8ory

Solution NMR structure of Notch1 L1740-1743 TMD

Method: SOLUTION NMR Dmax: 54.5 Å Quality: REASONABLE

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

Notch 1 extracellular truncation

OrganismNot specified

UniProt P46531

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 monomer Monomer Protein × 1 PDB declaration: monomeric(1) Consistent with protein copy count Chain A; UniProt 1734–1757 Mutation:A1740L, A1741L, A1742L, A1743L No other associated polymer SOLUTION NMR NMR measurement conditions:pH 6.5;300 K;Pressure 1 NMR sample composition:500 uM Notch1 L1740-1743 TMD, trifluoroethanol/water 80/20 | trifluoroethanol/water 80/20 Resolution not provided

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 35 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name NOTC1_HUMAN
Isoform
PDB entities 1
Chains and sequence ranges Author chain A; PDBConstruct 4–27; UniProt 1734–1757

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 8ory

P(r) Distance Distribution P(r) Distribution

P(r) distribution for 8ory
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2. Structure Basics 2. Structure Basics

Entry ID entry_id8ory
Deposition date deposition_date2023-04-17
Structure title titleSolution NMR structure of Notch1 L1740-1743 TMD
Keywords keywordsNotch1 L1740-1743, gamma secretase, transmembrane, MEMBRANE PROTEIN; MEMBRANE PROTEIN
Experimental Method methodSOLUTION NMR

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

Radius of gyration Rg (Guinier) rg_guinier14.01
Radius of gyration Rg (electron density) rg_electron14.66
Forward intensity I(0) i0144995000.00
Molecular weight molecular_weight141310.0 kDa
Excluded volume excluded_volume193440 ų
Envelope volume envelope_volume18713 ų
Hydration-shell volume shell_volume9368 ų
Envelope diameter envelope_diameter59.4
Shell Rg shell_rg22.59
Envelope Rg envelope_rg19.25
Shape Rg shape_rg14.51
Total Rg total_rg15.67
Total atoms total_atoms21680
Residues n_residues1200
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 dmax54.5
Rg (real space) rg_real14.53
Rg uncertainty (real space) rg_real_error0.76
I(0) (real space) i0_real1.4500e+08
I(0) uncertainty (real space) i0_real_error1.8960e+06
Rg (reciprocal space) rg_reciprocal14.49
I(0) (reciprocal space) i0_reciprocal145000000.0000
Solution quality estimate total_estimate0.6132
Solution quality rating solution_quality REASONABLE a REASONABLE solution
P(r) peaks n_peaks5
Primary peak position r_peak_primary5.5
Skewness Skewness skewness0.532
Kurtosis Kurtosis kurtosis-0.782
Angular range angular_range— – 0.5000 −1
Current regularization parameter α current_alpha0.0000
Highest regularization parameter α highest_alpha3654.0000
Real-space data points n_real_points80
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.000; Stabil: 0.991; Sysdev: 1.000; Positv: 1.000; Valcen: 0.001; Smooth: 0.993

5. Crystallography and Experiment 5. Crystallography & Experiment

6. Entities and Polymers Entities & Polymers (1)

8. Citations (1)

9. Files and Curves (10)