1pb5

NMR Structure of a Prototype LNR Module from Human Notch1

Method: SOLUTION NMR Dmax: 29.1 Å Quality: GOOD

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

Neurogenic locus notch homolog protein 1

Homo sapiens

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 1447–1481 Fragment:First LNR module CA CALCIUM ION × 1 SOLUTION NMR NMR measurement conditions:pH 6.5;298 K;Ionic strength (raw mmCIF value) 10mM Ca2+;Pressure ambient NMR measurement conditions:pH 7;283 K;Ionic strength (raw mmCIF value) 10mM Ca2+, 50mM PIPES;Pressure ambient NMR sample composition:1mM LNRA U-15N, 10mM Ca2+, 0.5mM DSS pH 6.5 | 90% H2O/10% D2O NMR sample composition:1mM LNRA U-15N,13C, 10mM Ca2+, 0.5mM DSS pH 6.5 | 90% H2O/10% D2O NMR sample composition:1.5mM LNRA U-15N,13C, 10 mM Ca2+, 0.5mM DSS, 50 mM deuterated PIPES pH 7.0 | 90% H2O/10% D2O 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 1–35; UniProt 1447–1481

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 1pb5

P(r) Distance Distribution P(r) Distribution

P(r) distribution for 1pb5
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2. Structure Basics 2. Structure Basics

Entry ID entry_id1pb5
Deposition date deposition_date2003-05-14
Structure title titleNMR Structure of a Prototype LNR Module from Human Notch1
Keywords keywordsNotch signaling, LIN12/Notch repeat, calcium-binding domain, protein module, disulfide bond, SIGNALING PROTEIN; SIGNALING PROTEIN
Experimental Method methodSOLUTION NMR

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

Radius of gyration Rg (Guinier) rg_guinier8.28
Radius of gyration Rg (electron density) rg_electron8.73
Forward intensity I(0) i078653900.00
Molecular weight molecular_weight59984.0 kDa
Excluded volume excluded_volume68817 ų
Envelope volume envelope_volume6490 ų
Hydration-shell volume shell_volume6032 ų
Envelope diameter envelope_diameter35.1
Shell Rg shell_rg14.69
Envelope Rg envelope_rg10.54
Shape Rg shape_rg8.77
Total Rg total_rg8.82
Total atoms total_atoms7408
Residues n_residues560
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 dmax29.1
Rg (real space) rg_real8.32
Rg uncertainty (real space) rg_real_error0.36
I(0) (real space) i0_real7.8650e+07
I(0) uncertainty (real space) i0_real_error9.4490e+05
Rg (reciprocal space) rg_reciprocal8.32
I(0) (reciprocal space) i0_reciprocal78650000.0000
Solution quality estimate total_estimate0.8463
Solution quality rating solution_quality GOOD a GOOD solution
P(r) peaks n_peaks2
Primary peak position r_peak_primary9.6
Skewness Skewness skewness0.493
Kurtosis Kurtosis kurtosis0.072
Angular range angular_range— – 0.5000 −1
Current regularization parameter α current_alpha0.0000
Highest regularization parameter α highest_alpha13120.0000
Real-space data points n_real_points80
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.731; Stabil: 0.997; Sysdev: 1.000; Positv: 1.000; Valcen: 0.898; Smooth: 0.917

5. Crystallography and Experiment 5. Crystallography & Experiment

6. Entities and Polymers Entities & Polymers (2)

7. Fold Classification (SCOP + CATH) 1 domains

SCOP 2.08 (1 domains)

Domain ID domain_idd1pb5a_
Class classg — Small proteins
Fold Fold foldg.65 — Notch domain
Superfamily Superfamily superfamilyg.65.1 — Notch domain
Family Family familyg.65.1.1 — Notch domain

8. Citations (1)

9. Files and Curves (10)