3j9v

Yeast V-ATPase state 3

Method: ELECTRON MICROSCOPY Dmax: 254.4 Å Quality: GOOD

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

V-type proton ATPase subunit a, vacuolar isoform

OrganismNot specified

UniProt P32563

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 × 28 PDB declaration: 28-meric(28) Consistent with protein copy count Chain b; UniProt 1–840 Not recorded V-type proton ATPase subunit C × 1 (P31412) V-type proton ATPase subunit D × 1 (P32610) V-type proton ATPase subunit F × 1 (P39111) V-type proton ATPase catalytic subunit A × 3 (P17255) V-type proton ATPase subunit B × 3 (P16140) V-type proton ATPase subunit d × 1 (P32366) V-type proton ATPase subunit G × 3 (P48836) V-type proton ATPase subunit E × 3 (P22203) V-type proton ATPase subunit H × 1 (P41807) V-type proton ATPase subunit c × 10 (P25515) ELECTRON MICROSCOPY cryo-EM buffer:50 mM Tris-HCl, 150 mM NaCl, 0.02% w/v dodecylmaltoside;pH 7.4;50 mM Tris-HCl, 150 mM NaCl, 0.02% w/v dodecylmaltoside cryo-EM vitrification conditions:Blot for 23 seconds before freezing;77 K;Cryogen OTHER;Blot for 23 seconds before freezing in ethane/propane mixture (FEI VITROBOT MARK III). Resolution 8.30 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.

31 other PDB entries and 31 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name VPH1_YEAST
Isoform
PDB entities 1
Chains and sequence ranges Author chain b; PDBConstruct 1–840; UniProt 1–840

V-type proton ATPase subunit C

OrganismNot specified

UniProt P31412

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 × 28 PDB declaration: 28-meric(28) Consistent with protein copy count Chain O; UniProt 1–392 Not recorded V-type proton ATPase subunit a, vacuolar isoform × 1 (P32563) V-type proton ATPase subunit D × 1 (P32610) V-type proton ATPase subunit F × 1 (P39111) V-type proton ATPase catalytic subunit A × 3 (P17255) V-type proton ATPase subunit B × 3 (P16140) V-type proton ATPase subunit d × 1 (P32366) V-type proton ATPase subunit G × 3 (P48836) V-type proton ATPase subunit E × 3 (P22203) V-type proton ATPase subunit H × 1 (P41807) V-type proton ATPase subunit c × 10 (P25515) ELECTRON MICROSCOPY cryo-EM buffer:50 mM Tris-HCl, 150 mM NaCl, 0.02% w/v dodecylmaltoside;pH 7.4;50 mM Tris-HCl, 150 mM NaCl, 0.02% w/v dodecylmaltoside cryo-EM vitrification conditions:Blot for 23 seconds before freezing;77 K;Cryogen OTHER;Blot for 23 seconds before freezing in ethane/propane mixture (FEI VITROBOT MARK III). Resolution 8.30 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.

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

View Construct and Data Evidence
UniProt name VATC_YEAST
Isoform
PDB entities 2
Chains and sequence ranges Author chain O; PDBConstruct 1–392; UniProt 1–392

V-type proton ATPase subunit D

OrganismNot specified

UniProt P32610

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 × 28 PDB declaration: 28-meric(28) Consistent with protein copy count Chain M; UniProt 1–256 Not recorded V-type proton ATPase subunit a, vacuolar isoform × 1 (P32563) V-type proton ATPase subunit C × 1 (P31412) V-type proton ATPase subunit F × 1 (P39111) V-type proton ATPase catalytic subunit A × 3 (P17255) V-type proton ATPase subunit B × 3 (P16140) V-type proton ATPase subunit d × 1 (P32366) V-type proton ATPase subunit G × 3 (P48836) V-type proton ATPase subunit E × 3 (P22203) V-type proton ATPase subunit H × 1 (P41807) V-type proton ATPase subunit c × 10 (P25515) ELECTRON MICROSCOPY cryo-EM buffer:50 mM Tris-HCl, 150 mM NaCl, 0.02% w/v dodecylmaltoside;pH 7.4;50 mM Tris-HCl, 150 mM NaCl, 0.02% w/v dodecylmaltoside cryo-EM vitrification conditions:Blot for 23 seconds before freezing;77 K;Cryogen OTHER;Blot for 23 seconds before freezing in ethane/propane mixture (FEI VITROBOT MARK III). Resolution 8.30 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 21 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name VATD_YEAST
Isoform
PDB entities 3
Chains and sequence ranges Author chain M; PDBConstruct 1–256; UniProt 1–256

V-type proton ATPase subunit F

OrganismNot specified

UniProt P39111

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 × 28 PDB declaration: 28-meric(28) Consistent with protein copy count Chain N; UniProt 1–118 Not recorded V-type proton ATPase subunit a, vacuolar isoform × 1 (P32563) V-type proton ATPase subunit C × 1 (P31412) V-type proton ATPase subunit D × 1 (P32610) V-type proton ATPase catalytic subunit A × 3 (P17255) V-type proton ATPase subunit B × 3 (P16140) V-type proton ATPase subunit d × 1 (P32366) V-type proton ATPase subunit G × 3 (P48836) V-type proton ATPase subunit E × 3 (P22203) V-type proton ATPase subunit H × 1 (P41807) V-type proton ATPase subunit c × 10 (P25515) ELECTRON MICROSCOPY cryo-EM buffer:50 mM Tris-HCl, 150 mM NaCl, 0.02% w/v dodecylmaltoside;pH 7.4;50 mM Tris-HCl, 150 mM NaCl, 0.02% w/v dodecylmaltoside cryo-EM vitrification conditions:Blot for 23 seconds before freezing;77 K;Cryogen OTHER;Blot for 23 seconds before freezing in ethane/propane mixture (FEI VITROBOT MARK III). Resolution 8.30 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 23 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name VATF_YEAST
Isoform
PDB entities 4
Chains and sequence ranges Author chain N; PDBConstruct 1–118; UniProt 1–118

V-type proton ATPase catalytic subunit A

OrganismNot specified

UniProt P17255

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 × 28 PDB declaration: 28-meric(28) Consistent with protein copy count Chain A; UniProt 2–283 Chain A; UniProt 738–1071 Chain C; UniProt 2–283 Chain C; UniProt 738–1071 Chain E; UniProt 2–283 Chain E; UniProt 738–1071 Fragment:SEE REMARK 999 V-type proton ATPase subunit a, vacuolar isoform × 1 (P32563) V-type proton ATPase subunit C × 1 (P31412) V-type proton ATPase subunit D × 1 (P32610) V-type proton ATPase subunit F × 1 (P39111) V-type proton ATPase subunit B × 3 (P16140) V-type proton ATPase subunit d × 1 (P32366) V-type proton ATPase subunit G × 3 (P48836) V-type proton ATPase subunit E × 3 (P22203) V-type proton ATPase subunit H × 1 (P41807) V-type proton ATPase subunit c × 10 (P25515) ELECTRON MICROSCOPY cryo-EM buffer:50 mM Tris-HCl, 150 mM NaCl, 0.02% w/v dodecylmaltoside;pH 7.4;50 mM Tris-HCl, 150 mM NaCl, 0.02% w/v dodecylmaltoside cryo-EM vitrification conditions:Blot for 23 seconds before freezing;77 K;Cryogen OTHER;Blot for 23 seconds before freezing in ethane/propane mixture (FEI VITROBOT MARK III). Resolution 8.30 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.

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

View Construct and Data Evidence
UniProt name VATA_YEAST
Isoform
PDB entities 5
Chains and sequence ranges Author chain A; PDBConstruct 1–282; UniProt 2–283 Author chain A; PDBConstruct 283–616; UniProt 738–1071 Author chain C; PDBConstruct 1–282; UniProt 2–283 Author chain C; PDBConstruct 283–616; UniProt 738–1071 Author chain E; PDBConstruct 1–282; UniProt 2–283 Author chain E; PDBConstruct 283–616; UniProt 738–1071

V-type proton ATPase subunit B

OrganismNot specified

UniProt P16140

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 × 28 PDB declaration: 28-meric(28) Consistent with protein copy count Chain B; UniProt 1–517 Chain D; UniProt 1–517 Chain F; UniProt 1–517 Not recorded V-type proton ATPase subunit a, vacuolar isoform × 1 (P32563) V-type proton ATPase subunit C × 1 (P31412) V-type proton ATPase subunit D × 1 (P32610) V-type proton ATPase subunit F × 1 (P39111) V-type proton ATPase catalytic subunit A × 3 (P17255) V-type proton ATPase subunit d × 1 (P32366) V-type proton ATPase subunit G × 3 (P48836) V-type proton ATPase subunit E × 3 (P22203) V-type proton ATPase subunit H × 1 (P41807) V-type proton ATPase subunit c × 10 (P25515) ELECTRON MICROSCOPY cryo-EM buffer:50 mM Tris-HCl, 150 mM NaCl, 0.02% w/v dodecylmaltoside;pH 7.4;50 mM Tris-HCl, 150 mM NaCl, 0.02% w/v dodecylmaltoside cryo-EM vitrification conditions:Blot for 23 seconds before freezing;77 K;Cryogen OTHER;Blot for 23 seconds before freezing in ethane/propane mixture (FEI VITROBOT MARK III). Resolution 8.30 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.

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

View Construct and Data Evidence
UniProt name VATB_YEAST
Isoform
PDB entities 6
Chains and sequence ranges Author chain B; PDBConstruct 1–517; UniProt 1–517 Author chain D; PDBConstruct 1–517; UniProt 1–517 Author chain F; PDBConstruct 1–517; UniProt 1–517

V-type proton ATPase subunit d

OrganismNot specified

UniProt P32366

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 × 28 PDB declaration: 28-meric(28) Consistent with protein copy count Chain Q; UniProt 1–345 Not recorded V-type proton ATPase subunit a, vacuolar isoform × 1 (P32563) V-type proton ATPase subunit C × 1 (P31412) V-type proton ATPase subunit D × 1 (P32610) V-type proton ATPase subunit F × 1 (P39111) V-type proton ATPase catalytic subunit A × 3 (P17255) V-type proton ATPase subunit B × 3 (P16140) V-type proton ATPase subunit G × 3 (P48836) V-type proton ATPase subunit E × 3 (P22203) V-type proton ATPase subunit H × 1 (P41807) V-type proton ATPase subunit c × 10 (P25515) ELECTRON MICROSCOPY cryo-EM buffer:50 mM Tris-HCl, 150 mM NaCl, 0.02% w/v dodecylmaltoside;pH 7.4;50 mM Tris-HCl, 150 mM NaCl, 0.02% w/v dodecylmaltoside cryo-EM vitrification conditions:Blot for 23 seconds before freezing;77 K;Cryogen OTHER;Blot for 23 seconds before freezing in ethane/propane mixture (FEI VITROBOT MARK III). Resolution 8.30 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.

32 other PDB entries and 32 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name VA0D_YEAST
Isoform
PDB entities 7
Chains and sequence ranges Author chain Q; PDBConstruct 1–345; UniProt 1–345

V-type proton ATPase subunit G

OrganismNot specified

UniProt P48836

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 × 28 PDB declaration: 28-meric(28) Consistent with protein copy count Chain H; UniProt 1–114 Chain J; UniProt 1–114 Chain L; UniProt 1–114 Not recorded V-type proton ATPase subunit a, vacuolar isoform × 1 (P32563) V-type proton ATPase subunit C × 1 (P31412) V-type proton ATPase subunit D × 1 (P32610) V-type proton ATPase subunit F × 1 (P39111) V-type proton ATPase catalytic subunit A × 3 (P17255) V-type proton ATPase subunit B × 3 (P16140) V-type proton ATPase subunit d × 1 (P32366) V-type proton ATPase subunit E × 3 (P22203) V-type proton ATPase subunit H × 1 (P41807) V-type proton ATPase subunit c × 10 (P25515) ELECTRON MICROSCOPY cryo-EM buffer:50 mM Tris-HCl, 150 mM NaCl, 0.02% w/v dodecylmaltoside;pH 7.4;50 mM Tris-HCl, 150 mM NaCl, 0.02% w/v dodecylmaltoside cryo-EM vitrification conditions:Blot for 23 seconds before freezing;77 K;Cryogen OTHER;Blot for 23 seconds before freezing in ethane/propane mixture (FEI VITROBOT MARK III). Resolution 8.30 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.

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

View Construct and Data Evidence
UniProt name VATG_YEAST
Isoform
PDB entities 8
Chains and sequence ranges Author chain H; PDBConstruct 1–114; UniProt 1–114 Author chain J; PDBConstruct 1–114; UniProt 1–114 Author chain L; PDBConstruct 1–114; UniProt 1–114

V-type proton ATPase subunit E

OrganismNot specified

UniProt P22203

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 × 28 PDB declaration: 28-meric(28) Consistent with protein copy count Chain G; UniProt 1–233 Chain I; UniProt 1–233 Chain K; UniProt 1–233 Not recorded V-type proton ATPase subunit a, vacuolar isoform × 1 (P32563) V-type proton ATPase subunit C × 1 (P31412) V-type proton ATPase subunit D × 1 (P32610) V-type proton ATPase subunit F × 1 (P39111) V-type proton ATPase catalytic subunit A × 3 (P17255) V-type proton ATPase subunit B × 3 (P16140) V-type proton ATPase subunit d × 1 (P32366) V-type proton ATPase subunit G × 3 (P48836) V-type proton ATPase subunit H × 1 (P41807) V-type proton ATPase subunit c × 10 (P25515) ELECTRON MICROSCOPY cryo-EM buffer:50 mM Tris-HCl, 150 mM NaCl, 0.02% w/v dodecylmaltoside;pH 7.4;50 mM Tris-HCl, 150 mM NaCl, 0.02% w/v dodecylmaltoside cryo-EM vitrification conditions:Blot for 23 seconds before freezing;77 K;Cryogen OTHER;Blot for 23 seconds before freezing in ethane/propane mixture (FEI VITROBOT MARK III). Resolution 8.30 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.

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

View Construct and Data Evidence
UniProt name VATE_YEAST
Isoform
PDB entities 9
Chains and sequence ranges Author chain G; PDBConstruct 1–233; UniProt 1–233 Author chain I; PDBConstruct 1–233; UniProt 1–233 Author chain K; PDBConstruct 1–233; UniProt 1–233

V-type proton ATPase subunit H

OrganismNot specified

UniProt P41807

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 × 28 PDB declaration: 28-meric(28) Consistent with protein copy count Chain P; UniProt 1–478 Not recorded V-type proton ATPase subunit a, vacuolar isoform × 1 (P32563) V-type proton ATPase subunit C × 1 (P31412) V-type proton ATPase subunit D × 1 (P32610) V-type proton ATPase subunit F × 1 (P39111) V-type proton ATPase catalytic subunit A × 3 (P17255) V-type proton ATPase subunit B × 3 (P16140) V-type proton ATPase subunit d × 1 (P32366) V-type proton ATPase subunit G × 3 (P48836) V-type proton ATPase subunit E × 3 (P22203) V-type proton ATPase subunit c × 10 (P25515) ELECTRON MICROSCOPY cryo-EM buffer:50 mM Tris-HCl, 150 mM NaCl, 0.02% w/v dodecylmaltoside;pH 7.4;50 mM Tris-HCl, 150 mM NaCl, 0.02% w/v dodecylmaltoside cryo-EM vitrification conditions:Blot for 23 seconds before freezing;77 K;Cryogen OTHER;Blot for 23 seconds before freezing in ethane/propane mixture (FEI VITROBOT MARK III). Resolution 8.30 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.

24 other PDB entries and 26 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name VATH_YEAST
Isoform
PDB entities 10
Chains and sequence ranges Author chain P; PDBConstruct 1–478; UniProt 1–478

V-type proton ATPase subunit c

OrganismNot specified

UniProt P25515

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 × 28 PDB declaration: 28-meric(28) Consistent with protein copy count Chain R; UniProt 1–160 Chain S; UniProt 1–160 Chain T; UniProt 1–160 Chain U; UniProt 1–160 Chain V; UniProt 1–160 Chain W; UniProt 1–160 Chain X; UniProt 1–160 Chain Y; UniProt 1–160 Chain Z; UniProt 1–160 Chain a; UniProt 1–160 Not recorded V-type proton ATPase subunit a, vacuolar isoform × 1 (P32563) V-type proton ATPase subunit C × 1 (P31412) V-type proton ATPase subunit D × 1 (P32610) V-type proton ATPase subunit F × 1 (P39111) V-type proton ATPase catalytic subunit A × 3 (P17255) V-type proton ATPase subunit B × 3 (P16140) V-type proton ATPase subunit d × 1 (P32366) V-type proton ATPase subunit G × 3 (P48836) V-type proton ATPase subunit E × 3 (P22203) V-type proton ATPase subunit H × 1 (P41807) ELECTRON MICROSCOPY cryo-EM buffer:50 mM Tris-HCl, 150 mM NaCl, 0.02% w/v dodecylmaltoside;pH 7.4;50 mM Tris-HCl, 150 mM NaCl, 0.02% w/v dodecylmaltoside cryo-EM vitrification conditions:Blot for 23 seconds before freezing;77 K;Cryogen OTHER;Blot for 23 seconds before freezing in ethane/propane mixture (FEI VITROBOT MARK III). Resolution 8.30 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.

32 other PDB entries and 32 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name VATL1_YEAST
Isoform
PDB entities 11
Chains and sequence ranges Author chain R; PDBConstruct 1–160; UniProt 1–160 Author chain S; PDBConstruct 1–160; UniProt 1–160 Author chain T; PDBConstruct 1–160; UniProt 1–160 Author chain U; PDBConstruct 1–160; UniProt 1–160 Author chain V; PDBConstruct 1–160; UniProt 1–160 Author chain W; PDBConstruct 1–160; UniProt 1–160 Author chain X; PDBConstruct 1–160; UniProt 1–160 Author chain Y; PDBConstruct 1–160; UniProt 1–160 Author chain Z; PDBConstruct 1–160; UniProt 1–160 Author chain a; PDBConstruct 1–160; UniProt 1–160

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 3j9v

P(r) Distance Distribution P(r) Distribution

P(r) distribution for 3j9v
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2. Structure Basics 2. Structure Basics

Entry ID entry_id3j9v
Deposition date deposition_date2015-02-23
Structure title titleYeast V-ATPase state 3
Keywords keywordsV-ATPase, V-type ATPase, vacuolar-type ATPase, proton pump, HYDROLASE; HYDROLASE
Experimental Method methodELECTRON MICROSCOPY

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

Radius of gyration Rg (Guinier) rg_guinier74.22
Radius of gyration Rg (electron density) rg_electron75.13
Forward intensity I(0) i08742570000.00
Molecular weight molecular_weight819230.0 kDa
Excluded volume excluded_volume1036300 ų
Envelope volume envelope_volume1560000 ų
Hydration-shell volume shell_volume174620 ų
Envelope diameter envelope_diameter252.4
Shell Rg shell_rg74.71
Envelope Rg envelope_rg72.29
Shape Rg shape_rg75.09
Total Rg total_rg75.28
Total atoms total_atoms57659
Residues n_residues7451
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 dmax254.4
Rg (real space) rg_real74.70
Rg uncertainty (real space) rg_real_error1.95
I(0) (real space) i0_real8.7480e+09
I(0) uncertainty (real space) i0_real_error1.9560e+08
Rg (reciprocal space) rg_reciprocal73.47
I(0) (reciprocal space) i0_reciprocal8726000000.0000
Solution quality estimate total_estimate0.8273
Solution quality rating solution_quality GOOD a GOOD solution
P(r) peaks n_peaks1
Primary peak position r_peak_primary72.7
Skewness Skewness skewness0.439
Kurtosis Kurtosis kurtosis-0.363
Angular range angular_range— – 0.1050 −1
Current regularization parameter α current_alpha0.0839
Highest regularization parameter α highest_alpha1914000000.0000
Real-space data points n_real_points22
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.820; Stabil: 0.998; Sysdev: 1.000; Positv: 1.000; Valcen: 0.988; Smooth: 0.301

5. Crystallography and Experiment 5. Crystallography & Experiment

6. Entities and Polymers Entities & Polymers (11)

8. Citations (1)

9. Files and Curves (10)