_reciprocal58.64
I(0) (reciprocal space) i0_reciprocal4482000000.0000
Solution quality estimate total_estimate0.8631
Solution quality rating solution_quality GOOD a GOOD solution
P(r) peaks n_peaks1
Primary peak position r_peak_primary72.5
Skewness Skewness skewness0.279
Kurtosis Kurtosis kurtosis-0.288
Angular range angular_range— – 0.1350 −1
Current regularization parameter α current_alpha0.0001
Highest regularization parameter α highest_alpha552800000.0000
Real-space data points n_real_points28
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.804; Stabil: 1.000; Sysdev: 1.000; Positv: 1.000; Valcen: 0.984; Smooth: 0.822

5. Crystallography and Experiment 5. Crystallography & Experiment

6. Entities and Polymers Entities & Polymers (11)

8. Citations (1)

9. Files and Curves (10)