6ip2

NSF-D1D2 part in the whole 20S complex

Method: ELECTRON MICROSCOPY Dmax: 143.9 Å Quality: GOOD

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

Vesicle-fusing ATPase

Cricetulus griseus

UniProt P18708

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 homooligomer Homooligomer Protein × 6 PDB declaration: hexameric(6) Consistent with protein copy count Chain A; UniProt 1–744 Chain B; UniProt 1–744 Chain C; UniProt 1–744 Chain D; UniProt 1–744 Chain E; UniProt 1–744 Chain F; UniProt 1–744 Not recorded ATP ADENOSINE-5'-TRIPHOSPHATE × 12 ELECTRON MICROSCOPY cryo-EM buffer:pH 7.4 cryo-EM vitrification conditions:Cryogen ETHANE Resolution 3.70 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.

41 other PDB entries and 42 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name NSF_CRIGR
Isoform
PDB entities 1
Chains and sequence ranges Author chain A; PDBConstruct 26–769; UniProt 1–744 Author chain B; PDBConstruct 26–769; UniProt 1–744 Author chain C; PDBConstruct 26–769; UniProt 1–744 Author chain D; PDBConstruct 26–769; UniProt 1–744 Author chain E; PDBConstruct 26–769; UniProt 1–744 Author chain F; PDBConstruct 26–769; UniProt 1–744

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 6ip2

P(r) Distance Distribution P(r) Distribution

P(r) distribution for 6ip2
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2. Structure Basics 2. Structure Basics

Entry ID entry_id6ip2
Deposition date deposition_date2018-11-01
Structure title titleNSF-D1D2 part in the whole 20S complex
Keywords keywordsmembrane fusion, ATPase, HYDROLASE; HYDROLASE
Experimental Method methodELECTRON MICROSCOPY

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

Radius of gyration Rg (Guinier) rg_guinier46.40
Radius of gyration Rg (electron density) rg_electron45.58
Forward intensity I(0) i01802430000.00
Molecular weight molecular_weight352530.0 kDa
Excluded volume excluded_volume441990 ų
Envelope volume envelope_volume615880 ų
Hydration-shell volume shell_volume105880 ų
Envelope diameter envelope_diameter148.3
Shell Rg shell_rg55.18
Envelope Rg envelope_rg44.85
Shape Rg shape_rg45.59
Total Rg total_rg45.86
Total atoms total_atoms24660
Residues n_residues3120
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 dmax143.9
Rg (real space) rg_real46.02
Rg uncertainty (real space) rg_real_error0.81
I(0) (real space) i0_real1.8020e+09
I(0) uncertainty (real space) i0_real_error2.9440e+07
Rg (reciprocal space) rg_reciprocal46.40
I(0) (reciprocal space) i0_reciprocal1803000000.0000
Solution quality estimate total_estimate0.8880
Solution quality rating solution_quality GOOD a GOOD solution
P(r) peaks n_peaks2
Primary peak position r_peak_primary59.2
Skewness Skewness skewness0.052
Kurtosis Kurtosis kurtosis-0.512
Angular range angular_range— – 0.1700 −1
Current regularization parameter α current_alpha0.0000
Highest regularization parameter α highest_alpha178200000.0000
Real-space data points n_real_points35
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.891; Stabil: 1.000; Sysdev: 1.000; Positv: 1.000; Valcen: 0.948; Smooth: 0.919

5. Crystallography and Experiment 5. Crystallography & Experiment

6. Entities and Polymers Entities & Polymers (2)

8. Citations (1)

9. Files and Curves (10)